Emerging roles of allosteric modulators in the regulation of protein‐protein interactions (PPIs): A new paradigm for PPI drug discovery
Abstract
Protein‐protein interactions (PPIs) are closely implicated in various types of cellular activities and are thus pivotal to health and disease states. Given their fundamental roles in a wide range of biological processes, the modulation of PPIs has enormous potential in drug discovery. However, owing to the general properties of large, flat, and featureless interfaces of PPIs, previous attempts have demonstrated that the generation of therapeutic agents targeting PPI interfaces is challenging, rendering them almost “undruggable” for decades. To date, rapid progress in chemical and structural biology techniques has promoted the exploitation of allostery as a novel approach in drug discovery. By attaching to allosteric sites that are topologically and spatially distinct from PPI interfaces, allosteric modulators can achieve improved physiochemical properties. Thus, allosteric modulators may represent an alternative strategy to target intractable PPIs and have attracted intense pharmaceutical interest. In this review, we first briefly introduce the characteristics of PPIs and then present different approaches for investigating PPIs, as well as the latest methods for modulating PPIs. Importantly, we comprehensively review the recent progress in the development of allosteric modulators to inhibit or stabilize PPIs. Finally, we conclude with future perspectives on the discovery of allosteric PPI modulators, especially the application of computational methods to aid in allosteric PPI drug discovery.
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Allosteric sites are more ligandable than PPI interfaces, in general.
“Allostery has been suggested as a promising approach to modulating PPIs,261 since allosteric sites are more ligandable than PPI interfaces, in general.”
From Advancing Targeted Protein Degradation via Multiomics Profiling and Artificial Intelligence (2023) · cites this paper as [261]
Cites
Functional organization of the yeast proteome by systematic analysis of protein complexes
Gavin, A., Böesche, M., Krause, R., Grandi, P., Marzioch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A., Cruciat, C., et al. (2002) · Nature · doi:10.1038/415141a · Cited by 4,729 · see citing works
Microtubules as a target for anticancer drugs
Jordan, M. A., & Wilson, L. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1317 · Cited by 4,534 · see citing works
Promotion of microtubule assembly in vitro by taxol
SCHIFF, P. B., FANT, J., & HORWITZ, S. B. (1979) · Nature · doi:10.1038/277665a0 · Cited by 3,600 · see citing works
Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme.
Bredt, D. S., & Snyder, S. H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.2.682 · Cited by 3,308 · see citing works
Nitric oxide synthases: Roles, tolls, and controls
Nathan, C., & Xie, Q. W. (1994) · Cell · doi:10.1016/0092-8674(94)90266-6 · Cited by 2,920 · see citing works
Towards a proteome-scale map of the human protein–protein interaction network
Rual, J.-F. M., Venkatesan, K., Hao, T., Hirozane-Kishikawa, T., Dricot, A., Li, N., Berriz, G. F., Gibbons, F. D., Dreze, M., Ayivi-Guedehoussou, N., et al. (2005) · Nature · doi:10.1038/nature04209 · Cited by 2,904 · see citing works
A subcellular map of the human proteome
Thul, P. J., Åkesson, L., Wiking, M., Mahdessian, D., Geladaki, A., Ait Blal, H., Alm, T., Asplund, A., Björk, L., Breckels, L. M., et al. (2017) · Science · doi:10.1126/science.aal3321 · Cited by 2,813 · see citing works
Trends in GPCR drug discovery: new agents, targets and indications
Hauser, A. S., Attwood, M. M., Rask‐Andersen, M., Schiöth, H. B., & Gloriam, D. E. I. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.178 · Cited by 2,609 · see citing works
K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions
Ostrem, J. M., Peters, U., Sos, M. L., Wells, J. A., & Shokat, K. M. (2013) · Nature · doi:10.1038/nature12796 · Cited by 2,557 · see citing works
The structure and function of G-protein-coupled receptors
Rosenbaum, D. M., Rasmussen, S. G. F., & Kobilka, B. K. (2009) · Nature · doi:10.1038/nature08144 · Cited by 2,534 · cited 1× · see citing works
“GPCRs are a class of membrane proteins that lie at crucial nexuses of intracellular signaling networks.(159) G proteins are key effectors of GPCRs and consist of α‐ and βγ‐subunits.”
BackgroundA Human Protein-Protein Interaction Network: A Resource for Annotating the Proteome
Stelzl, U., Worm, U., Lalowski, M. M., Haenig, C., Brembeck, F. H., Goehler, H., Strödicke, M., Zenkner, M., Schoenherr, A., Koeppen, S., et al. (2005) · Cell · doi:10.1016/j.cell.2005.08.029 · Cited by 2,389 · see citing works
eIF4 Initiation Factors: Effectors of mRNA Recruitment to Ribosomes and Regulators of Translation
Gingras, A., Raught, B., & Sonenberg, N. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.913 · Cited by 2,103 · see citing works
A Comprehensive Survey of Ras Mutations in Cancer
Prior, I. A., Lewis, P. D., & Mattos, C. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-2612 · Cited by 2,063 · see citing works
Taxol stabilizes microtubules in mouse fibroblast cells.
Schiff, P. B., & Horwitz, S. B. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1561 · Cited by 1,971 · see citing works
The atomic structure of protein-protein recognition sites 1 1Edited by A. R. Fersht
Conte, L. L., Chothia, C., & Janin, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2439 · Cited by 1,967 · see citing works
Reaching for high-hanging fruit in drug discovery at protein–protein interfaces
Wells, J. A., & McClendon, C. L. (2007) · Nature · doi:10.1038/nature06526 · Cited by 1,963 · see citing works
Microtubule-binding agents: a dynamic field of cancer therapeutics
Dumontet, C., & Jordan, M. A. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3253 · Cited by 1,730 · see citing works
Protein detection using proximity-dependent DNA ligation assays
Fredriksson, S., Gullberg, M. T., Jarvius, J., Olsson, C., Pietras, K., Gustafsdottir, S., Östman, A., & Landegren, U. D. (2002) · Nature Biotechnology · doi:10.1038/nbt0502-473 · Cited by 1,511 · see citing works
Ras oncogenes: split personalities
Karnoub, A. E., & Weinberg, R. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2438 · Cited by 1,467 · see citing works
Architecture of the human interactome defines protein communities and disease networks
Huttlin, E. L., Bruckner, R. J., Paulo, J. A., Cannon, J. R., Ting, L., Baltier, K., Colby, G., Gebreab, F., Gygi, M. P., Parzen, H., et al. (2017) · Nature · doi:10.1038/nature22366 · Cited by 1,437 · see citing works
Nitric Oxide Synthases: Properties and Catalytic Mechanism
Griffith, O. W., & Stuehr, D. J. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.003423 · Cited by 1,311 · see citing works
Small molecules, big targets: drug discovery faces the protein–protein interaction challenge
Scott, D. E., Bayly, A. R., Abell, C., & Skidmore, J. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.29 · Cited by 1,137 · see citing works
Small-Molecule Inhibitors of Protein-Protein Interactions: Progressing toward the Reality
Arkin, M. R., Tang, Y., & Wells, J. A. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.09.001 · Cited by 1,065 · see citing works
Weitz‐Schmidt, G., Welzenbach, K., Brinkmann, V., Kamata, T., Kallen, J. A., Bruns, C., Cottens, S., Takada, Y., & Hommel, U. (2001) · Nature Medicine · doi:10.1038/89058 · Cited by 1,041 · see citing works
Targeting the PI3K pathway in cancer: are we making headway?
Janku, F., Yap, T. A., & Meric-Bernstam, F. (2018) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2018.28 · Cited by 1,033 · see citing works
Regulation of cap-dependent translation by eIF4E inhibitory proteins
Richter, J. D., & Sonenberg, N. (2005) · Nature · doi:10.1038/nature03205 · Cited by 972 · see citing works
Diversity of protein–protein interactions
Nooren, I. M. A., & Thornton, J. (2003) · EMBO Journal · doi:10.1093/emboj/cdg359 · Cited by 942 · see citing works
Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of Yeast
Hope, I. A., & Struhl, K. (1986) · Cell · doi:10.1016/0092-8674(86)90070-x · Cited by 918 · see citing works
An empirical framework for binary interactome mapping
Venkatesan, K., Rual, J.-F. M., Vázquez, A., Stelzl, U., Lemmens, I. H., Hirozane-Kishikawa, T., Hao, T., Zenkner, M., Xin, X., Goh, K. I., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1280 · Cited by 907 · see citing works
Nitric oxide synthase: Aspects concerning structure and catalysis
Marletta, M. A. (1994) · Cell · doi:10.1016/0092-8674(94)90268-2 · Cited by 862 · see citing works
The structure of protein-protein recognition sites.
Janin, J., & Chothia, C. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46181-3 · Cited by 824 · 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
Hot spots—A review of the protein–protein interface determinant amino‐acid residues
Moreira, I. S., Fernandes, P. A., & Ramos, M. J. (2007) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.21396 · Cited by 760 · see citing works
Protein function in the post-genomic era
Eisenberg, D. S., Marcotte, E. M., Xénarios, I., & Yeates, T. O. (2000) · Nature · doi:10.1038/35015694 · Cited by 749 · see citing works
GAIP and RGS4 Are GTPase-Activating Proteins for the Gi Subfamily of G Protein α Subunits
Berman, D. M., Wilkie, T. M., & Gilman, A. G. (1996) · Cell · doi:10.1016/s0092-8674(00)80117-8 · Cited by 729 · see citing works
Inhibition of α-helix-mediated protein–protein interactions using designed molecules
Azzarito, V., Long, K., Murphy, N. S., & Wilson, A. J. (2013) · Nature Chemistry · doi:10.1038/nchem.1568 · Cited by 727 · see citing works
Methods for the detection and analysis of protein–protein interactions
Berggård, T., Linse, S. S., & James, P. (2007) · PROTEOMICS · doi:10.1002/pmic.200700131 · Cited by 714 · see citing works
Analysis of protein complexes using mass spectrometry
Gingras, A., Gstaiger, M., Raught, B., & Aebersold, R. H. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2208 · Cited by 709 · see citing works
Ras history: The saga continues
Cox, A. D., & Der, C. J. (2010) · Small GTPases · doi:10.4161/sgtp.1.1.12178 · Cited by 706 · see citing works
Alushin, G. M., Lander, G. C., Kellogg, E. H., Zhang, R., Baker, D., & Nogales, E. (2014) · Cell · doi:10.1016/j.cell.2014.03.053 · Cited by 696 · see citing works
Xu, Y. Q., Piston, D. W., & Johnson, C. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.151 · Cited by 613 · see citing works
The fibronectin type III domain as a scaffold for novel binding proteins
Koide, A., Bailey, C. W., Huang, X., & Koide, S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2238 · Cited by 585 · see citing works
Dissecting protein–protein recognition sites
Chakrabarti, P., & Janin, J. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10085 · Cited by 571 · see citing works
Moerke, N., Aktas, H., Chen, H., Cantel, S., Reibarkh, M., Fahmy, A., Gross, J., Degterev, A., Yuan, J., Chorev, M., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.046 · Cited by 568 · see citing works
Core-binding factors in haematopoiesis and leukaemia
Speck, N. A., & Gilliland, D. G. (2002) · Nature reviews. Cancer · doi:10.1038/nrc840 · Cited by 563 · see citing works
How Ligands Illuminate GPCR Molecular Pharmacology
Wacker, D., Stevens, R. C., & Roth, B. L. (2017) · Cell · doi:10.1016/j.cell.2017.07.009 · Cited by 560 · see citing works
The role of nitric oxide in multiple sclerosis
Smith, K. J., & Lassmann, H. (2002) · The Lancet Neurology · doi:10.1016/s1474-4422(02)00102-3 · Cited by 531 · see citing works
Similarity of phylogenetic trees as indicator of protein–protein interaction
Pazos, F., & Valencia, A. (2001) · Protein Engineering Design and Selection · doi:10.1093/protein/14.9.609 · Cited by 521 · see citing works
Modulators of Protein–Protein Interactions
Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497 · see citing works
Molecular Mechanism of Action of Microtubule-Stabilizing Anticancer Agents
Prota, A. E., Bargsten, K., Zurwerra, D., Field, J. J., Díaz, J. F., Altmann, K., & Steinmetz, M. O. (2013) · Science · doi:10.1126/science.1230582 · Cited by 494 · see citing works
Site-directed ligand discovery
Erlanson, D. A., Braisted, A. C., Raphael, D. R., Randal, M., Stroud, R. M., Gordon, E. M., & Wells, J. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.17.9367 · Cited by 466 · see citing works
Hydrogen bonds and salt bridges across protein-protein interfaces
Xu, D., Tsai, C.-J., & Nussinov, R. (1997) · Protein Engineering Design and Selection · doi:10.1093/protein/10.9.999 · Cited by 457 · see citing works
The runx genes: gain or loss of function in cancer
Blyth, K., Cameron, E. R., & Neil, J. C. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1607 · Cited by 453 · see citing works
Lee, F. Y., Borzilleri, R. M., Fairchild, C. R., Kim, S., Long, B. H., Raventós-Suárez, C., Vite, G. D., Rose, W. C., & Kramer, R. A. (2001) · PubMed · Cited by 453 · see citing works
Disease-specific changes in regulator of G-protein signaling 4 (RGS4) expression in schizophrenia
Mirnics, K., Middleton, F. A., Stanwood, G. D., Lewis, D. A., & Levitt, P. (2001) · Molecular Psychiatry · doi:10.1038/sj.mp.4000866 · Cited by 446 · see citing works
Complex synthetic chemical libraries indexed with molecular tags.
Ohlmeyer, M. H. J., Swanson, R. N., Dillard, L. W., Reader, J. C., Asouline, G., KOBAYASHI, R., Wigler, M. H., & Still, W. C. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10922 · Cited by 445 · see citing works
Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability
Leuenberger, P., Ganscha, S., Kahraman, A., Cappelletti, V., Boersema, P. J., von Mering, C., Claassen, M., & Picotti, P. (2017) · Science · doi:10.1126/science.aai7825 · Cited by 413 · see citing works
Yusuf‐Makagiansar, H., Anderson, M. E., Yakovleva, T. V., Murray, J. S., & Siahaan, T. J. (2002) · Medicinal Research Reviews · doi:10.1002/med.10001 · Cited by 408 · see citing works
Mass Spectrometry–Based Proteomics and Network Biology
Bensimon, A., Heck, A. J. R., & Aebersold, R. H. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072909-100424 · Cited by 407 · see citing works
Regulators of G-Protein signalling as new central nervous system drug targets
Neubig, R. R., & Siderovski, D. P. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd747 · Cited by 403 · see citing works
Thorn, K. S., & Bogan, A. A. (2001) · Bioinformatics · doi:10.1093/bioinformatics/17.3.284 · Cited by 403 · see citing works
A Unified View of “How Allostery Works”
Tsai, C.-J., & Nussinov, R. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003394 · Cited by 401 · see citing works
Targeting protein–protein interactions as an anticancer strategy
Ivanov, A. A., Khuri, F. R., & Fu, H. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.04.007 · Cited by 401 · see citing works
An Approach to Spatiotemporally Resolve Protein Interaction Networks in Living Cells
Lobingier, B. T., Hüttenhain, R., Eichel, K., Miller, K. B., Ting, A. Y., von Zastrow, M., & Krogan, N. J. (2017) · Cell · doi:10.1016/j.cell.2017.03.022 · Cited by 401 · see citing works
Protein–protein interaction and quaternary structure
Janin, J., Bahadur, R. P., & Chakrabarti, P. (2008) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583508004708 · Cited by 400 · see citing works
Markman, M., & Mekhail, T. M. (2002) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.3.6.755 · Cited by 378 · see citing works
Sequence-based prediction of protein protein interaction using a deep-learning algorithm
Sun, T., Zhou, B., Lai, L., & Pei, J. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1700-2 · Cited by 376 · see citing works
Structure, function, and evolution of transient and obligate protein–protein interactions
Mintseris, J., & Weng, Z. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502667102 · Cited by 373 · see citing works
Ras Conformational Ensembles, Allostery, and Signaling
Lu, S., Jang, H., Muratcioglu, S., Gursoy, A., Keskin, O., Nussinov, R., & Zhang, J. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00542 · Cited by 355 · see citing works
Self-citationPhosphodiesterase 9A controls nitric-oxide-independent cGMP and hypertrophic heart disease
Lee, D. I., Zhu, G., Sasaki, T., Cho, G.-S., Hamdani, N., Holewinski, R., Jo, S.-H., Danner, T., Zhang, M., Rainer, P. P., et al. (2015) · Nature · doi:10.1038/nature14332 · Cited by 353 · see citing works
Avdulov, S. V., Li, S., Michalek, V. N., Burrichter, D., Peterson, M., Perlman, D., Manivel, J. C., Sonenberg, N., Yee, D., Bitterman, P. B., et al. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.05.024 · Cited by 341 · see citing works
Angers, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.060590697 · Cited by 341 · see citing works
Calculation of the free energy of association for protein complexes
Horton, N. C., & Lewis, M. (1992) · Protein Science · doi:10.1002/pro.5560010117 · Cited by 329 · see citing works
Allostery: an illustrated definition for the ‘second secret of life’
Fenton, A. W. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.05.009 · Cited by 320 · see citing works
Structure of the negative regulatory domain of p53 bound to S100B(betabeta).
Weber, D. J., Rust, R. R., & Baldisseri, D. M. (2000) · Nature Structural Biology · doi:10.1038/76797 · Cited by 313 · see citing works
Oncogenic protein interfaces: small molecules, big challenges
Nero, T. L., Morton, C. J., Holien, J. K., Wielens, J., & Parker, M. W. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3690 · Cited by 312 · see citing works
Tracey, W. R., Tse, J., & Carter, G. (1995) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)24521-9 · Cited by 310 · cited 1× · see citing works
“The results showed that the IC50 values for 18 against the dimerization of eNOS and nNOS were considerably higher than those for iNOS, which indicated that this compound specifically inhibited iNOS dimerization with a high potency.(190,191) Overall, the remarkable potency and isoform selectivity of 18 make it a starti…”
BackgroundMechanical Properties of the Cytoskeleton and CellsPreprint
Pegoraro, A. F., Janmey, P. A., & Weitz, D. A. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022038 · Cited by 301 · see citing works
The GRID: The General Repository for Interaction Datasets
Breitkreutz, B., Stark, C., & Tyers, M. (2003) · Genome biology · doi:10.1186/gb-2003-4-3-r23 · Cited by 294 · see citing works
BiGGER: A new (soft) docking algorithm for predicting protein interactions
Palma, P. N., Krippahl, L., Wampler, J. E., & Moura, J. J. G. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(20000601)39:4 · Cited by 292 · see citing works
Smith, M. C. P., & Gestwicki, J. E. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2012.10 · Cited by 285 · see citing works
Excitotoxicity and nitric oxide in parkinson's disease pathogenesis
Beal, M. F. (1998) · Annals of Neurology · doi:10.1002/ana.410440716 · Cited by 283 · see citing works
Inhibition of RAS function through targeting an allosteric regulatory site
Spencer-Smith, R., Koide, A., Zhou, Y., Eguchi, R. R., Sha, F., Gajwani, P., Santana, D., Gupta, A., Jacobs, M., Herrero-Garcia, E., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2231 · Cited by 283 · see citing works
Tan, Z., Xiao, L., Tang, M., Bai, F., Li, J., Li, L., Shi, F., Li, N., Li, Y., Du, Q., et al. (2018) · Theranostics · doi:10.7150/thno.21451 · Cited by 272 · see citing works
Tunçbağ, N., Gürsoy, A., Nussinov, R., & Keskin, Ö. (2011) · Nature Protocols · doi:10.1038/nprot.2011.367 · Cited by 264 · see citing works
Ruettinger, R. T., Wen, L., & Fulco, A. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60416-8 · Cited by 244 · see citing works
Mass spectrometry–based functional proteomics: from molecular machines to protein networks
Köcher, T., & Superti‐Furga, G. (2007) · Nature Methods · doi:10.1038/nmeth1093 · Cited by 240 · 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
The architecture of functional modules in the Hsp90 co‐chaperone Sti1/Hop
Schmid, A. B., Lagleder, S., Gräwert, M. A., Röhl, A., Hagn, F., Wandinger, S. K., Cox, M. B., Demmer, O., Richter, K., Groll, M., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2011.472 · Cited by 229 · see citing works
Allosite: a method for predicting allosteric sites
Huang, W., Lu, S., Huang, Z., Liu, X., Mou, L., Luo, Y., Zhao, Y., Liu, Y., Chen, Z., Hou, T., et al. (2013) · Bioinformatics · doi:10.1093/bioinformatics/btt399 · Cited by 227 · see citing works
Self-citationThe Structural Basis of Oncogenic Mutations G12, G13 and Q61 in Small GTPase K-Ras4B
Lu, S., Jang, H., Nussinov, R., & Zhang, J. (2016) · Scientific Reports · doi:10.1038/srep21949 · Cited by 219 · see citing works
Self-citationLifitegrast for the Treatment of Dry Eye Disease
Holland, E. J., Luchs, J., Karpecki, P. M., Nichols, K. K., Jackson, M. A., Sall, K. N., Tauber, J., Roy, M., Raychaudhuri, A., & Shojaei, A. (2016) · Ophthalmology · doi:10.1016/j.ophtha.2016.09.025 · Cited by 218 · see citing works
Analyzing Protein–Protein Interaction Networks
Koh, G. C. K. W., Porras, P., Aranda, B., Hermjakob, H., & Orchard, S. E. (2012) · Journal of Proteome Research · doi:10.1021/pr201211w · Cited by 209 · see citing works
Regulator of G Protein Signaling Proteins: Novel Multifunctional Drug Targets
Zhong, H., & Neubig, R. R. (2001) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)29606-3 · Cited by 208 · see citing works
Thiel, P., Kaiser, M., & Ottmann, C. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201107616 · Cited by 207 · see citing works
Baspinar, A., Cukuroglu, E., Nussinov, R., Keskin, Ö., & Gürsoy, A. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku397 · Cited by 201 · see citing works
McMillan, K., Adler, M., Auld, D. S., Baldwin, J. J., Blasko, E., Browne, L. J., Chelsky, D., Davey, D. D., Dolle, R. E., Eagen, K. A., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1506 · Cited by 200 · see citing works
Targeting Protein-Protein Interaction by Small Molecules
Jin, L., Wang, W., & Fang, G. (2014) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-140028 · Cited by 195 · see citing works
Lu, C., Shimaoka, M., Zang, Q. S., Takagi, J., & Springer, T. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041618598 · Cited by 192 · see citing works
Sinz, A. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201709559 · Cited by 192 · see citing works
Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view
Lu, S., Jang, H., Gu, S., Zhang, J., & Nussinov, R. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00911a · Cited by 188 · see citing works
Self-citationNitric oxide and inflammatory joint diseases
Stichtenoth, D. O., & Frölich, J. C. (1998) · Lara D. Veeken · doi:10.1093/rheumatology/37.3.246 · Cited by 180 · see citing works
Masters, B. S. S., McMillan, K., Sheta, E. A., Nishimura, J. S., Roman, L. J., & Pavel Martasek, E. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.5.8621055 · Cited by 180 · see citing works
Recent advances in microtubule-stabilizing agents
Cao, Y.-N., Zheng, L., Wang, D., Liang, X.-X., Gao, F., & Zhou, X. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.11.062 · Cited by 178 · see citing works
Allosteric Modulator Discovery: From Serendipity to Structure-Based Design
Lu, S., He, X., Ni, D., & Zhang, J. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01749 · Cited by 176 · see citing works
Self-citationGadek, T. R., Burdick, D. J., McDowell, R. S., Stanley, M. S., Marsters, J. C., Paris, K. J., Oare, D. A., Reynolds, M. E., Ladner, C., Zioncheck, K., et al. (2002) · Science · doi:10.1126/science.295.5557.1086 · Cited by 172 · see citing works
Joaquim Bellmunt, B., Szczylik, C. A., Feingold, J. M., Strahs, A. L., & Berkenblit, A. (2008) · Annals of Oncology · doi:10.1093/annonc/mdn066 · Cited by 170 · see citing works
Lu, S., Shen, Q., & Zhang, J. (2019) · Accounts of Chemical Research · doi:10.1021/acs.accounts.8b00570 · Cited by 166 · see citing works
Self-citationState-of-the-art strategies for targeting protein–protein interactions by small-molecule inhibitors
Sheng, C., Dong, G., Miao, Z., Zhang, W., & Wang, W. (2015) · Chemical Society Reviews · doi:10.1039/c5cs00252d · Cited by 165 · see citing works
Characterizing Protein–Protein Interactions Using Mass Spectrometry: Challenges and Opportunities
Smits, A. H., & Vermeulen, M. (2016) · Trends in biotechnology · doi:10.1016/j.tibtech.2016.02.014 · Cited by 162 · 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
The role of the integrin LFA‐1 in T‐lymphocyte migration
Smith, A. M., Stanley, P., Jones, K., Svensson, L. M., McDowall, A., & Hogg, N. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00537.x · Cited by 152 · see citing works
Improved Method for the Identification and Validation of Allosteric Sites
Song, K., Liu, X., Huang, W., Lu, S., Shen, Q., Zhang, L., & Zhang, J. (2017) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.7b00014 · Cited by 152 · see citing works
Self-citationAllosteric sites: remote control in regulation of protein activity
Guarnera, E., & Berezovsky, I. N. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.10.004 · Cited by 149 · see citing works
Harnessing Allostery: A Novel Approach to Drug Discovery
Lu, S., Li, S., & Zhang, J. (2014) · Medicinal Research Reviews · doi:10.1002/med.21317 · Cited by 146 · see citing works
Self-citationSmall Molecule Allosteric Modulators of G-Protein-Coupled Receptors: Drug–Target Interactions
Lu, S., & Zhang, J. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01844 · Cited by 144 · see citing works
Self-citationGuarnera, E., & Berezovsky, I. N. (2016) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004678 · Cited by 141 · see citing works
PARS: a web server for the prediction of Protein Allosteric and Regulatory Sites
Panjkovich, A., & Daura, X. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu002 · Cited by 139 · see citing works
The interaction of Ras with GTPase‐activating proteins
Wittinghofer, A., Scheffzek, K., & Ahmadian, M. R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00321-9 · Cited by 135 · see citing works
Shimaoka, M., Salas, A., Yang, W. Y., Weitz‐Schmidt, G., & Springer, T. A. (2003) · Immunity · doi:10.1016/s1074-7613(03)00238-3 · Cited by 135 · see citing works
Roman, D. L., Talbot, J. N., Roof, R. A., Sunahara, R. K., Traynor, J. R., & Neubig, R. R. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.028670 · Cited by 135 · see citing works
Last-Barney, K., Davidson, W. C., Cardozo, M. G., Frye, L. L., Grygon, C. A., Hopkins, J. L., Jeanfavre, D. D., Pav, S., Qian, C., Stevenson, J. M., et al. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0104249 · Cited by 131 · see citing works
Paclitaxel and docetaxel in the treatment of breast cancer
Saloustros, E. S., Mavroudis, D., & Georgoulias, V. (2008) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.9.15.2603 · Cited by 129 · see citing works
AlloSigMA: allosteric signaling and mutation analysis server
Guarnera, E., Tan, Z. W., Zheng, Z., & Berezovsky, I. N. (2017) · Bioinformatics · doi:10.1093/bioinformatics/btx430 · Cited by 129 · see citing works
Translating costimulation blockade to the clinic: lessons learned from three pathways
Ford, M. L., & Larsen, C. P. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2009.00776.x · Cited by 123 · see citing works
Recent advances in charting protein–protein interaction: mass spectrometry-based approaches
Gavin, A., Maeda, K., & Kühner, S. (2010) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.09.007 · Cited by 120 · see citing works
Mitra, A., & Sept, D. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.133884 · Cited by 119 · see citing works
Discovery of hidden allosteric sites as novel targets for allosteric drug design
Lu, S., Ji, M., Ni, D., & Zhang, J. (2017) · Drug Discovery Today · doi:10.1016/j.drudis.2017.10.001 · Cited by 118 · see citing works
Self-citationA small-molecule inhibitor of the aberrant transcription factor CBFβ-SMMHC delays leukemia in mice
Illendula, A., Pulikkan, J. A., Zong, H., Grembecka, J. E., Xue, L., Sen, S., Zhou, Y., Boulton, A. M., Kuntimaddi, A., Gao, Y., et al. (2015) · Science · doi:10.1126/science.aaa0314 · Cited by 114 · see citing works
Gorczynski, M. J., Grembecka, J. E., Zhou, Y., Kong, Y., Roudaia, L., Douvas, M. G., Newman, M. N., Bielnicka, I., Baber, G. B., Corpora, T., et al. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.09.006 · Cited by 114 · see citing works
Elevated levels of ΔFosB and RGS9 in striatum in Parkinson’s disease
Tekumalla, P. K., Calon, F., Rahman, Z. U., Birdi, S., Rajput, A. H., Hornykiewicz, O., Paolo, T. D., Bédard, P. J., & Nestler, E. J. (2001) · Biological Psychiatry · doi:10.1016/s0006-3223(01)01234-3 · Cited by 110 · see citing works
Cap‐Dependent Translation Initiation Factor e IF4E : An Emerging Anticancer Drug Target
Jia, Y., Polunovsky, V. A., Bitterman, P. B., & Wagner, C. R. (2012) · Medicinal Research Reviews · doi:10.1002/med.21260 · Cited by 109 · see citing works
Barile, E., & Pellecchia, M. (2014) · Chemical Reviews · doi:10.1021/cr500043b · Cited by 109 · see citing works
Paclitaxel for non-small cell lung cancer
Ramalingam, S., & Belani, C. P. (2004) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.5.8.1771 · Cited by 107 · see citing works
Liu, F., & Heck, A. J. R. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.10.006 · Cited by 107 · see citing works
Protein Domain Mimics as Modulators of Protein–Protein Interactions
Sawyer, N., Watkins, A. M., & Arora, P. S. (2017) · Accounts of Chemical Research · doi:10.1021/acs.accounts.7b00130 · Cited by 103 · see citing works
Zhong, M., Gadek, T. R., Bui, M., Wang, S., Burnier, J. P., Barr, K. J., Hanan, E. J., Oslob, J. D., Yu, C. H., Zhu, J., et al. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml2002482 · Cited by 102 · see citing works
Recent computational advances in the identification of allosteric sites in proteins
Lu, S., Huang, W., & Zhang, J. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.07.012 · Cited by 102 · see citing works
Self-citationSmall Molecule Inhibitor of CBFβ-RUNX Binding for RUNX Transcription Factor Driven Cancers
Illendula, A., Gilmour, J., Grembecka, J. E., Tirumala, V. S. S., Boulton, A. M., Kuntimaddi, A., Schmidt, C., Wang, L., Pulikkan, J. A., Zong, H., et al. (2016) · EBioMedicine · doi:10.1016/j.ebiom.2016.04.032 · Cited by 100 · see citing works
Peptidomimetic inhibitors of APC–Asef interaction block colorectal cancer migration
Jiang, H., Deng, R., Yang, X., Shang, J., Lu, S., Zhao, Y., Song, K., Liu, X., Zhang, Q., Chen, Y., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2442 · Cited by 100 · see citing works
Self-citationKengatharan, K. M., de Kimpe, S. J., & Thiemermann, C. (1996) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1996.tb16053.x · Cited by 99 · see citing works
IntPred: a structure-based predictor of protein–protein interaction sites
Northey, T. C., Barešić, A., & Martin, A. C. R. (2017) · Bioinformatics · doi:10.1093/bioinformatics/btx585 · Cited by 98 · see citing works
Alternative modulation of protein–protein interactions by small molecules
Fischer, G., Rossmann, M., & Hyvönen, M. (2015) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2015.04.006 · Cited by 97 · see citing works
Amici, M. D., Dallanoce, C., Holzgrabe, U., Tränkle, C., & Mohr, K. (2009) · Medicinal Research Reviews · doi:10.1002/med.20166 · Cited by 97 · see citing works
Papadopoulos, E., Jenni, S., Kabha, E., Takrouri, K., Yi, T., Salvi, N., Luna, R. E., Gavathiotis, E., Poornachandran, M., Arthanari, H., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1410250111 · Cited by 96 · see citing works
Allosteric Modulation: An Alternate Approach Targeting the Cannabinoid CB1 Receptor
Nguyen, T., Li, J., Thomas, B. F., Wiley, J. L., Kenakin, T., & Zhang, Y. (2016) · Medicinal Research Reviews · doi:10.1002/med.21418 · Cited by 95 · see citing works
AlloFinder: a strategy for allosteric modulator discovery and allosterome analyses
Huang, M., Song, K., Liu, X., Lu, S., Shen, Q., Wang, R., Gao, J., Hong, Y., Li, Q., Ni, D., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky374 · Cited by 92 · see citing works
Self-citationMarkowitz, J., Chen, I., Gitti, R. K., Baldisseri, D. M., Pan, Y., Udan, R. S., Carrier, F., MacKerell, A. D., & Weber, D. J. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0497038 · Cited by 91 · see citing works
Discovering cellular protein‐protein interactions: Technological strategies and opportunities
Titeca, K., Lemmens, I. H., Tavernier, J. H., & Eyckerman, S. (2018) · Mass Spectrometry Reviews · doi:10.1002/mas.21574 · Cited by 90 · see citing works
Chemical, Target, and Bioactive Properties of Allosteric Modulation
van Westen, G. J. P., Gaulton, A., & Overington, J. P. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003559 · Cited by 88 · see citing works
Chen, S., Hu, T., Zhang, J., Chen, J., Chen, K., Ding, J., Jiang, H., & Shen, X. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705240200 · Cited by 88 · see citing works
Self-citationThe concept of allosteric modulation: an overview
Changeux, J. (2012) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2012.07.007 · Cited by 86 · see citing works
Lu, S., Banerjee, A., Jang, H., Zhang, J., Gaponenko, V., & Nussinov, R. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.664755 · Cited by 86 · see citing works
Self-citationSmall molecule agents targeting the p53‐MDM2 pathway for cancer therapy
Wang, W., & Hu, Y. (2011) · Medicinal Research Reviews · doi:10.1002/med.20236 · Cited by 85 · see citing works
Target-Binding Proteins Based on the 10th Human Fibronectin Type III Domain (10Fn3)
Koide, S., Koide, A., & Lipovšek, D. (2012) · Methods in Enzymology · doi:10.1016/b978-0-12-396962-0.00006-9 · Cited by 84 · see citing works
Basse, M.-J., Betzi, S., Morelli, X., & Roche, P. (2016) · Database · doi:10.1093/database/baw007 · Cited by 83 · see citing works
Medicinal Chemistry Strategies to Disrupt the p53–MDM2/MDMX Interaction
Lemos, A., Leão, M., Soares, J., Palmeira, A., Pinto, M. M. M., Saraiva, L., & Sousa, M. E. (2016) · Medicinal Research Reviews · doi:10.1002/med.21393 · Cited by 83 · see citing works
Welzenbach, K., Hommel, U., & Weitz‐Schmidt, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110521200 · Cited by 81 · see citing works
Motions of Allosteric and Orthosteric Ligand-Binding Sites in Proteins are Highly Correlated
Ma, X., Meng, H., & Lai, L. (2016) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6b00039 · Cited by 81 · see citing works
Small molecule modulators of protein-protein interactions: selected case studies
Aeluri, M., Chamakuri, S., Dasari, B., Guduru, S. K. R., Jimmidi, R., Jogula, S., & Arya, P. (2014) · Chemical Reviews · doi:10.1021/cr4004049 · Cited by 79 · see citing works
Mignani, S. M., Kazzouli, S. E., Bousmina, M., & Majoral, J. (2013) · Chemical Reviews · doi:10.1021/cr400362r · Cited by 78 · see citing works
Bai, F., Morcos, F., Cheng, R. R., Jiang, H., & Onuchic, J. N. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615932113 · Cited by 76 · see citing works
Paclitaxel With and Without Pazopanib for Persistent or Recurrent Ovarian Cancer
Richardson, D. L., Sill, M. W., Coleman, R. L., Sood, A. K., Pearl, M. L., Kehoe, S. M., Carney, M. E., Hanjani, P., Le, L. V., Zhou, X. C., et al. (2017) · JAMA Oncology · doi:10.1001/jamaoncol.2017.4218 · Cited by 74 · see citing works
Inhibitors of Ras–SOS Interactions
Lu, S., Jang, H., Zhang, J., & Nussinov, R. (2016) · ChemMedChem · doi:10.1002/cmdc.201500481 · Cited by 72 · see citing works
Self-citationSjögren, B., & Neubig, R. R. (2010) · Molecular Pharmacology · doi:10.1124/mol.110.065219 · Cited by 71 · see citing works
Akasaka, K., Tamada, M., Wang, F., Kariya, K.-I., Shima, F., Kikuchi, A., Yamamoto, M., Shirouzu, M., Yokoyama, S., & Kataoka, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5353 · Cited by 69 · see citing works
The Mechanism of ATP-Dependent Allosteric Protection of Akt Kinase Phosphorylation
Lu, S., Deng, R., Jiang, H., Song, H., Li, S., Shen, Q., Huang, W., Nussinov, R., Yu, J., & Zhang, J. (2015) · Structure · doi:10.1016/j.str.2015.06.027 · Cited by 69 · see citing works
Self-citationAltered affinity of CBFβ-SMMHC for Runx1 explains its role in leukemogenesis
Lukasik, S. M., Zhang, L., Corpora, T., Tomanicek, S., Li, Y., Kundu, M., Hartman, K. L., Liu, P., Laue, T. M., Biltonen, R. L., et al. (2002) · Nature Structural Biology · doi:10.1038/nsb831 · Cited by 67 · see citing works
Bromley, S. K., & Dustin, M. L. (2002) · Immunology · doi:10.1046/j.1365-2567.2002.01441.x · Cited by 63 · see citing works
The Elephant in the Room: The Role of Microtubules in Cancer
Cirillo, L., Gotta, M., & Meraldi, P. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-57127-0_5 · Cited by 63 · see citing works
Bresciani, E., Carrington, B., Wincovitch, S., Jones, M. S., Gore, A. V., Weinstein, B. M., Sood, R. B., & Liu, P. (2014) · Blood · doi:10.1182/blood-2013-10-531988 · Cited by 59 · see citing works
Direct and Propagated Effects of Small Molecules on Protein–Protein Interaction Networks
Cesa, L. C., Mapp, A. K., & Gestwicki, J. E. (2015) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2015.00119 · Cited by 58 · see citing works
Wang, Q., Liu‐Chen, L., & Traynor, J. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.015453 · Cited by 57 · see citing works
Silvian, L. F., Friedman, J. E., Strauch, K., Cachero, T. G., Day, E. S., Qian, F., Cunningham, B. C., Fung, A. D., Sun, L., Su, L., et al. (2011) · ACS Chemical Biology · doi:10.1021/cb2000346 · Cited by 57 · see citing works
Microtubule actin cross‐linking factor 1, a novel potential target in cancer
Miao, Z., Ali, A., Hu, L., Zhao, F., Yin, C., Chen, C., Yang, T., & Qian, A. (2017) · Cancer Science · doi:10.1111/cas.13344 · Cited by 57 · see citing works
Identifying Allosteric Hotspots with Dynamics: Application to Inter- and Intra-species Conservation
Clarke, D., Sethi, A., Li, S., Kumar, S., Chang, R. W. F., Chen, J., & Gerstein, M. (2016) · Structure · doi:10.1016/j.str.2016.03.008 · Cited by 56 · see citing works
TOWARDS THE PREDICTION OF COMPLETE PROTEIN–PROTEIN INTERACTION NETWORKS
Gomez, S. M., & Rzhetsky, A. (2001) · Pacific Symposium on Biocomputing (PSB) · doi:10.1142/9789812799623_0039 · Cited by 55 · see citing works
Stabilization of protein–protein interactions by small molecules
Giordanetto, F., Schäfer, A., & Ottmann, C. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.08.005 · Cited by 55 · see citing works
Protein‐protein interactions as antibiotic targets: A medicinal chemistry perspective
Cossar, P. J., Lewis, P. J., & McCluskey, A. (2020) · Medicinal Research Reviews · doi:10.1002/med.21519 · Cited by 55 · see citing works
Designed covalent allosteric modulators: an emerging paradigm in drug discovery
Lu, S., & Zhang, J. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.11.013 · Cited by 53 · see citing works
Self-citationRecent advances in postmortem pathology and neurochemistry in schizophrenia
Dean, B., Boer, S., Gibbons, A. S., Money, T., & Scarr, E. (2009) · Current Opinion in Psychiatry · doi:10.1097/yco.0b013e328323d52e · Cited by 51 · see citing works
Methods for analyzing and quantifying protein–protein interaction
Syafrizayanti, S., Betzen, C., Hoheisel, J. D., & Kastelic, D. (2014) · Expert Review of Proteomics · doi:10.1586/14789450.2014.875857 · Cited by 51 · see citing works
Potin, D., Launay, M., Monatlik, F., Malabre, P., Fabreguettes, M., Fouquet, A., Maillet, M., Nicolaï, E., Dorgeret, L., Chevallier, F., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm0610806 · Cited by 51 · see citing works
The RGS protein inhibitor CCG-4986 is a covalent modifier of the RGS4 Gα-interaction face
Kimple, A. J., Willard, F. S., Giguère, P. M., Johnston, C. A., Mocanu, V., & Siderovski, D. P. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.06.002 · Cited by 50 · see citing works
The Yeast Two-Hybrid System: A Tool for Mapping Protein–Protein InteractionsPreprint
Mehla, J., Caufield, J. H., & Uetz, P. H. (2015) · Cold Spring Harbor Protocols · doi:10.1101/pdb.top083345 · Cited by 50 · see citing works
Wu, M., Li, C., Zhu, G., Wang, Y., Jules, J., Lü, Y., McConnell, M., Wang, Y., Shao, J., Li, Y.-P., et al. (2014) · Bone · doi:10.1016/j.bone.2014.04.031 · Cited by 50 · see citing works
Small Molecule Inhibitors of Regulators of G Protein Signaling (RGS) Proteins
Turner, E. M., Blazer, L. L., Neubig, R. R., & Husbands, S. M. (2011) · ACS Medicinal Chemistry Letters · doi:10.1021/ml200263y · Cited by 48 · see citing works
Strategies to Develop Inhibitors of Motif-Mediated Protein-Protein Interactions as Drug Leads
Corbi‐Verge, C., Garton, M., Nim, S., & Kim, P. M. (2016) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104805 · Cited by 48 · see citing works
3D-partner: a web server to infer interacting partners and binding models
Chen, Y.-C., Lo, Y., Hsu, W.-C., & Yang, J. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm346 · Cited by 46 · see citing works
Therapeutic Antagonists and the Conformational Regulation of the β2 Integrins
Shimaoka, M., & Springer, T. A. (2004) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026043387575 · Cited by 44 · see citing works
Ding, L., & Hegde, A. N. (2008) · Biological Psychiatry · doi:10.1016/j.biopsych.2008.10.026 · Cited by 43 · see citing works
Watterson, S. H., Xiao, Z., Dodd, D. S., Tortolani, D. R., Vaccaro, W. D., Potin, D., Launay, M., Stetsko, D. K., Skala, S., Davis, P. M., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100348u · Cited by 43 · see citing works
Özdemir, E. S., Jang, H., Gürsoy, A., Keskin, Ö., Li, Z., Sacks, D. B., & Nussinov, R. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001596 · Cited by 43 · see citing works
Zampanolide and dactylolide: cytotoxic tubulin-assembly agents and promising anticancer leads
Chen, Q., & Kingston, D. G. I. (2014) · Natural Product Reports · doi:10.1039/c4np00024b · Cited by 42 · see citing works
Toward understanding the molecular basis for chemical allosteric modulator design
Wang, Q., Zheng, M., Huang, Z., Liu, X., Zhou, H., Chen, Y., Shi, T., & Zhang, J. (2012) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2012.07.006 · Cited by 40 · see citing works
Self-citationRoman, D. L., Blazer, L. L., Monroy, C. A., & Neubig, R. R. (2010) · Molecular Pharmacology · doi:10.1124/mol.109.063388 · Cited by 40 · see citing works
Roman, D. L., Ota, S., & Neubig, R. R. (2009) · SLAS DISCOVERY · doi:10.1177/1087057109336590 · Cited by 40 · see citing works
Mo, X., Luo, Y., Ivanov, A. A., Su, R., Havel, J. J., Li, Z., Khuri, F. R., Du, Y., & Fu, H. (2015) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjv064 · Cited by 40 · see citing works
Bioluminescence Resonance Energy Transfer to Detect Protein-Protein Interactions in Live Cells
Brown, N. E., Blumer, J., & Hepler, J. R. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2425-7_30 · Cited by 37 · see citing works
Vashisth, H., Storaska, A. J., Neubig, R. R., & Brooks, C. L. (2013) · ACS Chemical Biology · doi:10.1021/cb400568g · Cited by 35 · see citing works
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Rational Design of Peptide-Based Inhibitors Disrupting Protein-Protein Interactions
Wang, X., Ni, D., Liu, Y., & Lu, S. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.682675 · Cited by 153 · see citing works
Self-citationNi, D., Wei, J., He, X., Rehman, A. U., Li, X., Qiu, Y., Pu, J., Lu, S., & Zhang, J. (2020) · Chemical Science · doi:10.1039/d0sc05131d · Cited by 137 · see citing works
Self-citationSequence-based drug design as a concept in computational drug design
Chen, L., Fan, Z., Chang, J., Yang, R., Hou, H., Guo, H., Zhang, Y., Yang, T., Zhou, C., Sui, Q., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39856-w · Cited by 129 · see citing works
Allosteric drugs and mutations: chances, challenges, and necessity
Guarnera, E., & Berezovsky, I. N. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.01.010 · Cited by 117 · see citing works
Lin, S., Lin, S., Hsu, J.-N., Chang, C., Chien, C., Wang, Y., Wu, H., Jeng, U., Kehn‐Hall, K., & Hou, M. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01913 · Cited by 108 · see citing works
Strategies for targeting undruggable targets
Zhang, G., Zhang, J., Gao, Y., Li, Y., & Li, Y. (2021) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2021.1969359 · Cited by 102 · see citing works
Self-citationMechanism of allosteric activation of SIRT6 revealed by the action of rationally designed activators
Lu, S., Chen, Y.-Y., Wei, J., Zhao, M., Ni, D., He, X., & Zhang, J. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.09.010 · Cited by 93 · see citing works
Self-citationNew drug discovery and development from natural products: Advances and strategies
Wang, Y., Wang, F., Liu, W., Geng, Y., Shi, Y., Yu, T., Zhang, B., Luo, Y., & Sun, X. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108752 · Cited by 96 · see citing works
Combining Allosteric and Orthosteric Drugs to Overcome Drug Resistance
Ni, D., Li, Y., Qiu, Y., Pu, J., Lu, S., & Zhang, J. (2020) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.02.001 · Cited by 91 · see citing works
Self-citationFight against novel coronavirus: A perspective of medicinal chemists
Amin, S. A., & Jha, T. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112559 · Cited by 80 · see citing works
Drugging K-RasG12C through covalent inhibitors: Mission possible?
Ni, D., Li, X., He, X., Zhang, H., Zhang, J., & Lu, S. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.06.007 · Cited by 73 · see citing works
Self-citationImpact of Allosteric Modulation in Drug Discovery: Innovation in Emerging Chemical Modalities
Han, B., Salituro, F. G., & Blanco, M.-J. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00655 · Cited by 74 · see citing works
ASD2023: towards the integrating landscapes of allosteric knowledgebase
He, J., Liu, X., Zhu, C., Zha, J., Li, Q., Zhao, M., Wei, J., Li, M., Wu, C., Wang, J., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad915 · Cited by 68 · see citing works
Self-citationAlong the allostery stream: Recent advances in computational methods for allosteric drug discovery
Ni, D., Chai, Z., Wang, Y., Li, M., Yu, Z., Liu, Y., Lu, S., & Zhang, J. (2021) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1585 · Cited by 67 · see citing works
Self-citationSmall molecules targeting protein–protein interactions for cancer therapy
Wu, D., Li, Y., Zheng, L., Xiao, H., Ouyang, L., Wang, G., & Sun, Q. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.05.035 · Cited by 71 · see citing works
Current Challenges and Opportunities in Designing Protein–Protein Interaction Targeted Drugs
Shin, W., Kumazawa, K., Imai, K., Hirokawa, T., & Kihara, D. (2020) · Advances and Applications in Bioinformatics and Chemistry · doi:10.2147/aabc.s235542 · Cited by 65 · see citing works
Fragment-based drug discovery supports drugging ‘undruggable’ protein–protein interactions
Wang, Z.-Z., Shi, X.-X., Huang, G.-Y., Hao, G., & Yang, G. (2023) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.01.008 · Cited by 64 · see citing works
Sun, S., Wu, S.-H., Kang, J.-B., Ma, Y.-Y., Chen, L., Cao, P., Chang, L., Ding, N., Xue, X., Li, N., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00030 · Cited by 53 · see citing works
Exploring the Allosteric Territory of Protein Function
Tee, W.-V., Tan, Z. W., Lee, K., Guarnera, E., & Berezovsky, I. N. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c00540 · Cited by 50 · see citing works
Advancing Targeted Protein Degradation via Multiomics Profiling and Artificial Intelligence
Duran-Frigola, M., Cigler, M., & Winter, G. E. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c11098 · Cited by 50 · see citing works
Yang, Y., Wang, K., Chen, H., & Feng, Z. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.113001 · Cited by 48 · see citing works
Harnessing Reversed Allosteric Communication: A Novel Strategy for Allosteric Drug Discovery
Fan, J., Liu, Y., Kong, R., Ni, D., Yu, Z., Lu, S., & Zhang, J. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01695 · Cited by 41 · see citing works
Self-citationComputational methods-guided design of modulators targeting protein-protein interactions (PPIs)
Qiu, Y., Li, X., He, X., Pu, J., Zhang, J., & Lu, S. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112764 · Cited by 41 · see citing works
Self-citationInsight into the mechanism of allosteric activation of PI3Kα by oncoprotein K-Ras4B
Li, X., Dai, J., Ni, D., He, X., Zhang, H., Zhang, J., Fu, Q., Liu, Y., & Lu, S. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.12.020 · Cited by 38 · see citing works
Self-citationComputational elucidation of allosteric communication in proteins for allosteric drug design
Ni, D., Liu, Y., Kong, R., Yu, Z., Lu, S., & Zhang, J. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.03.012 · Cited by 34 · see citing works
Self-citationRecent Discovery and Development of Inhibitors that Target CDK9 and Their Therapeutic Indications
Zhang, Y., Shan, L., Tang, W., Ge, Y., Li, C., & Zhang, J. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00312 · Cited by 31 · see citing works
Self-citationThe role of genomics and proteomics in drug discovery and its application in pharmacy
Dogiparthi, L. K., Bukke, S. P. N., Thalluri, C., Thalamanchi, B., Vidya, K. P., Sree, G. N., Tatiparthi, H., Uppicherla, D., & Thummaginjala, K. P. (2025) · Discover Applied Sciences · doi:10.1007/s42452-025-07155-2 · Cited by 35 · see citing works
Natural allosteric modulators and their biological targets: molecular signatures and mechanisms
Bruder, M., Polo, G., & Trivella, D. B. B. (2020) · Natural Product Reports · doi:10.1039/c9np00064j · Cited by 30 · see citing works
Li, M.-Y., Wang, Y., Fan, J., Zhuang, H., Liu, Y., Ji, D., & Lu, S. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167730 · Cited by 31 · see citing works
Self-citationGuo, X.-Y., Yi, L., Yang, J., An, H., Yang, Z., & Wang, H. (2024) · Chemical Communications · doi:10.1039/d3cc05811e · Cited by 30 · see citing works
Yang, P., Zhu, Y., Zheng, Q., Meng, S., Wu, Y., Wen, S., Sun, Q., & Wang, G. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114789 · Cited by 30 · see citing works
Networks of Networks: An Essay on Multi-Level Biological Organization
Uversky, V. N., & Giuliani, A. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.706260 · Cited by 28 · see citing works
Protein–protein interaction and non-interaction predictions using gene sequence natural vector
Zhao, N., Zhuo, M., Tian, K., & Gong, X. (2022) · Communications Biology · doi:10.1038/s42003-022-03617-0 · Cited by 29 · see citing works
Applications of Solution NMR in Drug Discovery
Li, S., & Zhang, N. (2021) · Molecules · doi:10.3390/molecules26030576 · Cited by 26 · see citing works
Zhang, Z., Zhao, L., Wang, J., & Wang, C. (2024) · IEEE Journal of Biomedical and Health Informatics · doi:10.1109/jbhi.2024.3384238 · Cited by 25 · see citing works
A novel class of selective non-nucleoside inhibitors of human DNA methyltransferase 3A
Huang, S., Stillson, N. J., Sandoval, J. E., Yung, C., & Reich, N. O. (2021) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2021.127908 · Cited by 24 · see citing works
Gao, G., Li, J., Cao, Y., Li, X., Qian, Y., Wang, X., Li, M., Qiu, Y., Wu, T., Wang, L., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115858 · Cited by 24 · see citing works
Afonso, A. L., Cavaleiro, C. T., Castanho, M. A. R. B., Neves, V., & Cavaco, M. C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073117 · Cited by 23 · see citing works
Astl, L., & Verkhivker, G. M. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.07.008 · Cited by 21 · see citing works
Prediction and targeting of GPCR oligomer interfaces
Barreto, C. A. V., Baptista, S. J., Preto, A. J., Matos‐Filipe, P., Mourão, J., Melo, R., & Moreira, I. S. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.11.007 · Cited by 22 · see citing works
Dong, G., Zuo, J.-H., Yu, J., Xu, J., Gao, G., Li, G., Zhao, W. H., & Yu, B. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c02028 · Cited by 19 · see citing works
Trisciuzzi, D., Villoutreix, B. O., Siragusa, L., Baroni, M., Cruciani, G., & Nicolotti, O. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2218641 · Cited by 19 · see citing works
He, X., Huang, N., Qiu, Y., Zhang, J., Liu, Y., Yin, X., & Lu, S. (2021) · Molecules · doi:10.3390/molecules26040962 · Cited by 18 · see citing works
Self-citationHsu, J.-N., Chen, J., Lin, S., Hong, J.-Y., Chen, Y.-J., Jeng, U., Luo, S., & Hou, M. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.871499 · Cited by 18 · see citing works
Ju, H., Kim, K., Kim, B. I., & Woo, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020698 · Cited by 17 · see citing works
Liu, X., Tian, W., Cheng, J., Li, D., Liu, T., & Zhang, L. (2019) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2019.107194 · Cited by 17 · see citing works
Interface-aware molecular generative framework for protein–protein interaction modulators
Wang, J., Mao, J., Li, C., Xiang, H., Wang, X., Wang, S., Wang, Z., Chen, Y., Li, Y., No, K. T., et al. (2024) · Journal of Cheminformatics · doi:10.1186/s13321-024-00930-0 · Cited by 16 · see citing works
Extended Applications of Small-Molecule Covalent Inhibitors toward Novel Therapeutic Targets
Lee, J., & Park, S. B. (2022) · Pharmaceuticals · doi:10.3390/ph15121478 · Cited by 15 · see citing works
Zuo, K., Kranjc, A., Capelli, R., Rossetti, G., Nechushtai, R., & Carloni, P. (2023) · Physical Chemistry Chemical Physics · doi:10.1039/d3cp01388j · Cited by 15 · see citing works
Targeting cyclin-dependent kinases: From pocket specificity to drug selectivity
Huang, Y., Liu, W., Zhao, C., Shi, X., Zhao, Q., Jia, J., & Wang, A. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116547 · Cited by 17 · see citing works
Wei, J., Chen, F., Lu, X., Fan, J., Li, M., Huang, J., Liu, N., Zhang, J., Chai, Z., & Lu, S. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143324 · Cited by 14 · see citing works
Self-citationBarthel, T., Wollenhaupt, J., Lima, G. M. A., Wahl, M. C., & Weiss, M. S. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01165 · Cited by 14 · see citing works
Zhou, H., Shan, M., Qin, L., & Cheng, G. (2022) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2022.106379 · Cited by 13 · see citing works
Autopromotion of K-Ras4B Feedback Activation Through an SOS-Mediated Long-Range Allosteric Effect
He, X., Du, K., Wang, Y., Fan, J., Li, M., Ni, D., Lu, S., Bian, X., & Liu, Y. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.860962 · Cited by 13 · see citing works
Self-citationMeewan, I., Panmanee, J., Petchyam, N., & Lertvilai, P. (2024) · Scientific Reports · doi:10.1038/s41598-024-59933-4 · Cited by 13 · see citing works
Alvarado, W., Pérez-Lemus, G. R., Menéndez, C. A., Byléhn, F., & Pablo, J. (2021) · Molecular Systems Design & Engineering · doi:10.1039/d1me00119a · Cited by 13 · see citing works
Handling complexity in biological interactions
Vega, S., Abián, O., & Velázquez‐Campoy, A. (2019) · Journal of Thermal Analysis and Calorimetry · doi:10.1007/s10973-019-08610-0 · Cited by 13 · see citing works
Bao, Y., Xu, Y., Jia, F., Li, M., Xu, R., Zhang, F., & Guo, J. (2023) · Pest Management Science · doi:10.1002/ps.7699 · Cited by 12 · see citing works
Hu, K., Li, X., Asmamaw, M. D., Shi, X., & Liu, H. (2021) · Scientific Reports · doi:10.1038/s41598-021-00646-3 · Cited by 12 · see citing works
Hadi‐Alijanvand, H., Paola, L. D., Hu, G., Leitner, D. M., Verkhivker, G. M., Sun, P., Poudel, H., & Giuliani, A. (2022) · ACS Omega · doi:10.1021/acsomega.2c00154 · Cited by 12 · see citing works
Probing GPCR Dimerization Using Peptides
Farooq, Z., Howell, L. A., & McCormick, P. J. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.843770 · Cited by 10 · see citing works
Assessing the binding properties of <scp>CASP14</scp> targets and models
Egbert, M., Ghani, U., Ashizawa, R., Kotelnikov, S., Nguyen, T., Desta, I., Hashemi, N., Padhorny, D., Kozakov, D., & Vajda, S. (2021) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26209 · Cited by 10 · see citing works
Role of protein-protein interactions in allosteric drug design for DNA methyltransferases
Liang, Z. T., Zhu, Y., Liu, X., & Hu, G. (2020) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.12.005 · Cited by 10 · see citing works
Natural Product Modulators of Protein–Protein Interactions: A Comprehensive Review
Kamel, E. M., Allam, A. A., Rudayni, H. A., Alkhayl, F. F. A., Ahmed, N. A., & Lamsabhi, A. M. (2026) · Phytochemical Analysis · doi:10.1002/pca.70054 · Cited by 9 · see citing works
Kusova, A. M., Rakipov, I. T., & Zuev, Y. F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241311148 · Cited by 8 · see citing works
A Structure-Based Allosteric Modulator Design Paradigm
Li, M., Lan, X., Lu, X., & Zhang, J. (2023) · Health Data Science · doi:10.34133/hds.0094 · Cited by 7 · see citing works
Self-citationXu, Q., Liu, W., Liu, H., & Zheng, Z. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c00387 · Cited by 8 · see citing works
Protein-protein complexes as targets for drug discovery against infectious diseases
Akhter, Y., & Hussain, R. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.11.012 · Cited by 7 · see citing works
Fu, T., Zhang, H., & Zheng, Q. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c01264 · Cited by 7 · see citing works
Li, X., Li, B., Li, J., Yang, M., Bai, Y., Chen, K., Chen, K., & Mao, N. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1104942 · Cited by 6 · see citing works
Balkrishna, A., Sharma, D., Thapliyal, M., Arya, V., & Dabas, A. (2023) · In Silico Pharmacology · doi:10.1007/s40203-023-00179-9 · Cited by 6 · see citing works
Schreiber, S., & Jose, J. (2024) · Cells · doi:10.3390/cells13221858 · Cited by 5 · see citing works
A Bridge to Alkaloid Synthesis
Zhai, L., Tang, Y. H., Zhang, Y., Huang, S., Zhu, L., & Hong, R. (2021) · The Chemical Record · doi:10.1002/tcr.202100197 · Cited by 5 · see citing works
Descoberta de fármacos a partir de produtos naturais e a abordagem Molecular Power House (MPH)
Trivella, D. B. B., Bruder, M., Oliveira, F. C. B., Porcaro, R., Rustiguel, J. K. R., Ribeiro, L. B., de Felício, R., da Cunha, M. G., Nascimento, A. F. Z., Zeri, A. C. D. M., et al. (2022) · Revista Fitos · doi:10.32712/2446-4775.2022.1346 · Cited by 5 · see citing works
Mou, L., Ma, Z., Meng, X., Li, W., Liang, S., & Chen, X. (2020) · Medicinal Chemistry Research · doi:10.1007/s00044-020-02514-7 · Cited by 5 · see citing works
Teimouri, H., Haghighijoo, Z., Baumgartner, T. J., Singh, A. K., Wadsworth, P. A., Zhang, C., Chen, H., Zhou, J., & Laezza, F. (2025) · Journal of Cheminformatics · doi:10.1186/s13321-025-01122-0 · Cited by 4 · see citing works
Directional Engineering of Cyclic β-Hairpin Peptides for PET/CT Imaging of PD-L1
Liu, C., Zhang, S., Chen, J., Geng, H. R., Li, H., Zhang, Z., Lu, Q., Xu, L., Li, J., Zhang, H., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c21595 · Cited by 4 · see citing works
Advanced nanotechnologies for protein modulation: From Nano-PROTAC to Nano-APROM
Wang, J., Hu, X., Zhang, J., Wang, C., Dai, H., Lu(杨露), Y., Li, F., & Ling, D. (2026) · Journal of Controlled Release · doi:10.1016/j.jconrel.2026.114901 · Cited by 4 · see citing works
Self-citationComputational investigation of a ternary model of SnoN-SMAD3-SMAD4 complex
Ji, M., Ding, Y., Li, X., Mao, N., & Chen, J. (2019) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2019.107159 · Cited by 4 · see citing works
Silva, K. S. F. E., Lima, R. M., Lima, P. D. S., Baeza, L. C., da Silva, R. A., Soares, C. M. D. A., & Pereira, M. (2020) · Journal of Fungi · doi:10.3390/jof6040309 · Cited by 4 · see citing works
Fancher, A. T., Hua, Y., Close, D. A., Xu, W., McDermott, L. A., Strock, C. J., Santiago, U., Camacho, C. J., & Johnston, P. A. (2023) · SLAS DISCOVERY · doi:10.1016/j.slasd.2023.08.001 · Cited by 4 · see citing works
Lawson, A. D. G., MacCoss, M., Baeten, D., Macpherson, A., Shi, J., & Henry, A. J. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.668186 · Cited by 4 · see citing works
Wang, Y., & Wang, X. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2198699 · Cited by 4 · see citing works
Discovery of Bioactive Peptides Through Peptide Scanning
Iaculli, D., & Ballet, S. (2025) · Journal of Peptide Science · doi:10.1002/psc.70029 · Cited by 3 · see citing works
Lombardi, L., Granger, L. A., Shattock, R. J., & Williams, D. R. (2024) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.4c02178 · Cited by 3 · see citing works
Wu, L., Su, L., Deng, M., Hong, X., Wu, M., Zhang, M., Bouveret, E., & Yan, X. (2021) · Talanta · doi:10.1016/j.talanta.2021.122549 · Cited by 3 · see citing works
Yang, Y., Xu, M., Wang, K., Xia, L., Ning, Q., Wu, X., Zang, X., Lai, F., Chen, X., & Feng, Z. (2025) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2025.118366 · Cited by 1 · see citing works
Computational Structural Modeling to Discover PPI Modulators
Yang, X., & Ivanov, A. A. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781788016544-00087 · Cited by 1 · see citing works
Lu, B., Peng, Y., Shao, Q., Mao, L., & Qiao, H. (2022) · Birth Defects Research · doi:10.1002/bdr2.2002 · Cited by 1 · see citing works
Franco, H. E. O., Le, A. V., Chang, N. Y., & Hartman, M. C. T. (2023) · ChemBioChem · doi:10.1002/cbic.202300020 · Cited by 1 · see citing works
Wang, J., Ma, Y., Li, J., Zhang, Q., Pan, X., Lu, W. Z., & Zhang, J. (2021) · Drug Development Research · doi:10.1002/ddr.21866 · Cited by 1 · see citing works
Self-citationDrug design and repurposing with a sequence-to-drug paradigmPreprint
Chen, L., Fan, Z., Chang, J., Yang, R., Guo, H., Zhang, Y., Yang, T., Zhou, C., Chen, Z., Zheng, C., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.26.485909 · Cited by 1 · see citing works
Handling complexity in biological interactions: Allostery and cooperativity in proteins
Vega, S., Abián, O., & Velázquez‐Campoy, A. (2019) · DIGITAL.CSIC (Spanish National Research Council (CSIC))
Assay Development and High‐Throughput Screening
Carettoni, D., & Bader, B. (2021) · Burger's Medicinal Chemistry and Drug Discovery · doi:10.1002/0471266949.bmc165.pub2
(FAB01_033) The English Benedictine Connection - The Works of Charles Hansom in Australia
Andrews, B. (1989) · Fabrications
Doller, D. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00057-8
Research progress in small-molecule modulators of protein-protein interactions
Yang, B., & Qi, X. (2023) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/tb-2023-0034
Multi-scale Global Consistency Residue Feature Enhancement based Protein Structure Analysis
Li, Q., Du, B. Q., Qin, X. L., Zhang, J., & Xu, S. B. (2023) · International Conference on Communication and Information Processing (ICCIP) · doi:10.1145/3638884.3638889
Self-citationWaaje, A., Sarkar, M. S., & Islam, M. Z. (2024) · medRxiv · doi:10.1101/2024.09.10.24313452
Kuang, Z.-J., Li, Y.-K., Liu, Z., Zhao, J., Shi, L.-J., Akira-Kawai, & Wang, H. (2025) · bioRxiv · doi:10.1101/2025.05.23.655070
- Authors
- Ni, D., Lu, S., & Zhang, J.
- Affiliations
- Shanghai Jiao Tong University (CN)
- Corresponding author
- Lu, Shaoyong
- Zhang, Jian
- Venue
- Medicinal Research Reviews
- Publisher
- Wiley
- Published
- 2019-04-07
- Volume
- 39
- Issue
- 6
- Pages
- 2314-2342
- ISSN
- 0198-6325 (ISSN-L)
- 1098-1128
- OpenAlex
- W2939052792
- Cited by
- 116
- References
- 227
- Citations by year
- 2026: 10 · 2025: 15 · 2024: 13 · 2023: 17 · 2022: 18 · 2021: 18 · 2020: 16 · 2019: 8
- FWCI
- 1.39
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Medicinal Research Reviews (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (91753117, 81473137, 81322046, 21778037, 81603023)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Physical Sciences › Computer Science › Computational Theory and Mathematics › Computational Drug Discovery Methods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- protein-protein interaction, allosteric modulators, allosteric regulation, PPI inhibitors, undruggable targets, allosteric site, computer-aided drug design
- MeSH terms
- Allosteric Regulation, Allosteric Site, Animals, Humans, Protein Binding, GTP-Binding Proteins, Protein Interaction Mapping, Drug Discovery
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