Artículos de revistas sobre el tema "Proteins - Conformation Dynamics"
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Kang, Hyun-Seo y Michael Sattler. "Capturing dynamic conformational shifts in protein–ligand recognition using integrative structural biology in solution". Emerging Topics in Life Sciences 2, n.º 1 (20 de abril de 2018): 107–19. http://dx.doi.org/10.1042/etls20170090.
Texto completoGaraizar, Adiran, Ignacio Sanchez-Burgos, Rosana Collepardo-Guevara y Jorge R. Espinosa. "Expansion of Intrinsically Disordered Proteins Increases the Range of Stability of Liquid–Liquid Phase Separation". Molecules 25, n.º 20 (15 de octubre de 2020): 4705. http://dx.doi.org/10.3390/molecules25204705.
Texto completoBrouhard, Gary J. y Luke M. Rice. "The contribution of αβ-tubulin curvature to microtubule dynamics". Journal of Cell Biology 207, n.º 3 (10 de noviembre de 2014): 323–34. http://dx.doi.org/10.1083/jcb.201407095.
Texto completoGormal, Rachel S., Pranesh Padmanabhan, Ravikiran Kasula, Adekunle T. Bademosi, Sean Coakley, Jean Giacomotto, Ailisa Blum et al. "Modular transient nanoclustering of activated β2-adrenergic receptors revealed by single-molecule tracking of conformation-specific nanobodies". Proceedings of the National Academy of Sciences 117, n.º 48 (19 de noviembre de 2020): 30476–87. http://dx.doi.org/10.1073/pnas.2007443117.
Texto completoMizutani, Tadashi y Shigeyuki Yagi. "Linear tetrapyrroles as functional pigments in chemistry and biology". Journal of Porphyrins and Phthalocyanines 08, n.º 03 (marzo de 2004): 226–37. http://dx.doi.org/10.1142/s1088424604000210.
Texto completoRamirez-Mondragon, Carlos A., Megin E. Nguyen, Jozafina Milicaj, Bakar A. Hassan, Frank J. Tucci, Ramaiah Muthyala, Jiali Gao, Erika A. Taylor y Yuk Y. Sham. "Conserved Conformational Hierarchy across Functionally Divergent Glycosyltransferases of the GT-B Structural Superfamily as Determined from Microsecond Molecular Dynamics". International Journal of Molecular Sciences 22, n.º 9 (28 de abril de 2021): 4619. http://dx.doi.org/10.3390/ijms22094619.
Texto completoKulkarni, Prakash, Vitor B. P. Leite, Susmita Roy, Supriyo Bhattacharyya, Atish Mohanty, Srisairam Achuthan, Divyoj Singh et al. "Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma". Biophysics Reviews 3, n.º 1 (marzo de 2022): 011306. http://dx.doi.org/10.1063/5.0080512.
Texto completoWestenhoff, Sebastian, Elena Nazarenko, Erik Malmerberg, Jan Davidsson, Gergely Katona y Richard Neutze. "Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches". Acta Crystallographica Section A Foundations of Crystallography 66, n.º 2 (18 de febrero de 2010): 207–19. http://dx.doi.org/10.1107/s0108767309054361.
Texto completoYang, Jing, Jing Chen y Zibiao Li. "Structural Basis for the Structure–Activity Behaviour of Oxaliplatin and its Enantiomeric Analogues: A Molecular Dynamics Study of Platinum-DNA Intrastrand Crosslink Adducts". Australian Journal of Chemistry 69, n.º 4 (2016): 379. http://dx.doi.org/10.1071/ch15624.
Texto completoLi, Haiyan, Zanxia Cao, Guodong Hu, Liling Zhao, Chunling Wang y Jihua Wang. "Ligand-induced structural changes analysis of ribose-binding protein as studied by molecular dynamics simulations". Technology and Health Care 29 (25 de marzo de 2021): 103–14. http://dx.doi.org/10.3233/thc-218011.
Texto completoNehls, Thomas, Tim Heymann, Christian Meyners, Felix Hausch y Frederik Lermyte. "Fenton-Chemistry-Based Oxidative Modification of Proteins Reflects Their Conformation". International Journal of Molecular Sciences 22, n.º 18 (14 de septiembre de 2021): 9927. http://dx.doi.org/10.3390/ijms22189927.
Texto completoLenaz, Giorgio. "Lipid fluidity and membrane protein dynamics". Bioscience Reports 7, n.º 11 (1 de noviembre de 1987): 823–37. http://dx.doi.org/10.1007/bf01119473.
Texto completoEvich, Marina, Alexander M. Spring-Connell y Markus W. Germann. "Impact of modified ribose sugars on nucleic acid conformation and function". Heterocyclic Communications 23, n.º 3 (27 de junio de 2017): 155–65. http://dx.doi.org/10.1515/hc-2017-0056.
Texto completoZhong, Bozitao, Ge Song y Hai-Feng Chen. "Balanced Force Field ff03CMAP Improving the Dynamics Conformation Sampling of Phosphorylation Site". International Journal of Molecular Sciences 23, n.º 19 (25 de septiembre de 2022): 11285. http://dx.doi.org/10.3390/ijms231911285.
Texto completoZhang, Meiling, Thomas E. Frederick, Jamie VanPelt, David A. Case y Jeffrey W. Peng. "Coupled intra- and interdomain dynamics support domain cross-talk in Pin1". Journal of Biological Chemistry 295, n.º 49 (22 de septiembre de 2020): 16585–603. http://dx.doi.org/10.1074/jbc.ra120.015849.
Texto completoRoither, Bernhard, Chris Oostenbrink, Georg Pfeiler, Heinz Koelbl y Wolfgang Schreiner. "Pembrolizumab Induces an Unexpected Conformational Change in the CC′-loop of PD-1". Cancers 13, n.º 1 (22 de diciembre de 2020): 5. http://dx.doi.org/10.3390/cancers13010005.
Texto completoSinnaeve, Davy, Abir Ben Bouzayene, Emile Ottoy, Gert-Jan Hofman, Eva Erdmann, Bruno Linclau, Ilya Kuprov, José C. Martins, Vladimir Torbeev y Bruno Kieffer. "Fluorine NMR study of proline-rich sequences using fluoroprolines". Magnetic Resonance 2, n.º 2 (9 de noviembre de 2021): 795–813. http://dx.doi.org/10.5194/mr-2-795-2021.
Texto completoDay, Austin L., Per Greisen, Lindsey Doyle, Alberto Schena, Nephi Stella, Kai Johnsson, David Baker y Barry Stoddard. "Unintended specificity of an engineered ligand-binding protein facilitated by unpredicted plasticity of the protein fold". Protein Engineering, Design and Selection 31, n.º 10 (1 de octubre de 2018): 375–87. http://dx.doi.org/10.1093/protein/gzy031.
Texto completoKim, J. I., K. Eom y S. Na. "Mechanical Mass-Spring Model for Understanding Globular Motion of Proteins". Journal of Mechanics 32, n.º 2 (25 de enero de 2016): 123–29. http://dx.doi.org/10.1017/jmech.2015.109.
Texto completoLaugwitz, Jeannette M., Haleh H. Haeri, Anette Kaiser, Ulrike Krug, Dariush Hinderberger, Annette G. Beck-Sickinger y Peter Schmidt. "Probing the Y2 Receptor on Transmembrane, Intra- and Extra-Cellular Sites for EPR Measurements". Molecules 25, n.º 18 (10 de septiembre de 2020): 4143. http://dx.doi.org/10.3390/molecules25184143.
Texto completoSharma, Meenakshi, Nancy Jaiswal, Dinesh Kumar y Krishna Mohan Poluri. "Enhanced dynamics of conformationally heterogeneous T7 bacteriophage lysozyme native state attenuates its stability and activity". Biochemical Journal 476, n.º 3 (14 de febrero de 2019): 613–28. http://dx.doi.org/10.1042/bcj20180703.
Texto completoPistolesi, Sara, Nico Tjandra y Guillermo A. Bermejo. "Solution NMR studies of periplasmic binding proteins and their interaction partners". BioMolecular Concepts 2, n.º 1-2 (1 de abril de 2011): 53–64. http://dx.doi.org/10.1515/bmc.2011.005.
Texto completoTafi, A., Fabrizio Manetti, Federico Corelli, Stefano Alcaro y Maurizio Botta. "Structural flexibility of hyaluronan oligomers as probed by molecular modelling". Pure and Applied Chemistry 75, n.º 2-3 (1 de enero de 2003): 359–66. http://dx.doi.org/10.1351/pac200375020359.
Texto completoKrukenberg, Kristin A., Timothy O. Street, Laura A. Lavery y David A. Agard. "Conformational dynamics of the molecular chaperone Hsp90". Quarterly Reviews of Biophysics 44, n.º 2 (18 de marzo de 2011): 229–55. http://dx.doi.org/10.1017/s0033583510000314.
Texto completoTamrazi, Anobel, Kathryn E. Carlson, Alice L. Rodriguez y John A. Katzenellenbogen. "Coactivator Proteins as Determinants of Estrogen Receptor Structure and Function: Spectroscopic Evidence for a Novel Coactivator-Stabilized Receptor Conformation". Molecular Endocrinology 19, n.º 6 (1 de junio de 2005): 1516–28. http://dx.doi.org/10.1210/me.2004-0458.
Texto completoSun, Jixue, Zibin Li y Na Yang. "Mechanism of the Conformational Change of the Protein Methyltransferase SMYD3: A Molecular Dynamics Simulation Study". International Journal of Molecular Sciences 22, n.º 13 (2 de julio de 2021): 7185. http://dx.doi.org/10.3390/ijms22137185.
Texto completoVollmer, B., V. Pražák, D. Vasishtan, E. E. Jefferys, A. Hernandez-Duran, M. Vallbracht, B. G. Klupp et al. "The prefusion structure of herpes simplex virus glycoprotein B". Science Advances 6, n.º 39 (septiembre de 2020): eabc1726. http://dx.doi.org/10.1126/sciadv.abc1726.
Texto completoCaldararu, Octav, Vilhelm Ekberg, Derek T. Logan, Esko Oksanen y Ulf Ryde. "Exploring ligand dynamics in protein crystal structures with ensemble refinement". Acta Crystallographica Section D Structural Biology 77, n.º 8 (29 de julio de 2021): 1099–115. http://dx.doi.org/10.1107/s2059798321006513.
Texto completoLIEBOVITCH, LARRY S., NIKITA D. ARNOLD y LEV Y. SELECTOR. "NEURAL NETWORKS TO COMPUTE MOLECULAR DYNAMICS". Journal of Biological Systems 02, n.º 02 (junio de 1994): 193–228. http://dx.doi.org/10.1142/s0218339094000155.
Texto completoRen, Zhenning, Jumin Lee, Mahdi Muhammad Moosa, Yin Nian, Liya Hu, Zhichun Xu, Jason G. McCoy, Allan Chris M. Ferreon, Wonpil Im y Ming Zhou. "Structure of an EIIC sugar transporter trapped in an inward-facing conformation". Proceedings of the National Academy of Sciences 115, n.º 23 (21 de mayo de 2018): 5962–67. http://dx.doi.org/10.1073/pnas.1800647115.
Texto completoStewart, Chelsea M., Cosmo Z. Buffalo, J. Andrés Valderrama, Anna Henningham, Jason N. Cole, Victor Nizet y Partho Ghosh. "Coiled-coil destabilizing residues in the group A Streptococcus M1 protein are required for functional interaction". Proceedings of the National Academy of Sciences 113, n.º 34 (10 de agosto de 2016): 9515–20. http://dx.doi.org/10.1073/pnas.1606160113.
Texto completoLi, Qingxin y CongBao Kang. "Insights into Structures and Dynamics of Flavivirus Proteases from NMR Studies". International Journal of Molecular Sciences 21, n.º 7 (5 de abril de 2020): 2527. http://dx.doi.org/10.3390/ijms21072527.
Texto completoFidy, Judit, Monique Laberge, Beata Ullrich, Laszlo Polgar, Zoltan Szeltner, Jacques Gallay y Michel Vincent. "Tryptophan rotamers that report the conformational dynamics of proteins". Pure and Applied Chemistry 73, n.º 3 (1 de enero de 2001): 415–19. http://dx.doi.org/10.1351/pac200173030415.
Texto completoRief, Matthias, Filipp Oesterhelt, Hauke Clausen-Schaumann y Hermann E. Gaub. "Structural Forces in Biomolecules". Microscopy and Microanalysis 5, S2 (agosto de 1999): 1016–17. http://dx.doi.org/10.1017/s1431927600018407.
Texto completoCamacho, Inês S., Alina Theisen, Linus O. Johannissen, L. Aranzazú Díaz-Ramos, John M. Christie, Gareth I. Jenkins, Bruno Bellina, Perdita Barran y Alex R. Jones. "Native mass spectrometry reveals the conformational diversity of the UVR8 photoreceptor". Proceedings of the National Academy of Sciences 116, n.º 4 (4 de enero de 2019): 1116–25. http://dx.doi.org/10.1073/pnas.1813254116.
Texto completoLangan, Patricia S., Venu Gopal Vandavasi, Wojciech Kopec, Brendan Sullivan, Pavel V. Afonne, Kevin L. Weiss, Bert L. de Groot y Leighton Coates. "The structure of a potassium-selective ion channel reveals a hydrophobic gate regulating ion permeation". IUCrJ 7, n.º 5 (25 de julio de 2020): 835–43. http://dx.doi.org/10.1107/s2052252520008271.
Texto completoWen, Lai, Alex Marki, Payel Roy, Sara McArdle, Hao Sun, Zhichao Fan, Alexandre R. Gingras, Mark H. Ginsberg y Klaus Ley. "Recruitment of kindlin-3 to plasma membrane through its PH domain precedes high affinity β2 integrin activation and neutrophil arrest". Journal of Immunology 204, n.º 1_Supplement (1 de mayo de 2020): 220.7. http://dx.doi.org/10.4049/jimmunol.204.supp.220.7.
Texto completoTyagi, Vivek, Victor Vasquez-Montes, J. Alfredo Freites, Alexander Kyrychenko, Douglas J. Tobias y Alexey S. Ladokhin. "Effects of Cardiolipin on the Conformational Dynamics of Membrane-Anchored Bcl-xL". International Journal of Molecular Sciences 22, n.º 17 (30 de agosto de 2021): 9388. http://dx.doi.org/10.3390/ijms22179388.
Texto completoCraggs, Timothy D., Marko Sustarsic, Anne Plochowietz, Majid Mosayebi, Hendrik Kaju, Andrew Cuthbert, Johannes Hohlbein et al. "Substrate conformational dynamics facilitate structure-specific recognition of gapped DNA by DNA polymerase". Nucleic Acids Research 47, n.º 20 (23 de septiembre de 2019): 10788–800. http://dx.doi.org/10.1093/nar/gkz797.
Texto completoBeier, David H., Tucker J. Carrocci, Clarisse van der Feltz, U. Sandy Tretbar, Joshua C. Paulson, Nikolai Grabowski y Aaron A. Hoskins. "Dynamics of the DEAD-box ATPase Prp5 RecA-like domains provide a conformational switch during spliceosome assembly". Nucleic Acids Research 47, n.º 20 (6 de septiembre de 2019): 10842–51. http://dx.doi.org/10.1093/nar/gkz765.
Texto completoTarjányi, Tamás, Ferenc Bogár, Janos Minarovits, Márió Gajdács y Zsolt Tóth. "Interaction of KRSR Peptide with Titanium Dioxide Anatase (100) Surface: A Molecular Dynamics Simulation Study". International Journal of Molecular Sciences 22, n.º 24 (9 de diciembre de 2021): 13251. http://dx.doi.org/10.3390/ijms222413251.
Texto completoGoricanec, David, Ralf Stehle, Pascal Egloff, Simina Grigoriu, Andreas Plückthun, Gerhard Wagner y Franz Hagn. "Conformational dynamics of a G-protein α subunit is tightly regulated by nucleotide binding". Proceedings of the National Academy of Sciences 113, n.º 26 (13 de junio de 2016): E3629—E3638. http://dx.doi.org/10.1073/pnas.1604125113.
Texto completoMott, Helen R. y Darerca Owen. "Allostery and dynamics in small G proteins". Biochemical Society Transactions 46, n.º 5 (9 de octubre de 2018): 1333–43. http://dx.doi.org/10.1042/bst20170569.
Texto completoHu, Gang, Jiye Fu, Yi Qiao, Hao Meng, Zunliang Wang, Jing Tu y Zuhong Lu. "Molecular dynamics discrimination of the conformational states of calmodulin through solid-state nanopores". Physical Chemistry Chemical Physics 22, n.º 34 (2020): 19188–94. http://dx.doi.org/10.1039/d0cp02500c.
Texto completoLakomek, Nils-Alexander, Halenur Yavuz, Reinhard Jahn y Ángel Pérez-Lara. "Structural dynamics and transient lipid binding of synaptobrevin-2 tune SNARE assembly and membrane fusion". Proceedings of the National Academy of Sciences 116, n.º 18 (11 de abril de 2019): 8699–708. http://dx.doi.org/10.1073/pnas.1813194116.
Texto completoMartini, Silvia, Claudia Bonechi, Alberto Foletti y Claudio Rossi. "Water-Protein Interactions: The Secret of Protein Dynamics". Scientific World Journal 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/138916.
Texto completoDas, Ananya, Nichole Adiletta y Dmitri N. Ermolenko. "Interplay between Inter-Subunit Rotation of the Ribosome and Binding of Translational GTPases". International Journal of Molecular Sciences 24, n.º 8 (7 de abril de 2023): 6878. http://dx.doi.org/10.3390/ijms24086878.
Texto completoBiedermannová, Lada y Bohdan Schneider. "Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures". Acta Crystallographica Section D Biological Crystallography 71, n.º 11 (27 de octubre de 2015): 2192–202. http://dx.doi.org/10.1107/s1399004715015679.
Texto completoGiampà, Marco y Elvira Sgobba. "Insight to Functional Conformation and Noncovalent Interactions of Protein-Protein Assembly Using MALDI Mass Spectrometry". Molecules 25, n.º 21 (28 de octubre de 2020): 4979. http://dx.doi.org/10.3390/molecules25214979.
Texto completoDevlin, Jason, Jesus Alonso, Grant Keller, Sara Bobisse, Alexandre Harari y Brian Baker. "4094 Structural Determinants of Immunogenicity for Peptide-Based Immunotherapy". Journal of Clinical and Translational Science 4, s1 (junio de 2020): 16. http://dx.doi.org/10.1017/cts.2020.92.
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