Journal articles on the topic 'Assembly'
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1
Ghosh, Tarini Shankar, Varun Mehra, and Sharmila S. Mande. "Grid-Assembly: An oligonucleotide composition-based partitioning strategy to aid metagenomic sequence assembly." Journal of Bioinformatics and Computational Biology 13, no. 03 (May 15, 2015): 1541004. http://dx.doi.org/10.1142/s0219720015410048.
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Metagenomics approach involves extraction, sequencing and characterization of the genomic content of entire community of microbes present in a given environment. In contrast to genomic data, accurate assembly of metagenomic sequences is a challenging task. Given the huge volume and the diverse taxonomic origin of metagenomic sequences, direct application of single genome assembly methods on metagenomes are likely to not only lead to an immense increase in requirements of computational infrastructure, but also result in the formation of chimeric contigs. A strategy to address the above challenge would be to partition metagenomic sequence datasets into clusters and assemble separately the sequences in individual clusters using any single-genome assembly method. The current study presents such an approach that uses tetranucleotide usage patterns to first represent sequences as points in a three dimensional (3D) space. The 3D space is subsequently partitioned into "Grids". Sequences within overlapping grids are then progressively assembled using any available assembler. We demonstrate the applicability of the current Grid-Assembly method using various categories of assemblers as well as different simulated metagenomic datasets. Validation results indicate that the Grid-Assembly approach helps in improving the overall quality of assembly, in terms of the purity and volume of the assembled contigs.
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Zuo, Guang Zhou, Qing Zhang, and Ming Liu. "Virtual Assembly of Equipment in Large Steel Structure." Advanced Materials Research 255-260 (May 2011): 4166–70. http://dx.doi.org/10.4028/www.scientific.net/amr.255-260.4166.
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The equipment assembled in large steel structure is particular and complex, which must be assembled with a special process plan. Virtual assembly technology provides a feasible idea for equipment assembly. Assembly path planning is the key technology of Virtual assembly. We propose a method of assembly path planning based on the analysis of basic workflow in assembly path planning. Using our algorithm to assemble the equipment find encountered far fewer problems than previous.
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Kim, Boyoung, Minyong Choi, Seung-Woo Son, Deokwon Yun, and Sukjune Yoon. "Vision-force guided precise robotic assembly for 2.5D components in a semistructured environment." Assembly Automation 41, no. 2 (April 8, 2021): 200–207. http://dx.doi.org/10.1108/aa-03-2020-0039.
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Purpose Many manufacturing sites require precision assembly. Particularly, similar to cell phones, assembly at the sub-mm scale is not easy, even for humans. In addition, the system should assemble each part with adequate force and avoid breaking the circuits with excessive force. The purpose of this study is to assemble high precision components with relatively reasonable vision devices compared to previous studies. Design/methodology/approach This paper presents a vision-force guided precise assembly system using a force sensor and two charge coupled device (CCD) cameras without an expensive 3-dimensional (3D) sensor or computer-aided design model. The system accurately estimates 6 degrees-of-freedom (DOF) poses from a 2D image in real time and assembles parts with the proper force. Findings In this experiment, three connectors are assembled on a printed circuit board. This system obtains high accuracy under 1 mm and 1 degree error, which shows that this system is effective. Originality/value This is a new method for sub-mm assembly using only two CCD cameras and one force sensor.
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Choodoungkiattikun, Khanthamat, and Uttapol Smutkupt. "Designing the Assembly Capability Assessment Model for Thai Wooden Furniture." International Journal of Global Optimization and Its Application 1, no. 4 (December 31, 2022): 258–65. http://dx.doi.org/10.56225/ijgoia.v1i4.104.
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There are many aspects to consider the good assembly model for Thai wooden furniture. The main idea is the assembly can be made in difference ways. As a result, the easy to assemble means the efficiency to produce. The way how to make an assembly need to be considers. The assembly assessment model is evaluated from the assembly’s method, the assembly’s point, the assembly’s direction, the assembly’s difficulty and the assembly’s motion and time. All these assembly criteria needed to be set to make the assembly easier. Also, part’s size and weight and part’s direction can affect the result of the assembly. With these assembly criteria, Thai’s wooden furniture experts are choosing to select sub-criteria and compare all sub-criteria. Then, the Analytic Hierarchy Process (AHP) is used to calculate the weight of each sub-criterion. With the weight of all sub-criteria when the assessors evaluate the way the assembly makes, the overall score is calculated. The higher overall score means a good assembly model. The second idea is because the assembly can be adjustable and changeable, therefore the assembly’s sequence needed to be considered. The sequence assessment model is developed to calculate the assembly time. The sequence assessment model will use assembly relationship chart and AND/OR graph to set up all the assembly sequence from the beginning to the finished furniture. The smaller assembly time shows the good assembly.
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Ludgate, Laurie, Kuancheng Liu, Laurie Luckenbaugh, Nicholas Streck, Stacey Eng, Christian Voitenleitner, William E. Delaney, and Jianming Hu. "Cell-Free Hepatitis B Virus Capsid Assembly Dependent on the Core Protein C-Terminal Domain and Regulated by Phosphorylation." Journal of Virology 90, no. 12 (April 13, 2016): 5830–44. http://dx.doi.org/10.1128/jvi.00394-16.
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ABSTRACTMultiple subunits of the hepatitis B virus (HBV) core protein (HBc) assemble into an icosahedral capsid that packages the viral pregenomic RNA (pgRNA). The N-terminal domain (NTD) of HBc is sufficient for capsid assembly, in the absence of pgRNA or any other viral or host factors, under conditions of high HBc and/or salt concentrations. The C-terminal domain (CTD) is deemed dispensable for capsid assembly although it is essential for pgRNA packaging. We report here that HBc expressed in a mammalian cell lysate, rabbit reticulocyte lysate (RRL), was able to assemble into capsids when (low-nanomolar) HBc concentrations mimicked those achieved under conditions of viral replicationin vivoand were far below those used previously for capsid assemblyin vitro. Furthermore, at physiologically low HBc concentrations in RRL, the NTD was insufficient for capsid assembly and the CTD was also required. The CTD likely facilitated assembly under these conditions via RNA binding and protein-protein interactions. Moreover, the CTD underwent phosphorylation and dephosphorylation events in RRL similar to those seenin vivowhich regulated capsid assembly. Importantly, the NTD alone also failed to accumulate in mammalian cells, likely resulting from its failure to assemble efficiently. Coexpression of the full-length HBc rescued NTD assembly in RRL as well as NTD expression and assembly in mammalian cells, resulting in the formation of mosaic capsids containing both full-length HBc and the NTD. These results have important implications for HBV assembly during replication and provide a facile cell-free system to study capsid assembly under physiologically relevant conditions, including its modulation by host factors.IMPORTANCEHepatitis B virus (HBV) is an important global human pathogen and the main cause of liver cancer worldwide. An essential component of HBV is the spherical capsid composed of multiple copies of a single protein, the core protein (HBc). We have developed a mammalian cell-free system in which HBc is expressed at physiological (low) concentrations and assembles into capsids under near-physiological conditions. In this cell-free system, as in mammalian cells, capsid assembly depends on the C-terminal domain (CTD) of HBc, in contrast to other assembly systems in which HBc assembles into capsids independently of the CTD under conditions of nonphysiological protein and salt concentrations. Furthermore, the phosphorylation state of the CTD regulates capsid assembly and RNA encapsidation in the cell-free system in a manner similar to that seen in mammalian cells. This system will facilitate detailed studies on capsid assembly and RNA encapsidation under physiological conditions and identification of antiviral agents that target HBc.
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Ulbrich, Pavel, Sarka Haubova, Milan V. Nermut, Eric Hunter, Michaela Rumlova, and Tomas Ruml. "Distinct Roles for Nucleic Acid in In Vitro Assembly of Purified Mason-Pfizer Monkey Virus CANC Proteins." Journal of Virology 80, no. 14 (July 15, 2006): 7089–99. http://dx.doi.org/10.1128/jvi.02694-05.
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ABSTRACT In contrast to other retroviruses, Mason-Pfizer monkey virus (M-PMV) assembles immature capsids in the cytoplasm. We have compared the ability of minimal assembly-competent domains from M-PMV and human immunodeficiency virus type 1 (HIV-1) to assemble in vitro into virus-like particles in the presence and absence of nucleic acids. A fusion protein comprised of the capsid and nucleocapsid domains of Gag (CANC) and its N-terminally modified mutant (ΔProCANC) were used to mimic the assembly of the viral core and immature particles, respectively. In contrast to HIV-1, where CANC assembled efficiently into cylindrical structures, the same domains of M-PMV were assembly incompetent. The addition of RNA or oligonucleotides did not complement this defect. In contrast, the M-PMV ΔProCANC molecule was able to assemble into spherical particles, while that of HIV-1 formed both spheres and cylinders. For M-PMV, the addition of purified RNA increased the efficiency with which ΔProCANC formed spherical particles both in terms of the overall amount and the numbers of completed spheres. The amount of RNA incorporated was determined, and for both rRNA and MS2-RNA, quantities similar to that of genomic RNA were encapsidated. Oligonucleotides also stimulated assembly; however, they were incorporated into ΔProCANC spherical particles in trace amounts that could not serve as a stoichiometric structural component for assembly. Thus, oligonucleotides may, through a transient interaction, induce conformational changes that facilitate assembly, while longer RNAs appear to facilitate the complete assembly of spherical particles.
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Erickson, Harold P., David E. Anderson, and Masaki Osawa. "FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One." Microbiology and Molecular Biology Reviews 74, no. 4 (December 2010): 504–28. http://dx.doi.org/10.1128/mmbr.00021-10.
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SUMMARY FtsZ, a bacterial homolog of tubulin, is well established as forming the cytoskeletal framework for the cytokinetic ring. Recent work has shown that purified FtsZ, in the absence of any other division proteins, can assemble Z rings when incorporated inside tubular liposomes. Moreover, these artificial Z rings can generate a constriction force, demonstrating that FtsZ is its own force generator. Here we review light microscope observations of how Z rings assemble in bacteria. Assembly begins with long-pitch helices that condense into the Z ring. Once formed, the Z ring can transition to short-pitch helices that are suggestive of its structure. FtsZ assembles in vitro into short protofilaments that are ∼30 subunits long. We present models for how these protofilaments might be further assembled into the Z ring. We discuss recent experiments on assembly dynamics of FtsZ in vitro, with particular attention to how two regulatory proteins, SulA and MinC, inhibit assembly. Recent efforts to develop antibacterial drugs that target FtsZ are reviewed. Finally, we discuss evidence of how FtsZ generates a constriction force: by protofilament bending into a curved conformation.
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PADILLA, JENNIFER E., MATTHEW J. PATITZ, ROBERT T. SCHWELLER, NADRIAN C. SEEMAN, SCOTT M. SUMMERS, and XINGSI ZHONG. "ASYNCHRONOUS SIGNAL PASSING FOR TILE SELF-ASSEMBLY: FUEL EFFICIENT COMPUTATION AND EFFICIENT ASSEMBLY OF SHAPES." International Journal of Foundations of Computer Science 25, no. 04 (June 2014): 459–88. http://dx.doi.org/10.1142/s0129054114400061.
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In this paper we demonstrate the power of a model of tile self-assembly based on active glues which can dynamically change state. We formulate the Signal-passing Tile Assembly Model (STAM), based on the model of Padilla et al. [24] to be asynchronous, allowing any action of turning a glue on or off, attaching a new tile, or breaking apart an assembly to happen in any order. Within this highly generalized model we provide three new solutions to tile self-assembly problems that have been addressed within the abstract Tile Assembly Model and its variants, showing that signal passing tiles allow for substantial improvement across multiple complexity metrics. Our first result utilizes a recursive assembly process to achieve tile-type efficient assembly of linear structures, using provably fewer tile types than what is possible in standard tile assembly models. Our second system of signal-passing tiles simulates any Turing machine with high fuel efficiency by using only a constant number of tiles per computation step. Our third system assembles the discrete Sierpinski triangle, demonstrating that this pattern can be strictly self-assembled within the STAM. This result is of particular interest in that it is known that this pattern cannot self-assemble within a number of well studied tile self-assembly models. Notably, all of our constructions are at temperature 1, further demonstrating that signal-passing confers the power to bypass many restrictions found in standard tile assembly models.
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Crist, Rachael M., Siddhartha A. K. Datta, Andrew G. Stephen, Ferri Soheilian, Jane Mirro, Robert J. Fisher, Kunio Nagashima, and Alan Rein. "Assembly Properties of Human Immunodeficiency Virus Type 1 Gag-Leucine Zipper Chimeras: Implications for Retrovirus Assembly." Journal of Virology 83, no. 5 (December 10, 2008): 2216–25. http://dx.doi.org/10.1128/jvi.02031-08.
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ABSTRACT Expression of the retroviral Gag protein leads to formation of virus-like particles in mammalian cells. In vitro and in vivo experiments show that nucleic acid is also required for particle assembly. However, several studies have demonstrated that chimeric proteins in which the nucleocapsid domain of Gag is replaced by a leucine zipper motif can also assemble efficiently in mammalian cells. We have now analyzed assembly by chimeric proteins in which nucleocapsid of human immunodeficiency virus type 1 (HIV-1) Gag is replaced by either a dimerizing or a trimerizing zipper. Both proteins assemble well in human 293T cells; the released particles lack detectable RNA. The proteins can coassemble into particles together with full-length, wild-type Gag. We purified these proteins from bacterial lysates. These recombinant “Gag-Zipper” proteins are oligomeric in solution and do not assemble unless cofactors are added; either nucleic acid or inositol phosphates (IPs) can promote particle assembly. When mixed with one equivalent of IPs (which do not support assembly of wild-type Gag), the “dimerizing” Gag-Zipper protein misassembles into very small particles, while the “trimerizing” protein assembles correctly. However, addition of both IPs and nucleic acid leads to correct assembly of all three proteins; the “dimerizing” Gag-Zipper protein also assembles correctly if inositol hexakisphosphate is supplemented with other polyanions. We suggest that correct assembly requires both oligomeric association at the C terminus of Gag and neutralization of positive charges near its N terminus.
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Bi, Lie, Wenrong Wu, Juan Zhang, and Honggang Yang. "An assembly method for micro parts jointing with given space angle based on projection matching." Modern Physics Letters B 31, no. 05 (February 20, 2017): 1750041. http://dx.doi.org/10.1142/s0217984917500415.
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It is difficult to assemble micro parts jointing with given space angle as the parts assembled are not on the same flat and the visual depth of microscopic vision is small, which can cause the images gathered by the microscopic vision unintelligible and feature extraction difficult. For the problem, this paper presents an assembly method of micro parts based on projection matching. It can assemble micro parts jointing with given space angle accurately. Firstly, an ideal assembly model is established as the size of the micro parts through the drawing software. Secondly, a graphics algorithm based on the primitive information from CAD is designed. Thirdly, according to the pixel value calibration and the graphics algorithm, the projection pictures are shown on the control interface. Lastly, the control method of micro parts is proposed to assemble them with given space angle. And we accomplished an assembly experiment of micro-tube and micro-column in this way, whose assembly deviation is 0.12[Formula: see text]. Experiment results indicate that the angle between two micro parts assembled can be controlled within the given deviation.
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Colloms, Sean D., Christine A. Merrick, Femi J. Olorunniji, W. Marshall Stark, Margaret C. M. Smith, Anne Osbourn, Jay D. Keasling, and Susan J. Rosser. "Rapid metabolic pathway assembly and modification using serine integrase site-specific recombination." Nucleic Acids Research 42, no. 4 (November 12, 2013): e23-e23. http://dx.doi.org/10.1093/nar/gkt1101.
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Abstract Synthetic biology requires effective methods to assemble DNA parts into devices and to modify these devices once made. Here we demonstrate a convenient rapid procedure for DNA fragment assembly using site-specific recombination by ϕC31 integrase. Using six orthogonal attP/attB recombination site pairs with different overlap sequences, we can assemble up to five DNA fragments in a defined order and insert them into a plasmid vector in a single recombination reaction. ϕC31 integrase-mediated assembly is highly efficient, allowing production of large libraries suitable for combinatorial gene assembly strategies. The resultant assemblies contain arrays of DNA cassettes separated by recombination sites, which can be used to manipulate the assembly by further recombination. We illustrate the utility of these procedures to (i) assemble functional metabolic pathways containing three, four or five genes; (ii) optimize productivity of two model metabolic pathways by combinatorial assembly with randomization of gene order or ribosome binding site strength; and (iii) modify an assembled metabolic pathway by gene replacement or addition.
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Kato, J. Y., M. Matsuoka, D. K. Strom, and C. J. Sherr. "Regulation of cyclin D-dependent kinase 4 (cdk4) by cdk4-activating kinase." Molecular and Cellular Biology 14, no. 4 (April 1994): 2713–21. http://dx.doi.org/10.1128/mcb.14.4.2713-2721.1994.
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The accumulation of assembled holoenzymes composed of regulatory D-type cyclins and their catalytic partner, cyclin-dependent kinase 4 (cdk4), is rate limiting for progression through the G1 phase of the cell cycle in mammalian fibroblasts. Both the synthesis and assembly of D-type cyclins and cdk4 depend upon serum stimulation, but even when both subunits are ectopically overproduced, they do not assemble into complexes in serum-deprived cells. When coexpressed from baculoviral vectors in intact Sf9 insect cells, cdk4 assembles with D-type cyclins to form active protein kinases. In contrast, recombinant D-type cyclin and cdk4 subunits produced in insect cells or in bacteria do not assemble as efficiently into functional holoenzymes when combined in vitro but can be activated in the presence of lysates obtained from proliferating mammalian cells. Assembly of cyclin D-cdk4 complexes in coinfected Sf9 cells facilitates phosphorylation of cdk4 on threonine 172 by a cdk-activating kinase (CAK). Assembly can proceed in the absence of this modification, but cdk4 mutants which cannot be phosphorylated by CAK remain catalytically inactive. Therefore, formation of the cyclin D-cdk4 complex and phosphorylation of the bound catalytic subunit are independently regulated, and in addition to the requirement for CAK activity, serum stimulation is required to promote assembly of the complexes in mammalian cells.
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Kato, J. Y., M. Matsuoka, D. K. Strom, and C. J. Sherr. "Regulation of cyclin D-dependent kinase 4 (cdk4) by cdk4-activating kinase." Molecular and Cellular Biology 14, no. 4 (April 1994): 2713–21. http://dx.doi.org/10.1128/mcb.14.4.2713.
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The accumulation of assembled holoenzymes composed of regulatory D-type cyclins and their catalytic partner, cyclin-dependent kinase 4 (cdk4), is rate limiting for progression through the G1 phase of the cell cycle in mammalian fibroblasts. Both the synthesis and assembly of D-type cyclins and cdk4 depend upon serum stimulation, but even when both subunits are ectopically overproduced, they do not assemble into complexes in serum-deprived cells. When coexpressed from baculoviral vectors in intact Sf9 insect cells, cdk4 assembles with D-type cyclins to form active protein kinases. In contrast, recombinant D-type cyclin and cdk4 subunits produced in insect cells or in bacteria do not assemble as efficiently into functional holoenzymes when combined in vitro but can be activated in the presence of lysates obtained from proliferating mammalian cells. Assembly of cyclin D-cdk4 complexes in coinfected Sf9 cells facilitates phosphorylation of cdk4 on threonine 172 by a cdk-activating kinase (CAK). Assembly can proceed in the absence of this modification, but cdk4 mutants which cannot be phosphorylated by CAK remain catalytically inactive. Therefore, formation of the cyclin D-cdk4 complex and phosphorylation of the bound catalytic subunit are independently regulated, and in addition to the requirement for CAK activity, serum stimulation is required to promote assembly of the complexes in mammalian cells.
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Sun, Wen Lei, Yu Shan Cao, and Wei Sun. "The Research of Virtual Assembly of Cotton Picker Roller Based on Virtual Reality." Advanced Materials Research 156-157 (October 2010): 496–99. http://dx.doi.org/10.4028/www.scientific.net/amr.156-157.496.
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This paper took the roller of a new cotton picker as the example, drew its various parts and assemblyed overally in the three-dimensional mapping software environment of UG, imported the models into the virtual reality assembly platform by the interface between UG and VAPlatform, added the virtual hand and carried through the virtual assembly in the virtual scene based on the certain assembly restriction in UG. The paper realized the visualization of the assembly path, offered the foundation for the feasible assembly path, and finally obtained the reasonable assembly process, provided a set of reasonable operation guide for the workers to assemble the cotton pickers.
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Lu, Lei, Mark S. Ladinsky, and Tomas Kirchhausen. "Formation of the postmitotic nuclear envelope from extended ER cisternae precedes nuclear pore assembly." Journal of Cell Biology 194, no. 3 (August 8, 2011): 425–40. http://dx.doi.org/10.1083/jcb.201012063.
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During mitosis, the nuclear envelope merges with the endoplasmic reticulum (ER), and nuclear pore complexes are disassembled. In a current model for reassembly after mitosis, the nuclear envelope forms by a reshaping of ER tubules. For the assembly of pores, two major models have been proposed. In the insertion model, nuclear pore complexes are embedded in the nuclear envelope after their formation. In the prepore model, nucleoporins assemble on the chromatin as an intermediate nuclear pore complex before nuclear envelope formation. Using live-cell imaging and electron microscope tomography, we find that the mitotic assembly of the nuclear envelope primarily originates from ER cisternae. Moreover, the nuclear pore complexes assemble only on the already formed nuclear envelope. Indeed, all the chromatin-associated Nup107–160 complexes are in single units instead of assembled prepores. We therefore propose that the postmitotic nuclear envelope assembles directly from ER cisternae followed by membrane-dependent insertion of nuclear pore complexes.
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Isaji, Mamiko, Hisataka Iwata, Hiroshi Harayama, and Masashi Miyake. "The localization of LAP2β during pronuclear formation in bovine oocytes after fertilization or activation." Zygote 14, no. 2 (May 2006): 157–67. http://dx.doi.org/10.1017/s0967199406003613.
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SummaryWe have shown that the assembly of lamin-associated polypeptide (LAP) 2β was detected surrounding the chromatin mass around the time of extrusion of the second polar body (PB) in some fertilized oocytes, but not in most activated oocytes, by using A23187 and cycloheximide (CaA + CH). Here, we immunohistologically analysed the correlation between LAP2β assembly and chromatin condensation in fertilized and activated oocytes during the second meiosis. In bovine cumulus cells, the onset of LAP2β assembly was observed around anaphase chromosomes with strongly phosphorylated histone H3. No LAP2β assembled around the chromosomes in the first and second polar bodies and the alternative oocyte chromatin (oCh) if histone H3 was phosphorylated. Only histone H3 of oCh was completely dephosphorylated during the telophase II/G1 transition (Tel II/G1), and then LAP2β assembled around only the oCh without phosphorylated histone H3. In the oocytes activated by CaA + CH, LAP2β did not assemble around the condensed oCh during the Tel II/G1 transition, although their histone H3 dephosphorylation occurred rather rapidly compared with that of the fertilized oocytes. The patterns of histone H3 dephosphorylation and LAP2β assembly in oocytes activated by CaA alone showed greater similarity to those in fertilized oocytes than to those in oocytes activated by CaA + CH. These results show that LAP2β assembles around only oCh after complete dephosphorylation of histone H3 after fertilization and activation using CaA alone, and that the timing of histone H3 dephosphorylation and LAP2β assembly in these oocytes is different from that of somatic cells. The results also indicate that CH treatment inhibits LAP2β assembly around oCh but not histone H3 dephosphorylation.
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Moss, Eli L., Dylan G. Maghini, and Ami S. Bhatt. "Complete, closed bacterial genomes from microbiomes using nanopore sequencing." Nature Biotechnology 38, no. 6 (February 10, 2020): 701–7. http://dx.doi.org/10.1038/s41587-020-0422-6.
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AbstractMicrobial genomes can be assembled from short-read sequencing data, but the assembly contiguity of these metagenome-assembled genomes is constrained by repeat elements. Correct assignment of genomic positions of repeats is crucial for understanding the effect of genome structure on genome function. We applied nanopore sequencing and our workflow, named Lathe, which incorporates long-read assembly and short-read error correction, to assemble closed bacterial genomes from complex microbiomes. We validated our approach with a synthetic mixture of 12 bacterial species. Seven genomes were completely assembled into single contigs and three genomes were assembled into four or fewer contigs. Next, we used our methods to analyze metagenomics data from 13 human stool samples. We assembled 20 circular genomes, including genomes of Prevotella copri and a candidate Cibiobacter sp. Despite the decreased nucleotide accuracy compared with alternative sequencing and assembly approaches, our methods improved assembly contiguity, allowing for investigation of the role of repeat elements in microbial function and adaptation.
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Jiang, Wei, Yan Ling Han, Wei Dong, and Qiang Zhou. "Analysis for the Large Precise Equipment Assembly." Applied Mechanics and Materials 670-671 (October 2014): 915–19. http://dx.doi.org/10.4028/www.scientific.net/amm.670-671.915.
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In industrial and construction process, some precise equipments should be assembled on site. The assembly requirement is very high, and it is hard to assemble the accessories together. The paper is based on a real situation in construction to study the precise equipment assembly method. First, it introduces the situation on site and the parameter of the parts of equipment need to be assembled. Then show the cost for the traditional assembly method. Put forward a new method to do the work. At last, compare the advantage and disadvantage of the two methods. The new method mentioned in the paper will greatly improve the installation efficiency in the construction.
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Sakalian, Michael, Stephanie S. Dittmer, A. Dustin Gandy, Nathan D. Rapp, Aleš Zábranský, and Eric Hunter. "The Mason-Pfizer Monkey Virus Internal Scaffold Domain Enables In Vitro Assembly of Human Immunodeficiency Virus Type 1 Gag." Journal of Virology 76, no. 21 (November 1, 2002): 10811–20. http://dx.doi.org/10.1128/jvi.76.21.10811-10820.2002.
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ABSTRACT The Mason-Pfizer monkey virus (M-PMV) Gag protein possesses the ability to assemble into an immature capsid when synthesized in a reticulocyte lysate translation system. In contrast, the human immunodeficiency virus (HIV) Gag protein is incapable of assembly in parallel assays. To enable the assembly of HIV Gag, we have combined or inserted regions of M-PMV Gag into HIV Gag. By both biochemical and morphological criteria, several of these chimeric Gag molecules are capable of assembly into immature capsid-like structures in this in vitro system. Chimeric species containing large regions of M-PMV Gag fused to HIV Gag sequences failed to assemble, while species consisting of only the M-PMV p12 region, and its internal scaffold domain (ISD), fused to HIV Gag were capable of assembly, albeit at reduced kinetics compared to M-PMV Gag. The ability of the ISD to induce assembly of HIV Gag, which normally assembles at the plasma membrane, suggests a common requirement for a concentrating factor in retrovirus assembly. Despite the dramatic effect of the ISD on chimera assembly, the function of HIV Gag domains in that process was found to remain essential, since an assembly-defective mutant of HIV CA, M185A, abolished assembly when introduced into the chimera. This continued requirement for HIV Gag domain function in the assembly of chimeric molecules will allow this in vitro system to be used for the analysis of potential inhibitors of HIV immature particle assembly.
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Chapin, Samantha, Holly Everson, William Chapin, and Erik Komendera. "Built On-Orbit Robotically Assembled Gigatruss (BORG): Ground Robotic Demonstration." Aerospace 11, no. 6 (May 31, 2024): 447. http://dx.doi.org/10.3390/aerospace11060447.
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The next generation of large space infrastructure will require crucial advancements in current technology. Current methodologies focus on large deployable structures folded into cramped payload fairings or revolutionary assembly techniques requiring many moving components. Utilizing both in-space assembly and deployable concepts, a hybrid mixed assembly scheme was posed using smaller deployable units interspersed with rigid connecting elements to assemble these large architectures. The Built On-Orbit Robotically Assembled Gigatruss (BORG) structure allows for modularity in assembly and repair with the number of separate elements comprising the structure to be reduced, compared to strut-by-strut assembly. The following documents the process of constructing and running physical trials on a prototype BORG architecture. Additionally, a Semantic and Fiducial Aided Graph Simultaneous Localization and Mapping (SF-GraphSLAM) approach is taken to verify the relation of assembled and deployed truss elements to aid in error evaluation and state estimation. This technology demonstration stands as a proof of concept in verifying the viability of the BORG architecture as a method for large structure assembly.
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Sakalian, Michael, and Eric Hunter. "Separate Assembly and Transport Domains within the Gag Precursor of Mason-Pfizer Monkey Virus." Journal of Virology 73, no. 10 (October 1, 1999): 8073–82. http://dx.doi.org/10.1128/jvi.73.10.8073-8082.1999.
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ABSTRACT Mason-Pfizer monkey virus (M-PMV), the prototypical type D retrovirus, assembles immature capsids within the cytoplasm of the cell prior to plasma membrane interaction. Several mutants of M-PMV Gag have been described which display altered transport, assembly, or both. In this report, we describe the use of an in vitro synthesis and assembly system to distinguish between defects in intracellular transport and the process of assembly itself for two previously describedgag gene mutants. Matrix domain mutant R55W converts the type D morphogenesis of M-PMV particles into type C and has been hypothesized to alter the transport of Gag, redirecting it to the plasma membrane where assembly subsequently occurs. We show here that R55W can assemble in both the in vitro translation-assembly system and within inclusion bodies in bacteria and thus has retained the capacity to assemble in the cytoplasm. This supports the concept that R55 is located within a domain responsible for the transport of Gag to an intracellular site for assembly. In contrast, deletions within the p12 domain of M-PMV Gag had previously been shown to affect the efficiency of particle formation such that under low-level expression conditions, Gag would fail to assemble. We demonstrate here that the efficiency of assembly in the in vitro system mirrors that seen in cells under expression conditions similar to that of an infection. These results argue that the p12 domain of this D-type retrovirus plays a critical role in the membrane-independent assembly of immature capsids.
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Kuo, Chia Lung, and Jing Dae Huang. "Joint Design and Fabrication for Mechanical Elastic Self-deformation Micro-Assembly Technology." Materials Science Forum 505-507 (January 2006): 829–34. http://dx.doi.org/10.4028/www.scientific.net/msf.505-507.829.
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A microstructure assembled into another part using the mechanical elastic self-deformation assembly technology is proposed in the paper. To attain the self-deformation during assembling, the assembly joint on the microstructure is analytically designed as the feature with an appropriate taper and cross clearance. Take account of the accuracy, the whole process from micro-fabrication to micro-assembly is carefully planned and practiced under a micro-EDM machining center system which consists of vertical micro-EDM with dividing mechanism, and horizontal micro-machining mechanism, which is referred to as on-process micro-assembly. To illustrate the micro-assembly strategies and procedures, a micro-rotor production including assemble a tungsten carbide four-phase micro-rotor into an alumina base has been provided and discussed.
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Nguyen-Mau, Sao-Mai, So-Young Oh, Daphne I. Schneewind, Dominique Missiakas, and Olaf Schneewind. "Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly." Journal of Bacteriology 197, no. 19 (July 27, 2015): 3216–27. http://dx.doi.org/10.1128/jb.00492-15.
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ABSTRACTBacillus anthracisvegetative forms assemble an S-layer comprised of two S-layer proteins, Sap and EA1. A hallmark of S-layer proteins are their C-terminal crystallization domains, which assemble into a crystalline lattice once these polypeptides are deposited on the bacterial surface via association between their N-terminal S-layer homology domains and the secondary cell wall polysaccharide. Here we show thatslaQ, encoding a small cytoplasmic protein conserved among pathogenic bacilli elaborating S-layers, is required for the efficient secretion and assembly of Sap and EA1. S-layer protein precursors cosediment with SlaQ, and SlaQ appears to facilitate Sap assembly. Purified SlaQ polymerizes and when mixed with purified Sap promotes thein vitroformation of tubular S-layer structures. A model is discussed whereby SlaQ, in conjunction with S-layer secretion factors SecA2 and SlaP, promotes localized secretion and S-layer assembly inB. anthracis.IMPORTANCES-layer proteins are endowed with the propensity for self-assembly into crystalline arrays. Factors promoting S-layer protein assembly have heretofore not been reported. We identifiedBacillus anthracisSlaQ, a small cytoplasmic protein that facilitates S-layer protein assemblyin vivoandin vitro.
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Zhang, Yun Dian, and Peng Wang. "Developing of High-Power Sandwich Type Piezoelectric Transducer Automatic Assembly Machine." Applied Mechanics and Materials 602-605 (August 2014): 1034–38. http://dx.doi.org/10.4028/www.scientific.net/amm.602-605.1034.
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This paper discusses the basic parts of the assembly machine,calculate the relationship between torque and axial force,torque and voltage of the piezoelectric transducer.It also analysis the mechanical structure of mechanical.It introduces the motor’s control method .the successful assembly machine is used to assemble the piezoelectric transducer,the experiment indicates that with the increase of voltage, the resonance frequency increases,the impedance is on the decline,the static capacitance remains unchanged basically.And comparison of the assembled and the first assembly piezoelectric transducer,the latter has better performance.
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Kniert, Justine, Theodore dos Santos, Heather E. Eaton, Woo Jung Cho, Greg Plummer, and Maya Shmulevitz. "Reovirus uses temporospatial compartmentalization to orchestrate core versus outercapsid assembly." PLOS Pathogens 18, no. 9 (September 13, 2022): e1010641. http://dx.doi.org/10.1371/journal.ppat.1010641.
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Reoviridae virus family members, such as mammalian orthoreovirus (reovirus), encounter a unique challenge during replication. To hide the dsRNA from host recognition, the genome remains encapsidated in transcriptionally active proteinaceous core capsids that transcribe and release +RNA. De novo +RNAs and core proteins must repeatedly assemble into new progeny cores in order to logarithmically amplify replication. Reoviruses also produce outercapsid (OC) proteins μ1, σ3 and σ1 that assemble onto cores to create highly stable infectious full virions. Current models of reovirus replication position amplification of transcriptionally-active cores and assembly of infectious virions in shared factories, but we hypothesized that since assembly of OC proteins would halt core amplification, OC assembly is somehow regulated. Using kinetic analysis of virus +RNA, core and OC proteins, core assembly and whole virus assembly, assembly of OC proteins was found to be temporally delayed. All viral RNAs and proteins were made simultaneously, eliminating the possibility that delayed OC RNAs or proteins account for delayed OC assembly. High resolution fluorescence and electron microscopy revealed that core amplification occurred early during infection at peripheral core-only factories, while all OC proteins associated with lipid droplets (LDs) that coalesced near the nucleus in a μ1–dependent manner. Core-only factories transitioned towards the nucleus despite cycloheximide-mediated halting of new protein expression, while new core-only factories developed in the periphery. As infection progressed, OC assembly occurred at LD-and nuclear-proximal factories. Silencing of OC μ1 expression with siRNAs led to large factories that remained further from the nucleus, implicating μ1 in the transition to perinuclear factories. Moreover, late during infection, +RNA pools largely contributed to the production of de-novo viral proteins and fully-assembled infectious viruses. Altogether the results suggest an advanced model of reovirus replication with spatiotemporal segregation of core amplification, OC complexes and fully assembled virions.
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Life, Rachel B., Eun-Gyung Lee, Scott W. Eastman, and Maxine L. Linial. "Mutations in the Amino Terminus of Foamy Virus Gag Disrupt Morphology and Infectivity but Do Not Target Assembly." Journal of Virology 82, no. 13 (April 23, 2008): 6109–19. http://dx.doi.org/10.1128/jvi.00503-08.
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ABSTRACT Foamy viruses (FVs) assemble using pathways distinct from those of orthoretroviruses. FV capsid assembly takes place near the host microtubule-organizing center (MTOC). Assembled capsids then migrate by an unknown mechanism to the trans-Golgi network to colocalize with the FV glycoprotein, Env. Interaction with Env is required for FV capsid egress from cells; the amino terminus of FV Gag contains a cytoplasmic targeting/retention signal that is responsible for targeting assembly to the MTOC. A mutant Gag was constructed by addition of a myristylation (M) signal in an attempt to target assembly to the plasma membrane and potentially overcome the dependence upon Env for budding (S. W. Eastman and M. L. Linial, J. Virol. 75:6857-6864, 2001). Using this and additional mutants, we now show that assembly is not redirected to the plasma membrane. Addition of an M signal leads to gross morphological defects. The aberrant particles still assemble near the MTOC but do not produce infectious virus. Although extracellular Gag can be detected in a pelletable form in the absence of Env, the mutant particles contain very little genomic RNA and are less dense. Our analyses indicate that the amino terminus of Gag contains an Env interaction domain that is critical for bona fide egress of assembled capsids.
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Murugan, Arvind, Zorana Zeravcic, Michael P. Brenner, and Stanislas Leibler. "Multifarious assembly mixtures: Systems allowing retrieval of diverse stored structures." Proceedings of the National Academy of Sciences 112, no. 1 (December 22, 2014): 54–59. http://dx.doi.org/10.1073/pnas.1413941112.
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Self-assembly materials are traditionally designed so that molecular or mesoscale components form a single kind of large structure. Here, we propose a scheme to create “multifarious assembly mixtures,” which self-assemble many different large structures from a set of shared components. We show that the number of multifarious structures stored in the solution of components increases rapidly with the number of different types of components. However, each stored structure can be retrieved by tuning only a few parameters, the number of which is only weakly dependent on the size of the assembled structure. Implications for artificial and biological self-assembly are discussed.
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Li, Yu-Long, Dong-Xiu Xue, Bai-Dong Zhang, and Jin-Xian Liu. "An optimized approach for local de novo assembly of overlapping paired-end RAD reads from multiple individuals." Royal Society Open Science 5, no. 2 (February 2018): 171589. http://dx.doi.org/10.1098/rsos.171589.
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Restriction site-associated DNA (RAD) sequencing is revolutionizing studies in ecological, evolutionary and conservation genomics. However, the assembly of paired-end RAD reads with random-sheared ends is still challenging, especially for non-model species with high genetic variance. Here, we present an efficient optimized approach with a pipeline software, RADassembler, which makes full use of paired-end RAD reads with random-sheared ends from multiple individuals to assemble RAD contigs. RADassembler integrates the algorithms for choosing the optimal number of mismatches within and across individuals at the clustering stage, and then uses a two-step assembly approach at the assembly stage. RADassembler also uses data reduction and parallelization strategies to promote efficiency. Compared to other tools, both the assembly results based on simulation and real RAD datasets demonstrated that RADassembler could always assemble the appropriate number of contigs with high qualities, and more read pairs were properly mapped to the assembled contigs. This approach provides an optimal tool for dealing with the complexity in the assembly of paired-end RAD reads with random-sheared ends for non-model species in ecological, evolutionary and conservation studies. RADassembler is available at https://github.com/lyl8086/RADscripts.
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Kunkel, Meghan, Marta Lorinczi, René Rijnbrand, Stanley M. Lemon, and Stanley J. Watowich. "Self-Assembly of Nucleocapsid-Like Particles from Recombinant Hepatitis C Virus Core Protein." Journal of Virology 75, no. 5 (March 1, 2001): 2119–29. http://dx.doi.org/10.1128/jvi.75.5.2119-2129.2001.
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ABSTRACT Little is known about the assembly pathway and structure of hepatitis C virus (HCV) since insufficient quantities of purified virus are available for detailed biophysical and structural studies. Here, we show that bacterially expressed HCV core proteins can efficiently self-assemble in vitro into nucleocapsid-like particles. These particles have a regular, spherical morphology with a modal distribution of diameters of approximately 60 nm. Self-assembly of nucleocapsid-like particles requires structured RNA molecules. The 124 N-terminal residues of the core protein are sufficient for self-assembly into nucleocapsid-like particles. Inclusion of the carboxy-terminal domain of the core protein modifies the core assembly pathway such that the resultant particles have an irregular outline. However, these particles are similar in size and shape to those assembled from the 124 N-terminal residues of the core protein. These results provide novel opportunities to delineate protein-protein and protein-RNA interactions critical for HCV assembly, to study the molecular details of HCV assembly, and for performing high-throughput screening of assembly inhibitors.
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Wang, Weihao, Rufeng Zhang, Mingyu You, Hongjun Zhou, and Bin He. "3D Assembly Completion." Proceedings of the AAAI Conference on Artificial Intelligence 37, no. 3 (June 26, 2023): 2663–71. http://dx.doi.org/10.1609/aaai.v37i3.25365.
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Automatic assembly is a promising research topic in 3D computer vision and robotics. Existing works focus on generating assembly (e.g., IKEA furniture) from scratch with a set of parts, namely 3D part assembly. In practice, there are higher demands for the robot to take over and finish an incomplete assembly (e.g., a half-assembled IKEA furniture) with an off-the-shelf toolkit, especially in human-robot and multi-agent collaborations. Compared to 3D part assembly, it is more complicated in nature and remains unexplored yet. The robot must understand the incomplete structure, infer what parts are missing, single out the correct parts from the toolkit and finally, assemble them with appropriate poses to finish the incomplete assembly. Geometrically similar parts in the toolkit can interfere, and this problem will be exacerbated with more missing parts. To tackle this issue, we propose a novel task called 3D assembly completion. Given an incomplete assembly, it aims to find its missing parts from a toolkit and predict the 6-DoF poses to make the assembly complete. To this end, we propose FiT, a framework for Finishing the incomplete 3D assembly with Transformer. We employ the encoder to model the incomplete assembly into memories. Candidate parts interact with memories in a memory-query paradigm for final candidate classification and pose prediction. Bipartite part matching and symmetric transformation consistency are embedded to refine the completion. For reasonable evaluation and further reference, we design two standard toolkits of different difficulty, containing different compositions of candidate parts. We conduct extensive comparisons with several baseline methods and ablation studies, demonstrating the effectiveness of the proposed method.
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Zlotnick, A. "Simple Models and Simple Analyses of Virus Capsid Assembly." Journal of Theoretical Medicine 6, no. 2 (2005): 111–14. http://dx.doi.org/10.1080/10273660500149943.
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Assembly of even a simple virus is a complex reaction. Yet, in many cases, the capsids of isometric viruses assemble spontaneously and with high fidelityin vitro.In vitroreactions can be used as the basis for interpreting assemblyin vivo, searching for assembly-directed small molecules, or subverting normal assembly to generate novel structures. A model is required to interpret experimental observation of any complex reaction. To this end, we developed a thermodynamickinetic (master equation) model, in which assembly is described in terms of a cascade of low order reactions. The resulting model can readily be adjusted to match the specific features of a biological system. Simulations replicate experimental observations of assembly and lead to experimentally testable predictions. Analyses based on a basic model, in which only a single path from monomer to capsid was posited, are equally applicable to sparse and complete models that include selected intermediates and every possible intermediate, respectively.
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Contractor, Noshir. "Some assembly required: leveraging Web science to understand and enable team assembly." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 371, no. 1987 (March 28, 2013): 20120385. http://dx.doi.org/10.1098/rsta.2012.0385.
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Recent advances on the Web have generated unprecedented opportunities for individuals around the world to assemble into teams. And yet, because of the Web, the nature of teams and how they are assembled has changed radically. Today, many teams are ad hoc, agile, distributed, transient entities that are assembled from a larger primordial network of relationships within virtual communities. These assemblages possess the potential to unleash the high levels of creativity and innovation necessary for productively addressing many of the daunting challenges confronting contemporary society. This article argues that Web science is particularly well suited to help us realize this potential by making a substantial interdisciplinary intellectual investment in (i) advancing theories that explain our socio-technical motivations to form teams, (ii) the development of new analytic methods and models to untangle the unique influences of these motivations on team assembly, (iii) harvesting, curating and leveraging the digital trace data offered by the Web to test our models, and (iv) implementing recommender systems that use insights gleaned from our richer theoretical understanding of the motivations that lead to effective team assembly.
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Chuang, Chien-Hui, Aleesa J. Schlientz, Jie Yang, and Bruce Bowerman. "Microtubule assembly and pole coalescence: early steps in Caenorhabditiselegans oocyte meiosis I spindle assembly." Biology Open 9, no. 6 (June 3, 2020): bio052308. http://dx.doi.org/10.1242/bio.052308.
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ABSTRACTHow oocytes assemble bipolar meiotic spindles in the absence of centrosomes as microtubule organizing centers remains poorly understood. We have used live cell imaging in Caenorhabditis elegans to investigate requirements for the nuclear lamina and for conserved regulators of microtubule dynamics during oocyte meiosis I spindle assembly, assessing these requirements with respect to recently identified spindle assembly steps. We show that the nuclear lamina is required for microtubule bundles to form a peripheral cage-like structure that appears shortly after oocyte nuclear envelope breakdown and surrounds the oocyte chromosomes, although bipolar spindles still assembled in its absence. Although two conserved regulators of microtubule nucleation, RAN-1 and γ-tubulin, are not required for bipolar spindle assembly, both contribute to normal levels of spindle-associated microtubules and spindle assembly dynamics. Finally, the XMAP215 ortholog ZYG-9 and the nearly identical minus-end directed kinesins KLP-15/16 are required for proper assembly of the early cage-like structure of microtubule bundles, and for early spindle pole foci to coalesce into a bipolar structure. Our results provide a framework for assigning molecular mechanisms to recently described steps in C. elegans oocyte meiosis I spindle assembly.
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Bennett, Antonette, Robert McKenna, and Mavis Agbandje-McKenna. "A Comparative Analysis of the Structural Architecture of ssDNA Viruses." Computational and Mathematical Methods in Medicine 9, no. 34 (2008): 183–96. http://dx.doi.org/10.1080/17486700802168247.
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Virus assembly, utilizing a limited number of viral coat protein (CP or VP) building blocks, is an excellent example of a directed macromolecular interaction occurring in nature. Two basic principles govern the assembly of spherical (icosahedral) viruses: (i) Genetic Economy – the encapsidated genome encodes a single or few CPs that assemble a protective shell (the viral capsid); and (ii) specificity – the CPs have to fold to recognize each other and form exact CP–CP interfacial interactions during the assembly pathway. Using a variety of biophysical techniques, including X-ray crystallography and cryo-electron microscopy, combined with homology model building, biochemistry and molecular biology, the nature of the interactions between protein–protein subunits and protein–nucleic acid that facilitate viral capsid assembly have been studied. This review discusses both the similarities and differences that have been elucidated for ssDNAMicroviridae, Geminiviridae, and Parvoviridaevirus families. TheMicroviridaerepresent a family of bacteriophages that utilize several CPs and scaffold proteins to assemble aT= 1 icosahedral capsid, theGeminiviridaeplant viruses assemble a unique twinned quasi-isometric (geminate) pseudoT= 1 virion assembled from a single CP and theParvoviridaerepresent animal viruses whoseT= 1 capsids are formed from the common overlapping region of two to four VPs that have unique N-terminal extensions. A survey of the three-dimensional (3D) data available for these viruses shows that they utilize structural commonalities, facilitated by disparate CP/VP amino acid sequences for the successful assembly of mature infectious virions.
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Hercog, Darko, Primož Bencak, Uroš Vincetič, and Tone Lerher. "Product Assembly Assistance System Based on Pick-To-Light and Computer Vision Technology." Sensors 22, no. 24 (December 13, 2022): 9769. http://dx.doi.org/10.3390/s22249769.
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Product assembly is often one of the last steps in the production process. Product assembly is often carried out by workers (assemblers) rather than robots, as it is generally challenging to adapt automation to any product. When assembling complex products, it can take a long time before the assembler masters all the steps and can assemble the product independently. Training time has no added value; therefore, it should be reduced as much as possible. This paper presents a custom-developed system that enables the guided assembly of complex and diverse products using modern technologies. The system is based on pick-to-light (PTL) modules, used primarily in logistics as an additional aid in the order picking process, and Computer Vision technology. The designed system includes a personal computer (PC), several custom-developed PTL modules and a USB camera. The PC with a touchscreen visualizes the assembly process and allows the assembler to interact with the system. The developed PC application guides the operator through the assembly process by showing all the necessary assembly steps and parts. Two-step verification is used to ensure that the correct part is picked out of the bin, first by checking that the correct pushbutton on the PTL module has been pressed and second by using a camera with a Computer Vision algorithm. The paper is supported by a use case demonstrating that the proposed system reduces the assembly time of the used product. The presented solution is scalable and flexible as it can be easily adapted to show the assembly steps of another product.
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Gregorio, C. C., and V. M. Fowler. "Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: tropomodulin requires tropomyosin for assembly." Journal of Cell Biology 129, no. 3 (May 1, 1995): 683–95. http://dx.doi.org/10.1083/jcb.129.3.683.
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Tropomodulin is a pointed end capping protein for tropomyosin-coated actin filaments that is hypothesized to play a role in regulating the precise lengths of striated muscle thin filaments (Fowler, V. M., M. A. Sussman, P. G. Miller, B. E. Flucher, and M. P. Daniels. 1993. J. Cell Biol. 120:411-420; Weber, A., C. C. Pennise, G. G. Babcock, and V. M. Fowler. 1994, J. Cell Biol. 127:1627-1635). To gain insight into the mechanisms of thin filament assembly and the role of tropomodulin therein, we have characterized the temporal appearance, biosynthesis and mechanisms of assembly of tropomodulin onto the pointed ends of thin filaments during the formation of striated myofibrils in primary embryonic chick cardiomyocyte cultures. Our results demonstrate that tropomodulin is not assembled coordinately with other thin filament proteins. Double immunofluorescence staining and ultrastructural immunolocalization demonstrate that tropomodulin is incorporated in its characteristic sarcomeric location at the pointed ends of the thin filaments after the thin filaments have become organized into periodic I bands. In fact, tropomodulin assembles later than all other well characterized myofibrillar proteins studied including: actin, tropomyosin, alpha-actinin, titin, myosin and C-protein. Nevertheless, at steady state, a significant proportion (approximately 39%) of tropomodulin is present in a soluble pool throughout myofibril assembly. Thus, the absence of tropomodulin in some striated myofibrils is not due to limiting quantities of the protein. In addition, kinetic data obtained from [35S]methionine pulse-chase experiments indicate that tropomodulin assembles more slowly into myofibrils than does tropomyosin. This observation, together with results obtained using a novel permeabilized cell model for thin filament assembly, indicate that tropomodulin assembly is dependent on the prior association of tropomyosin with actin filaments. We conclude that tropomodulin is a late marker for the assembly of striated myofibrils in cardiomyocytes; its assembly appears to be linked to their maturity. We propose that tropomodulin is involved in maintaining and stabilizing the final lengths of thin filaments after they are assembled.
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Chen, Jinrong, Shihao Zhang, Yuhan Wang, Ruwen Xie, Lishang Liu, and Yan Deng. "In Vivo Self-Assembly Based Cancer Therapy Strategy." Journal of Biomedical Nanotechnology 16, no. 7 (July 1, 2020): 997–1017. http://dx.doi.org/10.1166/jbn.2020.2962.
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Nanotechnology has been widely applied in tumor imaging, diagnostic and therapy. Beside the prefabricated nanomaterials, constructing nanostructures in living cells through self-assemble provides an alternative strategy to treat cancer. In vivo self-assembly renders the conversion of compatible small molecules into assembled nanostructures with toxicity, and is expected to outperform the prefabricated nanotechnologies as the small molecules diffuse faster than their assembly form. Attributed to the specific tumor environment such as low pH, high ROS, high enzyme expression and so on, in vivo self-assembly could differentiate cancer cells from normal ones with high selectivity. The in vivo self-assembly based caner therapy has made considerable progress in the last decade with confirmed advantages such as high capacity, minimal drug resistance, high accumulation, enhanced retention and so on. This review summarized the in vivo self-assembly of nanostructures induced by the stimuli like pH, ROS, enzyme, metal ion, localized concentration, biominerization and their utilization in cancer therapy.
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Rumlova-Klikova, Michaela, Eric Hunter, Milan V. Nermut, Iva Pichova, and Tomas Ruml. "Analysis of Mason-Pfizer Monkey Virus Gag Domains Required for Capsid Assembly in Bacteria: Role of the N-Terminal Proline Residue of CA in Directing Particle Shape." Journal of Virology 74, no. 18 (September 15, 2000): 8452–59. http://dx.doi.org/10.1128/jvi.74.18.8452-8459.2000.
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ABSTRACT Mason-Pfizer monkey virus (M-PMV) preassembles immature capsids in the cytoplasm prior to transporting them to the plasma membrane. Expression of the M-PMV Gag precursor in bacteria results in the assembly of capsids indistinguishable from those assembled in mammalian cells. We have used this system to investigate the structural requirements for the assembly of Gag precursors into procapsids. A series of C- and N-terminal deletion mutants progressively lacking each of the mature Gag domains (matrix protein [MA]-pp24/16-p12-capsid protein [CA]-nucleocapsid protein [NC]-p4) were constructed and expressed in bacteria. The results demonstrate that both the CA and the NC domains are necessary for the assembly of macromolecular arrays (sheets) but that amino acid residues at the N terminus of CA define the assembly of spherical capsids. The role of these N-terminal domains is not based on a specific amino acid sequence, since both MA-CA-NC and p12-CA-NC polyproteins efficiently assemble into capsids. Residues N terminal of CA appear to prevent a conformational change in which the N-terminal proline plays a key role, since the expression of a CA-NC protein lacking this proline results in the assembly of spherical capsids in place of the sheets assembled by the CA-NC protein.
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Goldberg, M., H. Jenkins, T. Allen, W. G. Whitfield, and C. J. Hutchison. "Xenopus lamin B3 has a direct role in the assembly of a replication competent nucleus: evidence from cell-free egg extracts." Journal of Cell Science 108, no. 11 (November 1, 1995): 3451–61. http://dx.doi.org/10.1242/jcs.108.11.3451.
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Xenopus egg extracts which assemble replication competent nuclei in vitro were depleted of lamin B3 using monoclonal antibody L6 5D5 linked to paramagnetic beads. After depletion, the extracts were still capable of assembling nuclei around demembranated sperm heads. Using field emission in lens scanning electron microscopy (FEISEM) we show that most nuclei assembled in lamin B3-depleted extracts have continuous nuclear envelopes and well formed nuclear pores. However, several consistent differences were observed. Most nuclei were small and only attained diameters which were half the size of controls. In a small number of nuclei, nuclear pore baskets, normally present on the inner aspect of the nuclear envelope, appeared on its outer surface. Finally, the assembly of nuclear pores was slower in lamin B3-depleted extracts, indicating a slower overall rate of nuclear envelope assembly. The results of FEISEM were confirmed using conventional TEM thin sections, where again the majority of nuclei assembled in lamin B3-depleted extracts had well formed double unit membranes containing a high density of nuclear pores. Since nuclear envelope assembly was mostly normal but slow in these nuclei, the lamin content of ‘depleted’ extracts was investigated. While lamin B3 was recovered efficiently from cytosolic and membrane fractions by our procedure, a second minor lamin isoform, which has characteristics similar to those of the somatic lamin B2, remained in the extract. Thus it is likely that this lamin is necessary for nuclear envelope assembly. However, while lamin B2 did not co-precipitate with lamin B3 during immunodepletion experiments, several protein species did specifically associate with lamin B3 on paramagnetic immunobeads. The major protein species associated with lamin B3 migrated with molecular masses of 102 kDa and 57 kDa, respectively, on one-dimensional polyacrylamide gels. On two-dimensional O'Farrell gels the mobility of the 102 kDa protein was identical to the mobility of a major nuclear matrix protein, indicating a specific association between lamin B3 and other nuclear matrix proteins. Nuclei assembled in lamin B3-depleted extracts did not assemble a lamina, judged by indirect immunofluorescence, and failed to initiate semi-conservative DNA replication. However, by reinoculating depleted extracts with purified lamin B3, nuclear lamina assembly and DNA replication could both be rescued. Thus it seems likely that the inability of lamin-depleted extracts to assemble a replication competent nucleus is a direct consequence of a failure to assemble a lamina.
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Chen, C. L. Philip, and C. A. Wichman. "A systematic approach for design and planning of mechanical assemblies." Artificial Intelligence for Engineering Design, Analysis and Manufacturing 7, no. 1 (February 1993): 19–36. http://dx.doi.org/10.1017/s0890060400000044.
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A system that integrates design and planning for mechanical assemblies is presented. The system integrates neural network computing that captures designer's design concept and rule-based system to generate a task-level assembly plan automatically. The design concept is expressed by a standard pattern format representing qualitative assembly information. A neural network model together with feature-based model translates the input pattern into a preliminary boundary representation (B-rep). Based on a refinement B-rep assembly representation, assembly plans are generated for practical use in a single-robot assembly workcell. A feasible assembly plan that minimizes tool changes and subassembly reorientations is generated from the system. A robust part collision detection algorithm to generate the precedence relationships among the assembly's components is included in the system. By contrast with many assembly planning systems that used a prolonged question-and-answering session or required knowledge beyond what is typically available in the design database, an automated assembly planning system presented here draws input relationships directly from the conceptual design and the geometry of the assembly. The system developed under this study extracts all reasoning information from the product model and permits the components to be assembled in a multitude of directions. Several experiments illustrate the effectiveness of the designed assembly planning system.
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Kolega, J., and D. L. Taylor. "Gradients in the concentration and assembly of myosin II in living fibroblasts during locomotion and fiber transport." Molecular Biology of the Cell 4, no. 8 (August 1993): 819–36. http://dx.doi.org/10.1091/mbc.4.8.819.
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Assembly and motor activity of myosin II affect shape, contractility, and locomotion of nonmuscle cells. We used fluorescent analogues and imaging techniques to elucidate the state of assembly and three-dimensional distribution of myosin II in living Swiss 3T3 fibroblasts. An analogue of myosin II that was covalently cross-linked in the 10S conformation and unable to assemble served as an indicator of the cytoplasmic volume accessible to 10S myosin II. Ratio-imaging of an analogue that can undergo 10S-->6S conversion versus the volume indicator revealed localized concentration of assembly-competent myosin II. In stationary serum-deprived cells and in cells locomoting at the edge of a wound, it was most concentrated in the peripheral cytoplasm, where fibers containing myosin II assemble, and least concentrated in the perinuclear cytoplasm, where they disassemble. Furthermore, fluorescence photobleaching recovery showed myosin II to be less mobile in the periphery than in perinuclear cytoplasm. These results indicate a gradient in the assembly of myosin II. Three-dimensional microscopy of living cells revealed that fibers containing myosin II were localized in the cortical cytoplasm, whereas myosin II was diffusely distributed in the deeper cytoplasm, suggesting that myosin II is assembled preferentially near the cell surface. Localized protein phosphorylation may play a role, because a kinase inhibitor, staurosporine, abolished the gradient of myosin II assembly.
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Campbell, Stephen, and Alan Rein. "In Vitro Assembly Properties of Human Immunodeficiency Virus Type 1 Gag Protein Lacking the p6 Domain." Journal of Virology 73, no. 3 (March 1, 1999): 2270–79. http://dx.doi.org/10.1128/jvi.73.3.2270-2279.1999.
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ABSTRACT Human immunodeficiency virus type 1 (HIV-1) normally assembles into particles of 100 to 120 nm in diameter by budding through the plasma membrane of the cell. The Gag polyprotein is the only viral protein that is required for the formation of these particles. We have used an in vitro assembly system to examine the assembly properties of purified, recombinant HIV-1 Gag protein and of Gag missing the C-terminal p6 domain (Gag Δp6). This system was used previously to show that the CA-NC fragment of HIV-1 Gag assembled into cylindrical particles. We now report that both HIV-1 Gag and Gag Δp6 assemble into small, 25- to 30-nm-diameter spherical particles in vitro. The multimerization of Gag Δp6 into units larger than dimers and the formation of spherical particles required nucleic acid. Removal of the nucleic acid with NaCl or nucleases resulted in the disruption of the multimerized complexes. We conclude from these results that (i) N-terminal extension of HIV-1 CA-NC to include the MA domain results in the formation of spherical, rather than cylindrical, particles; (ii) nucleic acid is required for the assembly and maintenance of HIV-1 Gag Δp6 virus-like particles in vitro and possibly in vivo; (iii) a wide variety of RNAs or even short DNA oligonucleotides will support assembly; (iv) protein-protein interactions within the particle must be relatively weak; and (v) recombinant HIV-1 Gag Δp6 and nucleic acid are not sufficient for the formation of normal-sized particles.
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Jiang, Dan Dan, Zhe Bo Zhou, Jian Xu, Liang Chen, and Ming Li. "Based on the Modeling and Simulation Analysis of the Spray Pump of Soildworks." Advanced Materials Research 989-994 (July 2014): 2745–48. http://dx.doi.org/10.4028/www.scientific.net/amr.989-994.2745.
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For the research of the mine large displacement spray pump in structure characteristics, each part of the spray pump should make use of Solidworks 3 d modeling, then assembled to be assembly at the same time. During the process of assemble, the assembly must be checked for interference. And simulate the spray pump motion, operation parameters are obtained according to the basic parameters and theoretical analysis. It’s of great significance to enhance the efficiency of the practical production in coal mine by bearing the main stress, testing and optimizing the performance of the crankshaft.
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Penny, Gervette M., and Susan K. Dutcher. "Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii." PLOS Genetics 20, no. 3 (March 18, 2024): e1011038. http://dx.doi.org/10.1371/journal.pgen.1011038.
Full textAbstract:
Motile cilia assembly utilizes over 800 structural and cytoplasmic proteins. Variants in approximately 58 genes cause primary ciliary dyskinesia (PCD) in humans, including the dynein arm (pre)assembly factor (DNAAF) gene DNAAF4. In humans, outer dynein arms (ODAs) and inner dynein arms (IDAs) fail to assemble motile cilia when DNAAF4 function is disrupted. In Chlamydomonas reinhardtii, a ciliated unicellular alga, the DNAAF4 ortholog is called PF23. The pf23-1 mutant assembles short cilia and lacks IDAs, but partially retains ODAs. The cilia of a new null allele (pf23-4) completely lack ODAs and IDAs and are even shorter than cilia from pf23-1. In addition, PF23 plays a role in the cytoplasmic modification of IC138, a protein of the two-headed IDA (I1/f). As most PCD variants in humans are recessive, we sought to test if heterozygosity at two genes affects ciliary function using a second-site non-complementation (SSNC) screening approach. We asked if phenotypes were observed in diploids with pairwise heterozygous combinations of 21 well-characterized ciliary mutant Chlamydomonas strains. Vegetative cultures of single and double heterozygous diploid cells did not show SSNC for motility phenotypes. When protein synthesis is inhibited, wild-type Chlamydomonas cells utilize the pool of cytoplasmic proteins to assemble half-length cilia. In this sensitized assay, 8 double heterozygous diploids with pf23 and other DNAAF mutations show SSNC; they assemble shorter cilia than wild-type. In contrast, double heterozygosity of the other 203 strains showed no effect on ciliary assembly. Immunoblots of diploids heterozygous for pf23 and wdr92 or oda8 show that PF23 is reduced by half in these strains, and that PF23 dosage affects phenotype severity. Reductions in PF23 and another DNAAF in diploids affect the ability to assemble ODAs and IDAs and impedes ciliary assembly. Thus, dosage of multiple DNAAFs is an important factor in cilia assembly and regeneration.
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Tellinghuisen, Timothy L., and Richard J. Kuhn. "Nucleic Acid-Dependent Cross-Linking of the Nucleocapsid Protein of Sindbis Virus." Journal of Virology 74, no. 9 (May 1, 2000): 4302–9. http://dx.doi.org/10.1128/jvi.74.9.4302-4309.2000.
Full textAbstract:
ABSTRACT The assembly of the alphavirus nucleocapsid core is a multistep event requiring the association of the nucleocapsid protein with nucleic acid and the subsequent oligomerization of capsid proteins into an assembled core particle. Although the mechanism of assembly has been investigated extensively both in vivo and in vitro, no intermediates in the core assembly pathway have been identified. Through the use of both truncated and mutant Sindbis virus nucleocapsid proteins and a variety of cross-linking reagents, a possible nucleic acid-protein assembly intermediate has been detected. The cross-linked species, a covalent dimer, has been detected only in the presence of nucleic acid and with capsid proteins capable of binding nucleic acid. Optimum nucleic acid-dependent cross-linking was seen at a protein-to-nucleic-acid ratio identical to that required for maximum binding of the capsid protein to nucleic acid. Identical results were observed when cross-linking in vitro assembled core particles of both Sindbis and Ross River viruses. Purified cross-linked dimers of truncated proteins and of mutant proteins that failed to assemble were found to incorporate into assembled core particles when present as minor components in assembly reactions, suggesting that the cross-linking traps an authentic intermediate in nucleocapsid core assembly. Endoproteinase Lys-C mapping of the position of the cross-link indicated that lysine 250 of one capsid protein was cross-linked to lysine 250 of an adjacent capsid protein. Examination of the position of the cross-link in relation to the existing model of the nucleocapsid core suggests that the cross-linked species is a cross-capsomere contact between a pentamer and hexamer at the quasi-threefold axis or is a cross-capsomere contact between hexamers at the threefold axis of the icosahedral core particle and suggests several possible assembly models involving a nucleic acid-bound dimer of capsid protein as an early step in the assembly pathway.
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Liu, Bo, and Yuh-Ru Julie Lee. "Spindle Assembly and Mitosis in Plants." Annual Review of Plant Biology 73, no. 1 (May 20, 2022): 227–54. http://dx.doi.org/10.1146/annurev-arplant-070721-084258.
Full textAbstract:
In contrast to well-studied fungal and animal cells, plant cells assemble bipolar spindles that exhibit a great deal of plasticity in the absence of structurally defined microtubule-organizing centers like the centrosome. While plants employ some evolutionarily conserved proteins to regulate spindle morphogenesis and remodeling, many essential spindle assembly factors found in vertebrates are either missing or not required for producing the plant bipolar microtubule array. Plants also produce proteins distantly related to their fungal and animal counterparts to regulate critical events such as the spindle assembly checkpoint. Plant spindle assembly initiates with microtubule nucleation on the nuclear envelope followed by bipolarization into the prophase spindle. After nuclear envelope breakdown, kinetochore fibers are assembled and unified into the spindle apparatus with convergent poles. Of note, compared to fungal and animal systems, relatively little is known about how plant cells remodel the spindle microtubule array during anaphase. Uncovering mitotic functions of novel proteins for spindle assembly in plants will illuminate both common and divergent mechanisms employed by different eukaryotic organisms to segregate genetic materials.
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Gor, Kavan, and Olivier Duss. "Emerging Quantitative Biochemical, Structural, and Biophysical Methods for Studying Ribosome and Protein–RNA Complex Assembly." Biomolecules 13, no. 5 (May 19, 2023): 866. http://dx.doi.org/10.3390/biom13050866.
Full textAbstract:
Ribosome assembly is one of the most fundamental processes of gene expression and has served as a playground for investigating the molecular mechanisms of how protein–RNA complexes (RNPs) assemble. A bacterial ribosome is composed of around 50 ribosomal proteins, several of which are co-transcriptionally assembled on a ~4500-nucleotide-long pre-rRNA transcript that is further processed and modified during transcription, the entire process taking around 2 min in vivo and being assisted by dozens of assembly factors. How this complex molecular process works so efficiently to produce an active ribosome has been investigated over decades, resulting in the development of a plethora of novel approaches that can also be used to study the assembly of other RNPs in prokaryotes and eukaryotes. Here, we review biochemical, structural, and biophysical methods that have been developed and integrated to provide a detailed and quantitative understanding of the complex and intricate molecular process of bacterial ribosome assembly. We also discuss emerging, cutting-edge approaches that could be used in the future to study how transcription, rRNA processing, cellular factors, and the native cellular environment shape ribosome assembly and RNP assembly at large.
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DeTomaso, A. W., G. Blanco, and R. W. Mercer. "The alpha and beta subunits of the Na,K-ATPase can assemble at the plasma membrane into functional enzyme." Journal of Cell Biology 127, no. 1 (October 1, 1994): 55–69. http://dx.doi.org/10.1083/jcb.127.1.55.
Full textAbstract:
Synthesis and assembly of most oligomeric plasma membrane proteins occurs in the ER. However, the role the ER plays in oligomerization is unknown. We have previously demonstrated that unassociated alpha and beta subunits of the Na,K-ATPase are targeted to the plasma membrane when individually expressed in baculovirus-infected Sf-9 cells. This unique property allows us to determine if assembly of these two polypeptides is restricted to the ER, or if it can also occur at the plasma membrane. To investigate the assembly of the Na,K-ATPase we have taken advantage of the ability of baculovirus-infected cells to fuse. Lowering the extracellular pH of the infected cells triggers an endogenously expressed viral protein to initiate plasma membrane fusion. When individual Sf-9 cells expressing either the Na,K-ATPase alpha or beta subunits are plated together and subjected to a mild acidic shock, they form large syncytia. In the newly continuous plasma membrane the separate alpha and beta polypeptides associate and assemble into functional Na,K-ATPase molecules. However, a hybrid ATPase molecule consisting of a Na,K-ATPase alpha subunit and a H,K-ATPase beta subunit, which efficiently assembles in the ER of coinfected cells, does not assemble at the plasma membrane of fused cells. When cells expressing the Na,K-ATPase alpha subunit are fused to cells coexpressing the Na,K-ATPase beta subunit and the H,K-ATPase beta subunit, the Na,K-ATPase alpha subunit selectively assembles with the Na,K-ATPase beta subunit. However, when cells are coinfected and expressing all three polypeptides, the Na,K-ATPase alpha subunit assembles with both beta subunits in the ER, in what appears to be a random fashion. These experiments demonstrate that assembly between some polypeptides is restricted to the ER, and suggests that the ability of the Na,K-ATPase alpha and beta subunits to leave the ER and assemble at the plasma membrane may represent a novel mechanism of regulation of activity.
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He, Xue-Yan, Yan-Jun Li, Chakrapani Kalyanaraman, Li-Li Qiu, Chen Chen, Qi Xiao, Wen-Xue Liu, et al. "GluA1 signal peptide determines the spatial assembly of heteromeric AMPA receptors." Proceedings of the National Academy of Sciences 113, no. 38 (September 6, 2016): E5645—E5654. http://dx.doi.org/10.1073/pnas.1524358113.
Full textAbstract:
AMPA-type glutamate receptors (AMPARs) mediate fast excitatory neurotransmission and predominantly assemble as heterotetramers in the brain. Recently, the crystal structures of homotetrameric GluA2 demonstrated that AMPARs are assembled with two pairs of conformationally distinct subunits, in a dimer of dimers formation. However, the structure of heteromeric AMPARs remains unclear. Guided by the GluA2 structure, we performed cysteine mutant cross-linking experiments in full-length GluA1/A2, aiming to draw the heteromeric AMPAR architecture. We found that the amino-terminal domains determine the first level of heterodimer formation. When the dimers further assemble into tetramers, GluA1 and GluA2 subunits have preferred positions, possessing a 1–2–1–2 spatial assembly. By swapping the critical sequences, we surprisingly found that the spatial assembly pattern is controlled by the excisable signal peptides. Replacements with an unrelated GluK2 signal peptide demonstrated that GluA1 signal peptide plays a critical role in determining the spatial priority. Our study thus uncovers the spatial assembly of an important type of glutamate receptors in the brain and reveals a novel function of signal peptides.
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Cheignon, Clémence, Fabrice Collin, Laurent Sabater, and Christelle Hureau. "Oxidative Damages on the Alzheimer’s Related-Aβ Peptide Alters Its Ability to Assemble." Antioxidants 12, no. 2 (February 13, 2023): 472. http://dx.doi.org/10.3390/antiox12020472.
Full textAbstract:
Oxidative stress that can lead to oxidation of the amyloid-β (Aβ) peptide is considered a key feature in Alzheimer’s disease (AD), influencing the ability of Aβ to assemble into β-sheet rich fibrils that are commonly found in senile plaques of AD patients. The present study aims at investigating the fallouts of Aβ oxidation on the assembly properties of the Aβ peptide. To accomplish this, we performed kinetics and analysis on an oxidized Aβ (oxAβ) peptide, resulting from the attack of reactive oxygen species (ROS) that are formed by the biologically relevant Cu/Aβ/dioxygen/ascorbate system. oxAβ was still able to assemble but displayed ill-defined and small oligomeric assemblies compared to the long and thick β-sheet rich fibrils from the non-oxidized counterpart. In addition, oxAβ does affect the assembly of the parent Aβ peptide. In a mixture of the two peptides, oxAβ has a mainly kinetic effect on the assembly of the Aβ peptide and was able to slow down the formation of Aβ fibril in a wide pH range [6.0–7.4]. However, oxAβ does not change the quantity and morphology of the Aβ fibrils formed to a significant extent. In the presence of copper or zinc di-cations, oxAβ assembled into weakly-structured aggregates rather than short, untangled Cu-Aβ fibrils and long untangled Zn-Aβ fibrils. The delaying effect of oxAβ on metal altered Aβ assembly was also observed. Hence, our results obtained here bring new insights regarding the tight interconnection between (i) ROS production leading to Aβ oxidation and (ii) Aβ assembly, in particular via the modulation of the Aβ assembly by oxAβ. It is the first time that co-assembly of oxAβ and Aβ under various environmental conditions (pH, metal ions …) are reported.