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Volumn 36, Issue 7, 2015, Pages 422-439

FDA-approved small-molecule kinase inhibitors

Author keywords

cancer; crystal structure; lipid kinase; protein kinase; serine threonine kinase; tyrosine kinase

Indexed keywords

AFATINIB; AXITINIB; BOSUTINIB; CERITINIB; CRIZOTINIB; DASATINIB; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE INHIBITOR; ERLOTINIB; GEFITINIB; IBRUTINIB; IMATINIB; LAPATINIB; LENVATINIB; LIPID KINASE INHIBITOR; NILOTINIB; NINTEDANIB; NON RECEPTOR TYROSINE KINASE INHIBITOR; PAZOPANIB; PHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE INHIBITOR; PONATINIB; REGORAFENIB; RUXOLITINIB; SORAFENIB; SUNITINIB; TOFACITINIB; TRAMETINIB; UNCLASSIFIED DRUG; UNINDEXED DRUG; VANDETANIB; VEMURAFENIB; ENZYME INHIBITOR; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN BINDING; PROTEIN KINASE INHIBITOR; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE KINASE;

EID: 84933181941     PISSN: 01656147     EISSN: 18733735     Source Type: Journal    
DOI: 10.1016/j.tips.2015.04.005     Document Type: Review
Times cited : (823)

References (110)
  • 1
    • 0035413607 scopus 로고    scopus 로고
    • Structural basis for control by phosphorylation
    • L.N. Johnson, and R.J. Lewis Structural basis for control by phosphorylation Chem. Rev. 101 2001 2209 2242
    • (2001) Chem. Rev. , vol.101 , pp. 2209-2242
    • Johnson, L.N.1    Lewis, R.J.2
  • 2
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • J.A. Adams Kinetic and catalytic mechanisms of protein kinases Chem. Rev. 101 2001 2271 2290
    • (2001) Chem. Rev. , vol.101 , pp. 2271-2290
    • Adams, J.A.1
  • 3
    • 84908371590 scopus 로고    scopus 로고
    • Advances in kinase targeting: Current clinical use and clinical trials
    • M. Rask-Andersen Advances in kinase targeting: current clinical use and clinical trials Trends Pharmacol. Sci. 35 2014 604 620
    • (2014) Trends Pharmacol. Sci. , vol.35 , pp. 604-620
    • Rask-Andersen, M.1
  • 4
    • 84891625661 scopus 로고    scopus 로고
    • Molecularly targeted cancer therapy: Some lessons from the past decade
    • M. Huang Molecularly targeted cancer therapy: some lessons from the past decade Trends Pharmacol. Sci. 35 2014 41 50
    • (2014) Trends Pharmacol. Sci. , vol.35 , pp. 41-50
    • Huang, M.1
  • 5
    • 64249135764 scopus 로고    scopus 로고
    • Novel agents on the horizon for cancer therapy
    • W.W. Ma, and A.A. Adjei Novel agents on the horizon for cancer therapy CA Cancer J. Clin. 59 2009 111 137
    • (2009) CA Cancer J. Clin. , vol.59 , pp. 111-137
    • Ma, W.W.1    Adjei, A.A.2
  • 6
    • 84922781885 scopus 로고    scopus 로고
    • Feedback and redundancy in receptor tyrosine kinase signaling: Relevance to cancer therapies
    • C. Sun, and R. Bernards Feedback and redundancy in receptor tyrosine kinase signaling: relevance to cancer therapies Trends Biochem. Sci. 39 2014 465 474
    • (2014) Trends Biochem. Sci. , vol.39 , pp. 465-474
    • Sun, C.1    Bernards, R.2
  • 7
    • 84903523652 scopus 로고    scopus 로고
    • Discovery and development of Janus kinase (JAK) inhibitors for inflammatory diseases
    • J.D. Clark Discovery and development of Janus kinase (JAK) inhibitors for inflammatory diseases J. Med. Chem. 57 2014 5023 5038
    • (2014) J. Med. Chem. , vol.57 , pp. 5023-5038
    • Clark, J.D.1
  • 8
    • 84879693217 scopus 로고    scopus 로고
    • New anti-inflammatory targets for chronic obstructive pulmonary disease
    • P.J. Barnes New anti-inflammatory targets for chronic obstructive pulmonary disease Nat. Rev. Drug Discov. 12 2013 543 559
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 543-559
    • Barnes, P.J.1
  • 9
    • 84928429443 scopus 로고    scopus 로고
    • Tetra-substituted pyridinylimidazoles as dual inhibitors of p38α mitogen-activated protein kinase and c-Jun N-terminal kinase 3 for potential treatment of neurodegenerative diseases
    • F. Muth Tetra-substituted pyridinylimidazoles as dual inhibitors of p38α mitogen-activated protein kinase and c-Jun N-terminal kinase 3 for potential treatment of neurodegenerative diseases J. Med. Chem. 58 2015 443 456
    • (2015) J. Med. Chem. , vol.58 , pp. 443-456
    • Muth, F.1
  • 10
    • 84961290875 scopus 로고    scopus 로고
    • An antiangiogenic isoform of VEGF-A contributes to impaired vascularization in peripheral artery disease
    • R. Kikuchi An antiangiogenic isoform of VEGF-A contributes to impaired vascularization in peripheral artery disease Nat. Med. 20 2014 1464 1471
    • (2014) Nat. Med. , vol.20 , pp. 1464-1471
    • Kikuchi, R.1
  • 11
    • 84923124525 scopus 로고    scopus 로고
    • An ERK/Cdk5 axis controls the diabetogenic actions of PPARγ
    • A.S. Banks An ERK/Cdk5 axis controls the diabetogenic actions of PPARγ Nature 517 2015 391 395
    • (2015) Nature , vol.517 , pp. 391-395
    • Banks, A.S.1
  • 12
    • 0001010573 scopus 로고
    • The enzymatic phosphorylation of proteins
    • G. Burnett, and E.P. Kennedy The enzymatic phosphorylation of proteins J. Biol. Chem. 211 1954 969 980
    • (1954) J. Biol. Chem. , vol.211 , pp. 969-980
    • Burnett, G.1    Kennedy, E.P.2
  • 13
    • 0000187410 scopus 로고
    • Conversion of phosphorylase b to phosphorylase a in muscle extracts
    • E.H. Fischer, and E.G. Krebs Conversion of phosphorylase b to phosphorylase a in muscle extracts J. Biol. Chem. 216 1955 121 132
    • (1955) J. Biol. Chem. , vol.216 , pp. 121-132
    • Fischer, E.H.1    Krebs, E.G.2
  • 14
    • 49749165001 scopus 로고
    • The phosphorylase b to a converting enzyme of rabbit skeletal muscle
    • E.G. Krebs, and E.H. Fischer The phosphorylase b to a converting enzyme of rabbit skeletal muscle Biochim. Biophys. Acta 20 1956 150 157
    • (1956) Biochim. Biophys. Acta , vol.20 , pp. 150-157
    • Krebs, E.G.1    Fischer, E.H.2
  • 15
    • 0014409394 scopus 로고
    • An adenosine 3′,5′-monophosphate-dependant protein kinase from rabbit skeletal muscle
    • D.A. Walsh An adenosine 3′,5′-monophosphate-dependant protein kinase from rabbit skeletal muscle J. Biol. Chem. 243 1968 3763 3765
    • (1968) J. Biol. Chem. , vol.243 , pp. 3763-3765
    • Walsh, D.A.1
  • 16
    • 0036097364 scopus 로고    scopus 로고
    • The origins of protein phosphorylation
    • P. Cohen The origins of protein phosphorylation Nat. Cell Biol. 4 2002 E127 E130
    • (2002) Nat. Cell Biol. , vol.4 , pp. E127-E130
    • Cohen, P.1
  • 17
    • 1242307380 scopus 로고    scopus 로고
    • JAK/STAT, Raf/MEK/ERK, PI3K/Akt and BCR-ABL in cell cycle progression and leukemogenesis
    • L.S. Steelman JAK/STAT, Raf/MEK/ERK, PI3K/Akt and BCR-ABL in cell cycle progression and leukemogenesis Leukemia 18 2004 189 218
    • (2004) Leukemia , vol.18 , pp. 189-218
    • Steelman, L.S.1
  • 18
    • 84874724662 scopus 로고    scopus 로고
    • Update on activities at the Universal Protein Resource (UniProt) in 2013
    • The UniProt Consortium Update on activities at the Universal Protein Resource (UniProt) in 2013 Nucleic Acids Res. 41 2013 D43 D47
    • (2013) Nucleic Acids Res. , vol.41 , pp. D43-D47
    • Uniprot Consortium, T.1
  • 19
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • G. Manning The protein kinase complement of the human genome Science 298 2002 1912 1934
    • (2002) Science , vol.298 , pp. 1912-1934
    • Manning, G.1
  • 20
    • 84865812140 scopus 로고    scopus 로고
    • ENCODE project writes eulogy for junk DNA
    • E. Pennisi ENCODE project writes eulogy for junk DNA Science 337 2012 1159 1161
    • (2012) Science , vol.337 , pp. 1159-1161
    • Pennisi, E.1
  • 21
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • D. Knighton Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase Science 253 1991 407 414
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.1
  • 22
    • 84921409244 scopus 로고    scopus 로고
    • Targeting conformational plasticity of protein kinases
    • M. Tong, and M.A. Seeliger Targeting conformational plasticity of protein kinases ACS Chem. Biol. 10 2015 190 200
    • (2015) ACS Chem. Biol. , vol.10 , pp. 190-200
    • Tong, M.1    Seeliger, M.A.2
  • 23
    • 1642323740 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Insights into drug design from structure
    • M.E.M. Noble Protein kinase inhibitors: insights into drug design from structure Science 303 2004 1800 1805
    • (2004) Science , vol.303 , pp. 1800-1805
    • Noble, M.E.M.1
  • 24
    • 84860524795 scopus 로고    scopus 로고
    • Structural approaches to obtain kinase selectivity
    • R.A. Norman Structural approaches to obtain kinase selectivity Trends Pharmacol. Sci. 33 2012 273 278
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 273-278
    • Norman, R.A.1
  • 25
    • 78650657590 scopus 로고    scopus 로고
    • Tinkering outside the kinase ATP box: Allosteric (type IV) and bivalent (type V) inhibitors of protein kinases
    • K.J. Cox Tinkering outside the kinase ATP box: allosteric (type IV) and bivalent (type V) inhibitors of protein kinases Future Med. Chem. 3 2010 29 43
    • (2010) Future Med. Chem. , vol.3 , pp. 29-43
    • Cox, K.J.1
  • 26
    • 84861722034 scopus 로고    scopus 로고
    • New directions in targeting protein kinases: Focusing upon true allosteric and bivalent inhibitors
    • V. Lamba, and I. Ghosh New directions in targeting protein kinases: focusing upon true allosteric and bivalent inhibitors Curr. Pharm. Des. 18 2012 2936 2945
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 2936-2945
    • Lamba, V.1    Ghosh, I.2
  • 27
    • 0024240990 scopus 로고
    • Blocking of EGF-dependent cell proliferation by EGF receptor kinase inhibitors
    • P. Yaish Blocking of EGF-dependent cell proliferation by EGF receptor kinase inhibitors Science 242 1988 933 935
    • (1988) Science , vol.242 , pp. 933-935
    • Yaish, P.1
  • 28
    • 0024434810 scopus 로고
    • Tyrphostins I: Synthesis and biological activity of protein tyrosine kinase inhibitors
    • A. Gazit Tyrphostins I: synthesis and biological activity of protein tyrosine kinase inhibitors J. Med. Chem. 32 1989 2344 2352
    • (1989) J. Med. Chem. , vol.32 , pp. 2344-2352
    • Gazit, A.1
  • 29
    • 84871730931 scopus 로고    scopus 로고
    • Approaches to discover non-ATP site kinase inhibitors
    • L.K. Gavrin, and E. Saiah Approaches to discover non-ATP site kinase inhibitors MedChemComm 4 2013 41 51
    • (2013) MedChemComm , vol.4 , pp. 41-51
    • Gavrin, L.K.1    Saiah, E.2
  • 30
    • 84925457876 scopus 로고    scopus 로고
    • A structural atlas of kinases inhibited by clinically approved drugs
    • Q. Wang A structural atlas of kinases inhibited by clinically approved drugs Methods Enzymol. 548 2014 23 67
    • (2014) Methods Enzymol. , vol.548 , pp. 23-67
    • Wang, Q.1
  • 31
    • 84872243145 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors: Views of selectivity, sensitivity, and clinical performance
    • A. Levitzki Tyrosine kinase inhibitors: views of selectivity, sensitivity, and clinical performance Annu. Rev. Pharmacol. Toxicol. 53 2013 161 185
    • (2013) Annu. Rev. Pharmacol. Toxicol. , vol.53 , pp. 161-185
    • Levitzki, A.1
  • 32
    • 0035810147 scopus 로고    scopus 로고
    • Efficacy and safety of a specific inhibitor of the BCR-ABL tyrosine kinase in chronic myeloid leukemia
    • B.J. Druker Efficacy and safety of a specific inhibitor of the BCR-ABL tyrosine kinase in chronic myeloid leukemia N. Eng. J. Med. 344 2001 1031 1037
    • (2001) N. Eng. J. Med. , vol.344 , pp. 1031-1037
    • Druker, B.J.1
  • 33
    • 84874310182 scopus 로고    scopus 로고
    • Structure and dynamic regulation of Abl kinases
    • S. Panjarian Structure and dynamic regulation of Abl kinases J. Biol. Chem. 288 2013 5443 5450
    • (2013) J. Biol. Chem. , vol.288 , pp. 5443-5450
    • Panjarian, S.1
  • 34
    • 84867690864 scopus 로고    scopus 로고
    • Systems-pharmacology dissection of a drug synergy in imatinib-resistant CML
    • G.E. Winter Systems-pharmacology dissection of a drug synergy in imatinib-resistant CML Nat. Chem. Biol. 8 2012 905 912
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 905-912
    • Winter, G.E.1
  • 35
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
    • B. Nagar Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571) Cancer Res. 62 2002 4236 4243
    • (2002) Cancer Res. , vol.62 , pp. 4236-4243
    • Nagar, B.1
  • 36
    • 84878843475 scopus 로고    scopus 로고
    • Mechanisms of resistance to BCR-ABL and other kinase inhibitors
    • A.J. Lamontanara Mechanisms of resistance to BCR-ABL and other kinase inhibitors Biochim. Biophys. Acta 1834 2013 1449 1459
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1449-1459
    • Lamontanara, A.J.1
  • 37
    • 84907292003 scopus 로고    scopus 로고
    • A therapeutically targetable mechanism of BCR-ABL-independent imatinib resistance in chronic myeloid leukemia
    • L. Ma A therapeutically targetable mechanism of BCR-ABL-independent imatinib resistance in chronic myeloid leukemia Sci. Transl. Med. 6 2014 252ra121
    • (2014) Sci. Transl. Med. , vol.6 , pp. 252ra121
    • Ma, L.1
  • 38
    • 84897114242 scopus 로고    scopus 로고
    • A conserved water-mediated hydrogen bond network defines bosutinib's kinase selectivity
    • N.M. Levinson, and S.G. Boxer A conserved water-mediated hydrogen bond network defines bosutinib's kinase selectivity Nat. Chem. Biol. 10 2014 127 132
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 127-132
    • Levinson, N.M.1    Boxer, S.G.2
  • 39
    • 0035979176 scopus 로고    scopus 로고
    • An essential role of the JAK-STAT pathway in ischemic preconditioning
    • Y-T. Xuan An essential role of the JAK-STAT pathway in ischemic preconditioning Proc. Natl. Acad. Sci. U.S.A. 98 2001 9050 9055
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9050-9055
    • Xuan, Y.-T.1
  • 40
    • 84898990827 scopus 로고    scopus 로고
    • Molecular pathways: Molecular basis for sensitivity and resistance to JAK kinase inhibitors
    • S.C. Meyer, and R.L. Levine Molecular pathways: molecular basis for sensitivity and resistance to JAK kinase inhibitors Clin. Cancer Res. 20 2014 2051 2059
    • (2014) Clin. Cancer Res. , vol.20 , pp. 2051-2059
    • Meyer, S.C.1    Levine, R.L.2
  • 41
    • 84908332830 scopus 로고    scopus 로고
    • Inhibiting Janus kinases to treat alopecia areata
    • S.J. Divito, and T.S. Kupper Inhibiting Janus kinases to treat alopecia areata Nat. Med. 20 2014 989 990
    • (2014) Nat. Med. , vol.20 , pp. 989-990
    • Divito, S.J.1    Kupper, T.S.2
  • 42
    • 84926046456 scopus 로고    scopus 로고
    • The impact of JAK-STAT signaling on muscle regeneration
    • J.D. Doles, and B.B. Olwin The impact of JAK-STAT signaling on muscle regeneration Nat. Med. 20 2014 1094 1095
    • (2014) Nat. Med. , vol.20 , pp. 1094-1095
    • Doles, J.D.1    Olwin, B.B.2
  • 43
    • 84916201113 scopus 로고    scopus 로고
    • Therapy for myeloproliferative neoplasms: When, which agent, and how?
    • H.L. Geyer, and R.A. Mesa Therapy for myeloproliferative neoplasms: when, which agent, and how? Blood 124 2014 3529 3537
    • (2014) Blood , vol.124 , pp. 3529-3537
    • Geyer, H.L.1    Mesa, R.A.2
  • 44
    • 77954385114 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of the TYK2 and JAK3 kinase domains in complex with CP-690550 and CMP-6
    • J.E. Chrencik Structural and thermodynamic characterization of the TYK2 and JAK3 kinase domains in complex with CP-690550 and CMP-6 J. Mol. Biol. 400 2010 413 433
    • (2010) J. Mol. Biol. , vol.400 , pp. 413-433
    • Chrencik, J.E.1
  • 45
    • 61349149899 scopus 로고    scopus 로고
    • Dissecting specificity in the Janus kinases: The structures of JAK-specific inhibitors complexed to the JAK1 and JAK2 protein tyrosine kinase domains
    • N.K. Williams Dissecting specificity in the Janus kinases: the structures of JAK-specific inhibitors complexed to the JAK1 and JAK2 protein tyrosine kinase domains J. Mol. Biol. 387 2009 219 232
    • (2009) J. Mol. Biol. , vol.387 , pp. 219-232
    • Williams, N.K.1
  • 46
    • 84929486174 scopus 로고    scopus 로고
    • Tricyclic covalent inhibitors selectively target Jak3 through an active-site thiol
    • E.R. Goedken Tricyclic covalent inhibitors selectively target Jak3 through an active-site thiol J. Biol. Chem. 298 2014 4573 4589
    • (2014) J. Biol. Chem. , vol.298 , pp. 4573-4589
    • Goedken, E.R.1
  • 47
    • 84921023407 scopus 로고    scopus 로고
    • Novel hinge-binding motifs for Janus kinase 3 inhibitors: A comprehensive structure-activity relationship study on tofacitinib bioisosteres
    • M. Gehringer Novel hinge-binding motifs for Janus kinase 3 inhibitors: a comprehensive structure-activity relationship study on tofacitinib bioisosteres ChemMedChem 9 2014 2516 2527
    • (2014) ChemMedChem , vol.9 , pp. 2516-2527
    • Gehringer, M.1
  • 48
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: The complexity of targeted inhibitors
    • N.E. Hynes, and H.A. Lane ERBB receptors and cancer: the complexity of targeted inhibitors Nat. Rev. Cancer 5 2005 341 354
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 49
    • 84914819493 scopus 로고    scopus 로고
    • Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations
    • P. Littlefield Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations Sci. Signal. 7 2014 ra114
    • (2014) Sci. Signal. , vol.7 , pp. ra114
    • Littlefield, P.1
  • 50
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: Towards the systems level
    • A. Citri, and Y. Yarden EGF-ERBB signalling: towards the systems level Nat. Rev. Mol. Cell Biol. 7 2006 505 516
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 51
    • 33847406095 scopus 로고    scopus 로고
    • Structures of lung cancer-derived EGFR mutants and inhibitor complexes: Mechanism of activation and insights into differential inhibitor sensitivity
    • C-H. Yun Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity Cancer Cell 11 2007 217 227
    • (2007) Cancer Cell , vol.11 , pp. 217-227
    • Yun, C.-H.1
  • 52
    • 84873406911 scopus 로고    scopus 로고
    • Insights into the aberrant activity of mutant EGFR kinase domain and drug recognition
    • K.S. Gajiwala Insights into the aberrant activity of mutant EGFR kinase domain and drug recognition Structure 21 2013 209 219
    • (2013) Structure , vol.21 , pp. 209-219
    • Gajiwala, K.S.1
  • 53
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor (erlotinib with EGFR)
    • J. Stamos Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor (erlotinib with EGFR) J. Biol. Chem. 277 2002 46265 46272
    • (2002) J. Biol. Chem. , vol.277 , pp. 46265-46272
    • Stamos, J.1
  • 54
    • 4644289313 scopus 로고    scopus 로고
    • A unique structure for epidermal growth factor receptor bound to GW572016 (lapatinib): Relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells
    • E.R. Wood A unique structure for epidermal growth factor receptor bound to GW572016 (lapatinib): relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells Cancer Res. 64 2004 6652 6659
    • (2004) Cancer Res. , vol.64 , pp. 6652-6659
    • Wood, E.R.1
  • 55
    • 40049099848 scopus 로고    scopus 로고
    • Mechanism of activation and inhibition of the HER4/ErbB4 kinase
    • C. Qiu Mechanism of activation and inhibition of the HER4/ErbB4 kinase Structure 16 2008 460 467
    • (2008) Structure , vol.16 , pp. 460-467
    • Qiu, C.1
  • 56
    • 84872511666 scopus 로고    scopus 로고
    • Strategies for the selective regulation of kinases with allosteric modulators: Exploiting exclusive structural features
    • Z. Fang Strategies for the selective regulation of kinases with allosteric modulators: exploiting exclusive structural features ACS Chem. Biol. 8 2013 58 70
    • (2013) ACS Chem. Biol. , vol.8 , pp. 58-70
    • Fang, Z.1
  • 57
    • 84903208494 scopus 로고    scopus 로고
    • Exploration of type II binding mode: A privileged approach for kinase inhibitor focused drug discovery?
    • Z. Zhao Exploration of type II binding mode: a privileged approach for kinase inhibitor focused drug discovery? ACS Chem. Biol. 9 2014 1230 1241
    • (2014) ACS Chem. Biol. , vol.9 , pp. 1230-1241
    • Zhao, Z.1
  • 58
    • 33845963343 scopus 로고    scopus 로고
    • Structure and chemical inhibition of the RET tyrosine kinase domain
    • P.P. Knowles Structure and chemical inhibition of the RET tyrosine kinase domain J. Biol. Chem. 281 2006 33577 33587
    • (2006) J. Biol. Chem. , vol.281 , pp. 33577-33587
    • Knowles, P.P.1
  • 59
    • 0037699954 scopus 로고    scopus 로고
    • The biology of VEGF and its receptors
    • N. Ferrara The biology of VEGF and its receptors Nat. Med. 9 2003 669 676
    • (2003) Nat. Med. , vol.9 , pp. 669-676
    • Ferrara, N.1
  • 60
    • 9244227572 scopus 로고    scopus 로고
    • Vascular endothelial growth factor B, a novel growth factor for endothelial cells
    • B. Olofsson Vascular endothelial growth factor B, a novel growth factor for endothelial cells Proc. Natl. Acad. Sci. U.S.A. 93 1996 2576 2581
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 2576-2581
    • Olofsson, B.1
  • 61
    • 84867816311 scopus 로고    scopus 로고
    • Molecular conformations, interactions, and properties associated with drug efficiency and clinical performance among VEGFR TK inhibitors
    • M. McTigue Molecular conformations, interactions, and properties associated with drug efficiency and clinical performance among VEGFR TK inhibitors Proc. Natl. Acad. Sci. U.S.A. 109 2012 18281 18289
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 18281-18289
    • McTigue, M.1
  • 62
    • 67649995940 scopus 로고    scopus 로고
    • Development of a fluorescent-tagged kinase assay system for the detection and characterization of allosteric kinase inhibitors
    • J.R. Simard Development of a fluorescent-tagged kinase assay system for the detection and characterization of allosteric kinase inhibitors J. Am. Chem. Soc. 131 2009 13286 13296
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13286-13296
    • Simard, J.R.1
  • 63
    • 49449117755 scopus 로고    scopus 로고
    • Discovery of 5-[[4-[(2,3-dimethyl-2H-indazol-6-yl)methylamino]-2-pyrimidinyl]amino]-2-methyl-benzenesulfonamide (pazopanib), a novel and potent vascular endothelial growth factor receptor inhibitor
    • P.A. Harris Discovery of 5-[[4-[(2,3-dimethyl-2H-indazol-6-yl)methylamino]-2-pyrimidinyl]amino]-2-methyl-benzenesulfonamide (pazopanib), a novel and potent vascular endothelial growth factor receptor inhibitor J. Med. Chem. 51 2008 4632 4640
    • (2008) J. Med. Chem. , vol.51 , pp. 4632-4640
    • Harris, P.A.1
  • 64
    • 84920711920 scopus 로고    scopus 로고
    • Distinct binding mode of multikinase inhibitor lenvatinib revealed by biochemical characterization
    • K. Okamoto Distinct binding mode of multikinase inhibitor lenvatinib revealed by biochemical characterization ACS Med. Chem. Lett. 6 2015 89 94
    • (2015) ACS Med. Chem. Lett. , vol.6 , pp. 89-94
    • Okamoto, K.1
  • 65
    • 37549057005 scopus 로고    scopus 로고
    • The anaplastic lymphoma kinase in the pathogenesis of cancer
    • R. Chiarle The anaplastic lymphoma kinase in the pathogenesis of cancer Nat. Rev. Cancer 8 2008 11 23
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 11-23
    • Chiarle, R.1
  • 66
    • 84905190188 scopus 로고    scopus 로고
    • ALK inhibitors in non-small cell lung cancer: Crizotinib and beyond
    • M.M. Awad, and A.T. Shaw ALK inhibitors in non-small cell lung cancer: crizotinib and beyond Clin. Adv. Hematol. Oncol. 12 2014 429 439
    • (2014) Clin. Adv. Hematol. Oncol. , vol.12 , pp. 429-439
    • Awad, M.M.1    Shaw, A.T.2
  • 67
    • 84879088863 scopus 로고    scopus 로고
    • Acquired resistance to crizotinib from a mutation in CD74-ROS1
    • M.M. Awad Acquired resistance to crizotinib from a mutation in CD74-ROS1 N. Eng. J. Med. 368 2013 2395 2401
    • (2013) N. Eng. J. Med. , vol.368 , pp. 2395-2401
    • Awad, M.M.1
  • 68
    • 80052806086 scopus 로고    scopus 로고
    • 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)
    • J.J. Cui 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) J. Med. Chem. 54 2011 6342 6363
    • (2011) J. Med. Chem. , vol.54 , pp. 6342-6363
    • Cui, J.J.1
  • 69
    • 84896957081 scopus 로고    scopus 로고
    • Ceritinib in ALK-rearranged non-small-cell lung cancer
    • A.T. Shaw Ceritinib in ALK-rearranged non-small-cell lung cancer N. Eng. J. Med. 370 2014 1189 1197
    • (2014) N. Eng. J. Med. , vol.370 , pp. 1189-1197
    • Shaw, A.T.1
  • 70
    • 84903466222 scopus 로고    scopus 로고
    • The ALK inhibitor ceritinib overcomes crizotinib resistance in non-small cell lung cancer
    • L. Friboulet The ALK inhibitor ceritinib overcomes crizotinib resistance in non-small cell lung cancer Cancer Discov. 4 2014 662 673
    • (2014) Cancer Discov. , vol.4 , pp. 662-673
    • Friboulet, L.1
  • 71
    • 3142595278 scopus 로고    scopus 로고
    • Crystal structure of the HGF β-chain in complex with the Sema domain of the Met receptor
    • J. Stamos Crystal structure of the HGF β-chain in complex with the Sema domain of the Met receptor EMBO J. 23 2004 2325 2335
    • (2004) EMBO J. , vol.23 , pp. 2325-2335
    • Stamos, J.1
  • 72
    • 51049117095 scopus 로고    scopus 로고
    • A high affinity hepatocyte growth factor-binding site in the immunoglobulin-like region of Met
    • C. Basilico A high affinity hepatocyte growth factor-binding site in the immunoglobulin-like region of Met J. Biol. Chem. 283 2008 21267 21277
    • (2008) J. Biol. Chem. , vol.283 , pp. 21267-21277
    • Basilico, C.1
  • 73
    • 78649420006 scopus 로고    scopus 로고
    • MET signalling: Principles and functions in development, organ regeneration and cancer
    • L. Trusolino MET signalling: principles and functions in development, organ regeneration and cancer Nat. Rev. Mol. Cell Biol. 11 2010 834 848
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 834-848
    • Trusolino, L.1
  • 74
    • 84919771755 scopus 로고    scopus 로고
    • MET and small-cell lung cancer
    • F. Gelsomino MET and small-cell lung cancer Cancers 6 2014 2100 2115
    • (2014) Cancers , vol.6 , pp. 2100-2115
    • Gelsomino, F.1
  • 75
    • 84920548555 scopus 로고    scopus 로고
    • Cabozantinib overcomes crizotinib resistance in ROS1 fusion positive cancer
    • R. Katayama Cabozantinib overcomes crizotinib resistance in ROS1 fusion positive cancer Clin. Cancer Res. 21 2015 166 174
    • (2015) Clin. Cancer Res. , vol.21 , pp. 166-174
    • Katayama, R.1
  • 76
    • 84867621201 scopus 로고    scopus 로고
    • Target binding properties and cellular activity of afatinib (BIBW 2992), an irreversible ErbB family blocker
    • F. Solca Target binding properties and cellular activity of afatinib (BIBW 2992), an irreversible ErbB family blocker J. Pharmacol. Exp. Ther. 343 2012 342 350
    • (2012) J. Pharmacol. Exp. Ther. , vol.343 , pp. 342-350
    • Solca, F.1
  • 77
    • 84897055483 scopus 로고    scopus 로고
    • Targeting Bruton's tyrosine kinase in B cell malignancies
    • R.W. Hendriks Targeting Bruton's tyrosine kinase in B cell malignancies Nat. Rev. Cancer 14 2014 219 232
    • (2014) Nat. Rev. Cancer , vol.14 , pp. 219-232
    • Hendriks, R.W.1
  • 78
    • 84879748062 scopus 로고    scopus 로고
    • Targeting BTK with ibrutinib in relapsed chronic lymphocytic leukemia
    • J.C. Byrd Targeting BTK with ibrutinib in relapsed chronic lymphocytic leukemia N. Eng. J. Med. 369 2013 32 42
    • (2013) N. Eng. J. Med. , vol.369 , pp. 32-42
    • Byrd, J.C.1
  • 79
    • 84895803751 scopus 로고    scopus 로고
    • Kinase inhibitors overachieve in CLL
    • K. Garber Kinase inhibitors overachieve in CLL Nat. Rev. Drug Discov. 13 2014 162 164
    • (2014) Nat. Rev. Drug Discov. , vol.13 , pp. 162-164
    • Garber, K.1
  • 80
    • 77249095150 scopus 로고    scopus 로고
    • Structures of human Bruton's tyrosine kinase in active and inactive conformations suggest a mechanism of activation for TEC family kinases
    • D.J. Marcotte Structures of human Bruton's tyrosine kinase in active and inactive conformations suggest a mechanism of activation for TEC family kinases Protein Sci. 19 2010 429 439
    • (2010) Protein Sci. , vol.19 , pp. 429-439
    • Marcotte, D.J.1
  • 81
    • 84868481873 scopus 로고    scopus 로고
    • Vemurafenib: The first drug approved for BRAF-mutant cancer
    • G. Bollag Vemurafenib: the first drug approved for BRAF-mutant cancer Nat. Rev. Drug Discov. 11 2012 873 886
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 873-886
    • Bollag, G.1
  • 82
    • 12144289677 scopus 로고    scopus 로고
    • Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF
    • P.T.C. Wan Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF Cell 116 2004 855 867
    • (2004) Cell , vol.116 , pp. 855-867
    • Wan, P.T.C.1
  • 83
    • 77956513286 scopus 로고    scopus 로고
    • Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma
    • G. Bollag Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma Nature 467 2010 596 599
    • (2010) Nature , vol.467 , pp. 596-599
    • Bollag, G.1
  • 84
    • 84921773577 scopus 로고    scopus 로고
    • Optimization of diarylthiazole B-Raf inhibitors: Identification of a compound endowed with high oral antitumor activity, mitigated hERG inhibition, and low paradoxical effect
    • M. Pulici Optimization of diarylthiazole B-Raf inhibitors: identification of a compound endowed with high oral antitumor activity, mitigated hERG inhibition, and low paradoxical effect ChemMedChem 10 2014 276 295
    • (2014) ChemMedChem , vol.10 , pp. 276-295
    • Pulici, M.1
  • 85
    • 84922103283 scopus 로고    scopus 로고
    • The biology and clinical development of MEK inhibitors for cancer
    • J.J. Luke The biology and clinical development of MEK inhibitors for cancer Drugs 74 2014 2111 2128
    • (2014) Drugs , vol.74 , pp. 2111-2128
    • Luke, J.J.1
  • 86
    • 79954576977 scopus 로고    scopus 로고
    • Discovery of a highly potent and selective MEK inhibitor: GSK1120212 (JTP-74057 DMSO solvate)
    • H. Abe Discovery of a highly potent and selective MEK inhibitor: GSK1120212 (JTP-74057 DMSO solvate) ACS Med. Chem. Lett. 2 2011 320 324
    • (2011) ACS Med. Chem. Lett. , vol.2 , pp. 320-324
    • Abe, H.1
  • 87
    • 79951722555 scopus 로고    scopus 로고
    • Discovery of TAK-733, a potent and selective MEK allosteric site inhibitor for the treatment of cancer
    • Q. Dong Discovery of TAK-733, a potent and selective MEK allosteric site inhibitor for the treatment of cancer Bioorg. Med. Chem. Lett. 21 2011 1315 1319
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 1315-1319
    • Dong, Q.1
  • 88
    • 84868224906 scopus 로고    scopus 로고
    • Combined BRAF and MEK inhibition in melanoma with BRAF V600 mutations
    • K.T. Flaherty Combined BRAF and MEK inhibition in melanoma with BRAF V600 mutations N. Eng. J. Med. 367 2012 1694 1703
    • (2012) N. Eng. J. Med. , vol.367 , pp. 1694-1703
    • Flaherty, K.T.1
  • 89
    • 84908257665 scopus 로고    scopus 로고
    • Combined BRAF and MEK inhibition versus BRAF inhibition alone in melanoma
    • G.V. Long Combined BRAF and MEK inhibition versus BRAF inhibition alone in melanoma N. Eng. J. Med. 371 2014 1877 1888
    • (2014) N. Eng. J. Med. , vol.371 , pp. 1877-1888
    • Long, G.V.1
  • 90
    • 78650636996 scopus 로고    scopus 로고
    • PI3K/Akt/mTOR pathway inhibitors in cancer: A perspective on clinical progress
    • P. Wu, and Y.Z. Hu PI3K/Akt/mTOR pathway inhibitors in cancer: a perspective on clinical progress Curr. Med. Chem. 17 2010 4326 4341
    • (2010) Curr. Med. Chem. , vol.17 , pp. 4326-4341
    • Wu, P.1    Hu, Y.Z.2
  • 91
    • 84922210268 scopus 로고    scopus 로고
    • Current treatment strategies for inhibiting mTOR in cancer
    • F. Chiarini Current treatment strategies for inhibiting mTOR in cancer Trends Pharmacol. Sci. 36 2015 124 135
    • (2015) Trends Pharmacol. Sci. , vol.36 , pp. 124-135
    • Chiarini, F.1
  • 92
    • 84899434901 scopus 로고    scopus 로고
    • Signaling through cyclin D-dependent kinases
    • Y.J. Choi, and L. Anders Signaling through cyclin D-dependent kinases Oncogene 33 2014 1890 1903
    • (2014) Oncogene , vol.33 , pp. 1890-1903
    • Choi, Y.J.1    Anders, L.2
  • 93
    • 84894211810 scopus 로고    scopus 로고
    • Overview of cyclins D1 function in cancer and the CDK inhibitor landscape: Past and present
    • M.C. Casimiro Overview of cyclins D1 function in cancer and the CDK inhibitor landscape: past and present Expert Opin. Investig. Drugs 23 2014 295 304
    • (2014) Expert Opin. Investig. Drugs , vol.23 , pp. 295-304
    • Casimiro, M.C.1
  • 94
    • 33745676300 scopus 로고    scopus 로고
    • Toward understanding the structural basis of cyclin-dependent kinase 6 specific inhibition
    • H. Lu, and U. Schulze-Gahmen Toward understanding the structural basis of cyclin-dependent kinase 6 specific inhibition J. Med. Chem. 49 2006 3826 3831
    • (2006) J. Med. Chem. , vol.49 , pp. 3826-3831
    • Lu, H.1    Schulze-Gahmen, U.2
  • 95
    • 0021828496 scopus 로고
    • Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation
    • M. Whitman Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation Nature 315 1985 239 242
    • (1985) Nature , vol.315 , pp. 239-242
    • Whitman, M.1
  • 96
    • 65649112446 scopus 로고    scopus 로고
    • PI3K inhibitors for cancer therapy: What has been achieved so far?
    • P. Wu PI3K inhibitors for cancer therapy: what has been achieved so far? Curr. Med. Chem. 16 2009 916 930
    • (2009) Curr. Med. Chem. , vol.16 , pp. 916-930
    • Wu, P.1
  • 97
    • 84896692766 scopus 로고    scopus 로고
    • Idelalisib and rituximab in relapsed chronic lymphocytic leukemia
    • R.R. Furman Idelalisib and rituximab in relapsed chronic lymphocytic leukemia N. Eng. J. Med. 370 2014 997 1007
    • (2014) N. Eng. J. Med. , vol.370 , pp. 997-1007
    • Furman, R.R.1
  • 98
    • 84901708950 scopus 로고    scopus 로고
    • CLL and NHL: The end of chemotherapy?
    • B.D. Cheson CLL and NHL: the end of chemotherapy? Blood 123 2014 3368 3370
    • (2014) Blood , vol.123 , pp. 3368-3370
    • Cheson, B.D.1
  • 99
    • 84903188335 scopus 로고    scopus 로고
    • 3K p110δ breaks regulatory T-cell-mediated immune tolerance to cancer
    • 3K p110δ breaks regulatory T-cell-mediated immune tolerance to cancer Nature 510 2014 407 411
    • (2014) Nature , vol.510 , pp. 407-411
    • Ali, K.1
  • 101
    • 84925815654 scopus 로고    scopus 로고
    • Structural, biochemical and biophysical characterization of idelalisib binding to phosphoinositide 3-kinase δ
    • J.R. Somoza Structural, biochemical and biophysical characterization of idelalisib binding to phosphoinositide 3-kinase δ J. Biol. Chem. 290 2015 8439 8446
    • (2015) J. Biol. Chem. , vol.290 , pp. 8439-8446
    • Somoza, J.R.1
  • 102
    • 84865060816 scopus 로고    scopus 로고
    • Small molecules targeting phosphoinositide 3-kinases
    • P. Wu, and Y. Hu Small molecules targeting phosphoinositide 3-kinases MedChemComm 3 2012 1337 1355
    • (2012) MedChemComm , vol.3 , pp. 1337-1355
    • Wu, P.1    Hu, Y.2
  • 103
    • 84901703641 scopus 로고    scopus 로고
    • Idelalisib, a selective inhibitor of phosphatidylinositol 3-kinase-δ, as therapy for previously treated indolent non-Hodgkin lymphoma
    • I.W. Flinn Idelalisib, a selective inhibitor of phosphatidylinositol 3-kinase-δ, as therapy for previously treated indolent non-Hodgkin lymphoma Blood 123 2014 3406 3413
    • (2014) Blood , vol.123 , pp. 3406-3413
    • Flinn, I.W.1
  • 104
    • 84901712964 scopus 로고    scopus 로고
    • Idelalisib, an inhibitor of phosphatidylinositol 3-kinase p110δ, for relapsed/refractory chronic lymphocytic leukemia
    • J.R. Brown Idelalisib, an inhibitor of phosphatidylinositol 3-kinase p110δ, for relapsed/refractory chronic lymphocytic leukemia Blood 123 2014 3390 3397
    • (2014) Blood , vol.123 , pp. 3390-3397
    • Brown, J.R.1
  • 105
    • 84893249799 scopus 로고    scopus 로고
    • PI3K and cancer: Lessons, challenges and opportunities
    • D.A. Fruman, and C. Rommel PI3K and cancer: lessons, challenges and opportunities Nat. Rev. Drug Discov. 13 2014 140 156
    • (2014) Nat. Rev. Drug Discov. , vol.13 , pp. 140-156
    • Fruman, D.A.1    Rommel, C.2
  • 106
    • 84964204680 scopus 로고    scopus 로고
    • Measurement of PIP3 levels reveals an unexpected role for p110β in early adaptive responses to p110α-specific inhibitors in luminal breast cancer
    • C. Costa Measurement of PIP3 levels reveals an unexpected role for p110β in early adaptive responses to p110α-specific inhibitors in luminal breast cancer Cancer Cell 27 2015 97 108
    • (2015) Cancer Cell , vol.27 , pp. 97-108
    • Costa, C.1
  • 107
    • 84929141919 scopus 로고    scopus 로고
    • Feedback suppression of PI3Kα signaling in PTEN-mutated tumors is relieved by selective inhibition of PI3Kβ
    • S. Schwartz Feedback suppression of PI3Kα signaling in PTEN-mutated tumors is relieved by selective inhibition of PI3Kβ Cancer Cell 27 2015 109 122
    • (2015) Cancer Cell , vol.27 , pp. 109-122
    • Schwartz, S.1
  • 108
    • 84919395951 scopus 로고    scopus 로고
    • An analysis of FDA-approved drugs for oncology
    • M.S. Kinch An analysis of FDA-approved drugs for oncology Drug Discov. Today 19 2014 1831 1835
    • (2014) Drug Discov. Today , vol.19 , pp. 1831-1835
    • Kinch, M.S.1
  • 109
    • 80755125575 scopus 로고    scopus 로고
    • Comprehensive analysis of kinase inhibitor selectivity
    • M.I. Davis Comprehensive analysis of kinase inhibitor selectivity Nat. Biotechnol. 29 2011 1046 1051
    • (2011) Nat. Biotechnol. , vol.29 , pp. 1046-1051
    • Davis, M.I.1
  • 110
    • 84891751622 scopus 로고    scopus 로고
    • The druggable genome: Evaluation of drug targets in clinical trials suggests major shifts in molecular class and indication
    • M. Rask-Andersen The druggable genome: evaluation of drug targets in clinical trials suggests major shifts in molecular class and indication Annu. Rev. Pharmacol. Toxicol. 54 2014 9 26
    • (2014) Annu. Rev. Pharmacol. Toxicol. , vol.54 , pp. 9-26
    • Rask-Andersen, M.1


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