Letteratura scientifica selezionata sul tema "Protein Biology"
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Articoli di riviste sul tema "Protein Biology":
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Tesi sul tema "Protein Biology":
Robinson, Ross Alexander. "Structural biology of protein - protein interactions". Thesis, University of Oxford, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.504517.
Li, Wei. "Protein-protein interaction specificity of immunity proteins for DNase colicins". Thesis, University of East Anglia, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.302033.
Song, Hong Chang. "The role of protein structure and heat shock protein 70 molecules in the import of peroxisomal proteins /". Thesis, McGill University, 1997. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=20867.
Laos, Roberto, e Steven A. Benner. "Linking chemistry and biology: protein sequences". Revista de Química, 2016. http://repositorio.pucp.edu.pe/index/handle/123456789/99314.
In the last twenty years, the number of complete genomes that have been sequenced and deposited in data banks has grown dramatically. This abundance in sequence information has supported the creation of the discipline known as paleogenetics. In this article, without going into complex algorithms, we present some key concepts for understanding how proteins have evolved in time. We then illustrate how paleogenetic analysis can be used in biotechnology. These examples highlight the connection between chemistry and biology, two disciplines that twenty years ago seemed to be more different than what they seem to be today.
Strasser, Rona. "Protein-protein interactions of receptors LdPEX5 and LPEX7 with PTS1 and PTS2 cargo proteins, and with glycosomal docking protein LdPEX14 for protein import into «Leishmania donovani»". Thesis, McGill University, 2014. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=122960.
Le glycosome est une structure subcellulaire unique qui se trouve dans le parasite Leishmania donovani. Cette organelle compartimente la machinerie enzymatique requise pour de multiples voies métaboliques, y compris la glycolyse. Le bon ciblage des enzymes du glycosome est essentiel pour la viabilité du parasite. Les protéines ciblées pour le glycosome ont une séquence signal topogénique, un PTS1 C-terminale ou un PTS2 N-terminale, qui est reconnue par les récepteurs cytosoliques, le LdPEX5 ou le LPEX7, respectivement. Ces complexes de récepteurs chargés s'interagissent avec la protéine LdPEX14, située du côté cytosolique de la membrane glycosomale, un événement requis pour le transport des protéines à travers la membrane du glycosome. Cependant, la voie complète d'importation de protéines glycosomales n'a pas été totalement élucidée. Ce travail a été entrepris pour mieux comprendre ces interactions protéine-protéine.La fraction cytosolique des parasites L.donovani a été utilisée pour déterminer les interactions protéine-protéine des récepteurs LdPEX5 et LPEX7. La chromatographie d'exclusion de taille, la focalisation isoélectrique, et les interactions d'affinité proteine-proteine ont montré que, dans les cytosols, ces récepteurs forment des grands complexes hétérologues. Les glycosomes purifiés ont été utilisés pour évaluer l'effet des complexes récepteur sur la conformation du LdPEX14. Une protéolyse limitée a montré que l'interaction du LdPEX14 chargé avec les complexes récepteur l'à protèger de la digestion à la surface de la membrane. L'électrophorèse sur gel natif a montré que le LdPEX14 forme des grands complexes de ~ 800 kDa et que lorsqu'il est associé à des complexes récepteur, le poids moléculaire des complexes LdPEX14 passe à ~ 1200 kDa. Les extractions avec le carbonate alcalin a déterminé que le LdPEX14 seul s'agit comme une protéine périphérique; mais son chargement avec des complexes récepteur l'entrainer à s'agir comme une protéine membranaire intégrale. L'insertion de LdPEX14 dans la membrane du glycosome conduit à l'insertion du LdPEX5 et LPEX7 dans la membrane aussi. L'association des complexes récepteur à causer LdPEX14 à subir un changement de conformation causant l'insertion profonde dans la membrane et l'augmentation de la taille des complexes.La purification du récepteur LPEX7 recombinante été entravée par son association avec la protéine chaperonne bactérienne GroEL. Une technique de repliement a été développé pour purifier LPEX7 en évitant l'association de protéines bactériennes. Les techniques de Far Western et d'affinité protéine-protéine ont montré que ce LPEX7 replier est spécifiquement associé à des protéines PTS2, le co-récepteur LdPEX5, et le LdPEX14. La cartographie des domaines d'interaction de LPEX7 a montré que l'interaction LPEX7-PTS2 nécessit le LPEX7 entière, alors que les motifs d'interaction avec LdPEX5 et LdPEX14 étaient situés dans sa région N-terminale.Il y a des métabolites glycosomal qui ne sont pas importés par la voie de l'importation glycosomale, mais par des transporteurs membranaires du glycosome. L-arginine est un de ces métabolites, substrat de l'enzyme glycosomale PTS1 arginase. L-arginine est récupéré dans le milieu extracellulaire par son transporteur, LdAAP3. Un fractionnement subcellulaire a été utilisés pour séparer les membranes plasmiques des glycosomes, et LdAAP3 a été localisé sur les deux membranes. De plus, des promastigotes de L. donovani sont capable de detecter le niveau de L-arginine dans le millieu, ce qui provoque une régulation positive de l'expression de LdAAP3 à la fois dans la membrane plasmique et dans la membrane du glycosome. Ces études fournissent des preuves que des transporteurs de métabolites spécifique sont présent dans la membrane du glycosome.Ensemble, ces études contribuent à l'élucidation de la fonction glycosomale de Leishmania donovani, et une meilleure compréhension de certains mécanismes nécessaires pour l'importation glycosomale.
Le, Min. "Protein coimmobilization: Reactions of vicinal thiol groups of proteins /". The Ohio State University, 1997. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487946776021788.
Rassadi, Roozbeh. "The effect of stress on nuclear protein transport : classical nuclear protein transport versus the nuclear transport of heat shock proteins". Thesis, McGill University, 1999. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=33476.
Under normal conditions, Aequorea victoria green fluorescent protein (GFP), carrying a classical nuclear localization sequence (cNLS-GFP) is nuclear. However, cNLS-GFP equilibrates throughout the cell upon exposure to heat, ethanol, H2O2 or starvation. Redistribution of the small GTPase Gsp1p, a soluble nuclear transport factor, correlates with cNLS-GFP equilibration. This suggests that a collapse of the Gsp1p gradient underlies the inhibition of classical nuclear protein import. In contrast to cNLS-GFP, the cytoplasmic heat shock protein Ssa4p accumulates in nuclei when classical nuclear import is inhibited. The N-terminal 236 amino acid residues of Ssa4p are sufficient for nuclear localization of Ssa4p-GFP upon heat and ethanol stress. The nuclear localization of Ssa4p(1--236)-GFP requires components of Gsp1-GTPase system, but is independent of Srp1p, the cNLS receptor.
Ssa4p(16--642)-GFP accumulates in nuclei of starving cells, mediated by a hydrophobic stretch of amino acid residues in its N-terminal domain. This nuclear localization is reversible upon addition of fresh medium and its export is sensitive to oxidants and temperature-dependent.
Field, James Edward John. "Engineering protein cages with synthetic biology". Thesis, Imperial College London, 2014. http://hdl.handle.net/10044/1/45404.
Sonnen, Andreas Franz-Peter. "Structural biology of protein-membrane interactions and membrane protein function". Thesis, University of Oxford, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.514997.
Lite, Thúy-Lan Võ. "The genetic landscape of protein-protein interaction specificity". Thesis, Massachusetts Institute of Technology, 2020. https://hdl.handle.net/1721.1/129035.
Cataloged from student-submitted PDF of thesis.
Includes bibliographical references.
Protein-protein interaction specificity is often encoded at the primary sequence level, and by just a few interfacial residues. Collectively, these residues have both positive and negative roles, promoting a desired, cognate interaction and preventing non-cognate interactions, respectively. However, for most protein-protein interactions, the contributions of individual specificity residues are poorly understood and often obscured by robustness and degeneracy of protein interfaces. Using bacterial toxin-antitoxin systems as a model, we use a variant of deep mutational scanning to dissect the positive and negative contributions of antitoxin residues that dictate toxin specificity. By screening a combinatorially complete library of antitoxin variants, we uncover a distribution of fitness effects for individual interface mutations measured across hundreds of genetic backgrounds. We show that positive and negative contributions to specificity are neither inherently coupled nor mutually exclusive. Further, we argue that the wild-type antitoxin may be optimized for specificity, because mutations that further destabilize the non-cognate interaction also weaken the cognate interaction. No mutations strengthen the cognate interaction. By comparing crystal structures of paralogous complexes, we provide a structural rationale for all of these observations. Finally, we use a library approach to identify hundreds of novel systems that are insulated from their parental systems, and that carry only two mutations - a negative specificity element on the toxin, and one on the antitoxin. This result demonstrates that highly similar (and in this case, nearly identical) complexes can be insulated using compensatory mutations of individually large effect. Collectively, this work provides a generalizable approach to understanding the logic of molecular recognition.
by Thúy-Lan Võ Lite.
Ph. D.
Ph.D. Massachusetts Institute of Technology, Department of Biology
Libri sul tema "Protein Biology":
T, McManus Michael, Laing William A e Allan Andrew C, a cura di. Protein-protein interactions in plant biology. Sheffield: Sheffield Academic Press, 2002.
Colin, Kleanthous, a cura di. Protein-protein recognition. Oxford: Oxford University Press, 2000.
A, Rice Phoebe, e Correll Carl C, a cura di. Protein-nucleic acid interactions: Structural biology. Cambridge: RSC Pub., 2008.
Gabriel, Waksman, a cura di. Proteomics and protein-protein interactions: Biology, chemistry, bionformatics, and drug design. New York: Springer, 2005.
Arnold, Revzin, a cura di. The Biology of nonspecific DNA-protein interactions. Boca Raton, Fla: CRC Press, 1990.
Donev, Rossen. Advances in protein chemistry and structural biology. Amsterdam: Elsevier, 2011.
Anders, Liljas, a cura di. Textbook of structural biology. New Jersey: World Scientific, 2008.
1948-, Walker John M., a cura di. New protein techniques. Clifton, N.J: Humana Press, 1988.
Matthews, Jacqueline M. Protein dimerization and oligomerization in biology. New York: Springer Science+Business Media, 2012.
Tropp, Burton E. Molecular biology: Genes to proteins. 3a ed. Sudbury, MA: Jones and Bartlett, 2008.
Capitoli di libri sul tema "Protein Biology":
Fung, Jia Jun, Karla Blöcher-Juárez e Anton Khmelinskii. "High-Throughput Analysis of Protein Turnover with Tandem Fluorescent Protein Timers". In Methods in Molecular Biology, 85–100. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1732-8_6.
Keskin, Ozlem, Attila Gursoy e Ruth Nussinov. "Principles of Protein Recognition and Properties of Protein-protein Interfaces". In Computational Biology, 53–65. London: Springer London, 2008. http://dx.doi.org/10.1007/978-1-84800-125-1_3.
Teng, Quincy. "Protein Dynamics". In Structural Biology, 289–310. Boston, MA: Springer US, 2012. http://dx.doi.org/10.1007/978-1-4614-3964-6_8.
Kodama, Hiroki, e Yoichi Nakata. "Protein Structures". In Theoretical Biology, 161–75. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-7132-6_5.
Gamage, Nadisha, Harish Cheruvara, Peter J. Harrison, James Birch, Charlie J. Hitchman, Monika Olejnik, Raymond J. Owens e Andrew Quigley. "High-Throughput Production and Optimization of Membrane Proteins After Expression in Mammalian Cells". In Methods in Molecular Biology, 79–118. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3147-8_5.
Barth, Marie, e Carla Schmidt. "Quantitative Cross-Linking of Proteins and Protein". In Methods in Molecular Biology, 385–400. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1024-4_26.
Gonzalez, Orland. "Protein–Protein Interaction Databases". In Encyclopedia of Systems Biology, 1786–90. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_1046.
Lu, Long Jason, e Minlu Zhang. "Protein-Protein Interaction Networks". In Encyclopedia of Systems Biology, 1790. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_878.
Szklarczyk, Damian, e Lars Juhl Jensen. "Protein-Protein Interaction Databases". In Methods in Molecular Biology, 39–56. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2425-7_3.
Neyfakh, A. A., e M. Ya Timofeeva. "Protein". In Molecular biology of development, 170–278. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4899-5370-4_3.
Atti di convegni sul tema "Protein Biology":
MUIR, TOM W. "EXPLORING CHROMATIN BIOLOGY USING PROTEIN CHEMISTRY". In 23rd International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2014. http://dx.doi.org/10.1142/9789814603836_0005.
Dunbrack, Roland L., Keith Dunker e Adam Godzik. "PROTEIN STRUCTURE PREDICTION IN BIOLOGY AND MEDICINE". In Proceedings of the Pacific Symposium. WORLD SCIENTIFIC, 1999. http://dx.doi.org/10.1142/9789814447331_0009.
Shahbazi, Zahra, Horea T. Ilies¸ e Kazem Kazerounian. "Protein Molecules as Natural Nano Bio Devices: Mobility Analysis". In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13021.
Tretyakova, A. V., E. O. Gerasimova, P. A. Krylov e V. V. Novochadov. "Phylogenetic analysis of the lubricin protein and surfactant-associated proteins B and C". In Mathematical Biology and Bioinformatics. Pushchino: IMPB RAS - Branch of KIAM RAS, 2022. http://dx.doi.org/10.17537/icmbb22.18.
Pedrazzini, Emanuela. "Protein-specific induction of the unfolded protein response by two maize gamma-zeins". In ASPB PLANT BIOLOGY 2020. USA: ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1383050.
Luo, Fei, Ondrej Halgas, Pratish Gawand e Sagar Lahiri. "Animal-free protein production using precision fermentation". In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/ntka8679.
Shi, Lei, Young-Rae Cho e Aidong Zhang. "ANN Based Protein Function Prediction Using Integrated Protein-Protein Interaction Data". In 2009 International Joint Conference on Bioinformatics, Systems Biology and Intelligent Computing. IEEE, 2009. http://dx.doi.org/10.1109/ijcbs.2009.98.
Kaseniit, Kristjan E., Samuel D. Perli e Timothy K. Lu. "Designing extensible protein-DNA interactions for synthetic biology". In 2011 IEEE Biomedical Circuits and Systems Conference (BioCAS). IEEE, 2011. http://dx.doi.org/10.1109/biocas.2011.6107799.
Mohan, Amrita, Shripad V. Bhagwat, David M. Epstein, Mark Miglarese e Jonathan A. Pachter. "Abstract 58: Understanding target biology using protein interactomes". In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-58.
Yong-Cui Wang, Xian-Wen Ren, Chun-Hua Zhang, Nai-Yang Deng e Xiang-Sun Zhang. "Evaluating the denoising techniques in protein-protein interaction prediction". In 2011 IEEE International Conference on Systems Biology (ISB). IEEE, 2011. http://dx.doi.org/10.1109/isb.2011.6033124.
Rapporti di organizzazioni sul tema "Protein Biology":
Zhou, C., e A. Zemla. Computational biology for target discovery and characterization: a feasibility study in protein-protein interaction detection. Office of Scientific and Technical Information (OSTI), febbraio 2009. http://dx.doi.org/10.2172/948981.
Williams, Thomas. Cell Biology Boardgame: Cell Survival: Transport. University of Dundee, marzo 2023. http://dx.doi.org/10.20933/100001281.
Rao, Christopher. Final report: The Systems Biology of Protein Acetylation in Fuel-Producing Microorganisms. Office of Scientific and Technical Information (OSTI), novembre 2018. http://dx.doi.org/10.2172/1483353.
Ecker, Joseph Robert, Shelly Trigg, Renee Garza, Haili Song, Andrew MacWilliams, Joseph Nery, Joaquin Reina et al. Next Generation Protein Interactomes for Plant Systems Biology and Biomass Feedstock Research. Office of Scientific and Technical Information (OSTI), novembre 2016. http://dx.doi.org/10.2172/1333859.
Pratt, L. R., A. E. Garcia e G. Hummer. Computer simulation of protein solvation, hydrophobic mapping, and the oxygen effect in radiation biology. Office of Scientific and Technical Information (OSTI), agosto 1997. http://dx.doi.org/10.2172/524859.
Wang, X. F., e M. Schuldiner. Systems biology approaches to dissect virus-host interactions to develop crops with broad-spectrum virus resistance. Israel: United States-Israel Binational Agricultural Research and Development Fund, 2020. http://dx.doi.org/10.32747/2020.8134163.bard.
Sheinerman, Felix. Report on the research conducted under the funding of the Sloan foundation postdoctoral fellowship in Computational Molecular Biology [Systematic study of protein-protein complexes] Final report. Office of Scientific and Technical Information (OSTI), giugno 2001. http://dx.doi.org/10.2172/810580.
Gupta, G., S. V. Santhana Mariappan, X. Chen, P. Catasti, L. A. III Silks, R. K. Moyzis, E. M. Bradbury e A. E. Garcia. Structural biology of disease-associated repetitive DNA sequences and protein-DNA complexes involved in DNA damage and repair. Office of Scientific and Technical Information (OSTI), luglio 1997. http://dx.doi.org/10.2172/505319.
Evans, John Spencer. Material lessons of biology: structure function studies of protein sequences involved in inorganic composite material formation. Final Technical Report. Office of Scientific and Technical Information (OSTI), settembre 2019. http://dx.doi.org/10.2172/1560814.
Ohad, Nir, e Robert Fischer. Control of Fertilization-Independent Development by the FIE1 Gene. United States Department of Agriculture, agosto 2000. http://dx.doi.org/10.32747/2000.7575290.bard.