KLIFS: A Knowledge-Based Structural Database To Navigate Kinase–Ligand Interaction Space

The protein kinase complement of the human genome

Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145

BAY 43-9006 Exhibits Broad Spectrum Oral Antitumor Activity and Targets the RAF/MEK/ERK Pathway and Receptor Tyrosine Kinases Involved in Tumor Progression and Angiogenesis

Wilhelm, S. M., Carter, C., Tang, L., Wilkie, D., McNabola, A., Rong, H., Chen, C., Zhang, X., Vincent, P., McHugh, M., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1443 · Cited by 4,017

Targeting cancer with small molecule kinase inhibitors

Zhang, J., Yang, P. L., & Gray, N. S. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2559 · Cited by 2,576

A quantitative analysis of kinase inhibitor selectivity

Karaman, M. W., Herrgard, S., Treiber, D. K., Gallant, P., Atteridge, C. E., Campbell, B. T., Chan, K. W., Ciceri, P., Davis, M. I., Edeen, P. T., et al. (2008) · Nature Biotechnology · doi:10.1038/nbt1358 · Cited by 2,466

Comprehensive analysis of kinase inhibitor selectivity

Davis, M. I., Hunt, J. P., Herrgard, S., Ciceri, P., Wodicka, L. M., Pallares, G., Hocker, M., Treiber, D. K., & Zarrinkar, P. P. (2011) · Nature Biotechnology · doi:10.1038/nbt.1990 · Cited by 2,409

Protein kinases — the major drug targets of the twenty-first century?

Cohen, P. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd773 · Cited by 2,186

The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP

Yun, C.-H., Mengwasser, K. E., Toms, A. V., Woo, M. S., Greulich, H., Wong, K.-K., Meyerson, M., & Eck, M. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709662105 · Cited by 2,118

In vivo antitumor activity of SU11248, a novel tyrosine kinase inhibitor targeting vascular endothelial growth factor and platelet-derived growth factor receptors: determination of a pharmacokinetic/pharmacodynamic relationship.

Mendel, D. B., Laird, A., Xin, X., Louie, S. G., Christensen, J. G., Li, G., Schreck, R., Abrams, T. J., Ngai, T. J., Lee, L. B., et al. (2003) · PubMed · Cited by 1,961

Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma

Bollag, G., Hirth, P., Tsai, J., Zhang, J., Ibrahim, P. N., Cho, H., Spevak, W., Zhang, C., Zhang, Y., Habets, G., et al. (2010) · Nature · doi:10.1038/nature09454 · Cited by 1,831

Structure of the Epidermal Growth Factor Receptor Kinase Domain Alone and in Complex with a 4-Anilinoquinazoline Inhibitor

Stamos, J., Sliwkowski, M. X., & Eigenbrot, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207135200 · Cited by 1,574

Characterization of AMN107, a selective inhibitor of native and mutant Bcr-Abl

Weisberg, E., Manley, P. W., Breitenstein, W., Brüggen, J., Cowan-Jacob, S. W., Ray, A., Huntly, B., Fabbro, D., Fendrich, G., Hall-Meyers, E., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.01.007 · Cited by 1,492

Regorafenib (BAY 73‐4506): A new oral multikinase inhibitor of angiogenic, stromal and oncogenic receptor tyrosine kinases with potent preclinical antitumor activity

Wilhelm, S. M., Dumas, J., Adnane, L., Lynch, M., Carter, C. A., Schütz, G., Thierauch, K., & Zopf, D. (2011) · International Journal of Cancer · doi:10.1002/ijc.25864 · Cited by 1,355

Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity

Tsai, J., Lee, J. T., Wang, W., Zhang, J., Cho, H., Mamo, S., Bremer, R., Gillette, S., Kong, J., Haass, N. K., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711741105 · Cited by 1,346

AP24534, a Pan-BCR-ABL Inhibitor for Chronic Myeloid Leukemia, Potently Inhibits the T315I Mutant and Overcomes Mutation-Based Resistance

O'Hare, T., Shakespeare, W. C., Zhu, X., Eide, C. A., Rivera, V. M., Wang, F., Adrian, L. T., Zhou, T., Huang, W.-S., Xu, Q., et al. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.09.028 · Cited by 1,259

A Unique Structure for Epidermal Growth Factor Receptor Bound to GW572016 (Lapatinib)

Wood, E. R., Truesdale, A. T., McDonald, O. B., Yuan, D., Hassell, A., Dickerson, S. H., Ellis, B., Pennisi, C., Horne, E., Lackey, K., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1168 · Cited by 1,122

Rational design of inhibitors that bind to inactive kinase conformations

Liu, Y., & Gray, N. S. (2006) · Nature Chemical Biology · doi:10.1038/nchembio799 · Cited by 1,094

In vitro Activity of Bcr-Abl Inhibitors AMN107 and BMS-354825 against Clinically Relevant Imatinib-Resistant Abl Kinase Domain Mutants

O'Hare, T., Walters, D. K., Stoffregen, E. P., Jia, T., Manley, P. W., Mestan, J., Cowan-Jacob, S. W., Lee, F. Y., Heinrich, M. C., Deininger, M. W. N., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0259 · Cited by 1,036

Novel mutant-selective EGFR kinase inhibitors against EGFR T790M

Zhou, W., Ercan, D., Chen, L., Yun, C.-H., Li, D., Capelletti, M., Cortot, A. B., Chirieac, L., Iacob, R. E., Padera, R., et al. (2009) · Nature · doi:10.1038/nature08622 · Cited by 1,013

Structure Based Drug Design of Crizotinib (PF-02341066), a Potent and Selective Dual Inhibitor of Mesenchymal–Epithelial Transition Factor (c-MET) Kinase and Anaplastic Lymphoma Kinase (ALK)

Cui, J. J., Tran-Dubé, M., Shen, H., Nambu, M., Kung, P.-P., Pairish, M., Jia, L., Meng, J., Funk, L., Botrous, I., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm2007613 · Cited by 932

BindingDB Entry 50022499: ZD1839 (Iressa): an orally active inhibitor of epidermal growth factor signaling with potential for cancer therapy.

BindingDB (2025) · PubMed · doi:10.7270/q2pc374f · Cited by 924

Preclinical characterization of the selective JAK1/2 inhibitor INCB018424: therapeutic implications for the treatment of myeloproliferative neoplasms

Quintás-Cardama, A., Vaddi, K., Liu, P., Manshouri, T., Li, J., Scherle, P. A., Caulder, E., Wen, X., Li, Y., Waeltz, P., et al. (2010) · Blood · doi:10.1182/blood-2009-04-214957 · Cited by 843

BindingDB Entry 50022536: Induction of apoptosis and cell cycle arrest by CP-358,774, an inhibitor of epidermal growth factor receptor tyrosine kinase.

BindingDB (2025) · PubMed · doi:10.7270/q2dr317m · Cited by 843

Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site

Pargellis, C., Tong, L., Churchill, L., Cirillo, P. F., Gilmore, T., Graham, A. G., Grob, P. M., Hickey, E. R., Moss, N., Pav, S., et al. (2002) · Nature Structural Biology · doi:10.1038/nsb770 · Cited by 833

An Orally Available Small-Molecule Inhibitor of c-Met, PF-2341066, Exhibits Cytoreductive Antitumor Efficacy through Antiproliferative and Antiangiogenic Mechanisms

Zou, H. Y., Li, Q., Lee, J. H., Arango, M. E., McDonnell, S. R., Yamazaki, S., Koudriakova, T. B., Alton, G., Cui, J. J., Kung, P.-P., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4443 · Cited by 745

Phospho.ELM: a database of phosphorylation sites--update 2011

Dinkel, H., Chica, C., Via, A., Gould, C. M., Jensen, L. J., Gibson, T. J., & Diella, F. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq1104 · Cited by 740

The Protein Data Bank: A Computer‐Based Archival File for Macromolecular Structures

BERNSTEIN, F. C., KOETZLE, T. F., WILLIAMS, G. J. B., MEYER, E. F., BRICE, M. D., RODGERS, J. R., KENNARD, O., SHIMANOUCHI, T., & TASUMI, M. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11885.x · Cited by 735

The Structure of Dasatinib (BMS-354825) Bound to Activated ABL Kinase Domain Elucidates Its Inhibitory Activity against Imatinib-Resistant ABL Mutants

Tokarski, J. S., Newitt, J. A., Chang, C. Y. J., Cheng, J. D., Wittekind, M., Kiefer, S. E., Kish, K., Lee, F. Y. F., Borzillerri, R., Lombardo, L. J., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4187 · Cited by 700

Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition

Ohren, J. F., Chen, H., Pavlovsky, A., Whitehead, C., Zhang, E., Kuffa, P., Yan, C., McConnell, P., Spessard, C., Banotai, C., et al. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb859 · Cited by 626

Discovery of 7-Methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1 H-indol-5-yl)-7 H-pyrrolo[2,3-d]pyrimidin-4-amine (GSK2606414), a Potent and Selective First-in-Class Inhibitor of Protein Kinase R (PKR)-like Endoplasmic Reticulum Kinase (PERK)

Axten, J. M., Medina, J. R., Feng, Y., Shu, A., Romeril, S. P., Grant, S. W., Li, W. H. H., Heerding, D. A., Minthorn, E., Mencken, T., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300713s · Cited by 617

GSK1120212 (JTP-74057) Is an Inhibitor of MEK Activity and Activation with Favorable Pharmacokinetic Properties for Sustained In Vivo Pathway Inhibition

Gilmartin, A. G., Bleam, M. R., Groy, A., Moss, K. G., Minthorn, E. A., Kulkarni, S. G., Rominger, C. M., Erskine, S., Fisher, K. E., Yang, J., et al. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-2200 · Cited by 587

ZD6474, an orally available inhibitor of KDR tyrosine kinase activity, efficiently blocks oncogenic RET kinases.

Carlomagno, F., Vitagliano, D., Guida, T., Ciardiello, F., Tortora, G., Vecchio, G., Ryan, A. J., Fontanini, G., Fusco, A., & Santoro, M. M. (2002) · PubMed · Cited by 569

Structural Interaction Fingerprint (SIFt): A Novel Method for Analyzing Three-Dimensional Protein−Ligand Binding Interactions

Deng, Z., Chuaqui, C., & Singh, J. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm030331x · Cited by 563

Through the “Gatekeeper Door”: Exploiting the Active Kinase Conformation

Zuccotto, F., Ardini, E., Casale, E., & Angiolini, M. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901443h · Cited by 518

Pharmacokinetic-pharmacodynamic correlation from mouse to human with pazopanib, a multikinase angiogenesis inhibitor with potent antitumor and antiangiogenic activity

Kumar, R., Knick, V. B., Rudolph, S. K., Johnson, J. H., Crosby, R. M., Crouthamel, M.-C., Hopper, T. M., Miller, C. G., Harrington, L. E., Onori, J. A., et al. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-0193 · Cited by 517

Molecular Recognition of Protein Kinase Binding Pockets for Design of Potent and Selective Kinase Inhibitors

Liao, J. J.-L. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm0608107 · Cited by 507

A selective small molecule inhibitor of c-Met kinase inhibits c-Met-dependent phenotypes in vitro and exhibits cytoreductive antitumor activity in vivo.

Christensen, J. G., Schreck, R., Burrows, J., Kuruganti, P. A., Chan, E., Le, P., Chen, J., Wang, X., Ruslim, L., Blake, R. A., et al. (2003) · PubMed · Cited by 497

Reversible targeting of noncatalytic cysteines with chemically tuned electrophiles

Serafimova, I. M., Pufall, M. A., Krishnan, S., Duda, K., Cohen, M. S., Maglathlin, R. L., McFarland, J. M., Miller, R. M., Frödin, M., & Taunton, J. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.925 · Cited by 493

Fragment-Based Lead Discovery Using X-ray Crystallography

Hartshorn, M. J., Murray, C. W., Cleasby, A., Frederickson, M., Tickle, I. J., & Jhoti, H. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm0495778 · Cited by 422

SKI-606, a 4-anilino-3-quinolinecarbonitrile dual inhibitor of Src and Abl kinases, is a potent antiproliferative agent against chronic myelogenous leukemia cells in culture and causes regression of K562 xenografts in nude mice.

Golas, J. M., Arndt, K. T., Etienne, C., Lucas, J., Nardin, D., Gibbons, J. J., Frost, P., Ye, F., Boschelli, D. H., & Boschelli, F. (2003) · PubMed · Cited by 408

Optimizing Fragment and Scaffold Docking by Use of Molecular Interaction Fingerprints

Marcou, G., & Rognan, D. (2007) · Journal of Chemical Information and Modeling · doi:10.1021/ci600342e · Cited by 408

Combinations of BRAF, MEK, and PI3K/mTOR Inhibitors Overcome Acquired Resistance to the BRAF Inhibitor GSK2118436 Dabrafenib, Mediated by NRAS or MEK Mutations

Greger, J. G., Eastman, S. D., Zhang, V., Bleam, M. R., Hughes, A. M., Smitheman, K. N., Dickerson, S. H., Laquerre, S. G., Liu, L., & Gilmer, T. M. (2012) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-11-0989 · Cited by 363

A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases

Fedorov, O., Marsden, B., Pogacic, V., Rellos, P., Müller, S., Bullock, A. N., Schwaller, J., Sundström, M., & Knapp, S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708800104 · Cited by 359

Inhibition of Tumor Cell Growth, Invasion, and Metastasis by EXEL-2880 (XL880, GSK1363089), a Novel Inhibitor of HGF and VEGF Receptor Tyrosine Kinases

Qian, F., Engst, S., Yamaguchi, K., Yu, P., Won, K.-A., Mock, L., Lou, T., Tan, J., Li, C., Tam, D., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4889 · Cited by 350

Discovery of Potent and Selective Covalent Inhibitors of JNK

Zhang, T., Inesta-Vaquera, F., Niepel, M., Zhang, J., Ficarro, S. B., Machleidt, T., Xie, T., Marto, J. A., Kim, N., Sim, T., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.11.010 · Cited by 349

Identification of N-(4-Piperidinyl)-4-(2,6-dichlorobenzoylamino)-1 H-pyrazole-3-carboxamide (AT7519), a Novel Cyclin Dependent Kinase Inhibitor Using Fragment-Based X-Ray Crystallography and Structure Based Drug Design

Wyatt, P. G., Woodhead, A. J., Berdini, V., Boulstridge, J. A., Carr, M. G., Cross, D. M., Davis, D. J., Devine, L. A., Early, T. R., Feltell, R. E., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800382h · Cited by 340

Targeting protein kinases in central nervous system disorders

Chico, L. K., Van Eldik, L. J., & Watterson, D. M. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2999 · Cited by 298

The (un)targeted cancer kinome

Fedorov, O., Müller, S., & Knapp, S. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.297 · Cited by 292

Selectively Nonselective Kinase Inhibition: Striking the Right Balance

Morphy, R. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901132v · Cited by 292

Structure of the Kinase Domain of an Imatinib-Resistant Abl Mutant in Complex with the Aurora Kinase Inhibitor VX-680

Young, M. A., Shah, N. P., Chao, L. H., Seeliger, M., Milanov, Z. V., Biggs, W. H., Treiber, D. K., Patel, H. K., Zarrinkar, P. P., Lockhart, D. J., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2788 · Cited by 276

Structural and Thermodynamic Characterization of the TYK2 and JAK3 Kinase Domains in Complex with CP-690550 and CMP-6

Chrencik, J. E., Patny, A., Leung, I. K., Korniski, B., Emmons, T. L., Hall, T., Weinberg, R. A., Gormley, J. A., Williams, J. M., Day, J. E., et al. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.05.020 · Cited by 227

Kinase inhibitors and the case for CH…O hydrogen bonds in protein–ligand binding

Pierce, A. C., Sandretto, K. L., & Bemis, G. W. (2002) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10259 · Cited by 225

Identification of Novel Purine and Pyrimidine Cyclin-Dependent Kinase Inhibitors with Distinct Molecular Interactions and Tumor Cell Growth Inhibition Profiles

Arris, C. E., Boyle, F. T., Calvert, A. H., Curtin, N. J., Endicott, J. A., Garman, E. F., Gibson, A. E., Golding, B. T., Grant, S., Griffin, R. J., et al. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm990628o · Cited by 215

Conformational Control Inhibition of the BCR-ABL1 Tyrosine Kinase, Including the Gatekeeper T315I Mutant, by the Switch-Control Inhibitor DCC-2036

Chan, W. W., Wise, S. C., Kaufman, M. D., Ahn, Y. M., Ensinger, C. L., Haack, T., Hood, M. M., Jones, J., Lord, J. W., Lu, W. P., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.03.003 · Cited by 208

Targeting protein kinases for the development of anti-inflammatory drugs

Cohen, P. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.01.015 · Cited by 207

Crystal Structure-Based Virtual Screening for Fragment-like Ligands of the Human Histamine H 1 Receptor

de Graaf, C., Kooistra, A. J., Vischer, H. F., Katritch, V., Kuijer, M., Shiroishi, M., Iwata, S., Shimamura, T., Stevens, R. C., de Esch, I. J. P., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm2011589 · Cited by 204

Specific CLK Inhibitors from a Novel Chemotype for Regulation of Alternative Splicing

Fedorov, O., Huber, K., Eisenreich, A., Filippakopoulos, P., King, O., Bullock, A. N., Szklarczyk, D., Jensen, L. J., Fabbro, D., Trappe, J., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.11.009 · Cited by 204

Structure-guided development of affinity probes for tyrosine kinases using chemical genetics

Blair, J. A., Rauh, D., Kung, C., Yun, C.-H., Fan, Q.-W., Rode, H., Zhang, C., Eck, M. J., Weiss, W. A., & Shokat, K. M. (2007) · Nature Chemical Biology · doi:10.1038/nchembio866 · Cited by 202

sc-PDB: an Annotated Database of Druggable Binding Sites from the Protein Data Bank

Kellenberger, E., Muller, P., Schalon, C., Bret, G., Foata, N., & Rognan, D. (2006) · Journal of Chemical Information and Modeling · doi:10.1021/ci050372x · Cited by 201

Pim-1 Ligand-bound Structures Reveal the Mechanism of Serine/Threonine Kinase Inhibition by LY294002

Jacobs, M. D., Black, J., Futer, O., Swenson, L., Hare, B., Fleming, M., & Saxena, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413155200 · Cited by 192

Discovery of a Potential Allosteric Ligand Binding Site in CDK2

Betzi, S., Alam, R., Martin, M., Lubbers, D. J., Han, H., Jakkaraj, S. R., Georg, G. I., & Schönbrunn, E. (2011) · ACS Chemical Biology · doi:10.1021/cb100410m · Cited by 188

Identification of Novel p38α MAP Kinase Inhibitors Using Fragment-Based Lead Generation

Gill, A. L., Frederickson, M., Cleasby, A., Woodhead, S. J., Carr, M. G., Woodhead, A. J., Walker, M. T., Congreve, M. S., Devine, L. A., Tisi, D., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049575n · Cited by 186

New Directions in Targeting Protein Kinases: Focusing Upon True Allosteric and Bivalent Inhibitors

Lamba, V., & Ghosh, I. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212800672813 · Cited by 182

Knowledge Based Prediction of Ligand Binding Modes and Rational Inhibitor Design for Kinase Drug Discovery

Ghose, A. K., Herbertz, T., Pippin, D. A., Salvino, J. M., & Mallamo, J. P. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800475y · Cited by 166

Optimization and SAR for dual ErbB-1/ErbB-2 tyrosine kinase inhibition in the 6-furanylquinazoline series

Petrov, K. G., Zhang, Y.-M., Carter, M., Cockerill, G. S., Dickerson, S., Gauthier, C. A., Guo, Y., Mook, R. A., Rusnak, D. W., Walker, A. L., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.05.090 · Cited by 166

Structural and Spectroscopic Analysis of the Kinase Inhibitor Bosutinib and an Isomer of Bosutinib Binding to the Abl Tyrosine Kinase Domain

Levinson, N. M., & Boxer, S. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029828 · Cited by 149

Identification of Inhibitors of Protein Kinase B Using Fragment-Based Lead Discovery

Saxty, G., Woodhead, S. J., Berdini, V., Davies, T. G., Verdonk, M. L., Wyatt, P. G., Boyle, R. G., Barford, D., Downham, R., Garrett, M. D., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm070091b · Cited by 141

c-Met Inhibitors with Novel Binding Mode Show Activity against Several Hereditary Papillary Renal Cell Carcinoma-related Mutations

Bellon, S. F., Kaplan‐Lefko, P. J., Yang, Y., Zhang, Y., Moriguchi, J., Rex, K. L., Johnson, C. W., Rose, P., Long, A. M., O'Connor, A. B., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705774200 · Cited by 141

Alignment-Free Ultra-High-Throughput Comparison of Druggable Protein−Ligand Binding Sites

Weill, N., & Rognan, D. (2010) · Journal of Chemical Information and Modeling · doi:10.1021/ci900349y · Cited by 125

Flipped Out: Structure-Guided Design of Selective Pyrazolylpyrrole ERK Inhibitors

Aronov, A. M., Baker, C., Bemis, G. W., Cao, J., Chen, G., Ford, P. J., Germann, U. A., Green, J., Hale, M. R., Jacobs, M. D., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm061381f · Cited by 123

Kinase-targeted libraries: The design and synthesis of novel, potent, and selective kinase inhibitors

Akritopoulou‐Zanze, I., & Hajduk, P. J. (2009) · Drug Discovery Today · doi:10.1016/j.drudis.2008.12.002 · Cited by 116

A simple and fuzzy method to align and compare druggable ligand‐binding sites

Schalon, C., Surgand, J.-S., Kellenberger, E., & Rognan, D. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21858 · Cited by 116

6-Ethynylthieno[3,2-d]- and 6-ethynylthieno[2,3-d]pyrimidin-4-anilines as tunable covalent modifiers of ErbB kinases

Wood, E. R., Shewchuk, L. M., Ellis, B., Brignola, P. S., Brashear, R. L., Caferro, T. R., Dickerson, S. H., Dickson, H. D., Donaldson, K. H., Gaul, M. D., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708281105 · Cited by 113

sc-PDB: a database for identifying variations and multiplicity of ‘druggable’ binding sites in proteins

Meslamani, J. E., Rognan, D., & Kellenberger, E. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr120 · Cited by 111

Structure-Based Design of Novel Class II c-Met Inhibitors: 1. Identification of Pyrazolone-Based Derivatives

Norman, M. H., Liu, L., Lee, M., Xi, N., Fellows, I. M., D’Angelo, N. D., Dominguez, C., Rex, K. L., Bellon, S. F., Kim, T., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm201330u · Cited by 106

Pharmacophore Fingerprint-Based Approach to Binding Site Subpocket Similarity and Its Application to Bioisostere Replacement

Wood, D. J., de Vlieg, J., Wagener, M., & Ritschel, T. (2012) · Journal of Chemical Information and Modeling · doi:10.1021/ci3000776 · Cited by 97

Kinase-likeness and Kinase-Privileged Fragments: Toward Virtual Polypharmacology

Aronov, A. M., McClain, B., Moody, C. S., & Murcko, M. A. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm701021b · Cited by 91

Small Molecule Recognition of c-Src via the Imatinib-Binding Conformation

Dar, A. C., Lopez, M. S., & Shokat, K. M. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.09.007 · Cited by 89

Pyrazolo[4,3- d ]pyrimidine Bioisostere of Roscovitine: Evaluation of a Novel Selective Inhibitor of Cyclin-Dependent Kinases with Antiproliferative Activity

Jorda, R., Havlı́ček, L., McNae, I. W., Walkinshaw, M. D., Voller, J., Šturc, A., Navrátilová, J., Kuzma, M., Mistrík, M., Bártek, J., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200064p · Cited by 88

Discovery of a potent and highly selective PDK1 inhibitor via fragment-based drug discovery

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Computational Modeling of Kinase Inhibitor Selectivity

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