Статті в журналах з теми "Multi-protein assembly"
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Siggers, Trevor, and Raluca Gordân. "Protein–DNA binding: complexities and multi-protein codes." Nucleic Acids Research 42, no. 4 (November 16, 2013): 2099–111. http://dx.doi.org/10.1093/nar/gkt1112.
Повний текст джерелаLi, Mei, Erik Dujardin, and Stephen Mann. "Programmed assembly of multi-layered protein/nanoparticle-carbon nanotube conjugates." Chemical Communications, no. 39 (2005): 4952. http://dx.doi.org/10.1039/b509109h.
Повний текст джерелаTørresen, Ole K., Bastiaan Star, Pablo Mier, Miguel A. Andrade-Navarro, Alex Bateman, Patryk Jarnot, Aleksandra Gruca, et al. "Tandem repeats lead to sequence assembly errors and impose multi-level challenges for genome and protein databases." Nucleic Acids Research 47, no. 21 (October 4, 2019): 10994–1006. http://dx.doi.org/10.1093/nar/gkz841.
Повний текст джерелаFarrugia, Thomas, Adam W. Perriman, Kamendra P. Sharma, and Stephen Mann. "Multi-enzyme cascade reactions using protein–polymer surfactant self-standing films." Chemical Communications 53, no. 13 (2017): 2094–97. http://dx.doi.org/10.1039/c6cc09809f.
Повний текст джерелаVenkatraman, Vishwesh, and David W. Ritchie. "Predicting Multi-Component Protein Assemblies Using an Ant Colony Approach." International Journal of Swarm Intelligence Research 3, no. 3 (July 2012): 19–31. http://dx.doi.org/10.4018/jsir.2012070102.
Повний текст джерелаXian, Yuejiao, Chitra B. Karki, Sebastian Miki Silva, Lin Li, and Chuan Xiao. "The Roles of Electrostatic Interactions in Capsid Assembly Mechanisms of Giant Viruses." International Journal of Molecular Sciences 20, no. 8 (April 16, 2019): 1876. http://dx.doi.org/10.3390/ijms20081876.
Повний текст джерелаTerzo, Esteban A., Shawn M. Lyons, John S. Poulton, Brenda R. S. Temple, William F. Marzluff, and Robert J. Duronio. "Distinct self-interaction domains promote Multi Sex Combs accumulation in and formation of the Drosophila histone locus body." Molecular Biology of the Cell 26, no. 8 (April 15, 2015): 1559–74. http://dx.doi.org/10.1091/mbc.e14-10-1445.
Повний текст джерелаMozdy, A. D., J. M. McCaffery, and J. M. Shaw. "Dnm1p Gtpase-Mediated Mitochondrial Fission Is a Multi-Step Process Requiring the Novel Integral Membrane Component Fis1p." Journal of Cell Biology 151, no. 2 (October 16, 2000): 367–80. http://dx.doi.org/10.1083/jcb.151.2.367.
Повний текст джерелаGuo, Zhen, Zhiwei Shen, Yujiao Wang, Tingyuan Tan, and Yi Zhang. "Peptides Co-Assembling into Hydrangea-Like Microstructures." Journal of Nanoscience and Nanotechnology 20, no. 5 (May 1, 2020): 3239–45. http://dx.doi.org/10.1166/jnn.2020.17393.
Повний текст джерелаTang, Jiakun, Ye Liu, Dongmei Qi, Lan Yang, Hui Chen, Chenhui Wang, and Xuli Feng. "Nucleus‐Targeted Delivery of Multi‐Protein Self‐Assembly for Combined Anticancer Therapy." Small 17, no. 25 (May 24, 2021): 2101219. http://dx.doi.org/10.1002/smll.202101219.
Повний текст джерелаJayalath, Kumudie, Sean Frisbie, Minhchau To, and Sanjaya Abeysirigunawardena. "Pseudouridine Synthase RsuA Captures an Assembly Intermediate That Is Stabilized by Ribosomal Protein S17." Biomolecules 10, no. 6 (May 30, 2020): 841. http://dx.doi.org/10.3390/biom10060841.
Повний текст джерелаChi, Wei, Jinfang Ma, and Lixin Zhang. "Regulatory factors for the assembly of thylakoid membrane protein complexes." Philosophical Transactions of the Royal Society B: Biological Sciences 367, no. 1608 (December 19, 2012): 3420–29. http://dx.doi.org/10.1098/rstb.2012.0065.
Повний текст джерелаWhitley, Paul, and Ismael Mingarro. "Stitching proteins into membranes, not sew simple." Biological Chemistry 395, no. 12 (December 1, 2014): 1417–24. http://dx.doi.org/10.1515/hsz-2014-0205.
Повний текст джерелаHahn, Hyunggu, Sang Ho Park, Hyun-Jung Kim, Sunghoon Kim, and Byung Woo Han. "The DRS–AIMP2–EPRS subcomplex acts as a pivot in the multi-tRNA synthetase complex." IUCrJ 6, no. 5 (August 24, 2019): 958–67. http://dx.doi.org/10.1107/s2052252519010790.
Повний текст джерелаBolanos-Garcia, Victor M., Qian Wu, Takashi Ochi, Dimitri Y. Chirgadze, Bancinyane Lynn Sibanda, and Tom L. Blundell. "Spatial and temporal organization of multi-protein assemblies: achieving sensitive control in information-rich cell-regulatory systems." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 370, no. 1969 (June 28, 2012): 3023–39. http://dx.doi.org/10.1098/rsta.2011.0268.
Повний текст джерелаRibbe, Markus W., Kamil Górecki, Mario Grosch, Joseph B. Solomon, Robert Quechol, Yiling A. Liu, Chi Chung Lee, and Yilin Hu. "Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly." Molecules 27, no. 19 (October 10, 2022): 6743. http://dx.doi.org/10.3390/molecules27196743.
Повний текст джерелаVonshak, Ohad, Yiftach Divon, Stefanie Förste, David Garenne, Vincent Noireaux, Reinhard Lipowsky, Sophia Rudorf, Shirley S. Daube, and Roy H. Bar-Ziv. "Programming multi-protein assembly by gene-brush patterns and two-dimensional compartment geometry." Nature Nanotechnology 15, no. 9 (July 20, 2020): 783–91. http://dx.doi.org/10.1038/s41565-020-0720-7.
Повний текст джерелаvan den Akker, Emile, Timothy J. Satchwell, Geoff Daniels, and Ashley M. Toye. "Mapping the Assembly of Band 3 and Rhesus Multi-Protein Complexes During Erythropoiesis." Blood 116, no. 21 (November 19, 2010): 812. http://dx.doi.org/10.1182/blood.v116.21.812.812.
Повний текст джерелаBergfort, Alexandra, Tarek Hilal, Benno Kuropka, İbrahim Avşar Ilik, Gert Weber, Tuğçe Aktaş, Christian Freund, and Markus C. Wahl. "The intrinsically disordered TSSC4 protein acts as a helicase inhibitor, placeholder and multi-interaction coordinator during snRNP assembly and recycling." Nucleic Acids Research 50, no. 5 (February 21, 2022): 2938–58. http://dx.doi.org/10.1093/nar/gkac087.
Повний текст джерелаMaghool, Shadi, N. Dinesha G. Cooray, David A. Stroud, David Aragão, Michael T. Ryan, and Megan J. Maher. "Structural and functional characterization of the mitochondrial complex IV assembly factor Coa6." Life Science Alliance 2, no. 5 (September 12, 2019): e201900458. http://dx.doi.org/10.26508/lsa.201900458.
Повний текст джерелаGupta, Swati, Jyoti Chhibber-Goel, Manmohan Sharma, Suhel Parvez, Karl Harlos, Amit Sharma, and Manickam Yogavel. "Crystal structures of the two domains that constitute the Plasmodium vivax p43 protein." Acta Crystallographica Section D Structural Biology 76, no. 2 (January 30, 2020): 135–46. http://dx.doi.org/10.1107/s2059798319016413.
Повний текст джерелаOrtolan, Tatiana G., Prasad Tongaonkar, David Lambertson, Li Chen, Cherylene Schauber, and Kiran Madura. "The DNA repair protein Rad23 is a negative regulator of multi-ubiquitin chain assembly." Nature Cell Biology 2, no. 9 (August 17, 2000): 601–8. http://dx.doi.org/10.1038/35023547.
Повний текст джерелаUchida, Masaki, Ben LaFrance, Chris C. Broomell, Peter E. Prevelige, and Trevor Douglas. "Higher Order Assembly of Virus-like Particles (VLPs) Mediated by Multi-valent Protein Linkers." Small 11, no. 13 (January 12, 2015): 1562–70. http://dx.doi.org/10.1002/smll.201402067.
Повний текст джерелаBurkinshaw, Brianne J., Sergio A. Souza, and Natalie C. J. Strynadka. "Structural analysis of SepL, an enteropathogenicEscherichia colitype III secretion-system gatekeeper protein." Acta Crystallographica Section F Structural Biology Communications 71, no. 10 (September 23, 2015): 1300–1308. http://dx.doi.org/10.1107/s2053230x15016064.
Повний текст джерелаTieu, Quinton, and Jodi Nunnari. "Mdv1p Is a Wd Repeat Protein That Interacts with the Dynamin-Related Gtpase, Dnm1p, to Trigger Mitochondrial Division." Journal of Cell Biology 151, no. 2 (October 16, 2000): 353–66. http://dx.doi.org/10.1083/jcb.151.2.353.
Повний текст джерелаSokolik, Chana G., Nasrin Qassem, and Jordan H. Chill. "The Disordered Cellular Multi-Tasker WIP and Its Protein–Protein Interactions: A Structural View." Biomolecules 10, no. 7 (July 21, 2020): 1084. http://dx.doi.org/10.3390/biom10071084.
Повний текст джерелаLecomte, F. J. L., N. Ismail, and S. High. "Making membrane proteins at the mammalian endoplasmic reticulum." Biochemical Society Transactions 31, no. 6 (December 1, 2003): 1248–52. http://dx.doi.org/10.1042/bst0311248.
Повний текст джерелаCherak, Stephana J., and Raymond J. Turner. "Assembly pathway of a bacterial complex iron sulfur molybdoenzyme." Biomolecular Concepts 8, no. 3-4 (September 26, 2017): 155–67. http://dx.doi.org/10.1515/bmc-2017-0011.
Повний текст джерелаSwapna, Lakshmipuram Seshadri, Nambudiry Rekha, and Narayanaswamy Srinivasan. "Accommodation of profound sequence differences at the interfaces of eubacterial RNA polymerase multi-protein assembly." Bioinformation 8, no. 1 (January 6, 2012): 6–12. http://dx.doi.org/10.6026/97320630008006.
Повний текст джерелаMaeda, Yoshiaki, and Hiroshi Matsui. "Genetically engineered protein nanowires: unique features in site-specific functionalization and multi-dimensional self-assembly." Soft Matter 8, no. 29 (2012): 7533. http://dx.doi.org/10.1039/c2sm25352f.
Повний текст джерелаMoshkanbaryans, Lia, Ling-Shan Chan, Kasper Engholm-Keller, Jesse Ray Wark, Phillip James Robinson, and Mark Evan Graham. "The interaction of assembly protein AP180 and clathrin is inhibited by multi-site phospho-mimetics." Neurochemistry International 129 (October 2019): 104474. http://dx.doi.org/10.1016/j.neuint.2019.104474.
Повний текст джерелаSrour, Batoul, Sylvain Gervason, Beata Monfort, and Benoit D’Autréaux. "Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter." Inorganics 8, no. 10 (October 3, 2020): 55. http://dx.doi.org/10.3390/inorganics8100055.
Повний текст джерелаKim, Hye-Youn, and Suntaek Hong. "Multi-Faceted Roles of DNAJB Protein in Cancer Metastasis and Clinical Implications." International Journal of Molecular Sciences 23, no. 23 (November 29, 2022): 14970. http://dx.doi.org/10.3390/ijms232314970.
Повний текст джерелаZechner, Ellen L., Silvia Lang, and Joel F. Schildbach. "Assembly and mechanisms of bacterial type IV secretion machines." Philosophical Transactions of the Royal Society B: Biological Sciences 367, no. 1592 (April 19, 2012): 1073–87. http://dx.doi.org/10.1098/rstb.2011.0207.
Повний текст джерелаSpalinger, Marianne R., Marlene Schwarzfischer, and Michael Scharl. "The Role of Protein Tyrosine Phosphatases in Inflammasome Activation." International Journal of Molecular Sciences 21, no. 15 (July 31, 2020): 5481. http://dx.doi.org/10.3390/ijms21155481.
Повний текст джерелаGROEMPING, Yvonne, and Katrin RITTINGER. "Activation and assembly of the NADPH oxidase: a structural perspective." Biochemical Journal 386, no. 3 (March 8, 2005): 401–16. http://dx.doi.org/10.1042/bj20041835.
Повний текст джерелаZhao, Ting, Liying Guan, Xuehua Ma, Baohui Chen, Mei Ding, and Wei Zou. "The cell cortex-localized protein CHDP-1 is required for dendritic development and transport in C. elegans neurons." PLOS Genetics 18, no. 9 (September 20, 2022): e1010381. http://dx.doi.org/10.1371/journal.pgen.1010381.
Повний текст джерелаGORDON, Donna M., Jing WANG, Boominathan AMUTHA, and Debkumar PAIN. "Self-association and precursor protein binding of Saccharomyces cerevisiae Tom40p, the core component of the protein translocation channel of the mitochondrial outer membrane." Biochemical Journal 356, no. 1 (May 8, 2001): 207–15. http://dx.doi.org/10.1042/bj3560207.
Повний текст джерелаHenderson, Richard, and Samar Hasnain. "`Cryo-EM': electron cryomicroscopy, cryo electron microscopy or something else?" IUCrJ 10, no. 5 (September 1, 2023): 519–20. http://dx.doi.org/10.1107/s2052252523006759.
Повний текст джерелаLarsson, Daniel S. D., Sandesh Kanchugal Kanchugal P, and Maria Selmer. "Structural Consequences of Deproteinating the 50S Ribosome." Biomolecules 12, no. 11 (October 31, 2022): 1605. http://dx.doi.org/10.3390/biom12111605.
Повний текст джерелаBergdahl, Roland, Christin Grundström, Patrik Storm, Wolfgang Schröder, and Uwe Sauer. "Photosystem II assembly factor HCF136 from A. thaliana at 1.67 Å resolution." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1170. http://dx.doi.org/10.1107/s2053273314088299.
Повний текст джерелаGuarneri, Flavia, Matteo Tonni, Giuseppe Sarli, Maria Beatrice Boniotti, Davide Lelli, Ilaria Barbieri, Giulia D'Annunzio, Giovanni Loris Alborali, Barbara Bacci, and Massimo Amadori. "Non-Assembled ORF2 Capsid Protein of Porcine Circovirus 2b Does Not Confer Protective Immunity." Pathogens 10, no. 9 (September 9, 2021): 1161. http://dx.doi.org/10.3390/pathogens10091161.
Повний текст джерелаLe, Sarah N., Christopher R. Brown, Stacy Harvey, Hinrich Boeger, Hans Elmlund, and Dominika Elmlund. "The TAFs of TFIID Bind and Rearrange the Topology of the TATA-Less RPS5 Promoter." International Journal of Molecular Sciences 20, no. 13 (July 4, 2019): 3290. http://dx.doi.org/10.3390/ijms20133290.
Повний текст джерелаConnelly, Rhykka Leanne, Kenneth Gasser, and Daniel Traber. "O07. CCK and NO coordinate the assembly of a multi-protein complex leading to Erk activation." Nitric Oxide 14, no. 4 (June 2006): 2–3. http://dx.doi.org/10.1016/j.niox.2006.04.011.
Повний текст джерелаHeyd, Jochen, and Stefan Birmanns. "Solving Complex Puzzles: Automated Protein Complex Assembly From Cryo-Electron Microscopy Data Via Multi-Resolution Modeling." Biophysical Journal 96, no. 3 (February 2009): 412a. http://dx.doi.org/10.1016/j.bpj.2008.12.2101.
Повний текст джерелаBrodehl, Andreas, Stephanie Holler, Jan Gummert, and Hendrik Milting. "The N-Terminal Part of the 1A Domain of Desmin Is a Hot Spot Region for Putative Pathogenic DES Mutations Affecting Filament Assembly." Cells 11, no. 23 (December 2, 2022): 3906. http://dx.doi.org/10.3390/cells11233906.
Повний текст джерелаPazour, Gregory J., Bethany L. Dickert, Yvonne Vucica, E. Scott Seeley, Joel L. Rosenbaum, George B. Witman, and Douglas G. Cole. "Chlamydomonas IFT88 and Its Mouse Homologue, Polycystic Kidney Disease Gene Tg737, Are Required for Assembly of Cilia and Flagella." Journal of Cell Biology 151, no. 3 (October 30, 2000): 709–18. http://dx.doi.org/10.1083/jcb.151.3.709.
Повний текст джерелаBryan, Nicole B., Andrea Dorfleutner, Yon Rojanasakul, and Christian Stehlik. "Pathogen-induced activation of inflammasomes requires intracellular redistribution of the apoptosis associated speck-like protein containing a caspase recruitment domain (ASC) (135.70)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 135.70. http://dx.doi.org/10.4049/jimmunol.182.supp.135.70.
Повний текст джерелаZhang, Shiyong, Jia Li, Qin Qin, Wei Liu, Chao Bian, Yunhai Yi, Minghua Wang, et al. "Whole-Genome Sequencing of Chinese Yellow Catfish Provides a Valuable Genetic Resource for High-Throughput Identification of Toxin Genes." Toxins 10, no. 12 (November 23, 2018): 488. http://dx.doi.org/10.3390/toxins10120488.
Повний текст джерелаLone, Moien, Qulsum Akhter, Mithilesh Kumar, Umar Maqbool, Mahaiwon Shadang, Shyam S. Chauhan, and Riyaz A. Mir. "ROLE OF R2TP COMPLEX IN LYMPHOMA AND ITS THERAPEUTIC POTENTIAL." International Journal of Advanced Research 8, no. 11 (November 30, 2020): 300–303. http://dx.doi.org/10.21474/ijar01/12010.
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