The DOI matches its Crossref record; 69 of the 69 references it cites were found in a registry or an index.
Induced fit, conformational selection and independent dynamic segments: an extended view of binding events
Open accessAbstract
Single molecule and NMR measurements of protein dynamics increasingly uncover the complexity of binding scenarios. Here, we describe an extended conformational selection model that embraces a repertoire of selection and adjustment processes. Induced fit can be viewed as a subset of this repertoire, whose contribution is affected by the bond types stabilizing the interaction and the differences between the interacting partners. We argue that protein segments whose dynamics are distinct from the rest of the protein ('discrete breathers') can govern conformational transitions and allosteric propagation that accompany binding processes and, as such, might be more sensitive to mutational events. Additionally, we highlight the dynamic complexity of binding scenarios as they relate to events such as aggregation and signalling, and the crowded cellular environment.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In a long-standing debate between the proponents of the “induced-fit” and the “conformational selection” binding mechanisms [21–23], the evidence pointing to the latter allows one to precompute the conformational ensemble of the interacting molecule(s) and dock the separate conformers with limited conformational search [24,25].”
From Challenges in protein docking (2020) · cites this paper as [22]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Even if we take P (A p ) equal to 1, and thus assume there are no problematic obstacles involved in generating the building blocks; and also eliminate the localization probability by collapsing chance to necessity (selforganization), P(A c ) can still pose huge obstacles to the chance configuration of the quaternary structure of operative biological systems (Csermely et al., 2010).”
From Using statistical methods to model the fine-tuning of molecular machines and systems (2020) · cites this paper as Csermely et al., 2010
Experimental — accuracy not yet measuredIn the citing paper
“The propagation of conformational change at certain locations228–230 can lead to large amplitude fluctuations of the linked domains.231”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [228]
In the citing paper
“In an induced fit scenario, the ligands bind to the single “open” protein structure and the interaction between a protein and a rigid binding partner induces a conformational change in the protein.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [184]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.
Monod, J., Wyman, J., & Changeux, J. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80285-6 · Cited by 7,681
The Energy Landscapes and Motions of Proteins
Frauenfelder, H., Sligar, S. G., & Wolynes, P. G. (1991) · Science · doi:10.1126/science.1749933 · Cited by 3,250
Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits *
Koshland, D. E., Némethy, G., & Filmer, D. (1966) · Biochemistry · doi:10.1021/bi00865a047 · Cited by 3,019
Macromolecular crowding: obvious but underappreciated
Ellis, R. J. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01938-7 · Cited by 2,309
Zhou, H., Rivas, G., & Minton, A. P. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125817 · Cited by 2,160
Application of a Theory of Enzyme Specificity to Protein Synthesis.
Koshland, D. (1958) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.44.2.98 · Cited by 2,140
Intrinsically unstructured proteins
Tompa, P. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02169-2 · Cited by 2,056
The role of dynamic conformational ensembles in biomolecular recognition
Boehr, D. D., Nussinov, R., & Wright, P. E. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.232 · Cited by 2,008
Self-citationEinfluss der Configuration auf die Wirkung der Enzyme
Fischer, E. (1894) · Berichte der deutschen chemischen Gesellschaft · doi:10.1002/cber.18940270364 · Cited by 1,841
Understanding protein non-folding
Uversky, V. N., & Dunker, A. K. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.01.017 · Cited by 1,221
Research works printed but not linked: 2
- Straub, F. B. and Szabolcsi, G. (1964) O dinamicseszkij aszpektah sztukturü fermentov. (On the dynamic aspects of protein structure) In: Molecular Biology, Problems and Perspectives (Braunstein, A. E., ed.), pp. 182–187 (in Russian), Izdat. Nauka
- Závodszky, 1966, Structure of glyceraldehyde-3-phosphate dehydrogenase and its alteration by coenzyme binding, Acta Biochim. Biophys. Acad. Sci. Hung., 1, 389
Cited by
Sorted by citations
Items 301–400 of 822
A structural appraisal of sterol carrier protein 2
Burgardt, N. I., Gianotti, A. R., Ferreyra, R. G., & Ermácora, M. R. (2017) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2017.03.002 · Cited by 30
Saavedra, J. M., Azócar, M. A., Rodríguez, V., Ramírez‐Sarmiento, C. A., Andrews, B. A., Asenjo, J. A., & Parra, L. P. (2018) · Biotechnology Journal · doi:10.1002/biot.201700669 · Cited by 30
Yu, Q., Ye, W., Wang, W., & Chen, H. (2013) · PLoS ONE · doi:10.1371/annotation/2212a861-273a-4c34-816a-ead5d0d8a7f5 · Cited by 30
Freitas, F. C., Ferreira, P. H. B., Favaro, D. C., & de Oliveira, R. J. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01320 · Cited by 29
Wijker, S., & Palmans, A. R. A. (2023) · ChemPlusChem · doi:10.1002/cplu.202300260 · Cited by 28
Molecular dynamics simulation of the induced‐fit binding process of DNA aptamer and L ‐argininamide
Lin, P., Tsai, C., Wu, J. W., Ruaan, R., & Chen, W. (2012) · Biotechnology Journal · doi:10.1002/biot.201200003 · Cited by 29
Ainsley, J., Mulholland, A. J., Black, G. W., Sparagano, O. A. E., Christov, C. Z., & Karabencheva‐Christova, T. G. (2018) · ACS Omega · doi:10.1021/acsomega.8b00385 · Cited by 29
Enhanced molecular dynamics sampling of drug target conformations
Rodriguez-Bussey, I., Doshi, U., & Hamelberg, D. (2015) · Biopolymers · doi:10.1002/bip.22740 · Cited by 28
Liu, X., Chen, J., & Chen, J. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.12.001 · Cited by 28
Computational Investigation of the Mechanism of Diels–Alderase PyrI4
Zou, Y., Yang, S., Sanders, J. N., Li, W., Yu, P., Wang, H., Tang, Z., Liu, W., & Houk, K. N. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c10813 · Cited by 28
High‐Affinity Disaccharide Binding by Tricyclic Synthetic Lectins
Sookcharoenpinyo, B., Klein, E., Ferrand, Y., Walker, D. B., Brotherhood, P. R., Ke, C., Crump, M. P., & Davis, A. P. (2012) · Angewandte Chemie · doi:10.1002/ange.201200447 · Cited by 28
Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology
Evans, R., Ramisetty, S. K., Kulkarni, P., & Weninger, K. (2023) · Biomolecules · doi:10.3390/biom13010124 · Cited by 27
The Action of Cytochromeb5on CYP2E1 and CYP2C19 Activities Requires Anionic Residues D58 and D65
Peng, H., & Auchus, R. J. (2012) · Biochemistry · doi:10.1021/bi301384n · Cited by 28
Mechanistic insights into thrombin's switch between “slow” and “fast” forms
Xiao, J., Melvin, R. L., & Salsbury, F. R. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp03671j · Cited by 28
Bohnuud, T., Kozakov, D., & Vajda, S. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003872 · Cited by 27
Molecular dynamics simulations for the structure-based drug design: targeting small-GTPases proteins
Parise, A., Cresca, S., & Magistrato, A. (2024) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2024.2387856 · Cited by 27
High-speed AFM reveals accelerated binding of agitoxin-2 to a K + channel by induced fit
Sumino, A., Sumikama, T., Uchihashi, T., & Oiki, S. (2019) · Science Advances · doi:10.1126/sciadv.aax0495 · Cited by 27
Minimal ensembles of side chain conformers for modeling protein–protein interactions
Beglov, D., Hall, D. R., Brenke, R., Shapovalov, M. V., Dunbrack, R. L., Kozakov, D., & Vajda, S. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.23222 · Cited by 28
Ortiz, J. F., MacDonald, M. L., Masterson, P., Uversky, V. N., & Siltberg-Liberles, J. (2013) · Genome Biology and Evolution · doi:10.1093/gbe/evt026 · Cited by 27
The Too Many Faces of PD-L1: A Comprehensive Conformational Analysis Study
Ahmed, M., & Barakat, K. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00655 · Cited by 27
Sen, S., & Udgaonkar, J. B. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009742 · Cited by 27
Redhair, M., & Atkins, W. M. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.109064 · Cited by 26
Liu, Z., Casey, T. M., Blackburn, M. E., Huang, X., Pham, L., de Vera, I. M. S., Carter, J. D., Kear‐Scott, J. L., Veloro, A. M., Galiano, L., et al. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp04556h · Cited by 26
Dynamic New World: Refining Our View of Protein Structure, Function and Evolution
Mannige, R. V. (2014) · Proteomes · doi:10.3390/proteomes2010128 · Cited by 26
Single-Molecule Observation of the Induction of k-Turn RNA Structure on Binding L7Ae Protein
Wang, J., Fessl, T., Schroeder, K. T., Ouellet, J., Liu, Y., Freeman, A. D. J., & Lilley, D. M. J. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.006 · Cited by 27
Joseph, P. R. B., Sawant, K. V., Isley, A., Pedroza, M., Garofalo, R., Richardson, R. M., & Rajarathnam, K. (2013) · Biochemical Journal · doi:10.1042/bj20130148 · Cited by 27
Significant Enhancement of Docking Sensitivity Using Implicit Ligand Sampling
Xu, M., & Lill, M. A. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci100457t · Cited by 25
Szalay, K. Z., & Csermely, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078059 · Cited by 26
Self-citationWeikl, T. R., & Boehr, D. D. (2012) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24123 · Cited by 26
Roche, C., Sour, A., & Sauvage, J. (2012) · Chemistry - A European Journal · doi:10.1002/chem.201200389 · Cited by 26
Dean, S. F., Whalen, K. L., & Spies, M. A. (2015) · ACS Central Science · doi:10.1021/acscentsci.5b00211 · Cited by 26
Specificity and stability of transient protein–protein interactions
Vishwanath, S., Sukhwal, A., Sowdhamini, R., & Srinivasan, N. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.12.010 · Cited by 27
Role of Ordered Proteins in the Folding-Upon-Binding of Intrinsically Disordered Proteins
Lawrence, C. W., Kumar, S., Noid, W. G., & Showalter, S. A. (2014) · The Journal of Physical Chemistry Letters · doi:10.1021/jz402729x · Cited by 25
Nguyen, N. A., Vidya, F. N. U., Yennawar, N. H., Wu, H., McShan, A. C., & Agarwal, V. (2024) · Nature Communications · doi:10.1038/s41467-024-45593-5 · Cited by 25
Jensen, K. S., Winther, J. R., & Teilum, K. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1096539 · Cited by 25
The physical basis and practical consequences of biological promiscuity
Copley, S. D. (2020) · Physical Biology · doi:10.1088/1478-3975/ab8697 · Cited by 27
Development and Structure Analysis of Crystal Forms of Apabetalone: Solvates and Polymorphs
Liu, Y., Zhang, X., Zhou, L., Du, S., Wu, S., & Gong, J. (2021) · Crystal Growth & Design · doi:10.1021/acs.cgd.1c00187 · Cited by 25
Zeng, J., Weng, J., Zhang, Y., Xia, F., Cui, Q., & Xu, X. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c04679 · Cited by 24
Magnesium Activates Microsecond Dynamics to Regulate Integrin-Collagen Recognition
Nunes, A. M., Minetti, C. A. S. A., Remeta, D. P., & Baum, J. (2018) · Structure · doi:10.1016/j.str.2018.05.010 · Cited by 25
Kumar, A., Melis, P. M., Genna, V., Cocco, E. E., Marrosu, M. G., & Pieroni, E. (2014) · Molecular BioSystems · doi:10.1039/c4mb00203b · Cited by 24
Moroy, G., Spérandio, O., Rielland, S., Khemka, S., Druart, K., Goyal, D., Pérahia, D., & Miteva, M. A. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.150 · Cited by 25
Conformational selection of allergen-antibody complexes—surface plasticity of paratopes and epitopes
Fernández‐Quintero, M. L., Loeffler, J. R., Waibl, F., Kamenik, A. S., Hofer, F., & Liedl, K. R. (2019) · Protein Engineering Design and Selection · doi:10.1093/protein/gzaa014 · Cited by 25
Pavan, M., Menin, S., Bassani, D., Sturlese, M., & Moro, S. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.909499 · Cited by 25
Conformational dynamics of supramolecular protein assemblies
Kim, D., Nguyen, C.-T., & Bathe, M. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.09.015 · Cited by 24
Matena, A., Sinnen, C., van den Boom, J., Wilms, C., Dybowski, J. N., Maltaner, R., Mueller, J. W., Link, N. M., Hoffmann, D. E., & Bayer, P. (2013) · Structure · doi:10.1016/j.str.2013.07.016 · Cited by 25
Kurkcuoglu, Z., & Doruker, P. (2016) · PLoS ONE · doi:10.1371/journal.pone.0158063 · Cited by 24
Binding mechanism and dynamic conformational change of C subunit of PKA with different pathways
Chu, W., Chu, X., & Wang, J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702599114 · Cited by 24
Influence of electric field on the amyloid-β(29-42) peptides embedded in a membrane bilayer
Lü, Y., Shi, X.-F., Salsbury, F. R., & Derreumaux, P. (2018) · The Journal of Chemical Physics · doi:10.1063/1.5018459 · Cited by 24
Qin, H., Lim, L., & Song, J. (2012) · BMC Biophysics · doi:10.1186/2046-1682-5-2 · Cited by 23
Zhang, L., Wu, S., Feng, Y., Wang, D., Jia, X., Liu, Z., Liu, J., & Wang, W. (2020) · Communications Biology · doi:10.1038/s42003-020-01149-z · Cited by 21
The native state conformational heterogeneity in the energy landscape of protein folding
Mishra, P., & Jha, S. K. (2022) · Biophysical Chemistry · doi:10.1016/j.bpc.2022.106761 · Cited by 22
Prion assemblies: structural heterogeneity, mechanisms of formation, and role in species barrier
Igel‐Egalon, A., Fornara, B., Rézaei, H., & Béringue, V. (2022) · Cell and Tissue Research · doi:10.1007/s00441-022-03700-2 · Cited by 24
Computational design of dynamic receptor—peptide signaling complexes applied to chemotaxis
Jefferson, R. E., Oggier, A., Füglistaler, A., Camviel, N., Hijazi, M., Villarreal, A. R., Arber, C., & Barth, P. (2023) · Nature Communications · doi:10.1038/s41467-023-38491-9 · Cited by 23
Do antibody CDR loops change conformation upon binding?
Liu, C. T., Denzler, L., Hood, O. E. C., & Martin, A. C. R. (2024) · mAbs · doi:10.1080/19420862.2024.2322533 · Cited by 23
Simko, G. I., & Csermely, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067159 · Cited by 23
Self-citationAssembly of the Five-Way Junction in the Ribosomal Small Subunit Using Hybrid MD-Go Simulations
Chen, K., Eargle, J., Lai, J., Kim, H., Abeysirigunawardena, S. C., Mayerle, M., Woodson, S. A., Ha, T., & Luthey-Schulten, Z. A. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp212614b · Cited by 23
Light on the structural communication in Ras GTPases
Raimondi, F., Felline, A., Portella, G., Orozco, M., & Fanelli, F. (2012) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2012.698379 · Cited by 23
Lawrence, C. W., Bonny, A. R., & Showalter, S. A. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.05.160 · Cited by 23
Zhu, L., Jiang, H., Sheong, F. K., Cui, X., Gao, X., Wang, Y., & Huang, X. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b12426 · Cited by 23
Exploring Binding Mechanisms in Nuclear Hormone Receptors by Monte Carlo and X-ray-derived Motions.
Grebner, C., Lecina, D., Gil, V., Ulander, J., Hansson, P., Dellsén, A., Tyrchan, C., Edman, K., Hogner, A., & Guallar, V. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.02.004 · Cited by 23
Cheng, X., & Jiang, H. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8719-7_1 · Cited by 23
Csermely, P., Nussinov, R., & Szilágyi, A. (2013) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026611313010002 · Cited by 23
Self-citationAllostery in pharmacology: Thermodynamics, evolution and design
Maksay, G. (2011) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2011.01.001 · Cited by 22
Lin, Y., Silvestre-Ryan, J., Himmel, M. E., Crowley, M. F., Beckham, G. T., & Chu, J. (2011) · Journal of the American Chemical Society · doi:10.1021/ja206692g · Cited by 22
Computational studies of LXR molecular interactions reveal an allosteric communication pathway
Burendahl, S., & Nilsson, L. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.23209 · Cited by 22
Transitions of CDR-L3 Loop Canonical Cluster Conformations on the Micro-to-Millisecond Timescale
Fernández‐Quintero, M. L., Math, B. A., Loeffler, J. R., & Liedl, K. R. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02652 · Cited by 22
Ezerski, J. C., Zhang, P., Jennings, N., Waxham, M. N., & Cheung, M. S. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.02.015 · Cited by 22
Dokainish, H. M., & Sugita, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010270 · Cited by 22
Organic Stereochemistry. Part 5
Testa, B., Vistoli, G., Pedretti, A., & Caldwell, J. (2013) · Helvetica Chimica Acta · doi:10.1002/hlca.201200473 · Cited by 22
Malloci, G., Serra, G., Bosin, A., & Vargiu, A. V. (2016) · Computation · doi:10.3390/computation4010005 · Cited by 22
Biswas, T., Pawale, V. S., Choudhury, D., & Roy, R. P. (2014) · Biochemistry · doi:10.1021/bi4016023 · Cited by 22
Song, C., Gu, J., Ren, H., Li, Z., Xie, D., Han, L., Qiao, J., Cheng, Z., Nie, Y., & Zhou, Z. (2025) · Biotechnology Advances · doi:10.1016/j.biotechadv.2025.108716 · Cited by 21
Huang, Y., & Liu, Z. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12021410 · Cited by 21
First Evidence of Polymorphism in Furosemide Solvates
Sonina, A. A., Minkov, V. S., Rychkov, D. A., Rybalova, T. V., & Boldyreva, E. V. (2017) · Crystal Growth & Design · doi:10.1021/acs.cgd.6b01191 · Cited by 21
Modeling Binding with Large Conformational Changes: Key Points in Ensemble-Docking Approaches
Motta, S., & Bonati, L. (2017) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.7b00125 · Cited by 21
Nunes, A. D. S., Campos, V. P., Mascarello, A., Stumpf, T. R., Chiaradia-Delatorre, L. D., Machado, A. R. T., Júnior, H. M. S., Yunes, R. A., Nunes, R. J., & de Oliveira, D. F. (2013) · Experimental Parasitology · doi:10.1016/j.exppara.2013.10.003 · Cited by 21
Revealing the Properties of Plant Defensins through Dynamics
Valente, A. P., Paula, V. S. D., & Almeida, F. C. L. (2013) · Molecules · doi:10.3390/molecules180911311 · Cited by 22
Veglia, G., & Cembran, A. (2013) · FEBS Journal · doi:10.1111/febs.12462 · Cited by 21
Disulfide driven folding for a conditionally disordered protein
Fraga, H., Pujols, J., Gil-García, M., Roque, A., Bernardo‐Seisdedos, G., Santambrogio, C., Bech‐Serra, J. J., Canals, F., Bernadó, P., Grandori, R., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-17259-4 · Cited by 21
Chen, X., Yao, H., Wang, H., Mao, Y., Liu, D., & Long, D. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201812902 · Cited by 21
Kinetic Selection and Relaxation of the Intrinsically Disordered Region of a Protein upon Binding
Tran, D. P., & Kitao, A. (2020) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.9b01203 · Cited by 21
Liu, G., Fang, Y. G., & Wu, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.453803 · Cited by 21
Silvestre-Ryan, J., Lin, Y., & Chu, J. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002023 · Cited by 20
What is so special about smell? Olfaction as a model system in neurobiology
Barwich, A. (2015) · Postgraduate Medical Journal · doi:10.1136/postgradmedj-2015-133249 · Cited by 20
Astl, L., Tse, A., & Verkhivker, G. M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8719-7_9 · Cited by 18
Ren, W., Dokainish, H., Shinobu, A., Oshima, H., & Sugita, Y. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c11600 · Cited by 22
Klinman, J. P. (2013) · FEBS Journal · doi:10.1111/febs.12477 · Cited by 20
Tuning RNA Flexibility with Helix Length and Junction Sequence
Sutton, J. L., & Pollack, L. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.10.039 · Cited by 20
Cross-Sequence Interactions between Human and Rat Islet Amyloid Polypeptides
Hu, R., Zhang, M., Patel, K., Wang, Q., Chang, Y., Gong, X., Zhang, G., & Zheng, J. (2014) · Langmuir · doi:10.1021/la500632d · Cited by 20
Mao, Y., Yao, H., Wang, H., Cheng, P., & Long, D. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201608653 · Cited by 20
Collins, A. P., & Anderson, P. C. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00441 · Cited by 19
Structural basis for the bi-functionality of human oxaloacetate decarboxylase FAHD1
Weiss, A. K. H., Naschberger, A., Loeffler, J. R., Gstach, H., Bowler, M. W., Holzknecht, M., Cappuccio, E., Pittl, A., Etemad, S., Dunzendorfer-Matt, T., et al. (2018) · Biochemical Journal · doi:10.1042/bcj20180750 · Cited by 19
Liu, Y., Jia, L., Wu, S., Xu, S., Zhang, X., Jiang, S., & Gong, J. (2019) · CrystEngComm · doi:10.1039/c8ce02074d · Cited by 20
Torchala, M., Gerguri, T., Chaleil, R. A. G., Gordon, P., Russell, F., Keshani, M., & Bates, P. A. (2019) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25851 · Cited by 19
Gaucher, J., Reille‐Seroussi, M., & Broussy, S. (2022) · Chemistry - A European Journal · doi:10.1002/chem.202200465 · Cited by 19
Chiral Self‐Sorting of Flexible Covalent Organic Pillars for Adaptive Molecular Recognition
Gao, S., Zhang, M., Zhang, Y., Wang, C., & Sue, A. C. ‐. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202509177 · Cited by 19
Gibbs, E. B., & Showalter, S. A. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b06934 · Cited by 19
Different modification pathways for m1A58 incorporation in yeast elongator and initiator tRNAs
Yared, M.-J., Yoluç, Y., Catala, M., Tisné, C., Kaiser, S., & Barraud, P. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad722 · Cited by 19
Access Path to the Ligand Binding Pocket May Play a Role in Xenobiotics Selection by AhR
Szöllősi, D., Erdei, Á., Gyimesi, G., Magyar, C., & Hegedűs, T. (2016) · PLoS ONE · doi:10.1371/journal.pone.0146066 · Cited by 20
Sahu, D., Bastidas, M., Lawrence, C. W., Noid, W. G., & Showalter, S. A. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.07.032 · Cited by 19
Metadata
- Authors
- Csermely, P., Palotai, R., & Nussinov, R.
- Affiliations
- Semmelweis University (HU)
- Tel Aviv University (IL)
- ORCID
- Nussinov, Ruth
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2010-10
- Volume
- 35
- Issue
- 10
- Pages
- 539-546
- ISSN
- 0968-0004 (ISSN-L)
- PMC
- PMC3018770
- OpenAlex
- W2096929343
- Cited by
- 821
- References
- 69
- Citations by year
- 2026: 40 · 2025: 47 · 2024: 33 · 2023: 23 · 2022: 43 · 2021: 36 · 2020: 56 · 2019: 48 · 2018: 44 · 2017: 49 · 2016: 60 · 2015: 58 · 2014: 75 · 2013: 73 · 2012: 72
- FWCI
- 5.87
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- arXiv (Cornell University) (submittedVersion)
- arXiv (Cornell University)
- Funders
- National Institutes of Health (HHSN261200800001C)
- National Cancer Institute (HHSN261200800001E), Z01BC010441)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- induced fit, conformational selection, protein-protein binding, protein dynamics, discrete breathers, conformational change, protein aggregation, cellular crowding
- MeSH terms
- Animals, Humans, Protein Binding, Protein Conformation, Proteins, Signal Transduction, Protein Folding
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
