Auswahl der wissenschaftlichen Literatur zum Thema „Protein Biology“
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Zeitschriftenartikel zum Thema "Protein Biology"
Prusiner, Stanley B., Michael R. Scott, Stephen J. DeArmond und Fred E. Cohen. „Prion Protein Biology“. Cell 93, Nr. 3 (Mai 1998): 337–48. http://dx.doi.org/10.1016/s0092-8674(00)81163-0.
Der volle Inhalt der QuelleRoy, Kasturi, und Ethan P. Marin. „Lipid Modifications in Cilia Biology“. Journal of Clinical Medicine 8, Nr. 7 (27.06.2019): 921. http://dx.doi.org/10.3390/jcm8070921.
Der volle Inhalt der QuelleHong. „“Cell-Free Synthetic Biology”: Synthetic Biology Meets Cell-Free Protein Synthesis“. Methods and Protocols 2, Nr. 4 (08.10.2019): 80. http://dx.doi.org/10.3390/mps2040080.
Der volle Inhalt der QuelleBirch, James, Harish Cheruvara, Nadisha Gamage, Peter J. Harrison, Ryan Lithgo und Andrew Quigley. „Changes in Membrane Protein Structural Biology“. Biology 9, Nr. 11 (16.11.2020): 401. http://dx.doi.org/10.3390/biology9110401.
Der volle Inhalt der QuelleAllen, James P. „Recent innovations in membrane-protein structural biology“. F1000Research 8 (22.02.2019): 211. http://dx.doi.org/10.12688/f1000research.16234.1.
Der volle Inhalt der QuelleFoster, Andrew W., Tessa R. Young, Peter T. Chivers und Nigel J. Robinson. „Protein metalation in biology“. Current Opinion in Chemical Biology 66 (Februar 2022): 102095. http://dx.doi.org/10.1016/j.cbpa.2021.102095.
Der volle Inhalt der QuelleLevy, Ezra, und Nikolai Slavov. „Single cell protein analysis for systems biology“. Essays in Biochemistry 62, Nr. 4 (02.08.2018): 595–605. http://dx.doi.org/10.1042/ebc20180014.
Der volle Inhalt der QuelleHolmes, Kenneth C. „Structural biology“. Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 354, Nr. 1392 (29.12.1999): 1977–84. http://dx.doi.org/10.1098/rstb.1999.0537.
Der volle Inhalt der QuelleNehme, Zeina, Natascha Roehlen, Punita Dhawan und Thomas F. Baumert. „Tight Junction Protein Signaling and Cancer Biology“. Cells 12, Nr. 2 (06.01.2023): 243. http://dx.doi.org/10.3390/cells12020243.
Der volle Inhalt der QuellePandey, Aditya, Kyungsoo Shin, Robin E. Patterson, Xiang-Qin Liu und Jan K. Rainey. „Current strategies for protein production and purification enabling membrane protein structural biology“. Biochemistry and Cell Biology 94, Nr. 6 (Dezember 2016): 507–27. http://dx.doi.org/10.1139/bcb-2015-0143.
Der volle Inhalt der QuelleDissertationen zum Thema "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.
Der volle Inhalt der QuelleLi, 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.
Der volle Inhalt der QuelleSong, 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.
Der volle Inhalt der QuelleLaos, Roberto, und Steven A. Benner. „Linking chemistry and biology: protein sequences“. Revista de Química, 2016. http://repositorio.pucp.edu.pe/index/handle/123456789/99314.
Der volle Inhalt der QuelleIn 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.
Der volle Inhalt der QuelleLe 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.
Der volle Inhalt der QuelleRassadi, 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.
Der volle Inhalt der QuelleUnder 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.
Der volle Inhalt der QuelleSonnen, 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.
Der volle Inhalt der QuelleLite, Thúy-Lan Võ. „The genetic landscape of protein-protein interaction specificity“. Thesis, Massachusetts Institute of Technology, 2020. https://hdl.handle.net/1721.1/129035.
Der volle Inhalt der QuelleCataloged 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
Bücher zum Thema "Protein Biology"
T, McManus Michael, Laing William A und Allan Andrew C, Hrsg. Protein-protein interactions in plant biology. Sheffield: Sheffield Academic Press, 2002.
Den vollen Inhalt der Quelle findenColin, Kleanthous, Hrsg. Protein-protein recognition. Oxford: Oxford University Press, 2000.
Den vollen Inhalt der Quelle findenA, Rice Phoebe, und Correll Carl C, Hrsg. Protein-nucleic acid interactions: Structural biology. Cambridge: RSC Pub., 2008.
Den vollen Inhalt der Quelle findenGabriel, Waksman, Hrsg. Proteomics and protein-protein interactions: Biology, chemistry, bionformatics, and drug design. New York: Springer, 2005.
Den vollen Inhalt der Quelle findenArnold, Revzin, Hrsg. The Biology of nonspecific DNA-protein interactions. Boca Raton, Fla: CRC Press, 1990.
Den vollen Inhalt der Quelle findenDonev, Rossen. Advances in protein chemistry and structural biology. Amsterdam: Elsevier, 2011.
Den vollen Inhalt der Quelle findenAnders, Liljas, Hrsg. Textbook of structural biology. New Jersey: World Scientific, 2008.
Den vollen Inhalt der Quelle finden1948-, Walker John M., Hrsg. New protein techniques. Clifton, N.J: Humana Press, 1988.
Den vollen Inhalt der Quelle findenMatthews, Jacqueline M. Protein dimerization and oligomerization in biology. New York: Springer Science+Business Media, 2012.
Den vollen Inhalt der Quelle findenTropp, Burton E. Molecular biology: Genes to proteins. 3. Aufl. Sudbury, MA: Jones and Bartlett, 2008.
Den vollen Inhalt der Quelle findenBuchteile zum Thema "Protein Biology"
Fung, Jia Jun, Karla Blöcher-Juárez und 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.
Der volle Inhalt der QuelleKeskin, Ozlem, Attila Gursoy und 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.
Der volle Inhalt der QuelleTeng, 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.
Der volle Inhalt der QuelleKodama, Hiroki, und 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.
Der volle Inhalt der QuelleGamage, Nadisha, Harish Cheruvara, Peter J. Harrison, James Birch, Charlie J. Hitchman, Monika Olejnik, Raymond J. Owens und 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.
Der volle Inhalt der QuelleBarth, Marie, und 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.
Der volle Inhalt der QuelleGonzalez, 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.
Der volle Inhalt der QuelleLu, Long Jason, und 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.
Der volle Inhalt der QuelleSzklarczyk, Damian, und 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.
Der volle Inhalt der QuelleNeyfakh, A. A., und 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.
Der volle Inhalt der QuelleKonferenzberichte zum Thema "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.
Der volle Inhalt der QuelleDunbrack, Roland L., Keith Dunker und 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.
Der volle Inhalt der QuelleShahbazi, Zahra, Horea T. Ilies¸ und 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.
Der volle Inhalt der QuelleTretyakova, A. V., E. O. Gerasimova, P. A. Krylov und 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.
Der volle Inhalt der QuellePedrazzini, 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.
Der volle Inhalt der QuelleLuo, Fei, Ondrej Halgas, Pratish Gawand und 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.
Der volle Inhalt der QuelleShi, Lei, Young-Rae Cho und 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.
Der volle Inhalt der QuelleKaseniit, Kristjan E., Samuel D. Perli und 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.
Der volle Inhalt der QuelleMohan, Amrita, Shripad V. Bhagwat, David M. Epstein, Mark Miglarese und 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.
Der volle Inhalt der QuelleYong-Cui Wang, Xian-Wen Ren, Chun-Hua Zhang, Nai-Yang Deng und 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.
Der volle Inhalt der QuelleBerichte der Organisationen zum Thema "Protein Biology"
Zhou, C., und A. Zemla. Computational biology for target discovery and characterization: a feasibility study in protein-protein interaction detection. Office of Scientific and Technical Information (OSTI), Februar 2009. http://dx.doi.org/10.2172/948981.
Der volle Inhalt der QuelleWilliams, Thomas. Cell Biology Boardgame: Cell Survival: Transport. University of Dundee, März 2023. http://dx.doi.org/10.20933/100001281.
Der volle Inhalt der QuelleRao, Christopher. Final report: The Systems Biology of Protein Acetylation in Fuel-Producing Microorganisms. Office of Scientific and Technical Information (OSTI), November 2018. http://dx.doi.org/10.2172/1483353.
Der volle Inhalt der QuelleEcker, 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), November 2016. http://dx.doi.org/10.2172/1333859.
Der volle Inhalt der QuellePratt, L. R., A. E. Garcia und G. Hummer. Computer simulation of protein solvation, hydrophobic mapping, and the oxygen effect in radiation biology. Office of Scientific and Technical Information (OSTI), August 1997. http://dx.doi.org/10.2172/524859.
Der volle Inhalt der QuelleWang, X. F., und 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.
Der volle Inhalt der QuelleSheinerman, 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), Juni 2001. http://dx.doi.org/10.2172/810580.
Der volle Inhalt der QuelleGupta, G., S. V. Santhana Mariappan, X. Chen, P. Catasti, L. A. III Silks, R. K. Moyzis, E. M. Bradbury und 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), Juli 1997. http://dx.doi.org/10.2172/505319.
Der volle Inhalt der QuelleEvans, 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), September 2019. http://dx.doi.org/10.2172/1560814.
Der volle Inhalt der QuelleOhad, Nir, und Robert Fischer. Control of Fertilization-Independent Development by the FIE1 Gene. United States Department of Agriculture, August 2000. http://dx.doi.org/10.32747/2000.7575290.bard.
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