Статті в журналах з теми "Ligand Recognition"
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Vijayrajratnam, Sukhithasri, Anju Choorakottayil Pushkaran, Aathira Balakrishnan, Anil Kumar Vasudevan, Raja Biswas, and Chethampadi Gopi Mohan. "Understanding the molecular differential recognition of muramyl peptide ligands by LRR domains of human NOD receptors." Biochemical Journal 474, no. 16 (July 27, 2017): 2691–711. http://dx.doi.org/10.1042/bcj20170220.
Повний текст джерелаSmyth, Mark J., Jeremy Swann, Janice M. Kelly, Erika Cretney, Wayne M. Yokoyama, Andreas Diefenbach, Thomas J. Sayers, and Yoshihiro Hayakawa. "NKG2D Recognition and Perforin Effector Function Mediate Effective Cytokine Immunotherapy of Cancer." Journal of Experimental Medicine 200, no. 10 (November 15, 2004): 1325–35. http://dx.doi.org/10.1084/jem.20041522.
Повний текст джерелаGasparri, Federica, Jesper Wengel, Thomas Grutter, and Stephan A. Pless. "Molecular determinants for agonist recognition and discrimination in P2X2 receptors." Journal of General Physiology 151, no. 7 (May 24, 2019): 898–911. http://dx.doi.org/10.1085/jgp.201912347.
Повний текст джерелаBaron, Riccardo, and J. Andrew McCammon. "Molecular Recognition and Ligand Association." Annual Review of Physical Chemistry 64, no. 1 (April 2013): 151–75. http://dx.doi.org/10.1146/annurev-physchem-040412-110047.
Повний текст джерелаBaron, Riccardo, Piotr Setny, and J. Andrew McCammon. "Water in Cavity−Ligand Recognition." Journal of the American Chemical Society 132, no. 34 (August 9, 2010): 12091–97. http://dx.doi.org/10.1021/ja1050082.
Повний текст джерелаAnand, Praveen, Deepesh Nagarajan, Sumanta Mukherjee, and Nagasuma Chandra. "ABS–Scan: In silico alanine scanning mutagenesis for binding site residues in protein–ligand complex." F1000Research 3 (September 9, 2014): 214. http://dx.doi.org/10.12688/f1000research.5165.1.
Повний текст джерелаAnand, Praveen, Deepesh Nagarajan, Sumanta Mukherjee, and Nagasuma Chandra. "ABS–Scan: In silico alanine scanning mutagenesis for binding site residues in protein–ligand complex." F1000Research 3 (December 1, 2014): 214. http://dx.doi.org/10.12688/f1000research.5165.2.
Повний текст джерелаMcMillan, Jourdan K. P., Patrick O’Donnell, and Sandra P. Chang. "Pattern recognition receptor ligand-induced differentiation of human transitional B cells." PLOS ONE 17, no. 8 (August 30, 2022): e0273810. http://dx.doi.org/10.1371/journal.pone.0273810.
Повний текст джерелаLeboffe, Loris, Alessandra di Masi, Fabio Polticelli, Viviana Trezza, and Paolo Ascenzi. "Structural Basis of Drug Recognition by Human Serum Albumin." Current Medicinal Chemistry 27, no. 30 (September 8, 2020): 4907–31. http://dx.doi.org/10.2174/0929867326666190320105316.
Повний текст джерелаDiamond, M. S., J. Garcia-Aguilar, J. K. Bickford, A. L. Corbi, and T. A. Springer. "The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands." Journal of Cell Biology 120, no. 4 (February 15, 1993): 1031–43. http://dx.doi.org/10.1083/jcb.120.4.1031.
Повний текст джерелаGalano-Frutos, Juan J., M. Carmen Morón, and Javier Sancho. "The mechanism of water/ion exchange at a protein surface: a weakly bound chloride in Helicobacter pylori apoflavodoxin." Physical Chemistry Chemical Physics 17, no. 43 (2015): 28635–46. http://dx.doi.org/10.1039/c5cp04504e.
Повний текст джерелаKoehler, Melanie, Anny Fis, Hermann J. Gruber, and Peter Hinterdorfer. "AFM-Based Force Spectroscopy Guided by Recognition Imaging: A New Mode for Mapping and Studying Interaction Sites at Low Lateral Density." Methods and Protocols 2, no. 1 (January 8, 2019): 6. http://dx.doi.org/10.3390/mps2010006.
Повний текст джерелаGil, Diana, Adam G. Schrum, Balbino Alarcón, and Ed Palmer. "T cell receptor engagement by peptide–MHC ligands induces a conformational change in the CD3 complex of thymocytes." Journal of Experimental Medicine 201, no. 4 (February 21, 2005): 517–22. http://dx.doi.org/10.1084/jem.20042036.
Повний текст джерелаVivat, V., D. Gofflo, T. Garcia, J.-M. Wurtz, W. Bourguet, D. Philibert, and H. Gronemeyer. "Sequences in the ligand-binding domains of the human androgen and progesterone receptors which determine their distinct ligand identities." Journal of Molecular Endocrinology 18, no. 2 (April 1997): 147–60. http://dx.doi.org/10.1677/jme.0.0180147.
Повний текст джерелаGinsberg, M. H., J. C. Loftus, S. D'Souza, and E. F. Plow. "Ligand binding to integrins: Common and ligand specific recognition mechanisms." Cell Differentiation and Development 32, no. 3 (December 1990): 203–13. http://dx.doi.org/10.1016/0922-3371(90)90033-s.
Повний текст джерелаNegi, Ajay Singh, and Ajay Kumar Sood. "Electric Field–Enhanced Sensitivity of Grafted Ligands and Receptors." Clinical Chemistry 54, no. 2 (February 1, 2008): 366–70. http://dx.doi.org/10.1373/clinchem.2007.094417.
Повний текст джерелаHutchens, T. W., and J. O. Porath. "Protein recognition of immobilized ligands: promotion of selective adsorption." Clinical Chemistry 33, no. 9 (September 1, 1987): 1502–8. http://dx.doi.org/10.1093/clinchem/33.9.1502.
Повний текст джерелаMATSUI, Masakazu. "Ligand design for ion size recognition." Bunseki kagaku 45, no. 3 (1996): 209–23. http://dx.doi.org/10.2116/bunsekikagaku.45.209.
Повний текст джерелаSuehiro, Kazuhisa, Jeffrey W. Smith, and Edward F. Plow. "The Ligand Recognition Specificity of Integrins." Journal of Biological Chemistry 271, no. 17 (April 26, 1996): 10365–71. http://dx.doi.org/10.1074/jbc.271.17.10365.
Повний текст джерелаSuehiro, Kazuhisa, and Edward F. Plow. "Ligand Recognition by .BETA.3 Integrins." Keio Journal of Medicine 46, no. 3 (1997): 111–14. http://dx.doi.org/10.2302/kjm.46.111.
Повний текст джерелаMulhbacher, Jérôme, and Daniel A. Lafontaine. "Ligand recognition determinants of guanine riboswitches." Nucleic Acids Research 35, no. 16 (August 2007): 5568–80. http://dx.doi.org/10.1093/nar/gkm572.
Повний текст джерелаSpringer, Barry A., Stephen G. Sligar, John S. Olson, and George N. Jr Phillips. "Mechanisms of Ligand Recognition in Myoglobin." Chemical Reviews 94, no. 3 (May 1994): 699–714. http://dx.doi.org/10.1021/cr00027a007.
Повний текст джерелаStephanos, Joseph J., Scott A. Farina, and Anthony W. Addison. "Iron ligand recognition by monomeric hemoglobins." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1295, no. 2 (July 1996): 209–21. http://dx.doi.org/10.1016/0167-4838(96)00041-6.
Повний текст джерелаYuan, Xiaojing, and Yechun Xu. "Recent Trends and Applications of Molecular Modeling in GPCR–Ligand Recognition and Structure-Based Drug Design." International Journal of Molecular Sciences 19, no. 7 (July 20, 2018): 2105. http://dx.doi.org/10.3390/ijms19072105.
Повний текст джерелаKaur, Punit, Pradeep Sharma, Shavait Yamini, Divya Dube, Nisha Pandey, Mau Sinha, Sujata Sharma, and Tej P. Singh. "Molecular Basis of Ligand Recognition by Mammalian Peptidoglycan Recognition Protein." Biophysical Journal 104, no. 2 (January 2013): 547a. http://dx.doi.org/10.1016/j.bpj.2012.11.3034.
Повний текст джерелаCao, Ruyin, Alejandro Giorgetti, Andreas Bauer, Bernd Neumaier, Giulia Rossetti, and Paolo Carloni. "Role of Extracellular Loops and Membrane Lipids for Ligand Recognition in the Neuronal Adenosine Receptor Type 2A: An Enhanced Sampling Simulation Study." Molecules 23, no. 10 (October 12, 2018): 2616. http://dx.doi.org/10.3390/molecules23102616.
Повний текст джерелаTakagi, J. "Structural basis for ligand recognition by RGD (Arg-Gly-Asp)-dependent integrins." Biochemical Society Transactions 32, no. 3 (June 1, 2004): 403–6. http://dx.doi.org/10.1042/bst0320403.
Повний текст джерелаAndersen-Nissen, Erica, Kelly D. Smith, Richard Bonneau, Roland K. Strong, and Alan Aderem. "A conserved surface on Toll-like receptor 5 recognizes bacterial flagellin." Journal of Experimental Medicine 204, no. 2 (February 5, 2007): 393–403. http://dx.doi.org/10.1084/jem.20061400.
Повний текст джерелаLi, Chaoqun, Xiaojia Zhao, Xiaomin Zhu, Pengtao Xie, and Guangju Chen. "Structural Studies of the 3′,3′-cGAMP Riboswitch Induced by Cognate and Noncognate Ligands Using Molecular Dynamics Simulation." International Journal of Molecular Sciences 19, no. 11 (November 9, 2018): 3527. http://dx.doi.org/10.3390/ijms19113527.
Повний текст джерелаWu, Yiran, Liting Zeng, and Suwen Zhao. "Ligands of Adrenergic Receptors: A Structural Point of View." Biomolecules 11, no. 7 (June 24, 2021): 936. http://dx.doi.org/10.3390/biom11070936.
Повний текст джерелаMasson, Thibaut, Corinne Landras Guetta, Eugénie Laigre, Anne Cucchiarini, Patricia Duchambon, Marie-Paule Teulade-Fichou, and Daniela Verga. "BrdU immuno-tagged G-quadruplex ligands: a new ligand-guided immunofluorescence approach for tracking G-quadruplexes in cells." Nucleic Acids Research 49, no. 22 (December 7, 2021): 12644–60. http://dx.doi.org/10.1093/nar/gkab1166.
Повний текст джерелаTateing, Suriya, and Nuttee Suree. "Decoding molecular recognition of inhibitors targeting HDAC2 via molecular dynamics simulations and configurational entropy estimation." PLOS ONE 17, no. 8 (August 18, 2022): e0273265. http://dx.doi.org/10.1371/journal.pone.0273265.
Повний текст джерелаHOWL, John, and Mark WHEATLEY. "Molecular recognition of peptide and non-peptide ligands by the extracellular domains of neurohypophysial hormone receptors." Biochemical Journal 317, no. 2 (July 15, 1996): 577–82. http://dx.doi.org/10.1042/bj3170577.
Повний текст джерелаGuzelj, Samo, Tihomir Tomašič, and Žiga Jakopin. "Novel Scaffolds for Modulation of NOD2 Identified by Pharmacophore-Based Virtual Screening." Biomolecules 12, no. 8 (July 29, 2022): 1054. http://dx.doi.org/10.3390/biom12081054.
Повний текст джерелаByzova, Tatiana V., та Edward F. Plow. "Activation of αVβ3 on Vascular Cells Controls Recognition of Prothrombin". Journal of Cell Biology 143, № 7 (28 грудня 1998): 2081–92. http://dx.doi.org/10.1083/jcb.143.7.2081.
Повний текст джерелаRobertson, Michael J., Justin G. Meyerowitz, Ouliana Panova, Kenneth Borrelli, and Georgios Skiniotis. "Plasticity in ligand recognition at somatostatin receptors." Nature Structural & Molecular Biology 29, no. 3 (February 24, 2022): 210–17. http://dx.doi.org/10.1038/s41594-022-00727-5.
Повний текст джерелаIshiguro, M. "ligand Recognition and Structural Change of GPCR." Seibutsu Butsuri 41, supplement (2001): S20. http://dx.doi.org/10.2142/biophys.41.s20_3.
Повний текст джерелаCIERNIEWSKI, Czeslaw S., and Jolanta NIEWIAROWSKA. "Ligand Recognition by Cytoadhesins in Vascular Biology." Journal of Clinical Biochemistry and Nutrition 28, no. 3 (2000): 201–15. http://dx.doi.org/10.3164/jcbn.28.201.
Повний текст джерелаVerdino, P., C. Aldag, D. Hilvert, and I. A. Wilson. "Antibodies: specificity and promiscuity of ligand recognition." Acta Crystallographica Section A Foundations of Crystallography 62, a1 (August 6, 2006): s38. http://dx.doi.org/10.1107/s0108767306099247.
Повний текст джерелаSchmidt, Hayden R., Robin M. Betz, Ron O. Dror та Andrew C. Kruse. "Structural basis for σ1 receptor ligand recognition". Nature Structural & Molecular Biology 25, № 10 (жовтень 2018): 981–87. http://dx.doi.org/10.1038/s41594-018-0137-2.
Повний текст джерелаChoi, Mihwa, Keiko Yamamoto, Hiroyuki Masuno, Kinichi Nakashima, Tetsuya Taga, and Sachiko Yamada. "Ligand recognition by the vitamin D receptor." Bioorganic & Medicinal Chemistry 9, no. 7 (July 2001): 1721–30. http://dx.doi.org/10.1016/s0968-0896(01)00060-8.
Повний текст джерелаTakagi, Junichi. "Structural basis for ligand recognition by integrins." Current Opinion in Cell Biology 19, no. 5 (October 2007): 557–64. http://dx.doi.org/10.1016/j.ceb.2007.09.002.
Повний текст джерелаRiccardi, Laura, Luca Gabrielli, Xiaohuan Sun, Federico De Biasi, Federico Rastrelli, Fabrizio Mancin, and Marco De Vivo. "Nanoparticle-Based Receptors Mimic Protein-Ligand Recognition." Chem 3, no. 1 (July 2017): 92–109. http://dx.doi.org/10.1016/j.chempr.2017.05.016.
Повний текст джерелаKanlikilicer, Pinar, Nilay Budeyri, Berna Sariyar Akbulut, Amable Hortacsu, and Elif Ozkirimli. "Dynamic Analysis of Beta-lactamase Ligand Recognition." Biophysical Journal 96, no. 3 (February 2009): 443a. http://dx.doi.org/10.1016/j.bpj.2008.12.2274.
Повний текст джерелаDavis, Mark M., J. Jay Boniface, Ziv Reich, Daniel Lyons, Johannes Hampl, Bernhard Arden та Yueh-hsiu Chien. "LIGAND RECOGNITION BY αβ T CELL RECEPTORS". Annual Review of Immunology 16, № 1 (квітень 1998): 523–44. http://dx.doi.org/10.1146/annurev.immunol.16.1.523.
Повний текст джерелаSmith, Richard D., Liegi Hu, Jayson A. Falkner, Mark L. Benson, Jason P. Nerothin, and Heather A. Carlson. "Exploring protein–ligand recognition with Binding MOAD." Journal of Molecular Graphics and Modelling 24, no. 6 (May 2006): 414–25. http://dx.doi.org/10.1016/j.jmgm.2005.08.002.
Повний текст джерелаHeiring, Christoph, Björn Dahlbäck, and Yves A. Muller. "Ligand Recognition and Homophilic Interactions in Tyro3." Journal of Biological Chemistry 279, no. 8 (November 17, 2003): 6952–58. http://dx.doi.org/10.1074/jbc.m311750200.
Повний текст джерелаSun, Shuguang, and Kathryn Thomasson. "Molecular recognition of a tris(histidine) ligand." Chemical Communications, no. 4 (1998): 519–20. http://dx.doi.org/10.1039/a706711i.
Повний текст джерелаBrodsky, Igor, and Ruslan Medzhitov. "Two Modes of Ligand Recognition by TLRs." Cell 130, no. 6 (September 2007): 979–81. http://dx.doi.org/10.1016/j.cell.2007.09.009.
Повний текст джерелаKéry, Vladimír, Jiři J. F. Křepinský, Christopher D. Warren, Peter Capek, and Philip D. Stahl. "Ligand recognition by purified human mannose receptor." Archives of Biochemistry and Biophysics 298, no. 1 (October 1992): 49–55. http://dx.doi.org/10.1016/0003-9861(92)90092-b.
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