Protein Allostery and Conformational Dynamics
Open accessAbstract
The functions of many proteins are regulated through allostery, whereby effector binding at a distal site changes the functional activity (e.g., substrate binding affinity or catalytic efficiency) at the active site. Most allosteric studies have focused on thermodynamic properties, in particular, substrate binding affinity. Changes in substrate binding affinity by allosteric effectors have generally been thought to be mediated by conformational transitions of the proteins or, alternatively, by changes in the broadness of the free energy basin of the protein conformational state without shifting the basin minimum position. When effector binding changes the free energy landscape of a protein in conformational space, the change affects not only thermodynamic properties but also dynamic properties, including the amplitudes of motions on different time scales and rates of conformational transitions. Here we assess the roles of conformational dynamics in allosteric regulation. Two cases are highlighted where NMR spectroscopy and molecular dynamics simulation have been used as complementary approaches to identify residues possibly involved in allosteric communication. Perspectives on contentious issues, for example, the relationship between picosecond-nanosecond local and microsecond-millisecond conformational exchange dynamics, are presented.
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AlphaFold, which predicts single ranked structures for a protein sequence, is unable to address directly allosteric mechanisms, which are based on populations of conformational states in ensembles.
“AlphaFold, which predicts single ranked structures for a protein sequence, is unable to address directly allosteric mechanisms, which are based on the populations of conformational states in the ensembles.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [103]
In thermal fluctuation allostery, soft global modes of motion rather than more local ones are recruited to enable allosteric cooperativity.
“A feature of this mechanism, first formalized by Cooper and Dryden (1984) and termed thermal fluctuations allostery by the author or “dynamic allostery” elsewhere (Guo and Zhou, 2016; Kern and Zuiderweg, 2003; Schueler-Furman and Wodak, 2016, is that soft global modes of motion rather than more local ones are recruited to enable allosteric cooperativity.”
From Allostery in Its Many Disguises: From Theory to Applications (2019) · cites this paper as Guo and Zhou, 2016
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The Role of Conformational Dynamics and Allostery in Modulating Protein Evolution
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“Rather than forming a new structure, a ligand binding to a remote site promotes a shift in the dynamics of all residues in the protein, changing the distribution of accessible conformational states in the ensemble and, thus, promoting easier access to certain conformers for allosteric regulations while restricting oth…”
BackgroundAlphaFold, Artificial Intelligence (AI), and Allostery
Nussinov, R., Zhang, M., Liu, Y., & Jang, H. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04346 · Cited by 190 · see citing works
Engineering enzyme microenvironments for enhanced biocatalysis
Lancaster, L., Abdallah, W., Banta, S. A., & Wheeldon, I. R. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00085a · Cited by 182 · see citing works
PI3K inhibitors: review and new strategies
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Allosteric Modulator Discovery: From Serendipity to Structure-Based Design
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Role of Conformational Dynamics in the Evolution of Retro-Aldolase Activity
Romero‐Rivera, A., Garcia‐Borràs, M., & Osuna, S. (2017) · ACS Catalysis · doi:10.1021/acscatal.7b02954 · Cited by 168 · see citing works
The challenge of predicting distal active site mutations in computational enzyme design
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“108 In the generated graph, two pairs of nodes (residues) are connected with an edge if the distance between two representative atoms is below a certain threshold.”
BackgroundInfluentialLoop dynamics and the evolution of enzyme activity
Corbella, M., Pinto, G., & Kamerlin, S. C. L. (2023) · Nature Reviews Chemistry · doi:10.1038/s41570-023-00495-w · Cited by 158 · see citing works
Perspective: Identification of collective variables and metastable states of protein dynamics
Sittel, F., & Stock, G. (2018) · The Journal of Chemical Physics · doi:10.1063/1.5049637 · Cited by 146 · see citing works
In silico Methods for Design of Kinase Inhibitors as Anticancer Drugs
Gagić, Ž., Ružić, D., Djoković, N., Djikić, T., & Nikolic, K. M. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00873 · Cited by 144 · see citing works
“Therefore, molecular-dynamics-based approaches, even though being computationally intensive, could detect previously unknown conformations and hidden allosteric binding pockets (Guo and Zhou, 2016; Lu et al., 2018a).”
BackgroundProtospacer Adjacent Motif-Induced Allostery Activates CRISPR-Cas9
Palermo, G., Ricci, C. G., Fernando, A., Basak, R., Jínek, M., Rivalta, I., Batista, V. S., & McCammon, J. A. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b05313 · Cited by 139 · see citing works
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Programmable DNA switches and their applications
Harroun, S. G., Prévost-Tremblay, C., Lauzon, D., Desrosiers, A., Wang, X., Pedro, L., & Vallée‐Bélisle, A. (2018) · Nanoscale · doi:10.1039/c7nr07348h · Cited by 131 · see citing works
Single-molecule FRET methods to study the dynamics of proteins at work
Mazal, H., & Haran, G. (2019) · Current Opinion in Biomedical Engineering · doi:10.1016/j.cobme.2019.08.007 · Cited by 130 · see citing works
Allosteric Motions of the CRISPR–Cas9 HNH Nuclease Probed by NMR and Molecular Dynamics
East, K. W., Newton, J. C., Morzan, U. N., Narkhede, Y. B., Acharya, A., Skeens, E., Jogl, G., Batista, V. S., Palermo, G., & Lisi, G. P. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b10521 · Cited by 122 · see citing works
Long-range allosteric signaling in red light–regulated diguanylyl cyclases
Gourinchas, G., Etzl, S., Göbl, C., Vide, U., Madl, T., & Winkler, A. (2017) · Science Advances · doi:10.1126/sciadv.1602498 · Cited by 124 · see citing works
“The appreciation of dynamically driven allostery (43) and the possibility to both activate and inhibit enzymatic activity in similar systems allow the conclusion that the rational design of sensor-effector Fig.”
BackgroundDirect observation of ultrafast large-scale dynamics of an enzyme under turnover conditions
Aviram, H. Y., Pirchi, M., Mazal, H., Barak, Y., Riven, I., & Haran, G. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1720448115 · Cited by 122 · see citing works
Intrinsic dynamics is evolutionarily optimized to enable allosteric behavior
Zhang, Y., Doruker, P., Kaynak, B., Zhang, S., Krieger, J., Li, H., & Bahar, İ. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.11.002 · Cited by 113 · see citing works
Bending forces and nucleotide state jointly regulate F-actin structure
Reynolds, M. J., Hachicho, C., Carl, A. G., Gong, R., & Alushin, G. M. (2022) · Nature · doi:10.1038/s41586-022-05366-w · Cited by 116 · see citing works
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Photon-by-Photon Hidden Markov Model Analysis for Microsecond Single-Molecule FRET Kinetics
Pirchi, M., Tsukanov, R., Khamis, R., Tomov, T. E., Berger, Y., Khara, D. C., Volkov, H., Haran, G., & Nir, E. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b10726 · Cited by 107 · see citing works
Integrated Computational Approaches and Tools for Allosteric Drug Discovery
Amamuddy, O. S., Veldman, W., Manyumwa, C. V., Khairallah, A., Agajanian, S., Odeyemi, O., Verkhivker, G. M., & Bishop, Ö. T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030847 · Cited by 105 · see citing works
“The phenomenon is also extended to include entropic changes, which may prevail even when no conformational change may be apparent [39–41].”
BackgroundFunctional plasticity and evolutionary adaptation of allosteric regulation
Leander, M., Yuan, Y., Meger, A., Cui, Q., & Raman, S. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002613117 · Cited by 95 · see citing works
A Dynamic Tetracationic Macrocycle Exhibiting Photoswitchable Molecular Encapsulation
Wu, H., Chen, Y., Zhang, L. J., Anamimoghadam, O., Shen, D., Liu, Z., Cai, K., Pezzato, C., Stern, C. L., Liu, Y., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b10526 · Cited by 98 · see citing works
Advances in NMR Methods To Map Allosteric Sites: From Models to Translation
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Liang, Z. T., Verkhivker, G. M., & Hu, G. (2019) · Briefings in Bioinformatics · doi:10.1093/bib/bbz029 · Cited by 85 · see citing works
Rational design of allosteric modulators: Challenges and successes
Chatzigoulas, A., & Cournia, Z. (2021) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1529 · Cited by 87 · see citing works
“Intriguingly, this feature reflects the bidirectional regulation between allosteric and orthosteric sites.(60) Therefore, signaling bias and probe dependence are allosteric features that have the potential to lead to unambiguous and precise allosteric ligand design.”
BackgroundBiotechnological and protein-engineering implications of ancestral protein resurrection
Risso, V. A., Sánchez‐Ruiz, J. M., & Ozkan, S. B. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.02.007 · Cited by 85 · see citing works
Verkhivker, G. M., Agajanian, S., Hu, G., & Tao, P. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00136 · Cited by 76 · see citing works
“…2008, 2009; del Sol et al., 2009; Csermely et al., 2010, Zhuravlev and Papoian, 2010; Ma et al., 2011; Wrabl et al., 2011; Hilser et al., 2012; Nussinov, 2012; Motlagh et al., 2014; Tsai and Nussinov, 2014; Nussinov and Tsai, 2015; Guo and Zhou, 2016; Liu and Nussinov, 2016; Astl et al., 2019).”
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Computational approaches to investigating allostery
Schueler‐Furman, O., & Wodak, S. J. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.06.017 · Cited by 72 · see citing works
Time-resolved observation of protein allosteric communication
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Real-time observation of ligand-induced allosteric transitions in a PDZ domain
Božović, O., Zanobini, C., Gulzar, A., Janković, B. G., Buhrke, D., Post, M., Wolf, S., Stock, G., & Hamm, P. M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2012999117 · Cited by 70 · see citing works
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Allostery: Allosteric Cancer Drivers and Innovative Allosteric Drugs
Nussinov, R., Zhang, M., Maloney, R., Liu, Y., Tsai, C.-J., & Jang, H. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167569 · Cited by 66 · see citing works
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“3 For example, the classic induced fit model postulates that ligand binding to one subunit of a protein causes a conformational change in other subunits.”
BackgroundEnhanced specificity mutations perturb allosteric signaling in CRISPR-Cas9
Nierzwicki, Ł., East, K. W., Morzan, U. N., Arantes, P., Batista, V. S., Lisi, G. P., & Palermo, G. (2021) · eLife · doi:10.7554/elife.73601 · Cited by 65 · see citing works
“We therefore 375 suggest that the allosteric crosstalk can be targeted for improving the system’s specificity, as reported for 376 other allosteric proteins.(21,37,38) In this respect, the critical hotspots identified here (Figure 6) offer novel 377”
Verkhivker, G. M., & Paola, L. D. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c10637 · Cited by 56 · see citing works
“65 − 69 These models can also link the allosteric mechanisms of proteins to their functional role in regulatory processes and signaling events.”
BackgroundA non-equilibrium approach to allosteric communication
Stock, G., & Hamm, P. M. (2018) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2017.0187 · Cited by 56 · see citing works
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McShan, A. C., Devlin, C. A., Overall, S. A., Park, J., Toor, J. S., Moschidi, D., Flores‐Solis, D., Choi, H. S. J., Tripathi, S. M., Procko, E., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1915562116 · Cited by 63 · see citing works
“Thus, future MD simulation experiments validated through measurements of dynamics by NMR and other biophysical techniques will be invaluable in understanding the exact molecular determinants that regulate MHC-I dynamics, given that protein dynamics involve transitions between multiple conformational basins with relati…”
Das, N., & Sen, P. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c03897 · Cited by 63 · see citing works
Machine learning approaches in predicting allosteric sites
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Redox-Responsive Host–Guest Chemistry of a Flexible Cage with Naphthalene Walls
Jia, F., Schröder, H. V., Yang, L., von Eßen, C., Sobottka, S., Sarkar, B., Rissanen, K. T., Jiang, W., & Schalley, C. A. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b11685 · Cited by 60 · see citing works
Induced Fit of C 2 H 2 in a Flexible MOF Through Cooperative Action of Open Metal Sites
Zeng, H., Xie, M., Huang, Y., Zhao, Y., Xie, X., Bai, J., Wan, M., Krishna, R., Lu, W., & Li, D. (2019) · Angewandte Chemie · doi:10.1002/ange.201904160 · Cited by 59 · see citing works
Structure and dynamics underlying elementary ligand binding events in human pacemaking channels
Goldschen-Ohm, M. P., Klenchin, V. A., White, D. S., Cowgill, J. B., Cui, Q., Goldsmith, R. H., & Chanda, B. (2016) · eLife · doi:10.7554/elife.20797 · Cited by 58 · see citing works
Establishing the allosteric mechanism in CRISPR‐Cas9
Nierzwicki, Ł., Arantes, P. R., Saha, A., & Palermo, G. (2020) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1503 · Cited by 58 · see citing works
Leander, M., Liu, Z., Cui, Q., & Raman, S. (2022) · eLife · doi:10.7554/elife.79932 · Cited by 54 · see citing works
Time Evolution of the Millisecond Allosteric Activation of Imidazole Glycerol Phosphate Synthase
Calvó‐Tusell, C., Maria‐Solano, M. A., Osuna, S., & Feixas, F. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c12629 · Cited by 54 · see citing works
Perspectives on Computational Enzyme Modeling: From Mechanisms to Design and Drug Development
Nam, K., Shao, Y., Major, D. T., & Wolf‐Watz, M. (2024) · ACS Omega · doi:10.1021/acsomega.3c09084 · Cited by 57 · see citing works
“19,23,283 287 While more comprehensive reviews are available elsewhere, 21,65,66,279 our discussion here focuses on protein allostery within the context of protein dynamics and conformational landscapes.”
BackgroundTerahertz Spectroscopy of Tetrameric Peptides
Neu, J., Stone, E. A., Spies, J. A., Storch, G., Hatano, A. S., Mercado, B. Q., Miller, S. J., & Schmuttenmaer, C. A. (2019) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.9b01091 · Cited by 55 · see citing works
High-fidelity, hyper-accurate, and evolved mutants rewire atomic-level communication in CRISPR-Cas9
Skeens, E., Sinha, S., Ahsan, M., D’Ordine, A. M., Jogl, G., Palermo, G., & Lisi, G. P. (2024) · Science Advances · doi:10.1126/sciadv.adl1045 · Cited by 50 · see citing works
“The combination of these approaches can comprehensively describe allosteric mechanisms in large biomolecules ( 18 – 23 ).”
Das, N., & Sen, P. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00599 · Cited by 51 · see citing works
Does Ras Activate Raf and PI3K Allosterically?
Nussinov, R., Tsai, C., & Jang, H. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01231 · Cited by 50 · see citing works
Wieteska, Ł., Shahidi, S., & Zhuravleva, A. (2017) · eLife · doi:10.7554/elife.29430 · Cited by 50 · see citing works
“More broadly, our findings present experimental evidence that highlights the role of conformational dynamics in allosteric regulation (Wrabl et al., 2011; Guo and Zhou, 2016) of complex multidomain systems such as molecular chaperones.”
BackgroundAllosteric Regulation of Mammalian Pantothenate Kinase
Subramanian, C., Yun, M., Yao, J., Sharma, L. K., Lee, R. E., Jr., White, S. W., Jackowski, S., & Rock, C. O. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.748061 · Cited by 49 · see citing works
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Cadherin cis and trans interactions are mutually cooperative
Thompson, C. J., Vu, V. H., Leckband, D. E., & Schwartz, D. K. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2019845118 · Cited by 49 · see citing works
Substrate-Based Allosteric Regulation of a Homodimeric Enzyme
Mehrabi, P., Pietrantonio, C. D., Kim, T. H., Sljoka, A., Taverner, K., Ing, C. E., Kruglyak, N., Pomès, R., PAI, E. F., & Prosser, R. S. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b03703 · Cited by 48 · see citing works
Allostery, and how to define and measure signal transduction
Nussinov, R., Tsai, C., & Jang, H. (2022) · Biophysical Chemistry · doi:10.1016/j.bpc.2022.106766 · Cited by 45 · see citing works
New Insights into the Cooperativity and Dynamics of Dimeric Enzymes
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Astl, L., & Verkhivker, G. M. (2019) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.9b00119 · Cited by 43 · see citing works
Prolyl Isomerase Pin1 in Human Cancer: Function, Mechanism, and Significance
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NMR and computational methods for molecular resolution of allosteric pathways in enzyme complexes
East, K. W., Skeens, E., Cui, J. Y., Belato, H. B., Mitchell, B. P., Hsu, R. V., Batista, V. S., Palermo, G., & Lisi, G. P. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00609-z · Cited by 45 · see citing works
Incorporation of sensing modalities into de novo designed fluorescence-activating proteins
Klima, J. C., Doyle, L., Lee, J. D., Rappleye, M., Gagnon, L., Lee, M. Y., de Barros, E. P., Vorobieva, A. A., Dou, J., Bremner, S. B., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-18911-w · Cited by 45 · see citing works
Robust Determination of Protein Allosteric Signaling Pathways
Botello‐Smith, W. M., & Luo, Y. (2019) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.8b01197 · Cited by 44 · see citing works
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The shortest path method (SPM) webserver for computational enzyme design
Casadevall, G., Casadevall, J., Duran, C., & Osuna, S. (2024) · Protein Engineering Design and Selection · doi:10.1093/protein/gzae005 · Cited by 42 · see citing works
Allostery of multidomain proteins with disordered linkers
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Unveiling the RNA-mediated allosteric activation discloses functional hotspots in CRISPR-Cas13a
Sinha, S., Vargas, A. M. M., Arantes, P. R., Patel, A. C., O’Connell, M. R., & Palermo, G. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1127 · Cited by 41 · see citing works
“This observation reflects the biophysical basis of protein allostery ( 43 ,44 ).”
Huang, R., Hua, J., Ru, M., Meng, Y., Wang, L., Huang, Y., Yan, S., Zhang, Q., & Xu, W. (2024) · ACS Nano · doi:10.1021/acsnano.4c05017 · Cited by 41 · see citing works
Visualizing single-stranded nucleic acids in solution
Plumridge, A., Meisburger, S. P., & Pollack, L. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1297 · Cited by 41 · see citing works
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Catalytic Three‐Component Machinery: Control of Catalytic Activity by Machine Speed
Paul, I., Goswami, A., Mittal, N., & Schmittel, M. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201709644 · Cited by 40 · see citing works
Dynamics of Solid Proteins by Means of Nuclear Magnetic Resonance Relaxometry
Kruk, D., Masiewicz, E., Borkowska, A., Rochowski, P., Fries, P. H., Broche, L., & Lurie, D. J. (2019) · Biomolecules · doi:10.3390/biom9110652 · Cited by 39 · see citing works
“The correlation times might correspond to global motions of whole protein domains leading to conformational changes [64].”
BackgroundEmerging Methods and Applications to Decrypt Allostery in Proteins and Nucleic Acids
Arantes, P. R., Patel, A. C., & Palermo, G. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167518 · Cited by 40 · see citing works
Bcr-Abl Allosteric Inhibitors: Where We Are and Where We Are Going to
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Role of Proteome Physical Chemistry in Cell Behavior
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Applications of NMR and computational methodologies to study protein dynamics
Narayanan, C., Bafna, K., Roux, L. D., Agarwal, P. K., & Doucet, N. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.05.002 · Cited by 38 · see citing works
“MD simulations have been used in combination with NMR to identify allosteric networks of conformational motions that play an important role in enzyme function 10,56,57 .”
MethodEffect of ligand binding on a protein with a complex folding landscape
Mazal, H., Aviram, H. Y., Riven, I., & Haran, G. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp03327c · Cited by 37 · see citing works
Conformational control of mechanical networks
Kim, J. Z., Lu, Z., Strogatz, S. H., & Bassett, D. S. (2019) · Nature Physics · doi:10.1038/s41567-019-0475-y · Cited by 37 · see citing works
Advanced Sampling Methods for Multiscale Simulation of Disordered Proteins and Dynamic Interactions
Gong, X., Zhang, Y., & Chen, J. (2021) · Biomolecules · doi:10.3390/biom11101416 · Cited by 37 · see citing works
Das, N., & Sen, P. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d1cp04842b · Cited by 36 · see citing works
Probing allosteric communication with combined molecular dynamics simulations and network analysis
Bernetti, M., Bosio, S., Bresciani, V., Falchi, F., & Masetti, M. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102820 · Cited by 35 · see citing works
Macromolecular crowding effects on protein dynamics
Das, N., Khan, T., Halder, B., Ghosh, S., & Sen, P. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.136248 · Cited by 35 · see citing works
Bocharov, E. V., Sharonov, G. V., Bocharova, O. V., & Pavlov, K. V. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.01.025 · Cited by 35 · see citing works
“1 to 1 s [74,75], so that sequential phosphorylations of several residues is on the timescale of seconds.”
BackgroundRecognition of protein allosteric states and residues: Machine learning approaches
Zhou, H.-Y., Dong, Z., & Tao, P. (2018) · Journal of Computational Chemistry · doi:10.1002/jcc.25218 · Cited by 36 · see citing works
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Autoinhibition can identify rare driver mutations and advise pharmacology
Nussinov, R., Tsai, C., & Jang, H. (2019) · The FASEB Journal · doi:10.1096/fj.201901341r · Cited by 35 · see citing works
Božović, O., Janković, B. G., & Hamm, P. M. (2020) · Nature Communications · doi:10.1038/s41467-020-19689-7 · Cited by 35 · see citing works
Son, A., Kim, W., Park, J., Lee, W., Lee, Y., Choi, S., & Kim, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179725 · Cited by 36 · see citing works
“Advanced NMR techniques and MD simulations have revealed how allosteric signals propagate through protein structures, providing insights into the design of allosteric drugs and the evolution of protein function [23].”
BackgroundZhang, Y., Liu, Y., Li, W., & Han, W. (2024) · LWT · doi:10.1016/j.lwt.2024.117019 · Cited by 36 · see citing works
Hinge-Shift Mechanism Modulates Allosteric Regulations in Human Pin1
Campitelli, P., Guo, J., Zhou, H., & Ozkan, S. B. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.7b11971 · Cited by 35 · see citing works
Self-citation
- Authors
- Guo, J., & Zhou, H.-X.
- Affiliations
- Henan Normal University (CN)
- Florida State University (US)
- Corresponding author
- Zhou, Huan-Xiang
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2016-02-15
- Volume
- 116
- Issue
- 11
- Pages
- 6503-6515
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- PMC
- PMC5011433
- OpenAlex
- W2283818235
- Cited by
- 484
- References
- 99
- Citations by year
- 2026: 66 · 2025: 59 · 2024: 54 · 2023: 58 · 2022: 41 · 2021: 37 · 2020: 43 · 2019: 48 · 2018: 35 · 2017: 26 · 2016: 17
- FWCI
- 3.80
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Chemical Reviews (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Department of Health and Human Services (GM058187)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- protein allostery, conformational dynamics, allosteric regulation, free energy landscape, conformational change, substrate affinity, allosteric effectors, NMR spectroscopy, molecular dynamics simulation
- MeSH terms
- NIMA-Interacting Peptidylprolyl Isomerase, Allosteric Regulation, Protein Binding, Protein Conformation, Proteins, Thermodynamics, Nuclear Magnetic Resonance, Biomolecular, Catalytic Domain, Molecular Dynamics Simulation
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