Статті в журналах з теми "Protein association"
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Grueninger, D., N. Treiber, M. O. P. Ziegler, J. W. A. Koetter, M. S. Schulze, and G. E. Schulz. "Designed Protein-Protein Association." Science 319, no. 5860 (January 11, 2008): 206–9. http://dx.doi.org/10.1126/science.1150421.
Повний текст джерелаCamacho, Carlos J., and Sandor Vajda. "Protein–protein association kinetics and protein docking." Current Opinion in Structural Biology 12, no. 1 (February 2002): 36–40. http://dx.doi.org/10.1016/s0959-440x(02)00286-5.
Повний текст джерелаPan, Albert C., Daniel Jacobson, Konstantin Yatsenko, Duluxan Sritharan, Thomas M. Weinreich, and David E. Shaw. "Atomic-level characterization of protein–protein association." Proceedings of the National Academy of Sciences 116, no. 10 (February 13, 2019): 4244–49. http://dx.doi.org/10.1073/pnas.1815431116.
Повний текст джерелаGiles, K. "Interactions underlying subunit association in cholinesterases." Protein Engineering Design and Selection 10, no. 6 (June 1, 1997): 677–85. http://dx.doi.org/10.1093/protein/10.6.677.
Повний текст джерелаErickson, Harold P. "Co-operativity in protein-protein association." Journal of Molecular Biology 206, no. 3 (April 1989): 465–74. http://dx.doi.org/10.1016/0022-2836(89)90494-4.
Повний текст джерелаLumry, R., and R. B. Gregory. "Dynamical factors in protein-protein association." Journal of Molecular Liquids 42 (October 1989): 113–44. http://dx.doi.org/10.1016/0167-7322(89)80029-7.
Повний текст джерелаKarplus, M., and J. Janin. "Comment on: `The entropy cost of protein association'." Protein Engineering, Design and Selection 12, no. 3 (March 1999): 185–86. http://dx.doi.org/10.1093/protein/12.3.185.
Повний текст джерелаBrandsdal, B. O., and A. O. Smalås. "Evaluation of protein–protein association energies by free energy perturbation calculations." Protein Engineering, Design and Selection 13, no. 4 (April 2000): 239–45. http://dx.doi.org/10.1093/protein/13.4.239.
Повний текст джерелаSuratanee, Apichat, and Kitiporn Plaimas. "Heterogeneous Network Model to Identify Potential Associations Between Plasmodium vivax and Human Proteins." International Journal of Molecular Sciences 21, no. 4 (February 15, 2020): 1310. http://dx.doi.org/10.3390/ijms21041310.
Повний текст джерелаZheng, W., N. P. Schafer, A. Davtyan, G. A. Papoian, and P. G. Wolynes. "Predictive energy landscapes for protein-protein association." Proceedings of the National Academy of Sciences 109, no. 47 (November 5, 2012): 19244–49. http://dx.doi.org/10.1073/pnas.1216215109.
Повний текст джерелаSchreiber, G., G. Haran, and H. X. Zhou. "Fundamental Aspects of Protein−Protein Association Kinetics." Chemical Reviews 109, no. 3 (March 11, 2009): 839–60. http://dx.doi.org/10.1021/cr800373w.
Повний текст джерелаHelms, Volkhard, Mazen Ahmad, Alexander Spaar, and Wei Gu. "Computer Simulation of Protein-Protein Association Processes." Biophysical Journal 96, no. 3 (February 2009): 75a. http://dx.doi.org/10.1016/j.bpj.2008.12.288.
Повний текст джерелаPan, Albert C., Daniel Jacobson, Konstantin Borisov, Duluxan Sritharan, Thomas M. Weinreich, and David E. Shaw. "Atomic-Level Characterization of Protein-Protein Association." Biophysical Journal 114, no. 3 (February 2018): 557a. http://dx.doi.org/10.1016/j.bpj.2017.11.3045.
Повний текст джерелаBetts, Matthew J., and Michael J. E. Sternberg. "An analysis of conformational changes on protein–protein association: implications for predictive docking." Protein Engineering, Design and Selection 12, no. 4 (April 1999): 271–83. http://dx.doi.org/10.1093/protein/12.4.271.
Повний текст джерелаBrems, David N., Leila A. Alter, Michael J. Beckage, Ronald E. Chance, Richard D. DiMarchi, L. Kenney Green, Harlan B. Long, Allen H. Pekar, James E. Shields, and Bruce H. Frank. "Altering the association properties of insulin by amino acid replacement." "Protein Engineering, Design and Selection" 5, no. 6 (1992): 527–33. http://dx.doi.org/10.1093/protein/5.6.527.
Повний текст джерелаHope, John N., Hao-Chia Chen та J. Fidding Hejtmancik. "βA3/Al-crystallin association: role of the N-terminal arm". "Protein Engineering, Design and Selection" 7, № 3 (1994): 445–51. http://dx.doi.org/10.1093/protein/7.3.445.
Повний текст джерелаBethea, Deidra, Sheng-Jiun Wu, Jinquan Luo, Linus Hyun, Eilyn R. Lacy, Alexey Teplyakov, Steven A. Jacobs, Karyn T. O'Neil, Gary L. Gilliland, and Yiqing Feng. "Mechanisms of self-association of a human monoclonal antibody CNTO607." Protein Engineering, Design and Selection 25, no. 10 (August 22, 2012): 531–38. http://dx.doi.org/10.1093/protein/gzs047.
Повний текст джерелаGabdoulline, Razif R., and Rebecca C. Wade. "Protein-protein association: investigation of factors influencing association rates by Brownian dynamics simulations." Journal of Molecular Biology 306, no. 5 (March 2001): 1139–55. http://dx.doi.org/10.1006/jmbi.2000.4404.
Повний текст джерелаRamly, Balqis, Nor Afiqah-Aleng, and Zeti-Azura Mohamed-Hussein. "Protein–Protein Interaction Network Analysis Reveals Several Diseases Highly Associated with Polycystic Ovarian Syndrome." International Journal of Molecular Sciences 20, no. 12 (June 18, 2019): 2959. http://dx.doi.org/10.3390/ijms20122959.
Повний текст джерелаRajagopal, Nandhini, and Shikha Nangia. "Obtaining Protein Association Energy Landscape for Integral Membrane Proteins." Journal of Chemical Theory and Computation 15, no. 11 (October 8, 2019): 6444–55. http://dx.doi.org/10.1021/acs.jctc.9b00626.
Повний текст джерелаZhou, Chun, Qimeng Wu, Ziliang Ye, Mengyi Liu, Zhuxian Zhang, Yuanyuan Zhang, Huan Li, et al. "Inverse Association Between Variety of Proteins With Appropriate Quantity From Different Food Sources and New-Onset Hypertension." Hypertension 79, no. 5 (May 2022): 1017–27. http://dx.doi.org/10.1161/hypertensionaha.121.18222.
Повний текст джерелаBen-Naim, Arieh. "On the driving forces for protein-protein association." Journal of Chemical Physics 125, no. 2 (July 14, 2006): 024901. http://dx.doi.org/10.1063/1.2205860.
Повний текст джерелаQin, Sanbo, and Huan-Xiang Zhou. "Automated Prediction of Protein-Protein Association Rate Constants." Biophysical Journal 100, no. 3 (February 2011): 386a. http://dx.doi.org/10.1016/j.bpj.2010.12.2295.
Повний текст джерелаKovalenko, I. B., A. M. Abaturova, A. N. Diakonova, O. S. Knyazeva, D. M. Ustinin, S. S. Khruschev, G. Yu Riznichenko, and A. B. Rubin. "Computer Simulation of Protein-Protein Association in Photosynthesis." Mathematical Modelling of Natural Phenomena 6, no. 7 (2011): 39–54. http://dx.doi.org/10.1051/mmnp/20116704.
Повний текст джерелаGilmore, Jason M., Deanna L. Auberry, Julia L. Sharp, Amanda M. White, Kevin K. Anderson, and Don S. Daly. "A Bayesian estimator of protein–protein association probabilities." Bioinformatics 24, no. 13 (May 22, 2008): 1554–55. http://dx.doi.org/10.1093/bioinformatics/btn238.
Повний текст джерелаElefsinioti, Antigoni, Ömer Sinan Saraç, Anna Hegele, Conrad Plake, Nina C. Hubner, Ina Poser, Mihail Sarov, et al. "Large-scaleDe NovoPrediction of Physical Protein-Protein Association." Molecular & Cellular Proteomics 10, no. 11 (August 11, 2011): M111.010629. http://dx.doi.org/10.1074/mcp.m111.010629.
Повний текст джерелаBen-Naim, A. "Solvent effects on protein association and protein folding." Biopolymers 29, no. 3 (February 15, 1990): 567–96. http://dx.doi.org/10.1002/bip.360290312.
Повний текст джерелаRuvinsky, Anatoly M., Tatsiana Kirys, Alexander V. Tuzikov, and Ilya A. Vakser. "Side-Chain Conformational Changes upon Protein–Protein Association." Journal of Molecular Biology 408, no. 2 (April 2011): 356–65. http://dx.doi.org/10.1016/j.jmb.2011.02.030.
Повний текст джерелаPrat-Gay, Gonzalo de. "Association of complementary fragments and the elucidation of protein folding pathways." "Protein Engineering, Design and Selection" 9, no. 10 (1996): 843–47. http://dx.doi.org/10.1093/protein/9.10.843.
Повний текст джерелаHejtmancik, J. F., P. T. Wingfield, C. Chambers, P. Russell, H. C. Chen, Y. V. Sergeev, and J. N. Hope. "Association properties of betaB2- and betaA3-crystallin: ability to form dimers." Protein Engineering Design and Selection 10, no. 11 (November 1, 1997): 1347–52. http://dx.doi.org/10.1093/protein/10.11.1347.
Повний текст джерелаDimitrova, Maria, Isabelle Imbert, Marie Paule Kieny, and Catherine Schuster. "Protein-Protein Interactions between Hepatitis C Virus Nonstructural Proteins." Journal of Virology 77, no. 9 (May 1, 2003): 5401–14. http://dx.doi.org/10.1128/jvi.77.9.5401-5414.2003.
Повний текст джерелаLee, Dong Heon, Chen Yao, Arunoday Bhan, Thorsten Schlaeger, Joshua Keefe, Benjamin A. T. Rodriguez, Shih-Jen Hwang, Ming-Huei Chen, Daniel Levy, and Andrew D. Johnson. "Integrative Genomic Analysis Reveals Four Protein Biomarkers for Platelet Traits." Circulation Research 127, no. 9 (October 9, 2020): 1182–94. http://dx.doi.org/10.1161/circresaha.119.316447.
Повний текст джерелаSzczepaniak, Andrzej, Karin Frank, and Jacek Rybka. "Membrane Association of the Rieske Iron-Sulfur Protein." Zeitschrift für Naturforschung C 50, no. 7-8 (August 1, 1995): 535–42. http://dx.doi.org/10.1515/znc-1995-7-811.
Повний текст джерелаMayer, Melanie L., and Philip Hieter. "Protein networks—built by association." Nature Biotechnology 18, no. 12 (December 2000): 1242–43. http://dx.doi.org/10.1038/82342.
Повний текст джерелаMukhopadhyay, Somnath, and Allyn C. Howlett. "CB1 receptor-G protein association." European Journal of Biochemistry 268, no. 3 (February 2001): 499–505. http://dx.doi.org/10.1046/j.1432-1327.2001.01810.x.
Повний текст джерелаGoldman, Nick, Jeffrey L. Thorne, and David T. Jones. "Assessing the Impact of Secondary Structure and Solvent Accessibility on Protein Evolution." Genetics 149, no. 1 (May 1, 1998): 445–58. http://dx.doi.org/10.1093/genetics/149.1.445.
Повний текст джерелаKabli, Fatima, Reda Mohamed Hamou, and Abdelmalek Amine. "Protein Classification Using N-gram Technique and Association Rules." International Journal of Software Innovation 6, no. 2 (April 2018): 77–89. http://dx.doi.org/10.4018/ijsi.2018040106.
Повний текст джерелаDong, C., Y. Mahamat-Saleh, A. Racine, P. Jantchou, S. Chan, A. Hart, F. Carbonnel, and M. C. Boutron-Ruault. "OP17 Protein intakes and risk of inflammatory bowel disease in the European Prospective Investigation into Cancer and Nutrition cohort (EPIC-IBD)." Journal of Crohn's and Colitis 14, Supplement_1 (January 2020): S015. http://dx.doi.org/10.1093/ecco-jcc/jjz203.016.
Повний текст джерелаChasman, D. I., and R. D. Kornberg. "GAL4 protein: purification, association with GAL80 protein, and conserved domain structure." Molecular and Cellular Biology 10, no. 6 (June 1990): 2916–23. http://dx.doi.org/10.1128/mcb.10.6.2916-2923.1990.
Повний текст джерелаChasman, D. I., and R. D. Kornberg. "GAL4 protein: purification, association with GAL80 protein, and conserved domain structure." Molecular and Cellular Biology 10, no. 6 (June 1990): 2916–23. http://dx.doi.org/10.1128/mcb.10.6.2916.
Повний текст джерелаBest, Robert B., Wenwei Zheng, and Jeetain Mittal. "Balanced Protein–Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association." Journal of Chemical Theory and Computation 10, no. 11 (October 16, 2014): 5113–24. http://dx.doi.org/10.1021/ct500569b.
Повний текст джерелаKendellen, Megan F., Katharine S. Barrientos, and Christopher M. Counter. "POT1 Association with TRF2 Regulates Telomere Length." Molecular and Cellular Biology 29, no. 20 (August 3, 2009): 5611–19. http://dx.doi.org/10.1128/mcb.00286-09.
Повний текст джерелаZiaunys, Mantas, Kamile Mikalauskaite, Lukas Krasauskas, and Vytautas Smirnovas. "Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers." International Journal of Molecular Sciences 24, no. 11 (May 25, 2023): 9277. http://dx.doi.org/10.3390/ijms24119277.
Повний текст джерелаSaveanu, Cosmin, Abdelkader Namane, Pierre-Emmanuel Gleizes, Alice Lebreton, Jean-Claude Rousselle, Jacqueline Noaillac-Depeyre, Nicole Gas, Alain Jacquier, and Micheline Fromont-Racine. "Sequential Protein Association with Nascent 60S Ribosomal Particles." Molecular and Cellular Biology 23, no. 13 (July 1, 2003): 4449–60. http://dx.doi.org/10.1128/mcb.23.13.4449-4460.2003.
Повний текст джерелаLivesay, D. R., and S. Subramaniam. "Conserved sequence and structure association motifs in antibody-protein and antibody-hapten complexes." Protein Engineering Design and Selection 17, no. 5 (June 8, 2004): 463–72. http://dx.doi.org/10.1093/protein/gzh058.
Повний текст джерелаXavier, K. Asish, Shawn M. McDonald, J. Andrew McCammon, and Richard C. Willson. "Association and dissociation kinetics of bobwhite quail lysozyme with monoclonal antibody HyHEL-5." Protein Engineering, Design and Selection 12, no. 1 (January 1999): 79–83. http://dx.doi.org/10.1093/protein/12.1.79.
Повний текст джерелаDhusia, Kalyani, Zhaoqian Su, and Yinghao Wu. "Using Coarse-Grained Simulations to Characterize the Mechanisms of Protein–Protein Association." Biomolecules 10, no. 7 (July 15, 2020): 1056. http://dx.doi.org/10.3390/biom10071056.
Повний текст джерелаMilligan, Graeme. "G protein-coupled receptors: oligomerisation and association with accessory proteins." Seminars in Cell & Developmental Biology 15, no. 3 (June 2004): 261. http://dx.doi.org/10.1016/j.semcdb.2003.12.014.
Повний текст джерелаSartor, O., J. H. Sameshima, and K. C. Robbins. "Differential association of cellular proteins with family protein-tyrosine kinases." Journal of Biological Chemistry 266, no. 10 (April 1991): 6462–66. http://dx.doi.org/10.1016/s0021-9258(18)38140-7.
Повний текст джерелаRapuano, Roberta, and Giuseppe Graziano. "On the Molecular Driving Force of Protein–Protein Association." Biophysica 2, no. 3 (August 25, 2022): 240–47. http://dx.doi.org/10.3390/biophysica2030023.
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