Статті в журналах з теми "Protein Conformers"
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Ознайомтеся з топ-50 статей у журналах для дослідження на тему "Protein Conformers".
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Schneider, Bohdan, Jiří Černý, Daniel Svozil, Petr Čech, Jean-Christophe Gelly, and Alexandre G. de Brevern. "Bioinformatic analysis of the protein/DNA interface." Nucleic Acids Research 42, no. 5 (December 11, 2013): 3381–94. http://dx.doi.org/10.1093/nar/gkt1273.
Повний текст джерелаVerdonk, Marcel L., Paul N. Mortenson, Richard J. Hall, Michael J. Hartshorn, and Christopher W. Murray. "Protein−Ligand Docking against Non-Native Protein Conformers." Journal of Chemical Information and Modeling 48, no. 11 (October 28, 2008): 2214–25. http://dx.doi.org/10.1021/ci8002254.
Повний текст джерелаXu, Aoshuang, Fenglei Li, Howard Robinson, and Edward S. Yeung. "Can Protein Conformers Be Fractionated by Crystallization?" Analytical Chemistry 85, no. 13 (June 12, 2013): 6372–77. http://dx.doi.org/10.1021/ac400762x.
Повний текст джерелаMahajan, Swapnil, and Yves-Henri Sanejouand. "Jumping between protein conformers using normal modes." Journal of Computational Chemistry 38, no. 18 (May 3, 2017): 1622–30. http://dx.doi.org/10.1002/jcc.24803.
Повний текст джерелаMa, Jiyan, Jingjing Zhang, and Runchuan Yan. "Recombinant Mammalian Prions: The “Correctly” Misfolded Prion Protein Conformers." Viruses 14, no. 9 (August 31, 2022): 1940. http://dx.doi.org/10.3390/v14091940.
Повний текст джерелаde Groot, J., and H. H. J. de Jongh. "The presence of heat-stable conformers of ovalbumin affects properties of thermally formed aggregates." Protein Engineering Design and Selection 16, no. 12 (December 1, 2003): 1035–40. http://dx.doi.org/10.1093/protein/gzg123.
Повний текст джерелаBeglov, Dmitri, David R. Hall, Ryan Brenke, Maxim V. Shapovalov, Roland L. Dunbrack, Dima Kozakov, and Sandor Vajda. "Minimal ensembles of side chain conformers for modeling protein-protein interactions." Proteins: Structure, Function, and Bioinformatics 80, no. 2 (November 22, 2011): 591–601. http://dx.doi.org/10.1002/prot.23222.
Повний текст джерелаOrellana, Laura, Johan Gustavsson, Cathrine Bergh, Ozge Yoluk, and Erik Lindahl. "eBDIMS server: protein transition pathways with ensemble analysis in 2D-motion spaces." Bioinformatics 35, no. 18 (February 19, 2019): 3505–7. http://dx.doi.org/10.1093/bioinformatics/btz104.
Повний текст джерелаWalsh, Daniel J., Abigail M. Schwind, Geoffrey P. Noble, and Surachai Supattapone. "Conformational diversity in purified prions produced in vitro." PLOS Pathogens 19, no. 1 (January 10, 2023): e1011083. http://dx.doi.org/10.1371/journal.ppat.1011083.
Повний текст джерелаBarreca, Maria, Nunzio Iraci, Silvia Biggi, Violetta Cecchetti, and Emiliano Biasini. "Pharmacological Agents Targeting the Cellular Prion Protein." Pathogens 7, no. 1 (March 7, 2018): 27. http://dx.doi.org/10.3390/pathogens7010027.
Повний текст джерелаSahini, Victor, and Gabriela Ionita. "Evidence of changes in hydrophilic/hydrophobic balance and in chemical activity of HSA induced by thermal treatments." Open Chemistry 9, no. 2 (April 1, 2011): 245–52. http://dx.doi.org/10.2478/s11532-010-0148-2.
Повний текст джерелаGuo, Xiang, Jincheng Han, Ray Luo, and Hai-Feng Chen. "Conformation dynamics of the intrinsically disordered protein c-Myb with the ff99IDPs force field." RSC Advances 7, no. 47 (2017): 29713–21. http://dx.doi.org/10.1039/c7ra04133k.
Повний текст джерелаChen, Shih-Cheng, and René C. L. Olsthoorn. "In Vitro and In Vivo Studies of the RNA Conformational Switch in Alfalfa Mosaic Virus." Journal of Virology 84, no. 3 (November 18, 2009): 1423–29. http://dx.doi.org/10.1128/jvi.01443-09.
Повний текст джерелаFutamura, Akinori, Sotaro Hieda, Yukiko Mori, Kensaku Kasuga, Azusa Sugimoto, Hideyo Kasai, Takeshi Kuroda та ін. "Toxic Amyloid-β42 Conformer May Accelerate the Onset of Alzheimer’s Disease in the Preclinical Stage". Journal of Alzheimer's Disease 80, № 2 (23 березня 2021): 639–46. http://dx.doi.org/10.3233/jad-201407.
Повний текст джерелаGhaemmaghami, Sina, Julie Ullman, Misol Ahn, Susan St. Martin, and Stanley B. Prusiner. "Chemical Induction of Misfolded Prion Protein Conformers in Cell Culture." Journal of Biological Chemistry 285, no. 14 (December 2, 2009): 10415–23. http://dx.doi.org/10.1074/jbc.m109.045112.
Повний текст джерелаYoung, Lawrence J., and Lewis M. Siegel. "Activated conformers of Escherichia coli sulfite reductase heme protein subunit." Biochemistry 27, no. 14 (July 12, 1988): 4991–99. http://dx.doi.org/10.1021/bi00414a007.
Повний текст джерелаKuprowski, Mark C., and Lars Konermann. "Signal Response of Coexisting Protein Conformers in Electrospray Mass Spectrometry." Analytical Chemistry 79, no. 6 (March 2007): 2499–506. http://dx.doi.org/10.1021/ac0620056.
Повний текст джерелаNowalk, Andrew J., Kevin G. Vaughan, Billy W. Day, Sarah B. Tencza, and Timothy A. Mietzner. "Metal-Dependent Conformers of the Periplasmic Ferric Ion Binding Protein†." Biochemistry 36, no. 42 (October 1997): 13054–59. http://dx.doi.org/10.1021/bi971413o.
Повний текст джерелаBouvignies, Guillaume, Pramodh Vallurupalli, and Lewis E. Kay. "Visualizing Side Chains of Invisible Protein Conformers by Solution NMR." Journal of Molecular Biology 426, no. 3 (February 2014): 763–74. http://dx.doi.org/10.1016/j.jmb.2013.10.041.
Повний текст джерелаSmirnova, Irina, Vladimir Kasho, Xiaoxu Jiang, Els Pardon, Jan Steyaert, and H. Ronald Kaback. "Transient conformers of LacY are trapped by nanobodies." Proceedings of the National Academy of Sciences 112, no. 45 (October 28, 2015): 13839–44. http://dx.doi.org/10.1073/pnas.1519485112.
Повний текст джерелаXu, Xingjian, Igor Dikiy, Matthew R. Evans, Leandro P. Marcelino, and Kevin H. Gardner. "Fragile protein folds: sequence and environmental factors affecting the equilibrium of two interconverting, stably folded protein conformations." Magnetic Resonance 2, no. 1 (March 10, 2021): 63–76. http://dx.doi.org/10.5194/mr-2-63-2021.
Повний текст джерелаAkasaka, Kazuyuki. "Exploring the entire conformational space of proteins by high-pressure NMR." Pure and Applied Chemistry 75, no. 7 (January 1, 2003): 927–36. http://dx.doi.org/10.1351/pac200375070927.
Повний текст джерелаMaki, Takahito, Masahito Sawahata, Ichiro Akutsu, Shohei Amaike, Genki Hiramatsu, Daisuke Uta, Naotaka Izuo, Takahiko Shimizu, Kazuhiro Irie та Toshiaki Kume. "APP Knock-In Mice Produce E22P-Aβ Exhibiting an Alzheimer’s Disease-like Phenotype with Dysregulation of Hypoxia-Inducible Factor Expression". International Journal of Molecular Sciences 23, № 21 (31 жовтня 2022): 13259. http://dx.doi.org/10.3390/ijms232113259.
Повний текст джерелаHromadkova, Lenka, Mohammad Khursheed Siddiqi, He Liu, and Jiri G. Safar. "Populations of Tau Conformers Drive Prion-like Strain Effects in Alzheimer’s Disease and Related Dementias." Cells 11, no. 19 (September 26, 2022): 2997. http://dx.doi.org/10.3390/cells11192997.
Повний текст джерелаGumerov, Dmitry R., Andras Dobo, and Igor A. Kaltashov. "Protein—Ion Charge-State Distributions in Electrospray Ionization Mass Spectrometry: Distinguishing Conformational Contributions from Masking Effects." European Journal of Mass Spectrometry 8, no. 2 (April 2002): 123–29. http://dx.doi.org/10.1255/ejms.480.
Повний текст джерелаKurpiewska, Katarzyna, and Krzysztof Lewiński. "High pressure macromolecular crystallography for structural biology: a review." Open Life Sciences 5, no. 5 (October 1, 2010): 531–42. http://dx.doi.org/10.2478/s11535-010-0044-y.
Повний текст джерелаScott, M. R., D. Groth, J. Tatzelt, M. Torchia, P. Tremblay, S. J. DeArmond, and S. B. Prusiner. "Propagation of prion strains through specific conformers of the prion protein." Journal of virology 71, no. 12 (1997): 9032–44. http://dx.doi.org/10.1128/jvi.71.12.9032-9044.1997.
Повний текст джерелаBroersen, Kerensa, Mireille Weijers, Jolan de Groot, Rob J. Hamer, and de Jongh. "Effect of Protein Charge on the Generation of Aggregation-Prone Conformers." Biomacromolecules 8, no. 5 (May 2007): 1648–56. http://dx.doi.org/10.1021/bm0612283.
Повний текст джерелаMuir, T. W., M. J. Williams, and S. B. H. Kent. "Detection of Synthetic Protein Isomers and Conformers by Electrospray Mass Spectrometry." Analytical Biochemistry 224, no. 1 (January 1995): 100–109. http://dx.doi.org/10.1006/abio.1995.1013.
Повний текст джерелаYan, Xin, and Robert B. Denman. "Conformational-Dependent and Independent RNA Binding to the Fragile X Mental Retardation Protein." Journal of Nucleic Acids 2011 (2011): 1–14. http://dx.doi.org/10.4061/2011/246127.
Повний текст джерелаPogonin, Aleksandr E., George A. Gamov, Maksim N. Zavalishin, and Valentin A. Sharnin. "CONFORMATIONAL BEHAVIOR OF HYDRAZONE DERIVED FROM PYRIDOXAL 5’-PHOSPHATE AND ISONIAZID." IZVESTIYA VYSSHIKH UCHEBNYKH ZAVEDENIY KHIMIYA KHIMICHESKAYA TEKHNOLOGIYA 61, no. 12 (December 12, 2018): 101–7. http://dx.doi.org/10.6060/ivkkt.20186112.5846.
Повний текст джерелаChampenois, E. G., D. M. Sanchez, J. Yang, J. P. Figueira Nunes, A. Attar, M. Centurion, R. Forbes, et al. "Conformer-specific photochemistry imaged in real space and time." Science 374, no. 6564 (October 8, 2021): 178–82. http://dx.doi.org/10.1126/science.abk3132.
Повний текст джерелаRolfsson, Ottar, Katerina Toropova, Victoria Morton, Simona Francese, Gabriella Basnak, Gary S. Thompson, Stephen W. Homans, et al. "RNA Packing Specificity and Folding during Assembly of the Bacteriophage MS2." Computational and Mathematical Methods in Medicine 9, no. 3-4 (2008): 339–49. http://dx.doi.org/10.1080/17486700802168445.
Повний текст джерелаNikiforovich, G. V., S. Galaktionov, J. Balodis, and G. R. Marshall. "Novel approach to computer modeling of seven-helical transmembrane proteins: current progress in the test case of bacteriorhodopsin." Acta Biochimica Polonica 48, no. 1 (March 31, 2001): 53–64. http://dx.doi.org/10.18388/abp.2001_5111.
Повний текст джерелаAhinko, Mira, Sami T. Kurkinen, Sanna P. Niinivehmas, Olli T. Pentikäinen, and Pekka A. Postila. "A Practical Perspective: The Effect of Ligand Conformers on the Negative Image-Based Screening." International Journal of Molecular Sciences 20, no. 11 (June 6, 2019): 2779. http://dx.doi.org/10.3390/ijms20112779.
Повний текст джерелаHsueh, Shu-Shun, S. S. (Steven) Wang, Shu-Han Chen, Chia-Lin Wang, W. (Josephine) Wu та Ta-Hsien Lin. "Insights to Human γD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations". International Journal of Molecular Sciences 23, № 3 (29 січня 2022): 1591. http://dx.doi.org/10.3390/ijms23031591.
Повний текст джерелаYu, Hongjun, Tania J. Lupoli, Amanda Kovach, Xing Meng, Gongpu Zhao, Carl F. Nathan, and Huilin Li. "ATP hydrolysis-coupled peptide translocation mechanism of Mycobacterium tuberculosis ClpB." Proceedings of the National Academy of Sciences 115, no. 41 (September 26, 2018): E9560—E9569. http://dx.doi.org/10.1073/pnas.1810648115.
Повний текст джерелаJosefson, Rebecca, Rebecca Andersson, and Thomas Nyström. "How and why do toxic conformers of aberrant proteins accumulate during ageing?" Essays in Biochemistry 61, no. 3 (May 24, 2017): 317–24. http://dx.doi.org/10.1042/ebc20160085.
Повний текст джерелаLaine, Roney O., and Alfred F. Esser. "Detection of refolding conformers of complement protein C9 during insertion into membranes." Nature 341, no. 6237 (September 1989): 63–65. http://dx.doi.org/10.1038/341063a0.
Повний текст джерелаShvartsburg, Alexandre A., and Richard D. Smith. "Separation of Protein Conformers by Differential Ion Mobility in Hydrogen-Rich Gases." Analytical Chemistry 85, no. 14 (June 25, 2013): 6967–73. http://dx.doi.org/10.1021/ac4015963.
Повний текст джерелаCavatorta, P., L. Masotti, A. G. Szabo, D. Juretic, P. Piccio, and E. Quagliariello. "Fluorescence spectral resolution of myelin basic protein conformers in complexes with lysophosphatidylcholine." Cell Biophysics 13, no. 3 (December 1988): 201–15. http://dx.doi.org/10.1007/bf02918376.
Повний текст джерелаJung, Byung Chul, Yoon-Ju Lim, Eun-Jin Bae, Jun Sung Lee, Min Sun Choi, Michael K. Lee, He-Jin Lee, Yoon Suk Kim та Seung-Jae Lee. "Amplification of distinct α-synuclein fibril conformers through protein misfolding cyclic amplification". Experimental & Molecular Medicine 49, № 4 (квітень 2017): e314-e314. http://dx.doi.org/10.1038/emm.2017.1.
Повний текст джерелаPurves, Randy W., Barbara Ells, David A. Barnett, and Roger Guevremont. "Combining HD exchange and ESI-FAIMS-MS for detecting gas-phase conformers of equine cytochrome c." Canadian Journal of Chemistry 83, no. 11 (November 1, 2005): 1961–68. http://dx.doi.org/10.1139/v05-215.
Повний текст джерелаRother, Kristian, Mathias Dunkel, Elke Michalsky, Silke Trissl, Andrean Goede, Ulf Leser, and Robert Preissner. "A structural keystone for drug design." Journal of Integrative Bioinformatics 3, no. 1 (June 1, 2006): 21–31. http://dx.doi.org/10.1515/jib-2006-19.
Повний текст джерелаPanicker, Sumith R., Indranil Biswas, Hemant Giri, Xiaofeng Cai та Alireza R. Rezaie. "PKC (Protein Kinase C)-δ Modulates AT (Antithrombin) Signaling in Vascular Endothelial Cells". Arteriosclerosis, Thrombosis, and Vascular Biology 40, № 7 (липень 2020): 1748–62. http://dx.doi.org/10.1161/atvbaha.120.314479.
Повний текст джерелаDuque Velásquez, Camilo, Chae Kim, Tracy Haldiman, Chiye Kim, Allen Herbst, Judd Aiken, Jiri G. Safar, and Debbie McKenzie. "Chronic wasting disease (CWD) prion strains evolve via adaptive diversification of conformers in hosts expressing prion protein polymorphisms." Journal of Biological Chemistry 295, no. 15 (February 28, 2020): 4985–5001. http://dx.doi.org/10.1074/jbc.ra120.012546.
Повний текст джерелаYuan, Jue, Xiangzhu Xiao, John McGeehan, Zhiqian Dong, Ignazio Cali, Hisashi Fujioka, Qingzhong Kong, Geoff Kneale, Pierluigi Gambetti, and Wen-Quan Zou. "Insoluble Aggregates and Protease-resistant Conformers of Prion Protein in Uninfected Human Brains." Journal of Biological Chemistry 281, no. 46 (September 20, 2006): 34848–58. http://dx.doi.org/10.1074/jbc.m602238200.
Повний текст джерелаGiven, James A., and Michael K. Gilson. "A hierarchical method for generating low-energy conformers of a protein-ligand complex." Proteins: Structure, Function, and Genetics 33, no. 4 (December 1, 1998): 475–95. http://dx.doi.org/10.1002/(sici)1097-0134(19981201)33:4<475::aid-prot3>3.0.co;2-b.
Повний текст джерелаOhkawa, Kousaku, Masakazu Hachisu, Takaomi Nomura, Ryoichi Arai, Kimio Hirabayashi, Masuhiro Tsukada, and Koji Abe. "Chain Conformational Study on Underwater Silk Proteins from Caddisfly, Stenopsyche marmorata - Implication of a Fiber-Forming Mechanism." Advanced Materials Research 796 (September 2013): 3–8. http://dx.doi.org/10.4028/www.scientific.net/amr.796.3.
Повний текст джерелаCostanzo, Maddalena, and Chiara Zurzolo. "The cell biology of prion-like spread of protein aggregates: mechanisms and implication in neurodegeneration." Biochemical Journal 452, no. 1 (April 25, 2013): 1–17. http://dx.doi.org/10.1042/bj20121898.
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