Dynamic Allostery: Linkers Are Not Merely Flexible

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Regulation of Aurora-A Kinase Gene Expression via GABP Recruitment of TRAP220/MED1

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Molecular Dynamics Reveal the Essential Role of Linker Motions in the Function of Cullin–RING E3 Ligases

Liu, J., & Nussinov, R. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.01.022 · Cited by 37 · see citing works

Amplification of signaling via cellular allosteric relay and protein disorder

Ma, B., & Nussinov, R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903024106 · Cited by 36 · see citing works

Functionally important positions can comprise the majority of a protein's architecture

Tungtur, S. K., Parente, D. J., & Swint‐Kruse, L. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22985 · Cited by 35 · see citing works

Crystal structure of Taq DNA polymerase in complex with an inhibitory Fab: The Fab is directed against an intermediate in the helix-coil dynamics of the enzyme

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Structural Insights into the Architecture and Allostery of Full-Length AMP-Activated Protein Kinase

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Biochemical Characterization of the Transcriptional Regulator BzdR from Azoarcus sp. CIB

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Regulation of Syk by Phosphorylation on Serine in the Linker Insert

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Subdividing Repressor Function: DNA Binding Affinity, Selectivity, and Allostery Can Be Altered by Amino Acid Substitution of Nonconserved Residues in a LacI/GalR Homologue

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Rbx1 Flexible Linker Facilitates Cullin-RING Ligase Function Before Neddylation and After Deneddylation

Liu, J., & Nussinov, R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.05.021 · Cited by 26 · see citing works

Arsenic Metalation of Seaweed Fucus vesiculosus Metallothionein: The Importance of the Interdomain Linker in Metallothionein

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Macromolecular dynamics in crowded environments

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Organization of cell–regulatory systems through modular–protein–interaction domains

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Mesoscopic dynamics of diffusion-influenced enzyme kinetics

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Sequences at the Interface of the Fifth Immunoglobulin Domain and First Fibronectin Type III Repeat of the Neural Cell Adhesion Molecule Are Critical for Its Polysialylation

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Processes of fungal proteome evolution and gain of function: gene duplication and domain rearrangement

Cohen-Gihon, I., Sharan, R., & Nussinov, R. (2011) · Physical Biology · doi:10.1088/1478-3975/8/3/035009 · Cited by 20 · see citing works

The Kv1.2 potassium channel: The position of an N-glycan on the extracellular linkers affects its protein expression and function

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Independent and Cooperative Motions of the Kv1.2 Channel: Voltage Sensing and Gating

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Functional Chimeras of the Phosphodiesterase 5 and 10 Tandem GAF Domains

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During Transitions Proteins Make Fleeting Bonds

Boehr, D. D. (2009) · Cell · doi:10.1016/j.cell.2009.11.031 · Cited by 12 · see citing works

Allostery in Disease and in Drug Discovery

Nussinov, R., & Tsai, C. (2013) · Cell · doi:10.1016/j.cell.2013.03.034 · Cited by 764 · see citing works

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436 · see citing works

The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery

Papaleo, E., Saladino, G., Lambrughi, M., Lindorff‐Larsen, K., Gervasio, F. L., & Nussinov, R. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00623 · Cited by 426 · see citing works

Emerging Computational Methods for the Rational Discovery of Allosteric Drugs

Wagner, J., Lee, C. T., Durrant, J. D., Malmstrom, R. D., Feher, V. A., & Amaro, R. E. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00631 · Cited by 230 · see citing works

Coarse-grained molecular simulations of large biomolecules

Takada, S. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.01.010 · Cited by 221 · see citing works

Functional roles of transiently and intrinsically disordered regions within proteins

Uversky, V. N. (2015) · FEBS Journal · doi:10.1111/febs.13202 · Cited by 215 · see citing works

Allosteric post-translational modification codes

Nussinov, R., Tsai, C.-J., Xin, F., & Radivojac, P. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.07.001 · Cited by 211 · see citing works

Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose

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Bridging the gap: bitopic ligands of G-protein-coupled receptors

Lane, J. R., Sexton, P. M., & Christopoulos, A. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2012.10.003 · Cited by 181 · see citing works

NMR approaches for structural analysis of multidomain proteins and complexes in solution

Göbl, C., Madl, T., Simon, B., & Sattler, M. (2014) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2014.05.003 · Cited by 175 · see citing works

The Underappreciated Role of Allostery in the Cellular Network

Nussinov, R., Tsai, C., & Ma, B. (2013) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-083012-130257 · Cited by 174 · see citing works

Protein contact network topology: a natural language for allostery

Paola, L. D., & Giuliani, A. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.03.001 · Cited by 163 · see citing works

Principles of Allosteric Interactions in Cell Signaling

Nussinov, R., Tsai, C.-J., & Liu, J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja510028c · Cited by 154 · see citing works

Topochemical Synthesis of Single-Crystalline Hydrogen-Bonded Cross-Linked Organic Frameworks and Their Guest-Induced Elastic Expansion

Jiang, X., Cui, X.-Z., Duncan, A. J. E., Li, L., Hughes, R. P., Staples, R. J., Alexandrov, E. V., Proserpio, D. M., Wu, Y., & Ke, C. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b05232 · Cited by 144 · see citing works

The Different Ways through Which Specificity Works in Orthosteric and Allosteric Drugs

Nussinov, R., & Tsai, C. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212799436377 · Cited by 139 · see citing works

Sodium-calcium exchangers (NCX): molecular hallmarks underlying the tissue-specific and systemic functions

Khananshvili, D. (2013) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-013-1405-y · Cited by 136 · see citing works

Disordered Proteinaceous Machines

Fuxreiter, M., Tóth-Petróczy, Á., Kraut, D. A., Matouschek, A. T., Lim, R. Y. H., Xue, B., Kurgan, L., & Uversky, V. N. (2014) · Chemical Reviews · doi:10.1021/cr4007329 · Cited by 133 · see citing works

Harnessing glycosylation to improve cellulase activity

Beckham, G. T., Dai, Z., Matthews, J. F., Momany, M., Payne, C. M., Adney, W. S., Baker, S., & Himmel, M. E. (2011) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2011.11.030 · Cited by 130 · see citing works

Multiple conformational selection and induced fit events take place in allosteric propagation

Nussinov, R., Ma, B., & Tsai, C. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.10.002 · Cited by 130 · see citing works

Tracing the origin and evolution of pseudokinases across the tree of life

Kwon, A., Scott, S. T., Taujale, R., Yeung, W., Kochut, K. J., Eyers, P. A., & Kannan, N. (2019) · Science Signaling · doi:10.1126/scisignal.aav3810 · Cited by 127 · see citing works

Protein Modeling: What Happened to the “Protein Structure Gap”?

Schwede, T. F. (2013) · Structure · doi:10.1016/j.str.2013.08.007 · Cited by 125 · see citing works

Accuracy of Current All-Atom Force-Fields in Modeling Protein Disordered States

Palazzesi, F., Prakash, M. K., Bonomi, M., & Barducci, A. (2014) · Journal of Chemical Theory and Computation · doi:10.1021/ct500718s · Cited by 120 · see citing works

Dynamics in multi-domain protein recognition of RNA

Mackereth, C. D., & Sattler, M. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.03.013 · Cited by 122 · see citing works

Cellulase Linkers Are Optimized Based on Domain Type and Function: Insights from Sequence Analysis, Biophysical Measurements, and Molecular Simulation

Sammond, D. W., Payne, C. M., Brunecky, R., Himmel, M. E., Crowley, M. F., & Beckham, G. T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048615 · Cited by 114 · see citing works

Signaling through dynamic linkers as revealed by PKA

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Structural dynamics flexibility informs function and evolution at a proteome scale

Gerek, Z. N., Kumar, S., & Ozkan, S. B. (2013) · Evolutionary Applications · doi:10.1111/eva.12052 · Cited by 104 · see citing works

Induced Fit or Conformational Selection? The Role of the Semi-closed State in the Maltose Binding Protein

Bucher, D., Grant, B. J., & McCammon, J. A. (2011) · Biochemistry · doi:10.1021/bi201481a · Cited by 100 · see citing works

Energy landscapes of functional proteins are inherently risky

Gershenson, A., Gierasch, L. M., Pastore, A., & Radford, S. E. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1670 · Cited by 100 · see citing works

Dynamic allostery governs cyclophilin A–HIV capsid interplay

Lu, M., Hou, G., Zhang, H., Suiter, C. L., Ahn, J., Byeon, I. L., Perilla, J. R., LANGMEAD, C. J., Hung, I., Gor’kov, P. L., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516920112 · Cited by 88 · see citing works

The emergence of protein complexes: quaternary structure, dynamics and allostery

Perica, T., Marsh, J. A., Sousa, F. L., Natan, E., Colwell, L. J., Ahnert, S. E., & Teichmann, S. A. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120056 · Cited by 83 · see citing works

Allosteric control of transcription in G nt R family of transcription regulators: A structural overview

Jain, D. (2015) · IUBMB Life · doi:10.1002/iub.1401 · Cited by 82 · see citing works

Selective Molecular Recognition in Amyloid Growth and Transmission and Cross-Species Barriers

Ma, B., & Nussinov, R. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.11.023 · Cited by 81 · see citing works

Local and global anatomy of antibody‐protein antigen recognition

Wang, M., Zhu, D. S., Zhu, J., Nussinov, R., & Ma, B. (2017) · Journal of Molecular Recognition · doi:10.1002/jmr.2693 · Cited by 76 · see citing works

Antigen binding allosterically promotes Fc receptor recognition

Zhao, J., Nussinov, R., & Ma, B. (2018) · mAbs · doi:10.1080/19420862.2018.1522178 · Cited by 79 · see citing works

Structure and Function of Fusicoccadiene Synthase, a Hexameric Bifunctional Diterpene Synthase

Chen, M., Chou, W. K. W., Toyomasu, T., Cane, D. E., & Christianson, D. W. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00960 · Cited by 79 · see citing works

Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains

Arbesú, M., Iruela, G., Fuentes, H., Teixeira, J. M. C., & Pons, M. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00039 · Cited by 79 · see citing works

Cutting Edge: Evidence for a Dynamically Driven T Cell Signaling Mechanism

Hawse, W. F., Champion, M. M., Joyce, M. V., Hellman, L. M., Hossain, M., Ryan, V. H., Pierce, B. G., Weng, Z., & Baker, B. M. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200952 · Cited by 77 · see citing works

Allosteric Regulation at the Crossroads of New Technologies: Multiscale Modeling, Networks, and Machine Learning

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

Transient Electrostatic Interactions Dominate the Conformational Equilibrium Sampled by Multidomain Splicing Factor U2AF65: A Combined NMR and SAXS Study

Huang, J., Warner, L., Sanchez, C., Gabel, F., Madl, T., Mackereth, C. D., Sattler, M., & Blackledge, M. J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja502030n · Cited by 76 · see citing works

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

Designing Chimeric Molecules for Drug Discovery by Leveraging Chemical Biology

Borsari, C., Trader, D. J., Tait, A., & Costi, M. P. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01456 · Cited by 75 · see citing works

Sequence-to-conformation relationships of disordered regions tethered to folded domains of proteins

Mittal, A., Holehouse, A. S., Cohan, M. C., & Pappu, R. V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.012 · Cited by 72 · see citing works

Novel approaches for the rational design of PROTAC linkers

Zagidullin, A. A., Milyukov, V. A., Rizvanov, A. A., & Bulatov, E. (2020) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2020.00023 · Cited by 70 · see citing works

Mapping the Interaction Sites between AMPA Receptors and TARPs Reveals a Role for the Receptor N-Terminal Domain in Channel Gating

Cais, O., Herguedas, B., Krol, K., Cull-Candy, S. G., Farrant, M., & Greger, I. H. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.029 · Cited by 67 · see citing works

Structured Crowding and Its Effects on Enzyme Catalysis

Ma, B., & Nussinov, R. (2013) · Topics in current chemistry · doi:10.1007/128_2012_316 · Cited by 63 · see citing works

Segmental, Domain‐Selective Perdeuteration and Small‐Angle Neutron Scattering for Structural Analysis of Multi‐Domain Proteins

Sonntag, M., Jagtap, P. K. A., Simon, B., Appavou, M., Geerlof, A., Stehle, R., Gabel, F., Hennig, J., & Sattler, M. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201702904 · Cited by 62 · see citing works

Large-Scale Conformational Dynamics Control H5N1 Influenza Polymerase PB2 Binding to Importin α

Delaforge, E., Milles, S., Bouvignies, G., Bouvier, D., Boivin, S., Salvi, N., Maurin, D., Martel, A., Round, A. R., Lemke, E. A., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b07765 · Cited by 59 · see citing works

Same but not alike: Structure, flexibility and energetics of domains in multi-domain proteins are influenced by the presence of other domains

Vishwanath, S., de Brevern, A. G., & Srinivasan, N. (2018) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006008 · Cited by 59 · see citing works

A mechanism for acetylcholine receptor gating based on structure, coupling, phi, and flip

Gupta, S., Chakraborty, S., Vij, R., & Auerbach, A. L. (2016) · The Journal of General Physiology · doi:10.1085/jgp.201611673 · Cited by 57 · see citing works

Intrinsic protein disorder in oncogenic KRAS signaling

Nussinov, R., Jang, H., Tsai, C., Liao, T.-J., Li, S., Fushman, D., & Zhang, J. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2564-3 · Cited by 57 · see citing works

Flexible Cullins in Cullin-RING E3 Ligases Allosterically Regulate Ubiquitination

Liu, J., & Nussinov, R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277236 · Cited by 52 · see citing works

Fab-PEG-Fab as a Potential Antibody Mimetic

Khalili, H., Godwin, A., Choi, J.-W., Lever, R., Khaw, P. T., & Brocchini, S. (2013) · Bioconjugate Chemistry · doi:10.1021/bc400246z · Cited by 49 · see citing works

How do disordered regions achieve comparable functions to structured domains?

Latysheva, N. S., Flock, T., Weatheritt, R. J., Chavali, S., & Babu, M. M. (2015) · Protein Science · doi:10.1002/pro.2674 · Cited by 50 · 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

The structural basis for cancer treatment decisions

Nussinov, R., Jang, H., & Tsai, C. (2014) · Oncotarget · doi:10.18632/oncotarget.2439 · Cited by 51 · see citing works

The spatial structure of cell signaling systems

Nussinov, R. (2013) · Physical Biology · doi:10.1088/1478-3975/10/4/045004 · Cited by 49 · see citing works

Atomistic Kinetic Model for Population Shift and Allostery in Biomolecules

Long, D., & Brüschweiler, R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja208813t · Cited by 48 · see citing works

Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins

Stetz, G., & Verkhivker, G. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0143752 · Cited by 45 · see citing works

Changes in signal transducer and activator of transcription 3 (STAT3) dynamics induced by complexation with pharmacological inhibitors of Src homology 2 (SH2) domain dimerization

Resetca, D., Haftchenary, S., Gunning, P. T., & Wilson, D. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.595454 · Cited by 47 · see citing works

Autoinhibition in Ras effectors Raf, PI3Kα, and RASSF5: a comprehensive review underscoring the challenges in pharmacological intervention

Nussinov, R., Zhang, M., Tsai, C., Liao, T.-J., Fushman, D., & Jang, H. (2018) · Biophysical Reviews · doi:10.1007/s12551-018-0461-0 · Cited by 46 · see citing works

A broad view of scaffolding suggests that scaffolding proteins can actively control regulation and signaling of multienzyme complexes through allostery

Nussinov, R., Ma, B., & Tsai, C. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.12.014 · Cited by 45 · see citing works

Glycosylation of Cellulases

Greene, E. R., Himmel, M. E., Beckham, G. T., & Tan, Z. (2015) · Advances in carbohydrate chemistry and biochemistry · doi:10.1016/bs.accb.2015.08.001 · Cited by 45 · see citing works

Oligomerization and nanocluster organization render specificity

Nussinov, R., Jang, H., & Tsai, C. (2014) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12124 · Cited by 44 · see citing works

Twists and turns in ubiquitin‐like protein conjugation cascades

Schulman, B. A. (2011) · Protein Science · doi:10.1002/pro.750 · Cited by 45 · see citing works

An atomistic view of Hsp70 allosteric crosstalk: from the nucleotide to the substrate binding domain and back

Chiappori, F., Ivan Merelli, A., Milanesi, L., Colombo, G., & Morra, G. (2016) · Scientific Reports · doi:10.1038/srep23474 · Cited by 43 · see citing works

Folding of multidomain proteins: Biophysical consequences of tethering even in apparently independent folding

Arviv, O., & Levy, Y. (2012) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24161 · Cited by 41 · see citing works

Research progress and the biotechnological applications of multienzyme complex

Jiang, Y., Zhang, X., Yuan, H., Huang, D., Wang, R., Liu, H., & Wang, T. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11121-4 · Cited by 41 · see citing works

Two-state dynamics of the SH3–SH2 tandem of Abl kinase and the allosteric role of the N-cap

Corbi‐Verge, C., Marinelli, F., Ruano, A. Z., Ruiz‐Sanz, J., Luque, I., & Faraldo‐Gómez, J. D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303966110 · Cited by 41 · see citing works

Carbohydrate Affinity for the Glucose–Galactose Binding Protein Is Regulated by Allosteric Domain Motions

Ortega, G., Castaño, D., Diercks, T., & Millet, Ó. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3092938 · Cited by 41 · see citing works

Allosteric Partial Inhibition of Monomeric Proteases. Sulfated Coumarins Induce Regulation, not just Inhibition, of Thrombin

Verespy, S., Mehta, A. Y., Afosah, D. K., Al‐Horani, R. A., & Desai, U. R. (2016) · Scientific Reports · doi:10.1038/srep24043 · Cited by 40 · see citing works

Conformational Dynamics and Allostery in Pyruvate Kinase

Donovan, K. A., Zhu, S., Liuni, P., Peng, F., Kessans, S. A., Wilson, D. J., & Dobson, R. C. J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.676270 · Cited by 39 · see citing works

Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker

Seul, A., Müller, J. J., Andres, D., Stettner, E., Heinemann, U., & Seckler, R. (2014) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004714002685 · Cited by 39 · see citing works

Computational and Experimental Analyses Reveal the Essential Roles of Interdomain Linkers in the Biological Function of Chemotaxis Histidine Kinase CheA

Wang, X., Wu, C. F., Vu, A., Shea, J., & Dahlquist, F. W. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3056694 · Cited by 37 · see citing works

Folded domain charge properties influence the conformational behavior of disordered tails

Taneja, I., & Holehouse, A. S. (2021) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2021.08.002 · Cited by 30 · see citing works

Allosteric Regulation of Serine Protease HtrA2 through Novel Non-Canonical Substrate Binding Pocket

Bejugam, P. R., Kuppili, R. R., Singh, N., Gadewal, N. S., Chaganti, L. K., Sastry, G. M., & Bose, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055416 · Cited by 37 · see citing works

Conserved linker regions and their regulation determine multiple chromatin-binding modes of UHRF1

Tauber, M., & Fischle, W. (2015) · Nucleus · doi:10.1080/19491034.2015.1026022 · Cited by 36 · see citing works

Disorder driven allosteric control of protein activity

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Reassembly and co-crystallization of a family 9 processive endoglucanase from its component parts: structural and functional significance of the intermodular linker

Petkun, S., Grinberg, I. R., Lamed, R., Jindou, S., Burstein, T., Yaniv, O., Shoham, Y., Shimon, L. J. W., Bayer, E. A., & Frolow, F. (2015) · PeerJ · doi:10.7717/peerj.1126 · Cited by 36 · see citing works

A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins

Aiyer, S., Swapna, G. V. T., Ma, L.-C., Liu, G., Hao, J., Chalmers, G., Jacobs, B. C., Montelione, G. T., & Roth, M. J. (2021) · Structure · doi:10.1016/j.str.2021.01.010 · Cited by 35 · see citing works

The role of allostery in the ubiquitin–proteasome system

Liu, J., & Nussinov, R. (2012) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2012.742856 · Cited by 35 · see citing works

Candidate Binding Sites for Allosteric Inhibition of the SARS-CoV-2 Main Protease from the Analysis of Large-Scale Molecular Dynamics Simulations

Carli, M., Sormani, G., Rodríguez, Á., & Laio, A. (2020) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.0c03182 · Cited by 35 · see citing works

Engineering an Allosteric Control of Protein Function

Vishweshwaraiah, Y. L., Chen, J., & Dokholyan, N. V. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c11640 · Cited by 33 · see citing works

Prediction of allosteric communication pathways in proteins

Haliloǧlu, T., Hacisuleyman, A., & Erman, B. (2022) · Bioinformatics · doi:10.1093/bioinformatics/btac380 · Cited by 34 · see citing works

How do dynamic cellular signals travel long distances?

Nussinov, R. (2011) · Molecular BioSystems · doi:10.1039/c1mb05205e · Cited by 33 · see citing works

Regulation of the EphA2 receptor intracellular region by phosphomimetic negative charges in the kinase-SAM linker

Lechtenberg, B. C., Gehring, M. P., Light, T. P., Horne, C. R., Matsumoto, M. W., Hristova, K. A., & Pasquale, E. B. (2021) · Nature Communications · doi:10.1038/s41467-021-27343-z · Cited by 33 · see citing works

A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering

Borges, J. C., Seraphim, T. V., Dores-Silva, P. R., & Barbosa, L. R. S. (2016) · Biophysical Reviews · doi:10.1007/s12551-016-0194-x · Cited by 32 · see citing works

Pioneer in Molecular Biology: Conformational Ensembles in Molecular Recognition, Allostery, and Cell Function

Nussinov, R. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169044 · Cited by 33 · see citing works

Thermodynamic Protein Destabilization by GFP Tagging: A Case of Interdomain Allostery

Sokolovski, M., Bhattacherjee, A., Kessler, N., Levy, Y., & Horovitz, A. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.04.032 · Cited by 31 · see citing works

Interaction of the M4 Segment with Other Transmembrane Segments Is Required for Surface Expression of Mammalian α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors

Salussolia, C. L., Corrales, A., Talukder, I., Kazi, R., Akgül, G., Bowen, M. E., & Wollmuth, L. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.268839 · Cited by 31 · see citing works

Determination of the Individual Roles of the Linker Residues in the Interdomain Motions of Calmodulin Using NMR Chemical Shifts

Kukić, P., Camilloni, C., Cavalli, A., & Vendruscolo, M. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.02.002 · Cited by 30 · see citing works

K-Ras4B/calmodulin/PI3Kα: A promising new adenocarcinoma-specific drug target?

Nussinov, R., Muratcioğlu, S., Tsai, C., Jang, H., Gürsoy, A., & Keskin, Ö. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2016.1135131 · Cited by 30 · see citing works

The diversity of molecular interactions involving intrinsically disordered proteins: A molecular modeling perspective

Clerc, I., Sagar, A., Barducci, A., Sibille, N., Bernadó, P., & Cortés, J. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.06.031 · Cited by 29 · see citing works

Small Molecule Targeting of Protein–Protein Interactions through Allosteric Modulation of Dynamics

Cossins, B. P., & Lawson, A. D. G. (2015) · Molecules · doi:10.3390/molecules200916435 · Cited by 29 · see citing works

Protein Function Analysis through Machine Learning

Avery, C., Patterson, J., Grear, T. J., Frater, T. D., & Jacobs, D. J. (2022) · Biomolecules · doi:10.3390/biom12091246 · Cited by 29 · see citing works

Functional phylotyping approach for assessing intraspecific diversity of Ruminococcus albus within the rumen microbiome

Grinberg, I. R., Yin, G., Borovok, I., Miller, M. E. B., Yeoman, C. J., Dassa, B., Yu, Z., Mizrahi, I., Flint, H. J., Bayer, E. A., et al. (2015) · FEMS Microbiology Letters · doi:10.1093/femsle/fnu047 · Cited by 29 · see citing works

Exploring modular allostery via interchangeable regulatory domains

Fan, Y., Cross, P. J., Jameson, G. B., & Parker, E. J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1717621115 · Cited by 28 · see citing works

Identification of potential allosteric communication pathways between functional sites of the bacterial ribosome by graph and elastic network models

Güzel, P., & Kürkçüoğlu, Ö. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.09.005 · Cited by 28 · see citing works

Nanoscale protein dynamics: A new frontier for neutron spin echo spectroscopy

Callaway, D. J. E., Farago, B., & Bu, Z. (2013) · The European Physical Journal E · doi:10.1140/epje/i2013-13076-1 · Cited by 27 · see citing works

The intramolecular allostery of GRB2 governing its interaction with SOS1 is modulated by phosphotyrosine ligands

Jasemi, N. S. K., Herrmann, C., Estirado, E. M., Gremer, L., Willbold, D., Brunsveld, L., Dvorský, R., & Ahmadian, M. R. (2021) · Biochemical Journal · doi:10.1042/bcj20210105 · Cited by 26 · see citing works

Cyclic AMP-induced Conformational Changes in Mycobacterial Protein Acetyltransferases

Nambi, S., Badireddy, S., Visweswariah, S. S., & Anand, G. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.328112 · Cited by 26 · see citing works

The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery

Papaleo, E., Saladino, G., Lambrughi, M., Lindorff‐Larsen, K., Gervasio, F. L., & Nussinov, R. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00623 · Cited by 426 · see citing works

Dynamically Driven Protein Allostery Exhibits Disparate Responses for Fast and Slow Motions

Guo, J., & Zhou, H. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.04.035 · Cited by 29 · see citing works

Allostery and Conformational Dynamics in Protein Evolution

Ozkan, S. B. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.11.2217

The Origin of Allosteric Functional Modulation: Multiple Pre-existing Pathways

del Sol, A., Tsai, C., Ma, B., & Nussinov, R. (2009) · Structure · doi:10.1016/j.str.2009.06.008 · Cited by 365 · see citing works

Allostery and Structural Dynamics in Protein Evolution

Campitelli, P., & Ozkan, S. B. (2019) · Springer eBooks · doi:10.1007/978-3-030-30363-1_9 · Cited by 2 · see citing works