Allosteric Conformational Barcodes Direct Signaling in the Cell

Wnt/β-catenin signaling and disease

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The Energy Landscapes and Motions of Proteins

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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 · see citing works

β-Arrestins and Cell Signaling

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Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins

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Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

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Structure and dynamics of molecular networks: A novel paradigm of drug discovery

Csermely, P., Korcsmáros, T., Kiss, H., London, G., & Nussinov, R. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.01.016 · Cited by 889 · see citing works

Is allostery an intrinsic property of all dynamic proteins?

Gunasekaran, K., Ma, B., & Nussinov, R. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20232 · Cited by 882 · see citing works

Perceiving the epigenetic landscape through histone readers

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Induced fit, conformational selection and independent dynamic segments: an extended view of binding events

Csermely, P., Palotai, R., & Nussinov, R. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.009 · Cited by 821 · 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

Sequential Application of Anticancer Drugs Enhances Cell Death by Rewiring Apoptotic Signaling Networks

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Allostery and cooperativity revisited

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Allosteric regulation and catalysis emerge via a common route

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Folding funnels, binding funnels, and protein function

Tsai, C., Kumar, S., Ma, B., & Nussinov, R. (1999) · Protein Science · doi:10.1110/ps.8.6.1181 · Cited by 648 · see citing works

Distinct Phosphorylation Sites on the β 2 -Adrenergic Receptor Establish a Barcode That Encodes Differential Functions of β-Arrestin

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Activation of the Sire-family tyrosine kinase Hck by SH3 domain displacement

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Folding funnels and binding mechanisms

Ma, B., Kumar, S., Tsai, C.-J., & Nussinov, R. (1999) · Protein Engineering, Design and Selection · doi:10.1093/protein/12.9.713 · Cited by 594 · see citing works

Molecular Mechanism of β-Arrestin-Biased Agonism at Seven-Transmembrane Receptors

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Seven Transmembrane Receptors as Shapeshifting Proteins: The Impact of Allosteric Modulation and Functional Selectivity on New Drug Discovery

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Information Transduction Capacity of Noisy Biochemical Signaling Networks

Cheong, R., Rhee, A., Wang, C. J., Nemenman, I. M., & Levchenko, A. (2011) · Science · doi:10.1126/science.1204553 · Cited by 524 · see citing works

The COP9 Signalosome

Wei, N., & Deng, X. W. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111301.112449 · Cited by 492 · see citing works

Posttranslational Modification of p53: Cooperative Integrators of FunctionPreprint

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Cooperative binding of two acetylation marks on a histone tail by a single bromodomain

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The COP9 signalosome: more than a protease

Wei, N., Serino, G., & Deng, X. L. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.09.004 · Cited by 413 · see citing works

Surface Sites for Engineering Allosteric Control in Proteins

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Formation of Regulatory Patterns During Signal Propagation in a Mammalian Cellular Network

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Proteasome assembly defect due to a proteasome subunit beta type 8 (PSMB8) mutation causes the autoinflammatory disorder, Nakajo-Nishimura syndrome

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Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms

Tsai, C., del Sol, A., & Nussinov, R. (2009) · Molecular BioSystems · doi:10.1039/b819720b · Cited by 324 · see citing works

Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms

Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310 · see citing works

The Hippo signaling pathway and stem cell biology

Ramos, A., & Camargo, F. D. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.04.006 · Cited by 288 · see citing works

The Src, Syk, and Tec family kinases: Distinct types of molecular switches

Bradshaw, J. M. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.03.001 · Cited by 257 · see citing works

Protein dynamics and allostery: an NMR view

Tzeng, S., & Kalodimos, C. G. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.10.007 · Cited by 256 · see citing works

Structural Basis for the Inhibition of Tyrosine Kinase Activity of ZAP-70

Deindl, S., Kadlecek, T. A., Brdička, T., Cao, X., Weiss, A., & Kuriyan, J. (2007) · Cell · doi:10.1016/j.cell.2007.03.039 · Cited by 237 · see citing works

Mapping allostery through the covariance analysis of NMR chemical shifts

Selvaratnam, R., Chowdhury, S., VanSchouwen, B., & Melacini, G. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017311108 · Cited by 228 · 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

Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl

Dou, H., Buetow, L., Hock, A., Sibbet, G. J., Vousden, K. H., & Huang, D. T. C. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2231 · Cited by 211 · see citing works

Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF

Mackereth, C. D., Madl, T., Bonnal, S., Simon, B., Zanier, K., Gasch, A., Rybin, V., Valcárcel, J., & Sattler, M. (2011) · Nature · doi:10.1038/nature10171 · Cited by 210 · see citing works

Differential G-protein-coupled Receptor Phosphorylation Provides Evidence for a Signaling Bar Code

Butcher, A. J., Prihandoko, R., Kong, K. C., McWilliams, P., Edwards, J. M., Bottrill, A. R., Mistry, S. C., & Tobin, A. B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.154526 · Cited by 203 · see citing works

Structural Coupling of SH2-Kinase Domains Links Fes and Abl Substrate Recognition and Kinase Activation

Filippakopoulos, P., Kofler, M., Hantschel, O. D., Gish, G. D., Grebien, F., Salah, E., Neudecker, P., Kay, L. E., Turk, B. E., Superti‐Furga, G., et al. (2008) · Cell · doi:10.1016/j.cell.2008.07.047 · Cited by 201 · see citing works

On the role of frustration in the energy landscapes of allosteric proteins

Ferreiro, D. U., Hegler, J. A., Komives, E. A., & Wolynes, P. G. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018980108 · Cited by 199 · see citing works

Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin

Włodarski, T., & Žagrović, B. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906966106 · Cited by 194 · see citing works

Allostery and population shift in drug discovery

Kar, G., Keskin, Ö., Gürsoy, A., & Nussinov, R. (2010) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2010.09.002 · Cited by 190 · 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

Dynamic protein–DNA recognition: beyond what can be seen

Fuxreiter, M., Simon, I., & Bondos, S. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.04.006 · Cited by 167 · see citing works

Molecular Mechanism of the Syk Activation Switch

Tsang, E. K., Giannetti, A. M., Shaw, D. E., Dinh, M. T., Tse, J. K. Y., Gandhi, S. C., Ho, H., Wang, S., Papp, E., & Bradshaw, J. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806340200 · Cited by 164 · see citing works

Activation-dependent Conformational Changes in β-Arrestin 2

Xiao, K., Shenoy, S. K., Nobles, K. N., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409785200 · Cited by 158 · see citing works

WNT secretion and signalling in human disease

Herr, P., Hausmann, G., & Basler, K. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.06.008 · Cited by 158 · see citing works

Turning a protein kinase on or off from a single allosteric site via disulfide trapping

Sadowsky, J., Burlingame, M. A., Wolan, D. W., McClendon, C. L., Jacobson, M. P., & Wells, J. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102376108 · Cited by 155 · see citing works

Eph, a Protein Family Coming of Age: More Confusion, Insight, or Complexity?

Lackmann, M., & Boyd, A. (2008) · Science Signaling · doi:10.1126/stke.115re2 · Cited by 150 · see citing works

Phosphorylation Barcoding as a Mechanism of Directing GPCR Signaling

Liggett, S. B. (2011) · Science Signaling · doi:10.1126/scisignal.2002331 · Cited by 147 · see citing works

p53 activates transcription by directing structural shifts in Mediator

Meyer, K. D., Lin, S., Bernecky, C., Gao, Y., & Taatjes, D. J. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1816 · Cited by 144 · see citing works

Allo-network drugs: harnessing allostery in cellular networks

Nussinov, R., Tsai, C., & Csermely, P. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.08.004 · Cited by 143 · see citing works

Engineering Signal Transduction Pathways

Kiel, C., Yus, E., & Serrano, L. G. (2010) · Cell · doi:10.1016/j.cell.2009.12.028 · Cited by 140 · see citing works

Protein–protein interaction networks: how can a hub protein bind so many different partners?

Tsai, C.-J., Ma, B., & Nussinov, R. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.07.007 · Cited by 138 · see citing works

Protein functional landscapes, dynamics, allostery: a tortuous path towards a universal theoretical framework

Zhuravlev, P. I., & Papoian, G. A. (2010) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000119 · Cited by 138 · see citing works

Intrinsic disorder: signaling via highly specific but short-lived association

Zhou, H. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.11.002 · Cited by 133 · see citing works

Hydrophobic folding units at protein‐protein interfaces: Implications to protein folding and to protein‐protein association

Tsai, C., & Nussinov, R. (1997) · Protein Science · doi:10.1002/pro.5560060707 · Cited by 125 · see citing works

A post-translational modification code for transcription factors: sorting through a sea of signals

Benayoun, B. A., & Veitia, R. A. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.02.003 · Cited by 121 · see citing works

Circadian Conformational Change of the Neurospora Clock Protein FREQUENCY Triggered by Clustered Hyperphosphorylation of a Basic Domain

Querfurth, C., Diernfellner, A. C. R., Gin, E., Malzahn, E., Höfer, T., & Brunner, M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.033 · Cited by 119 · see citing works

Dynamic interactions of proteins in complex networks: a more structured view

Stein, A., Pache, R. A., Bernadó, P., Pons, M., & Aloy, P. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07251.x · Cited by 118 · see citing works

Mediator Head module structure and functional interactions

Cai, G., Imasaki, T., Yamada, K., Cardelli, F., Takagi, Y., & Asturias, F. (2010) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.1757 · Cited by 108 · see citing works

Detection of allosteric signal transmission by information‐theoretic analysis of protein dynamics

Pandini, A., Fornili, A., Fraternali, F., & Kleinjung, J. (2011) · The FASEB Journal · doi:10.1096/fj.11-190868 · Cited by 106 · see citing works

A Disease-causing Mutation in the Active Site of Serine Palmitoyltransferase Causes Catalytic Promiscuity

Gable, K. S., Gupta, S. D., Han, G., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.122259 · Cited by 104 · see citing works

Ubiquitination-induced conformational change within the deiodinase dimer is a switch regulating enzyme activity

Sagar, G. D. V., Gereben, B., Callebaut, I., Mornon, J.-P., Zeöld, A., da Silva, W. S., Luongo, C., Dentice, M., Tente, S. M., Freitas, B. C. G., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00283-07 · Cited by 103 · see citing works

Coupling between global dynamics and signal transduction pathways: a mechanism of allostery for chaperonin GroEL

Chennubhotla, C., Yang, Z., & Bahar, I. (2008) · Molecular BioSystems · doi:10.1039/b717819k · Cited by 102 · see citing works

Insights into Krabbe disease from structures of galactocerebrosidase

Deane, J. E., Graham, S. C., Kim, N. N., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105639108 · Cited by 101 · see citing works

Glucocorticoids Modulate the mTOR Pathway in the Hippocampus: Differential Effects Depending on Stress History

Polman, J. A. E., Hunter, R. G., Speksnijder, N., van den Oever, J. M. E., Korobko, O. B., McEwen, B. S., de Kloet, E. R., & Datson, N. A. (2012) · Endocrinology · doi:10.1210/en.2012-1255 · Cited by 100 · see citing works

Conformational Control of the Ste5 Scaffold Protein Insulates Against MAP Kinase Misactivation

Zalatan, J. G., Coyle, S. M., Rajan, S., et al. (2012) · Science · doi:10.1126/science.1220683 · Cited by 93 · see citing works

Long-range structural effects of a Charcot–Marie–Tooth disease-causing mutation in human glycyl-tRNA synthetase

Xie, W., Nangle, L. A., Zhang, W., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703908104 · Cited by 90 · see citing works

Regulation of the catalytic activity of the EGF receptor

Endres, N., Engel, K., Das, R., Kovács, E., & Kuriyan, J. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.07.007 · Cited by 90 · see citing works

Computational Modeling of Allosteric Communication Reveals Organizing Principles of Mutation-Induced Signaling in ABL and EGFR Kinases

Dixit, A., & Verkhivker, G. M. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002179 · Cited by 81 · see citing works

Frameworks for Understanding Long-Range Intra-Protein Communication

Whitley, M. J., & Lee, A. R. (2009) · Current Protein and Peptide Science · doi:10.2174/138920309787847563 · Cited by 76 · see citing works

Allosteric inhibition of individual enzyme molecules trapped in lipid vesicles

Piwoński, H., Goomanovsky, M., Bensimon, D., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116670109 · Cited by 75 · see citing works

Crucial role of a shared extracellular loop in apamin sensitivity and maintenance of pore shape of small-conductance calcium-activated potassium (SK) channels

Weatherall, K. L., Seutin, V., Liégeois, J., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110724108 · Cited by 74 · see citing works

Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders

Cai, Y., Cronin, C. N., Engel, A. G., Ohno, K., Hersh, L. B., & Rodgers, D. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600221 · Cited by 73 · see citing works

Uniformly curated signaling pathways reveal tissue-specific cross-talks and support drug target discovery

Korcsmáros, T., Farkas, I. J., Szalay, M., Rovó, P., Fazekas, D., Spiró, Z., Böde, C., Lenti, K., Vellai, T., & Csermely, P. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq310 · Cited by 72 · see citing works

Chromatin Signaling to Kinetochores: Transregulation of Dam1 Methylation by Histone H2B Ubiquitination

Latham, J. A., Chosed, R. J., Wang, S., & Dent, S. (2011) · Cell · doi:10.1016/j.cell.2011.07.025 · Cited by 71 · see citing works

Evidence for DNA-Binding Domain–Ligand-Binding Domain Communications in the Androgen Receptor

Helsen, C., Dubois, V., Verfaillie, A., Young, J., Trekels, M., Vancraenenbroeck, R., Maeyer, M. D., & Claessens, F. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00151-12 · Cited by 63 · see citing works

Perturbation Waves in Proteins and Protein Networks: Applications of Percolation and Game Theories in Signaling and Drug Design

Antal, M., Böde, C., & Csermely, P. (2009) · Current Protein and Peptide Science · doi:10.2174/138920309787847617 · Cited by 62 · see citing works

Stabilization of HPV16 E6 protein by PDZ proteins, and potential implications for genome maintenance

Nicolaides, L., Davy, C. E., Raj, K., Kranjec, C., Banks, L., & Doorbar, J. (2011) · Virology · doi:10.1016/j.virol.2011.03.017 · Cited by 55 · see citing works

Kinetic Rate Constant Prediction Supports the Conformational Selection Mechanism of Protein Binding

Moal, I. H., & Bates, P. A. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002351 · Cited by 54 · see citing works

Rigidity and flexibility of biological networks

Gaspar, M. E., & Csermely, P. (2012) · Briefings in Functional Genomics · doi:10.1093/bfgp/els023 · Cited by 52 · see citing works

Poliovirus Induces Bax-Dependent Cell Death Mediated by c-Jun NH 2 -Terminal Kinase

Autret, A., Martin‐Latil, S., Mousson, L., Wirotius, A., Petit, F., Arnoult, D., Colbère-Garapin, F., Estaquier, J., & Blondel, B. (2007) · Journal of Virology · doi:10.1128/jvi.02690-06 · Cited by 52 · 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

Mediator head subcomplex Med11/22 contains a common helix bundle building block with a specific function in transcription initiation complex stabilization

Seizl, M., Larivière, L., Pfaffeneder, T., Wenzeck, L., & Cramer, P. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr229 · Cited by 47 · see citing works

In Silico Elucidation of the Recognition Dynamics of Ubiquitin

Long, D., & Brüschweiler, R. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002035 · Cited by 47 · see citing works

Structural basis for intersubunit signaling in a protein disaggregating machine

Biter, A. B., Lee, S., Sung, N., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207040109 · Cited by 45 · 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

Challenges ahead in signal transduction: MAPK as an example

Kiel, C., & Serrano, L. G. (2011) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2011.10.004 · Cited by 43 · see citing works

Conformational Control of the Binding of the Transactivation Domain of the MLL Protein and c-Myb to the KIX Domain of CREB

Korkmaz, E. N., Nussinov, R., & Haliloǧlu, T. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002420 · Cited by 40 · see citing works

Identification of the regions of the HPV 5 E6 protein involved in Bak degradation and inhibition of apoptosis

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Recognition of the F&H motif by the Lowe syndrome protein OCRL

Pirruccello, M., Swan, L. E., Folta‐Stogniew, E. J., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2071 · Cited by 34 · see citing works

Gene-specific transcription activation via long-range allosteric shape-shifting

Tsai, C., & Nussinov, R. (2011) · Biochemical Journal · doi:10.1042/bj20110972 · Cited by 34 · see citing works

Effect of the Y955C Mutation on Mitochondrial DNA Polymerase Nucleotide Incorporation Efficiency and Fidelity

Estep, P. A., & Johnson, K. A. (2011) · Biochemistry · doi:10.1021/bi200280r · Cited by 27 · see citing works

Biophysical Characterization of the Complex between Human Papillomavirus E6 Protein and Synapse-associated Protein 97

Celestine, N., Bach, A., Engström, Å., Strømgaard, K., Lundström, P., Ferguson, N. S., & Jemth, P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.190264 · Cited by 22 · see citing works

Promiscuity in protein‐RNA interactions: Conformational ensembles facilitate molecular recognition in the spliceosome

Boehr, D. D. (2011) · BioEssays · doi:10.1002/bies.201100152 · Cited by 15 · see citing works

The condensed chromatin fiber: an allosteric chemo-mechanical machine for signal transduction and genome processing

Lesne, A., Bécavin, C., & Victor, J. (2012) · Physical Biology · doi:10.1088/1478-3975/9/1/013001 · Cited by 13 · see citing works

Lymphotoxin-beta receptor expression and its related signaling pathways govern dendritic cell homeostasis and function

Trez, C. D. (2012) · Immunobiology · doi:10.1016/j.imbio.2012.06.010 · Cited by 11 · 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

AlphaFold, 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

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

ASD v3.0: unraveling allosteric regulation with structural mechanisms and biological networks

Shen, Q., Wang, G., Li, S., Liu, X., Lu, S., Chen, Z., Song, K., Yan, J., Geng, L., Huang, Z., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv902 · Cited by 122 · see citing works

Unraveling structural mechanisms of allosteric drug action

Nussinov, R., & Tsai, C.-J. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.03.006 · Cited by 119 · see citing works

Dynamic Protein Allosteric Regulation and Disease

Nussinov, R., Tsai, C.-J., & Jang, H. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-13-8719-7_2 · Cited by 18 · see citing works

The Molecules That Transmit Information into the Cell: The Intracellular Signaling Pathways

Chedrese, P. J., & Bertorello, A. M. (2009) · Springer eBooks · doi:10.1007/978-0-387-88186-7_3 · Cited by 3 · see citing works

Specificity in signaling pathways: assembly into multimolecular signaling complexes

(1998) · doi:10.1016/s0959-437x(98)80112-3 · Cited by 49 · see citing works

Zinc homeostasis and signaling in health and diseases

Fukada, T., Yamasaki, S., Nishida, K., Murakami, M., & Hirano, T. (2011) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-011-0797-4 · Cited by 600 · see citing works

Identification of Intercellular Signaling Changes Across Conditions and Their Influence on Intracellular Signaling Response From Multiple Single-Cell Datasets

Hao, M., Zou, X., & Jin, S. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.751158 · Cited by 18 · see citing works

Exploring the mechanisms of cellular signal transduction pathways and their implications for diseases

(2023) · doi:10.54254/2753-8818/22/20230998 · Cited by 1 · see citing works