Статті в журналах з теми "Ligand binding interactions"
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Marsh, Lorraine. "Strong Ligand-Protein Interactions Derived from Diffuse Ligand Interactions with Loose Binding Sites." BioMed Research International 2015 (2015): 1–6. http://dx.doi.org/10.1155/2015/746980.
Повний текст джерелаLeigh, David A. "Summing Up Ligand Binding Interactions." Chemistry & Biology 10, no. 12 (December 2003): 1143–44. http://dx.doi.org/10.1016/j.chembiol.2003.12.006.
Повний текст джерелаKaiser, Anette, and Irene Coin. "Capturing Peptide–GPCR Interactions and Their Dynamics." Molecules 25, no. 20 (October 15, 2020): 4724. http://dx.doi.org/10.3390/molecules25204724.
Повний текст джерелаLangelaan, David N., and Jan K. Rainey. "Membrane catalysis of peptide–receptor bindingThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 88, no. 2 (April 2010): 203–10. http://dx.doi.org/10.1139/o09-129.
Повний текст джерелаTozer, Eileen Collins, Paul E. Hughes, and Joseph C. Loftus. "Ligand binding and affinity modulation of integrins." Biochemistry and Cell Biology 74, no. 6 (December 1, 1996): 785–98. http://dx.doi.org/10.1139/o96-085.
Повний текст джерелаSharma, Ankur, Annapoorni Rangarajan, and Rajan R. Dighe. "Antibodies against the extracellular domain of human Notch1 receptor reveal the critical role of epidermal-growth-factor-like repeats 25–26in ligand binding and receptor activation." Biochemical Journal 449, no. 2 (December 14, 2012): 519–30. http://dx.doi.org/10.1042/bj20121153.
Повний текст джерелаUrien, S., P. Nguyen, S. Berlioz, F. Brée, F. Vacherot, and J. P. Tillement. "Characterization of discrete classes of binding sites of human serum albumin by application of thermodynamic principles." Biochemical Journal 302, no. 1 (August 15, 1994): 69–72. http://dx.doi.org/10.1042/bj3020069.
Повний текст джерелаKatzenellenbogen, J. A., and R. Muthyala. "Interactions of exogenous endocrine active substances with nuclear receptors." Pure and Applied Chemistry 75, no. 11-12 (January 1, 2003): 1797–817. http://dx.doi.org/10.1351/pac200375111797.
Повний текст джерелаMicovic, Vuk, Milovan Ivanovic та Ljiljana Dosen-Micovic. "Structural requirements for ligands of the δ-opioid receptor". Journal of the Serbian Chemical Society 74, № 11 (2009): 1207–17. http://dx.doi.org/10.2298/jsc0911207m.
Повний текст джерелаMoldogazieva, Nurbubu T., Daria S. Ostroverkhova, Nikolai N. Kuzmich, Vladimir V. Kadochnikov, Alexander A. Terentiev та Yuri B. Porozov. "Elucidating Binding Sites and Affinities of ERα Agonists and Antagonists to Human Alpha-Fetoprotein by In Silico Modeling and Point Mutagenesis". International Journal of Molecular Sciences 21, № 3 (30 січня 2020): 893. http://dx.doi.org/10.3390/ijms21030893.
Повний текст джерелаGonzález, Javier M., and S. Zoë Fisher. "Structural analysis of ibuprofen binding to human adipocyte fatty-acid binding protein (FABP4)." Acta Crystallographica Section F Structural Biology Communications 71, no. 2 (January 28, 2015): 163–70. http://dx.doi.org/10.1107/s2053230x14027897.
Повний текст джерелаCrabb, John W., Zuquin Nie, Yang Chen, Jeffrey D. Hulmes, Karen A. West, James T. Kapron, Sarah E. Ruuska, Noa Noy, and John C. Saari. "Cellular Retinaldehyde-binding Protein Ligand Interactions." Journal of Biological Chemistry 273, no. 33 (August 14, 1998): 20712–20. http://dx.doi.org/10.1074/jbc.273.33.20712.
Повний текст джерелаBode, Wolfram, and Robert Huber. "Ligand binding: proteinase-protein inhibitor interactions." Current Opinion in Structural Biology 1, no. 1 (February 1991): 45–52. http://dx.doi.org/10.1016/0959-440x(91)90010-q.
Повний текст джерелаSukalovic, Vladimir, Vukic Soskic, Deana Andric, Goran Roglic, and Sladjana Kostic-Rajacic. "Modeling key interactions between dopamine D2 receptor second extracellular loop and arylpiperazine ligands." Journal of the Serbian Chemical Society 77, no. 3 (2012): 259–77. http://dx.doi.org/10.2298/jsc111028212s.
Повний текст джерелаFolkertsma, Simon, Paula I. van Noort, Arnold de Heer, Peter Carati, Ralph Brandt, Arie Visser, Gerrit Vriend та Jacob de Vlieg. "The Use of in Vitro Peptide Binding Profiles and in Silico Ligand-Receptor Interaction Profiles to Describe Ligand-Induced Conformations of the Retinoid X Receptor α Ligand-Binding Domain". Molecular Endocrinology 21, № 1 (1 січня 2007): 30–48. http://dx.doi.org/10.1210/me.2006-0072.
Повний текст джерелаUrien, S., F. Brée, B. Testa та J. P. Tillement. "pH-dependency of basic ligand binding to α1-acid glycoprotein (orosomucoid)". Biochemical Journal 280, № 1 (15 листопада 1991): 277–80. http://dx.doi.org/10.1042/bj2800277.
Повний текст джерелаMondoro, TH, CD Wall, MM White, and LK Jennings. "Selective induction of a glycoprotein IIIa ligand-induced binding site by fibrinogen and von Willebrand factor." Blood 88, no. 10 (November 15, 1996): 3824–30. http://dx.doi.org/10.1182/blood.v88.10.3824.bloodjournal88103824.
Повний текст джерелаPolakovičová, M., та R. Čižmáriková. "Molecular Docking Study on the Binding Mode of Cardioselective Phenoxyaminopropanol Blocker into β-adrenergic Receptor Subtypes". Acta Facultatis Pharmaceuticae Universitatis Comenianae 59, № 2 (28 грудня 2012): 44–53. http://dx.doi.org/10.2478/v10219-012-0024-6.
Повний текст джерелаKobren, Shilpa Nadimpalli, and Mona Singh. "Systematic domain-based aggregation of protein structures highlights DNA-, RNA- and other ligand-binding positions." Nucleic Acids Research 47, no. 2 (December 7, 2018): 582–93. http://dx.doi.org/10.1093/nar/gky1224.
Повний текст джерелаLinne, Christine, Daniele Visco, Stefano Angioletti-Uberti, Liedewij Laan, and Daniela J. Kraft. "Direct visualization of superselective colloid-surface binding mediated by multivalent interactions." Proceedings of the National Academy of Sciences 118, no. 36 (August 31, 2021): e2106036118. http://dx.doi.org/10.1073/pnas.2106036118.
Повний текст джерелаZlatovic, Mario, Vladimir Sukalovic, Goran Roglic, Sladjana Kostic-Rajacic, and Deana Andric. "The influence of dispersive interactions on the binding affinities of ligands with an arylpiperazine moiety to the dopamine D2 receptor." Journal of the Serbian Chemical Society 74, no. 10 (2009): 1051–61. http://dx.doi.org/10.2298/jsc0910051z.
Повний текст джерелаSingh, Omkar, Kunal Sawariya, and Polamarasetty Aparoy. "Graphlet signature-based scoring method to estimate protein–ligand binding affinity." Royal Society Open Science 1, no. 4 (December 2014): 140306. http://dx.doi.org/10.1098/rsos.140306.
Повний текст джерелаColvin, Richard A., Gabriele S. V. Campanella, Lindsay A. Manice, and Andrew D. Luster. "CXCR3 Requires Tyrosine Sulfation for Ligand Binding and a Second Extracellular Loop Arginine Residue for Ligand-Induced Chemotaxis." Molecular and Cellular Biology 26, no. 15 (August 1, 2006): 5838–49. http://dx.doi.org/10.1128/mcb.00556-06.
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 джерелаFu, Yi, Ji Zhao, and Zhiguo Chen. "Insights into the Molecular Mechanisms of Protein-Ligand Interactions by Molecular Docking and Molecular Dynamics Simulation: A Case of Oligopeptide Binding Protein." Computational and Mathematical Methods in Medicine 2018 (December 4, 2018): 1–12. http://dx.doi.org/10.1155/2018/3502514.
Повний текст джерелаHussain, Rohanah, Edoardo Longo, and Giuliano Siligardi. "UV-Denaturation Assay to Assess Protein Photostability and Ligand-Binding Interactions Using the High Photon Flux of Diamond B23 Beamline for SRCD." Molecules 23, no. 8 (July 31, 2018): 1906. http://dx.doi.org/10.3390/molecules23081906.
Повний текст джерелаJóźwiak, Krzysztof, and Anita Płazińska. "Structural Insights into Ligand—Receptor Interactions Involved in Biased Agonism of G-Protein Coupled Receptors." Molecules 26, no. 4 (February 6, 2021): 851. http://dx.doi.org/10.3390/molecules26040851.
Повний текст джерелаLecut, Christelle, Véronique Arocas, Hans Ulrichts, Anthony Elbaz, Jean-Luc Villeval, Jean-Jacques Lacapère, Hans Deckmyn, and Martine Jandrot-Perrus. "Identification of Residues within Human Glycoprotein VI Involved in the Binding to Collagen." Journal of Biological Chemistry 279, no. 50 (October 4, 2004): 52293–99. http://dx.doi.org/10.1074/jbc.m406342200.
Повний текст джерелаWang, Caihua, Juan Liu, Fei Luo, Zixing Deng, and Qian-Nan Hu. "Predicting target-ligand interactions using protein ligand-binding site and ligand substructures." BMC Systems Biology 9, Suppl 1 (2015): S2. http://dx.doi.org/10.1186/1752-0509-9-s1-s2.
Повний текст джерелаGettins, Peter G. W., and Klavs Dolmer. "A proximal pair of positive charges provides the dominant ligand-binding contribution to complement-like domains from the LRP (low-density lipoprotein receptor-related protein)." Biochemical Journal 443, no. 1 (March 14, 2012): 65–73. http://dx.doi.org/10.1042/bj20111867.
Повний текст джерелаGaboriaud, Christine, Lynn Gregory-Pauron, Florence Teillet, Nicole M. Thielens, Isabelle Bally, and Gérard J. Arlaud. "Structure and properties of the Ca2+-binding CUB domain, a widespread ligand-recognition unit involved in major biological functions." Biochemical Journal 439, no. 2 (September 28, 2011): 185–93. http://dx.doi.org/10.1042/bj20111027.
Повний текст джерелаIssa, Naiem T., Stephen W. Byers, and Sivanesan Dakshanamurthy. "ES-Screen: A Novel Electrostatics-Driven Method for Drug Discovery Virtual Screening." International Journal of Molecular Sciences 23, no. 23 (November 27, 2022): 14830. http://dx.doi.org/10.3390/ijms232314830.
Повний текст джерелаKumar, Prashant, and Paulina Maria Dominiak. "Combining Molecular Dynamic Information and an Aspherical-Atom Data Bank in the Evaluation of the Electrostatic Interaction Energy in Multimeric Protein-Ligand Complex: A Case Study for HIV-1 Protease." Molecules 26, no. 13 (June 24, 2021): 3872. http://dx.doi.org/10.3390/molecules26133872.
Повний текст джерелаValenzano, Kenneth J., Wendy Miller, Jared N. Kravitz, Philippe Samama, Dan Fitzpatrick, and Kevin Seeley. "Development of a Fluorescent Ligand-Binding Assay Using the AcroWell Filter Plate." Journal of Biomolecular Screening 5, no. 6 (December 2000): 455–61. http://dx.doi.org/10.1177/108705710000500608.
Повний текст джерелаJahmidi-Azizi, Nisrine, Stewart Gault, Charles S. Cockell, Rosario Oliva, and Roland Winter. "Ions in the Deep Subsurface of Earth, Mars, and Icy Moons: Their Effects in Combination with Temperature and Pressure on tRNA–Ligand Binding." International Journal of Molecular Sciences 22, no. 19 (October 8, 2021): 10861. http://dx.doi.org/10.3390/ijms221910861.
Повний текст джерелаAdasme, Melissa F., Katja L. Linnemann, Sarah Naomi Bolz, Florian Kaiser, Sebastian Salentin, V. Joachim Haupt, and Michael Schroeder. "PLIP 2021: expanding the scope of the protein–ligand interaction profiler to DNA and RNA." Nucleic Acids Research 49, W1 (May 5, 2021): W530—W534. http://dx.doi.org/10.1093/nar/gkab294.
Повний текст джерелаValley, Christopher, and Jonathan Sachs. "Stabilizing Interactions In TNF Ligand-receptor Binding." Biophysical Journal 96, no. 3 (February 2009): 446a. http://dx.doi.org/10.1016/j.bpj.2008.12.2292.
Повний текст джерелаBoz, Esra, and Matthias Stein. "Accurate Receptor-Ligand Binding Free Energies from Fast QM Conformational Chemical Space Sampling." International Journal of Molecular Sciences 22, no. 6 (March 17, 2021): 3078. http://dx.doi.org/10.3390/ijms22063078.
Повний текст джерелаJohansson, Lotta, Ann Båvner, Jane S. Thomsen, MatHias Färnegårdh, Jan-Åke Gustafsson, and Eckardt Treuter. "The Orphan Nuclear Receptor SHP Utilizes Conserved LXXLL-Related Motifs for Interactions with Ligand-Activated Estrogen Receptors." Molecular and Cellular Biology 20, no. 4 (February 15, 2000): 1124–33. http://dx.doi.org/10.1128/mcb.20.4.1124-1133.2000.
Повний текст джерелаMailfait, S., E. Thoreau, D. Belaiche, and P. Formstecher And B Sablonnie. "Critical role of the H6-H7 loop in the conformational adaptation of all-trans retinoic acid and synthetic retinoids within the ligand-binding site of RARalpha." Journal of Molecular Endocrinology 24, no. 3 (June 1, 2000): 353–64. http://dx.doi.org/10.1677/jme.0.0240353.
Повний текст джерелаBueschbell, Beatriz, Carlos Barreto, António Preto, Anke Schiedel, and Irina Moreira. "A Complete Assessment of Dopamine Receptor- Ligand Interactions through Computational Methods." Molecules 24, no. 7 (March 27, 2019): 1196. http://dx.doi.org/10.3390/molecules24071196.
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 джерелаCopoiu, Liviu, Pedro H. M. Torres, David B. Ascher, Tom L. Blundell, and Sony Malhotra. "ProCarbDB: a database of carbohydrate-binding proteins." Nucleic Acids Research 48, no. D1 (October 10, 2019): D368—D375. http://dx.doi.org/10.1093/nar/gkz860.
Повний текст джерелаBeshnova, Daria A., Joana Pereira, and Victor S. Lamzin. "Estimation of the protein–ligand interaction energy for model building and validation." Acta Crystallographica Section D Structural Biology 73, no. 3 (March 1, 2017): 195–202. http://dx.doi.org/10.1107/s2059798317003400.
Повний текст джерелаTu, L., A. Chen, M. D. Delahunty, K. L. Moore, S. R. Watson, R. P. McEver, and T. F. Tedder. "L-selectin binds to P-selectin glycoprotein ligand-1 on leukocytes: interactions between the lectin, epidermal growth factor, and consensus repeat domains of the selectins determine ligand binding specificity." Journal of Immunology 157, no. 9 (November 1, 1996): 3995–4004. http://dx.doi.org/10.4049/jimmunol.157.9.3995.
Повний текст джерелаChao, Hui, and Liang-Nian Ji. "DNA Interactions with Ruthenium(II) Polypyridine Complexes Containing Asymmetric Ligands." Bioinorganic Chemistry and Applications 3, no. 1-2 (2005): 15–28. http://dx.doi.org/10.1155/bca.2005.15.
Повний текст джерелаSzulc, Natalia A., Zuzanna Mackiewicz, Janusz M. Bujnicki, and Filip Stefaniak. "fingeRNAt—A novel tool for high-throughput analysis of nucleic acid-ligand interactions." PLOS Computational Biology 18, no. 6 (June 2, 2022): e1009783. http://dx.doi.org/10.1371/journal.pcbi.1009783.
Повний текст джерелаZheng, Fang, and Chang-Guo Zhan. "Computational Modeling of Solvent Effects on Protein-Ligand Interactions Using Fully Polarizable Continuum Model and Rational Drug Design." Communications in Computational Physics 13, no. 1 (January 2013): 31–60. http://dx.doi.org/10.4208/cicp.130911.121011s.
Повний текст джерелаvan Royen, Martin E., Sónia M. Cunha, Maartje C. Brink, Karin A. Mattern, Alex L. Nigg, Hendrikus J. Dubbink, Pernette J. Verschure, Jan Trapman, and Adriaan B. Houtsmuller. "Compartmentalization of androgen receptor protein–protein interactions in living cells." Journal of Cell Biology 177, no. 1 (April 9, 2007): 63–72. http://dx.doi.org/10.1083/jcb.200609178.
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