Articoli di riviste: "Protein Biology"

1

Prusiner, Stanley B., Michael R. Scott, Stephen J. DeArmond e Fred E. Cohen. "Prion Protein Biology". Cell 93, n. 3 (maggio 1998): 337–48. http://dx.doi.org/10.1016/s0092-8674(00)81163-0.

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Roy, Kasturi, e Ethan P. Marin. "Lipid Modifications in Cilia Biology". Journal of Clinical Medicine 8, n. 7 (27 giugno 2019): 921. http://dx.doi.org/10.3390/jcm8070921.

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Abstract (sommario):

Cilia are specialized cellular structures with distinctive roles in various signaling cascades. Ciliary proteins need to be trafficked to the cilium to function properly; however, it is not completely understood how these proteins are delivered to their final localization. In this review, we will focus on how different lipid modifications are important in ciliary protein trafficking and, consequently, regulation of signaling pathways. Lipid modifications can play a variety of roles, including tethering proteins to the membrane, aiding trafficking through facilitating interactions with transporter proteins, and regulating protein stability and abundance. Future studies focusing on the role of lipid modifications of ciliary proteins will help our understanding of how cilia maintain specific protein pools strictly connected to their functions.

3

Hong. "“Cell-Free Synthetic Biology”: Synthetic Biology Meets Cell-Free Protein Synthesis". Methods and Protocols 2, n. 4 (8 ottobre 2019): 80. http://dx.doi.org/10.3390/mps2040080.

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Since Nirenberg and Matthaei used cell-free protein synthesis (CFPS) to elucidate the genetic code in the early 1960s [1], the technology has been developed over the course of decades and applied to studying both fundamental and applied biology [2]. Cell-free synthetic biology integrating CFPS with synthetic biology has received attention as a powerful and rapid approach to characterize and engineer natural biological systems. The open nature of cell-free (or in vitro) biological platforms compared to in vivo systems brings an unprecedented level of control and freedom in design [3]. This versatile engineering toolkit has been used for debugging biological networks, constructing artificial cells, screening protein libraries, prototyping genetic circuits, developing biosensors, producing metabolites, and synthesizing complex proteins including antibodies, toxic proteins, membrane proteins, and novel proteins containing nonstandard (unnatural) amino acids. The Methods and Protocols “Cell-Free Synthetic Biology” Special Issue consists of a series of reviews, protocols, benchmarks, and research articles describing the current development and applications of cell-free synthetic biology in diverse areas. [...]

4

Birch, James, Harish Cheruvara, Nadisha Gamage, Peter J. Harrison, Ryan Lithgo e Andrew Quigley. "Changes in Membrane Protein Structural Biology". Biology 9, n. 11 (16 novembre 2020): 401. http://dx.doi.org/10.3390/biology9110401.

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Membrane proteins are essential components of many biochemical processes and are important pharmaceutical targets. Membrane protein structural biology provides the molecular rationale for these biochemical process as well as being a highly useful tool for drug discovery. Unfortunately, membrane protein structural biology is a difficult area of study due to low protein yields and high levels of instability especially when membrane proteins are removed from their native environments. Despite this instability, membrane protein structural biology has made great leaps over the last fifteen years. Today, the landscape is almost unrecognisable. The numbers of available atomic resolution structures have increased 10-fold though advances in crystallography and more recently by cryo-electron microscopy. These advances in structural biology were achieved through the efforts of many researchers around the world as well as initiatives such as the Membrane Protein Laboratory (MPL) at Diamond Light Source. The MPL has helped, provided access to and contributed to advances in protein production, sample preparation and data collection. Together, these advances have enabled higher resolution structures, from less material, at a greater rate, from a more diverse range of membrane protein targets. Despite this success, significant challenges remain. Here, we review the progress made and highlight current and future challenges that will be overcome.

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Allen, James P. "Recent innovations in membrane-protein structural biology". F1000Research 8 (22 febbraio 2019): 211. http://dx.doi.org/10.12688/f1000research.16234.1.

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Innovations are expanding the capabilities of experimental investigations of the structural properties of membrane proteins. Traditionally, three-dimensional structures have been determined by measuring x-ray diffraction using protein crystals with a size of least 100 μm. For membrane proteins, achieving crystals suitable for these measurements has been a significant challenge. The availabilities of micro-focus x-ray beams and the new instrumentation of x-ray free-electron lasers have opened up the possibility of using submicrometer-sized crystals. In addition, advances in cryo-electron microscopy have expanded the use of this technique for studies of protein crystals as well as studies of individual proteins as single particles. Together, these approaches provide unprecedented opportunities for the exploration of structural properties of membrane proteins, including dynamical changes during protein function.

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Foster, Andrew W., Tessa R. Young, Peter T. Chivers e Nigel J. Robinson. "Protein metalation in biology". Current Opinion in Chemical Biology 66 (febbraio 2022): 102095. http://dx.doi.org/10.1016/j.cbpa.2021.102095.

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Levy, Ezra, e Nikolai Slavov. "Single cell protein analysis for systems biology". Essays in Biochemistry 62, n. 4 (2 agosto 2018): 595–605. http://dx.doi.org/10.1042/ebc20180014.

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Abstract (sommario):

The cellular abundance of proteins can vary even between isogenic single cells. This variability between single-cell protein levels can have regulatory roles, such as controlling cell fate during apoptosis induction or the proliferation/quiescence decision. Here, we review examples connecting protein levels and their dynamics in single cells to cellular functions. Such findings were made possible by the introduction of antibodies, and subsequently fluorescent proteins, for tracking protein levels in single cells. However, in heterogeneous cell populations, such as tumors or differentiating stem cells, cellular decisions are controlled by hundreds, even thousands of proteins acting in concert. Characterizing such complex systems demands measurements of thousands of proteins across thousands of single cells. This demand has inspired the development of new methods for single-cell protein analysis, and we discuss their trade-offs, with an emphasis on their specificity and coverage. We finish by highlighting the potential of emerging mass-spec methods to enable systems-level measurement of single-cell proteomes with unprecedented coverage and specificity. Combining such methods with methods for quantitating the transcriptomes and metabolomes of single cells will provide essential data for advancing quantitative systems biology.

8

Holmes, Kenneth C. "Structural biology". Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 354, n. 1392 (29 dicembre 1999): 1977–84. http://dx.doi.org/10.1098/rstb.1999.0537.

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Protein crystallography has become a major technique for understanding cellular processes. This has come about through great advances in the technology of data collection and interpretation, particularly the use of synchrotron radiation. The ability to express eukaryotic genes in Escherichia coli is also important. Analysis of known structures shows that all proteins are built from about 1000 primeval folds. The collection of all primeval folds provides a basis for predicting structure from sequence. At present about 450 are known. Of the presently sequenced genomes only a fraction can be related to known proteins on the basis of sequence alone. Attempts are being made to determine all (or as many as possible) of the structures from some bacterial genomes in the expectation that structure will point to function more reliably than does sequence. Membrane proteins present a special problem. The next 20 years may see the experimental determination of another 40 000 protein structures. This will make considerable demands on synchrotron sources and will require many more biochemists than are currently available. The availability of massive structure databases will alter the way biochemistry is done.

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Nehme, Zeina, Natascha Roehlen, Punita Dhawan e Thomas F. Baumert. "Tight Junction Protein Signaling and Cancer Biology". Cells 12, n. 2 (6 gennaio 2023): 243. http://dx.doi.org/10.3390/cells12020243.

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Tight junctions (TJs) are intercellular protein complexes that preserve tissue homeostasis and integrity through the control of paracellular permeability and cell polarity. Recent findings have revealed the functional role of TJ proteins outside TJs and beyond their classical cellular functions as selective gatekeepers. This is illustrated by the dysregulation in TJ protein expression levels in response to external and intracellular stimuli, notably during tumorigenesis. A large body of knowledge has uncovered the well-established functional role of TJ proteins in cancer pathogenesis. Mechanistically, TJ proteins act as bidirectional signaling hubs that connect the extracellular compartment to the intracellular compartment. By modulating key signaling pathways, TJ proteins are crucial players in the regulation of cell proliferation, migration, and differentiation, all of which being essential cancer hallmarks crucial for tumor growth and metastasis. TJ proteins also promote the acquisition of stem cell phenotypes in cancer cells. These findings highlight their contribution to carcinogenesis and therapeutic resistance. Moreover, recent preclinical and clinical studies have used TJ proteins as therapeutic targets or prognostic markers. This review summarizes the functional role of TJ proteins in cancer biology and their impact for novel strategies to prevent and treat cancer.

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Pandey, Aditya, Kyungsoo Shin, Robin E. Patterson, Xiang-Qin Liu e Jan K. Rainey. "Current strategies for protein production and purification enabling membrane protein structural biology". Biochemistry and Cell Biology 94, n. 6 (dicembre 2016): 507–27. http://dx.doi.org/10.1139/bcb-2015-0143.

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Abstract (sommario):

Membrane proteins are still heavily under-represented in the protein data bank (PDB), owing to multiple bottlenecks. The typical low abundance of membrane proteins in their natural hosts makes it necessary to overexpress these proteins either in heterologous systems or through in vitro translation/cell-free expression. Heterologous expression of proteins, in turn, leads to multiple obstacles, owing to the unpredictability of compatibility of the target protein for expression in a given host. The highly hydrophobic and (or) amphipathic nature of membrane proteins also leads to challenges in producing a homogeneous, stable, and pure sample for structural studies. Circumventing these hurdles has become possible through the introduction of novel protein production protocols; efficient protein isolation and sample preparation methods; and, improvement in hardware and software for structural characterization. Combined, these advances have made the past 10–15 years very exciting and eventful for the field of membrane protein structural biology, with an exponential growth in the number of solved membrane protein structures. In this review, we focus on both the advances and diversity of protein production and purification methods that have allowed this growth in structural knowledge of membrane proteins through X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cryo-electron microscopy (cryo-EM).

11

Lee, Bong-Jin. "S2c2-1 Structure and Protein-Protein Interaction of Helicobacter Pylori Proteins(S2-c2: "Structural biology reveals macromolecular interaction",Symposia,Abstract,Meeting Program of EABS & BSJ 2006)". Seibutsu Butsuri 46, supplement2 (2006): S127. http://dx.doi.org/10.2142/biophys.46.s127_4.

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12

Downing, A. Kristina. "Introduction to Protein Architecture: the structural biology of proteins". Journal of Cell Science 114, n. 12 (15 giugno 2001): 2210. http://dx.doi.org/10.1242/jcs.114.12.2210.

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13

Stollar, Elliott J., e David P. Smith. "Uncovering protein structure". Essays in Biochemistry 64, n. 4 (25 settembre 2020): 649–80. http://dx.doi.org/10.1042/ebc20190042.

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Abstract (sommario):

Abstract Structural biology is the study of the molecular arrangement and dynamics of biological macromolecules, particularly proteins. The resulting structures are then used to help explain how proteins function. This article gives the reader an insight into protein structure and the underlying chemistry and physics that is used to uncover protein structure. We start with the chemistry of amino acids and how they interact within, and between proteins, we also explore the four levels of protein structure and how proteins fold into discrete domains. We consider the thermodynamics of protein folding and why proteins misfold. We look at protein dynamics and how proteins can take on a range of conformations and states. In the second part of this review, we describe the variety of methods biochemists use to uncover the structure and properties of proteins that were described in the first part. Protein structural biology is a relatively new and exciting field that promises to provide atomic-level detail to more and more of the molecules that are fundamental to life processes.

14

Henderson, Brian, e Andrew C. R. Martin. "Protein moonlighting: a new factor in biology and medicine". Biochemical Society Transactions 42, n. 6 (17 novembre 2014): 1671–78. http://dx.doi.org/10.1042/bst20140273.

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Abstract (sommario):

The phenomenon of protein moonlighting was discovered in the 1980s and 1990s, and the current definition of what constitutes a moonlighting protein was provided at the end of the 1990s. Since this time, several hundred moonlighting proteins have been identified in all three domains of life, and the rate of discovery is accelerating as the importance of protein moonlighting in biology and medicine becomes apparent. The recent re-evaluation of the number of protein-coding genes in the human genome (approximately 19000) is one reason for believing that protein moonlighting may be a more general phenomenon than the current number of moonlighting proteins would suggest, and preliminary studies of the proportion of proteins that moonlight would concur with this hypothesis. Protein moonlighting could be one way of explaining the seemingly small number of proteins that are encoded in the human genome. It is emerging that moonlighting proteins can exhibit novel biological functions, thus extending the range of the human functional proteome. The several hundred moonlighting proteins so far discovered play important roles in many aspects of biology. For example, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), heat-shock protein 60 (Hsp60) and tRNA synthetases play a wide range of biological roles in eukaryotic cells, and a growing number of eukaryotic moonlighting proteins are recognized to play important roles in physiological processes such as sperm capacitation, implantation, immune regulation in pregnancy, blood coagulation, vascular regeneration and control of inflammation. The dark side of protein moonlighting finds a range of moonlighting proteins playing roles in various human diseases including cancer, cardiovascular disease, HIV and cystic fibrosis. However, some moonlighting proteins are being tested for their therapeutic potential, including immunoglobulin heavy-chain-binding protein (BiP), for rheumatoid arthritis, and Hsp90 for wound healing. In addition, it has emerged over the last 20 years that a large number of bacterial moonlighting proteins play important roles in bacteria–host interactions as virulence factors and are therefore potential therapeutic targets in bacterial infections. So as we progress in the 21st Century, it is likely that moonlighting proteins will be seen to play an increasingly important role in biology and medicine. It is hoped that some of the major unanswered questions, such as the mechanism of evolution of protein moonlighting, the structural biology of moonlighting proteins and their role in the systems biology of cellular systems can be addressed during this period.

15

Scholtens, Denise, e Robert Gentleman. "Making Sense of High-Throughput Protein-Protein Interaction Data". Statistical Applications in Genetics and Molecular Biology 3, n. 1 (3 gennaio 2005): 1–31. http://dx.doi.org/10.2202/1544-6115.1107.

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Abstract (sommario):

Accurate systems biology modeling requires a complete catalog of protein complexes and their constituent proteins. We discuss a graph-theoretic/statistical algorithm for local dynamic modeling of protein complexes using data from affinity purification-mass spectrometry experiments. The algorithm readily accommodates multicomplex membership by individual proteins and dynamic complex composition, two biological realities not accounted for in existing topological descriptions of the overall protein network. A likelihood-based objective function guides the protein complex modeling algorithm. With an accurate complex membership catalog in place, systems biology can proceed with greater precision.

16

Chénieux, Jean-Claude. "Analyse d'ouvrage: Protein-Protein Interactions in Plant Biology". Acta Botanica Gallica 150, n. 1 (marzo 2003): 117. http://dx.doi.org/10.1080/12538078.2003.10515991.

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Pelletier, Joelle, e Sachdev Sidhu. "Mapping protein–protein interactions with combinatorial biology methods". Current Opinion in Biotechnology 12, n. 4 (agosto 2001): 340–47. http://dx.doi.org/10.1016/s0958-1669(00)00225-1.

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Murphy, Robert F., e Michael V. Boland. "Pattern Analysis Meets Cell Biology". Microscopy and Microanalysis 5, S2 (agosto 1999): 510–11. http://dx.doi.org/10.1017/s1431927600015877.

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Abstract (sommario):

The widespread availability of automated fluorescence microscope systems has led to an explosion in the acquisition of digital images by biologists. This has created a need for computer applications that automate the analysis of these images and an opportunity to develop new approaches to classical problems. An example is the determination of the subcellular location of a protein from immunofluorescence images (or, more recently, images of GFP fluorescence). Current practice is to compare such images to mental images that a cell biologist has developed over time, and to reach a tentative conclusion about the structure (i.e., organelle) that a protein is found in. Since this determination is subjective, it often must be followed up by double labeling with a marker protein from the suspected structure.As an initial exploration of the feasibility of automating the determination of subcellular location, we developed a system that is able to classify the localization patterns characteristic of five cellular molecules (proteins and DNA) in Chinese Hamster Ovary (CHO) cells. Images were acquired on an epifluorescence microscope after the cells had been fixed, permeabilized, and labeled with appropriate fluorescent reagents (usually antibodies conjugated to fluorescent dyes). The labels used were directed against a Golgi protein, a lysosomal protein, a nuclear protein, a cytoskeletal protein, and DNA.

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Clemens, Stephan. "The cell biology of zinc". Journal of Experimental Botany 73, n. 6 (2 novembre 2021): 1688–98. http://dx.doi.org/10.1093/jxb/erab481.

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Abstract Nearly 10% of all plant proteins belong to the zinc (Zn) proteome. They require Zn either for catalysis or as a structural element. Most of the protein-bound Zn in eukaryotic cells is found in the cytosol. The fundamental differences between transition metal cations in the stability of their complexes with organic ligands, as described by the Irving–Williams series, necessitate buffering of cytosolic Zn (the ‘free Zn’ pool) in the picomolar range (i.e. ~6 orders of magnitude lower than the total cellular concentration). Various metabolites and peptides, including nicotianamine, glutathione, and phytochelatins, serve as Zn buffers. They are hypothesized to supply Zn to enzymes, transporters, or the recently identified sensor proteins. Zn2+ acquisition is mediated by ZRT/IRT-like proteins. Metal tolerance proteins transport Zn2+ into vacuoles and the endoplasmic reticulum, the major Zn storage sites. Heavy metal ATPase-dependent efflux of Zn2+ is another mechanism to control cytosolic Zn. Spatially controlled Zn2+ influx or release from intracellular stores would result in dynamic modulation of cellular Zn pools, which may directly influence protein–protein interactions or the activities of enzymes involved in signaling cascades. Possible regulatory roles of such changes, as recently elucidated in mammalian cells, are discussed.

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Davies, Peter L., Choy L. Hew e Garth L. Fletcher. "Fish antifreeze proteins: physiology and evolutionary biology". Canadian Journal of Zoology 66, n. 12 (1 dicembre 1988): 2611–17. http://dx.doi.org/10.1139/z88-385.

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Abstract (sommario):

Many marine teleosts have adapted to ice-laden seawater by evolving antifreeze proteins and glycoproteins. These proteins are synthesized in the liver for export to the blood where they circulate at levels of up to 20 mg/mL. There are at least four distinct antifreeze protein classes differing in carbohydrate content, amino acid composition, protein sequence, and secondary structure. In addition to antifreeze structural diversity, fish species differ considerably with respect to mechanisms controlling seasonal regulation of plasma antifreeze concentrations. Some species synthesize antifreeze proteins immediately before the onset of freezing conditions, some synthesize them in response to such conditions, whereas others possess high concentrations all year. Endogenous rhythms, water temperature, photoperiod, and pituitary hormones have all been implicated as regulators of plasma antifreeze protein levels. The structural diversity of antifreeze proteins and their occurrence in a wide range of fish species suggest that they evolved separately and recently during Cenozoic glaciation. Invariably, the genes coding for these antifreeze proteins are amplified, sometimes as long tandem arrays, suggesting intense selective pressure to produce large amounts of protein. The distribution of antifreeze gene types among fish species suggests that they could serve as important tools for studying phylogenetic relationships.

21

Cao, Yi, Teri Yoo, Shulin Zhuang e Hongbin Li. "Protein–Protein Interaction Regulates Proteins’ Mechanical Stability". Journal of Molecular Biology 378, n. 5 (maggio 2008): 1132–41. http://dx.doi.org/10.1016/j.jmb.2008.03.046.

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Sarmiento, Corina, e Julio A. Camarero. "Biotechnological Applications of Protein Splicing". Current Protein & Peptide Science 20, n. 5 (27 marzo 2019): 408–24. http://dx.doi.org/10.2174/1389203720666190208110416.

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Abstract (sommario):

Protein splicing domains, also called inteins, have become a powerful biotechnological tool for applications involving molecular biology and protein engineering. Early applications of inteins focused on self-cleaving affinity tags, generation of recombinant polypeptide α-thioesters for the production of semisynthetic proteins and backbone cyclized polypeptides. The discovery of naturallyoccurring split-inteins has allowed the development of novel approaches for the selective modification of proteins both in vitro and in vivo. This review gives a general introduction to protein splicing with a focus on their role in expanding the applications of intein-based technologies in protein engineering and chemical biology.

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WAKATSUKI, Soichi. "Structural Biology of Protein Transport." Nihon Kessho Gakkaishi 45, n. 1 (2003): 26–31. http://dx.doi.org/10.5940/jcrsj.45.26.

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Pieta Perez, Vinícius, e Adriana Simon Coitinho. "Implications of Prion Protein Biology". Current Neurovascular Research 3, n. 3 (1 agosto 2006): 215–23. http://dx.doi.org/10.2174/156720206778018785.

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Chin, G. J. "STRUCTURAL BIOLOGY: Proton/Protein Transport". Science 293, n. 5527 (6 luglio 2001): 17b—17. http://dx.doi.org/10.1126/science.293.5527.17b.

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Go, Nobuhiro. "Physics and Biology of Protein". Progress of Theoretical Physics Supplement 170 (2007): 198–213. http://dx.doi.org/10.1143/ptps.170.198.

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Sifers, R. N. "CELL BIOLOGY: Protein Degradation Unlocked". Science 299, n. 5611 (28 febbraio 2003): 1330–31. http://dx.doi.org/10.1126/science.1082718.

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Grünberg, Raik, e Luis Serrano. "Strategies for protein synthetic biology". Nucleic Acids Research 38, n. 8 (10 aprile 2010): 2663–75. http://dx.doi.org/10.1093/nar/gkq139.

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Yang, L., S. Guo, Y. Li, S. Zhou e S. Tao. "Protein microarrays for systems biology". Acta Biochimica et Biophysica Sinica 43, n. 3 (21 gennaio 2011): 161–71. http://dx.doi.org/10.1093/abbs/gmq127.

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Plant, Nick. "Molecular biology II: protein function". Surgery (Oxford) 27, n. 4 (aprile 2009): 150–52. http://dx.doi.org/10.1016/j.mpsur.2009.02.012.

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Plant, Nick. "Molecular biology II: protein function". Surgery (Oxford) 30, n. 4 (aprile 2012): 169–73. http://dx.doi.org/10.1016/j.mpsur.2012.01.011.

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Plant, Nick. "Molecular biology II: protein function". Surgery (Oxford) 33, n. 3 (marzo 2015): 99–103. http://dx.doi.org/10.1016/j.mpsur.2015.01.002.

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Marín, Mónica, Tamara Fernández-Calero e Ricardo Ehrlich. "Protein folding and tRNA biology". Biophysical Reviews 9, n. 5 (24 settembre 2017): 573–88. http://dx.doi.org/10.1007/s12551-017-0322-2.

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Hurtley, S. M. "CELL BIOLOGY: Ancient Protein Sorting". Science 299, n. 5610 (21 febbraio 2003): 1153c—1153. http://dx.doi.org/10.1126/science.299.5610.1153c.

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Moroder, Luis, e Nediljko Budisa. "Synthetic Biology of Protein Folding". ChemPhysChem 11, n. 6 (21 aprile 2010): 1181–87. http://dx.doi.org/10.1002/cphc.201000035.

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Gomathy, Dr CK, Mr D. Surya Manohar e Vasavi Rajesh. "PROTEIN DATABASE IN COMPUTATIONAL BIOLOGY". INTERANTIONAL JOURNAL OF SCIENTIFIC RESEARCH IN ENGINEERING AND MANAGEMENT 07, n. 11 (1 novembre 2023): 1–11. http://dx.doi.org/10.55041/ijsrem26770.

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Abstract (sommario):

Protein data sets have turns into a Critical piece of computational science. Colossal measure of information for protein structure capability and especially arrangement are being created. Looking through information base is an initial step of study to track down new protein. We present the rudiments of protein underlying bioinformatics. Protein performs most fundamental natural and compound capability in a cell. They additionally assume significant part in primary, enzymatic, transport and administrative capabilities. not entirely settled by their design. This survey covers some fundamental of protein structure and related data sets and it is further developed subject of protein underlying bioinformatics. This work gives to investigate the capability of protein information bases on web. Keywords: Protein database, bioinformatics, protein structure, protein sequences

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Orr, Harry T. "Cell biology of spinocerebellar ataxia". Journal of Cell Biology 197, n. 2 (16 aprile 2012): 167–77. http://dx.doi.org/10.1083/jcb.201105092.

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Abstract (sommario):

Ataxia is a neurological disorder characterized by loss of control of body movements. Spinocerebellar ataxia (SCA), previously known as autosomal dominant cerebellar ataxia, is a biologically robust group of close to 30 progressive neurodegenerative diseases. Six SCAs, including the more prevalent SCA1, SCA2, SCA3, and SCA6 along with SCA7 and SCA17 are caused by expansion of a CAG repeat that encodes a polyglutamine tract in the affected protein. How the mutated proteins in these polyglutamine SCAs cause disease is highly debated. Recent work suggests that the mutated protein contributes to pathogenesis within the context of its “normal” cellular function. Thus, understanding the cellular function of these proteins could aid in the development of therapeutics.

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Hardy, David, Roslyn M. Bill, Anass Jawhari e Alice J. Rothnie. "Overcoming bottlenecks in the membrane protein structural biology pipeline". Biochemical Society Transactions 44, n. 3 (9 giugno 2016): 838–44. http://dx.doi.org/10.1042/bst20160049.

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Abstract (sommario):

Membrane proteins account for a third of the eukaryotic proteome, but are greatly under-represented in the Protein Data Bank. Unfortunately, recent technological advances in X-ray crystallography and EM cannot account for the poor solubility and stability of membrane protein samples. A limitation of conventional detergent-based methods is that detergent molecules destabilize membrane proteins, leading to their aggregation. The use of orthologues, mutants and fusion tags has helped improve protein stability, but at the expense of not working with the sequence of interest. Novel detergents such as glucose neopentyl glycol (GNG), maltose neopentyl glycol (MNG) and calixarene-based detergents can improve protein stability without compromising their solubilizing properties. Styrene maleic acid lipid particles (SMALPs) focus on retaining the native lipid bilayer of a membrane protein during purification and biophysical analysis. Overcoming bottlenecks in the membrane protein structural biology pipeline, primarily by maintaining protein stability, will facilitate the elucidation of many more membrane protein structures in the near future.

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Facchiano, A., e A. Marabotti. "Analysis of galactosemia-linked mutations of GALT enzyme using a computational biology approach". Protein Engineering, Design and Selection 23, n. 2 (11 dicembre 2009): 103–13. http://dx.doi.org/10.1093/protein/gzp076.

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Hurst, Jillian H., e Shelley B. Hooks. "Regulator of G-protein signaling (RGS) proteins in cancer biology". Biochemical Pharmacology 78, n. 10 (novembre 2009): 1289–97. http://dx.doi.org/10.1016/j.bcp.2009.06.028.

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Lin, Ya-Ling, Chia-Yi Chen, Ching-Ping Cheng e Long-Sen Chang. "Protein–protein interactions of KChIP proteins and Kv4.2". Biochemical and Biophysical Research Communications 321, n. 3 (agosto 2004): 606–10. http://dx.doi.org/10.1016/j.bbrc.2004.07.006.

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Qiu, Jiajun, Michael Bernhofer, Michael Heinzinger, Sofie Kemper, Tomas Norambuena, Francisco Melo e Burkhard Rost. "ProNA2020 predicts protein–DNA, protein–RNA, and protein–protein binding proteins and residues from sequence". Journal of Molecular Biology 432, n. 7 (marzo 2020): 2428–43. http://dx.doi.org/10.1016/j.jmb.2020.02.026.

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Hakes, Luke, John W. Pinney, David L. Robertson e Simon C. Lovell. "Protein-protein interaction networks and biology—what's the connection?" Nature Biotechnology 26, n. 1 (gennaio 2008): 69–72. http://dx.doi.org/10.1038/nbt0108-69.

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44

Jubb, Harry, Alicia P. Higueruelo, Anja Winter e Tom L. Blundell. "Structural biology and drug discovery for protein–protein interactions". Trends in Pharmacological Sciences 33, n. 5 (maggio 2012): 241–48. http://dx.doi.org/10.1016/j.tips.2012.03.006.

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Wales, Richard. "Optimizing Protein Expression: Producing Pure Protein for Structural Biology". BioProcessing Journal 3, n. 6 (30 dicembre 2004): 55–58. http://dx.doi.org/10.12665/j36.wales.

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46

Reddy Chichili, Vishnu Priyanka, Veerendra Kumar e J. Sivaraman. "Linkers in the structural biology of protein-protein interactions". Protein Science 22, n. 2 (8 gennaio 2013): 153–67. http://dx.doi.org/10.1002/pro.2206.

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Linsenmeier, Miriam, Andreas Küffner, Lenka Faltova, Maria Hondele, Karsten Weis e Paolo Arosio. "Protein Phase Transition: From Biology Towards New Protein Materials". Biophysical Journal 116, n. 3 (febbraio 2019): 465a—466a. http://dx.doi.org/10.1016/j.bpj.2018.11.2514.

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48

E, Beeram. "Mini review on Protein – Protein and DNA/RNA – protein interactions in biology". Asploro Journal of Biomedical and Clinical Case Reports 2, n. 2 (29 ottobre 2019): 82–83. http://dx.doi.org/10.36502/2019/asjbccr.6165.

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Abstract (sommario):

RNase H1 generally processes the RNA- DNA hybrids through non specific interaction between HBD and the ds RNA/DNA hybrid. There are no direct protein- protein interactions between the hybrid and HBD of RNase H1. The DNA binding region is highly conserved compared to RNA binding region and the Kd for RNA/DNA hybrid is less compared to ds RNA than to that of ds DNA [1]. HBD increases the processivity of RNase H1 and mutations in RNA binding region is tolerated compared to DBR. The RNA interacts between ɑ2 and β3 region with in the loop and with the protein in shallower minor groove.

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Martin, Andrew C. R. "Structural biology of moonlighting: lessons from antibodies". Biochemical Society Transactions 42, n. 6 (17 novembre 2014): 1704–8. http://dx.doi.org/10.1042/bst20140211.

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Abstract (sommario):

Protein moonlighting is the property of a number of proteins to have more than one function. However, the definition of moonlighting is somewhat imprecise with different interpretations of the phenomenon. True moonlighting occurs when an individual evolutionary protein domain has one well-accepted role and a secondary unrelated function. The ‘function’ of a protein domain can be defined at different levels. For example, although the function of an antibody variable fragment (Fv) could be described as ‘binding’, a more detailed definition would also specify the molecule to which the Fv region binds. Using this detailed definition, antibodies as a family are consummate moonlighters. However, individual antibodies do not moonlight; the multiple functions they exhibit (first binding a molecule and second triggering the immune response) are encoded in different domains and, in any case, are related in the sense that they are a part of what an antibody needs to do. Nonetheless, antibodies provide interesting lessons on the ability of proteins to evolve binding functions. Remarkably similar antibody sequences can bind completely different antigens, suggesting that evolving the ability to bind a protein can result from very subtle sequence changes.

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Sear, Richard P. "Specific protein–protein binding in many-component mixtures of proteins". Physical Biology 1, n. 2 (29 aprile 2004): 53–60. http://dx.doi.org/10.1088/1478-3967/1/2/001.

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