메뉴 건너뛰기




Volumn 103, Issue , 2016, Pages 26-48

Classification of small molecule protein kinase inhibitors based upon the structures of their drug-enzyme complexes

Author keywords

ATP binding site; Catalytic spine; K E D D; Protein kinase structure; Regulatory spine; Residence time

Indexed keywords

3 (2,3 DIHYDROXYPROPYL) 6 FLUORO 5 (2 FLUORO 4 IODOANILINO) 8 METHYLPYRIDO[2,3 D]PYRIMIDINE 4,7 DIONE; AFATINIB; AXITINIB; BOSUTINIB; CABOZANTINIB; CERITINIB; CRIZOTINIB; DASATINIB; ERLOTINIB; EVEROLIMUS; GEFITINIB; IBRUTINIB; IMATINIB; LAPATINIB; LENVATINIB; NILOTINIB; NINTEDANIB; PALBOCICLIB; PONATINIB; PROTEIN KINASE; PROTEIN KINASE INHIBITOR; RAPAMYCIN; RUXOLITINIB; SORAFENIB; SUNITINIB; TEMSIROLIMUS; TOFACITINIB; UNINDEXED DRUG; VANDETANIB; VEMURAFENIB;

EID: 84947744392     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2015.10.021     Document Type: Review
Times cited : (612)

References (109)
  • 4
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases - The major drug targets of the twenty-first century?
    • P. Cohen Protein kinases - the major drug targets of the twenty-first century? Nat. Rev. Drug Discov. 1 2002 309 315
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 309-315
    • Cohen, P.1
  • 5
    • 0141788346 scopus 로고    scopus 로고
    • STI-571: An anticancer protein-tyrosine kinase inhibitor
    • R. Roskoski Jr. STI-571: an anticancer protein-tyrosine kinase inhibitor Biochem. Biophys. Res. Commun. 309 2003 709 717
    • (2003) Biochem. Biophys. Res. Commun. , vol.309 , pp. 709-717
    • Roskoski, R.1
  • 6
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • D.R. Knighton, J.H. Zheng, L.F. Ten Eyck, V.A. Ashford, N.H. Xuong, S.S. Taylor, and et al. 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.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.H.5    Taylor, S.S.6
  • 7
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • D.R. Knighton, J.H. Zheng, L.F. Ten Eyck, N.H. Xuong, S.S. Taylor, and J.M. Sowadski Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase Science 253 1991 414 420
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Xuong, N.H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 9
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • S.K. Hanks, A.M. Quinn, and T. Hunter The protein kinase family: conserved features and deduced phylogeny of the catalytic domains Science 241 1988 42 52
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 11
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; Controlling activity through activation segment conformation
    • B. Nolen, S. Taylor, and G. Ghosh Regulation of protein kinases; controlling activity through activation segment conformation Mol. Cell 15 2004 661 675
    • (2004) Mol. Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 12
    • 0026701674 scopus 로고
    • A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor
    • N. Gotoh, A. Tojo, M. Hino, Y. Yazaki, and M. Shibuya A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor Biochem. Biophys. Res. Commun. 186 1992 768 774
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 768-774
    • Gotoh, N.1    Tojo, A.2    Hino, M.3    Yazaki, Y.4    Shibuya, M.5
  • 13
    • 0033573921 scopus 로고    scopus 로고
    • Mechanism of biological synergy between cellular Src and epidermal growth factor receptor
    • D.A. Tice, J.S. Biscardi, A.L. Nickles, and S.J. Parsons Mechanism of biological synergy between cellular Src and epidermal growth factor receptor Proc. Natl. Acad. Sci. U. S. A. 96 1999 1415 1420
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 1415-1420
    • Tice, D.A.1    Biscardi, J.S.2    Nickles, A.L.3    Parsons, S.J.4
  • 14
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • M. Huse, and J. Kuriyan The conformational plasticity of protein kinases Cell 109 2002 275 282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 15
    • 33845197964 scopus 로고    scopus 로고
    • Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism
    • A.P. Kornev, N.M. Haste, S.S. Taylor, and L.F. Ten Eyck Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism Proc. Natl. Acad. Sci. U. S. A. 103 2006 17783 17788
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 17783-17788
    • Kornev, A.P.1    Haste, N.M.2    Taylor, S.S.3    Ten Eyck, L.F.4
  • 17
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • J. Zhang, P.L. Yang, and N.S. Gray Targeting cancer with small molecule kinase inhibitors Nat. Rev. Cancer 9 2009 28 39
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 18
    • 79959476700 scopus 로고    scopus 로고
    • The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling
    • A.C. Dar, and K.M. Shokat The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling Annu. Rev. Biochem. 80 2011 769 795
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 769-795
    • Dar, A.C.1    Shokat, K.M.2
  • 19
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • J. Monod, J.P. Changeux, and F. Jacob Allosteric proteins and cellular control systems J. Mol. Biol. 6 1963 306 329
    • (1963) J. Mol. Biol. , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.P.2    Jacob, F.3
  • 20
    • 77950573400 scopus 로고    scopus 로고
    • Through the gatekeeper door: Exploiting the active kinase conformation
    • F. Zuccotto, E. Ardini, E. Casale, and M. Angiolini Through the gatekeeper door: exploiting the active kinase conformation J. Med. Chem. 53 2010 2681 2694
    • (2010) J. Med. Chem. , vol.53 , pp. 2681-2694
    • Zuccotto, F.1    Ardini, E.2    Casale, E.3    Angiolini, M.4
  • 21
    • 84871730931 scopus 로고    scopus 로고
    • Approaches to discover non-ATP site inhibitors
    • L.K. Gavrin, and E. Saiah Approaches to discover non-ATP site inhibitors Med. Chem. Commun. 4 2013 41
    • (2013) Med. Chem. Commun. , vol.4 , pp. 41
    • Gavrin, L.K.1    Saiah, E.2
  • 22
    • 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
  • 23
    • 33846899405 scopus 로고    scopus 로고
    • Molecular recognition of protein kinase binding pockets for design of potent and selective kinase inhibitors
    • J.J. Liao Molecular recognition of protein kinase binding pockets for design of potent and selective kinase inhibitors J. Med. Chem. 50 2007 409 424
    • (2007) J. Med. Chem. , vol.50 , pp. 409-424
    • Liao, J.J.1
  • 24
    • 84893065058 scopus 로고    scopus 로고
    • KLIFS: A knowledge-based structural database to navigate kinase-ligand interaction space
    • O.P. van Linden, A.J. Kooistra, R. Leurs, I.J. de Esch, and C. de Graaf KLIFS: a knowledge-based structural database to navigate kinase-ligand interaction space J. Med. Chem. 57 2014 249 277
    • (2014) J. Med. Chem. , vol.57 , pp. 249-277
    • Van Linden, O.P.1    Kooistra, A.J.2    Leurs, R.3    De Esch, I.J.4    De Graaf, C.5
  • 25
    • 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, W.G. Bornmann, P. Pellicena, T. Schindler, D.R. Veach, W.T. Miller, and et al. 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    Bornmann, W.G.2    Pellicena, P.3    Schindler, T.4    Veach, D.R.5    Miller, W.T.6
  • 26
    • 84928907224 scopus 로고    scopus 로고
    • Ten things you should know about protein kinases: IUPHAR review 14
    • D. Fabbro, S.W. Cowan-Jacob, and H. Moebitz Ten things you should know about protein kinases: IUPHAR review 14 Br. J. Pharmacol. 172 2015 2675 2700
    • (2015) Br. J. Pharmacol. , vol.172 , pp. 2675-2700
    • Fabbro, D.1    Cowan-Jacob, S.W.2    Moebitz, H.3
  • 27
    • 84934268456 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-AKT-mammalian target of rapamycin (PI3K-Akt-mTOR) signaling pathway in non-small cell lung cancer
    • P.Y. Yip Phosphatidylinositol 3-kinase-AKT-mammalian target of rapamycin (PI3K-Akt-mTOR) signaling pathway in non-small cell lung cancer Transl. Lung Cancer Res. 4 2015 165 176
    • (2015) Transl. Lung Cancer Res. , vol.4 , pp. 165-176
    • Yip, P.Y.1
  • 28
    • 84940581015 scopus 로고    scopus 로고
    • Pleiotropic roles in cancer biology for multifaceted proteins FKBPs
    • S. Romano, A. D'Angelillo, and M.F. Romano Pleiotropic roles in cancer biology for multifaceted proteins FKBPs Biochim. Biophys. Acta 1850 2015 2061 2068
    • (2015) Biochim. Biophys. Acta , vol.1850 , pp. 2061-2068
    • Romano, S.1    D'Angelillo, A.2    Romano, M.F.3
  • 30
    • 2442701289 scopus 로고    scopus 로고
    • The ERBB/HER receptor protein-tyrosine kinases and cancer
    • R. Roskoski Jr. The ErbB/HER receptor protein-tyrosine kinases and cancer Biochem. Biophys. Res. Commun. 319 2004 1 11
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 1-11
    • Roskoski, R.1
  • 31
    • 84890041471 scopus 로고    scopus 로고
    • The ERBB/HER family of protein-tyrosine kinases and cancer
    • R. Roskoski Jr. The ErbB/HER family of protein-tyrosine kinases and cancer Pharmacol. Res. 79 2014 34 74
    • (2014) Pharmacol. Res. , vol.79 , pp. 34-74
    • Roskoski, R.1
  • 32
    • 84903581634 scopus 로고    scopus 로고
    • ERBB/HER protein-tyrosine kinases: Structures and small molecule inhibitors
    • R. Roskoski Jr. ErbB/HER protein-tyrosine kinases: structures and small molecule inhibitors Pharmacol. Res. 87 2014 42 59
    • (2014) Pharmacol. Res. , vol.87 , pp. 42-59
    • Roskoski, R.1
  • 34
    • 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, T.J. Boggon, Y. Li, M.S. Woo, H. Greulich, M. Meyerson, and et al. 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    Boggon, T.J.2    Li, Y.3    Woo, M.S.4    Greulich, H.5    Meyerson, M.6
  • 35
    • 0034068319 scopus 로고    scopus 로고
    • Antitumor effect and potentiation of cytotoxic drugs activity in human cancer cells by ZD-1839 (Iressa), an epidermal growth factor receptor-selective tyrosine kinase inhibitor
    • F. Ciardiello, R. Caputo, R. Bianco, V. Damiano, G. Pomatico, S. De Placido, and et al. Antitumor effect and potentiation of cytotoxic drugs activity in human cancer cells by ZD-1839 (Iressa), an epidermal growth factor receptor-selective tyrosine kinase inhibitor Clin. Cancer Res. 6 2000 2053 2063
    • (2000) Clin. Cancer Res. , vol.6 , pp. 2053-2063
    • Ciardiello, F.1    Caputo, R.2    Bianco, R.3    Damiano, V.4    Pomatico, G.5    De Placido, S.6
  • 36
    • 84931374307 scopus 로고    scopus 로고
    • Use of the epidermal growth factor receptor inhibitors gefitinib, erlotinib, afatinib, dacomitinib, and icotinib in the treatment of non-small-cell lung cancer: A systematic review
    • P.M. Ellis, N. Coakley, R. Feld, S. Kuruvilla, and Y.C. Ung Use of the epidermal growth factor receptor inhibitors gefitinib, erlotinib, afatinib, dacomitinib, and icotinib in the treatment of non-small-cell lung cancer: a systematic review Curr. Oncol. 22 2015 e183 e215
    • (2015) Curr. Oncol. , vol.22 , pp. e183-e215
    • Ellis, P.M.1    Coakley, N.2    Feld, R.3    Kuruvilla, S.4    Ung, Y.C.5
  • 37
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
    • J. Stamos, M.X. Sliwkowski, and C. Eigenbrot Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor J. Biol. Chem. 277 2002 46265 46272
    • (2002) J. Biol. Chem. , vol.277 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 38
    • 84940093612 scopus 로고    scopus 로고
    • Perspectives in the treatment of pancreatic adenocarcinoma
    • A. Cid-Arregui, and V. Juarez Perspectives in the treatment of pancreatic adenocarcinoma World J. Gastroenterol. 21 2015 9297 9316
    • (2015) World J. Gastroenterol. , vol.21 , pp. 9297-9316
    • Cid-Arregui, A.1    Juarez, V.2
  • 39
    • 0015694748 scopus 로고
    • Letter: A new consistent chromosomal abnormality in chronic myelogenous leukaemia identified by quinacrine fluorescence and Giemsa staining
    • J.D. Rowley Letter: a new consistent chromosomal abnormality in chronic myelogenous leukaemia identified by quinacrine fluorescence and Giemsa staining Nature 243 1973 290 293
    • (1973) Nature , vol.243 , pp. 290-293
    • Rowley, J.D.1
  • 40
    • 0021346853 scopus 로고
    • Philadelphia chromosomal breakpoints are clustered within a limited region, bcr, on chromosome 22
    • J. Groffen, J.R. Stephenson, N. Heisterkamp, A. de Kein, C.R. Bartram, and G. Grosveld Philadelphia chromosomal breakpoints are clustered within a limited region, bcr, on chromosome 22 Cell 36 1984 93 99
    • (1984) Cell , vol.36 , pp. 93-99
    • Groffen, J.1    Stephenson, J.R.2    Heisterkamp, N.3    De Kein, A.4    Bartram, C.R.5    Grosveld, G.6
  • 41
    • 84931569737 scopus 로고    scopus 로고
    • Use of second- and third-generation tyrosine kinase inhibitors in the treatment of chronic myeloid leukemia: An evolving treatment paradigm
    • E. Jabbour, H. Kantarjian, and J. Cortes Use of second- and third-generation tyrosine kinase inhibitors in the treatment of chronic myeloid leukemia: an evolving treatment paradigm Clin. Lymphoma Myeloma Leuk. 15 2015 323 334
    • (2015) Clin. Lymphoma Myeloma Leuk. , vol.15 , pp. 323-334
    • Jabbour, E.1    Kantarjian, H.2    Cortes, J.3
  • 42
    • 33745283618 scopus 로고    scopus 로고
    • The structure of Dasatinib (BMS-354825) bound to activated ABL kinase domain elucidates its inhibitory activity against imatinib-resistant ABL mutants
    • J.S. Tokarski, J.A. Newitt, C.Y. Chang, J.D. Cheng, M. Wittekind, S.E. Kiefer, and et al. The structure of Dasatinib (BMS-354825) bound to activated ABL kinase domain elucidates its inhibitory activity against imatinib-resistant ABL mutants Cancer Res. 66 2006 5790 5797
    • (2006) Cancer Res. , vol.66 , pp. 5790-5797
    • Tokarski, J.S.1    Newitt, J.A.2    Chang, C.Y.3    Cheng, J.D.4    Wittekind, M.5    Kiefer, S.E.6
  • 43
    • 21144451094 scopus 로고    scopus 로고
    • In vitro activity of Bcr-Abl inhibitors AMN107 and BMS-354825 against clinically relevant imatinib-resistant Abl kinase domain mutants
    • T. O'Hare, D.K. Walters, E.P. Stoffregen, T. Jia, P.W. Manley, J. Mestan, and et al. In vitro activity of Bcr-Abl inhibitors AMN107 and BMS-354825 against clinically relevant imatinib-resistant Abl kinase domain mutants Cancer Res. 65 2005 4500 4505
    • (2005) Cancer Res. , vol.65 , pp. 4500-4505
    • O'Hare, T.1    Walters, D.K.2    Stoffregen, E.P.3    Jia, T.4    Manley, P.W.5    Mestan, J.6
  • 44
    • 3142676436 scopus 로고    scopus 로고
    • Overriding imatinib resistance with a novel ABL kinase inhibitor
    • N.P. Shah, C. Tran, F.Y. Lee, P. Chen, D. Norris, and C.L. Sawyers Overriding imatinib resistance with a novel ABL kinase inhibitor Science 305 2004 399 401
    • (2004) Science , vol.305 , pp. 399-401
    • Shah, N.P.1    Tran, C.2    Lee, F.Y.3    Chen, P.4    Norris, D.5    Sawyers, C.L.6
  • 45
    • 84906937473 scopus 로고    scopus 로고
    • Practical issues surrounding the explosion of tyrosine kinase inhibitors for the management of chronic myeloid leukemia
    • M.S. Mathisen, H.M. Kantarjian, J. Cortes, and E.J. Jabbour Practical issues surrounding the explosion of tyrosine kinase inhibitors for the management of chronic myeloid leukemia Blood Rev. 28 2014 179 187
    • (2014) Blood Rev. , vol.28 , pp. 179-187
    • Mathisen, M.S.1    Kantarjian, H.M.2    Cortes, J.3    Jabbour, E.J.4
  • 46
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • M.A. Lemmon, and J. Schlessinger Cell signaling by receptor tyrosine kinases Cell 141 2010 1117 1134
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 47
    • 84872288990 scopus 로고    scopus 로고
    • Anaplastic lymphoma kinase (ALK): Structure, oncogenic activation, and pharmacological inhibition
    • R. Roskoski Jr. Anaplastic lymphoma kinase (ALK): structure, oncogenic activation, and pharmacological inhibition Pharmacol. Res. 68 2013 68 94
    • (2013) Pharmacol. Res. , vol.68 , pp. 68-94
    • Roskoski, R.1
  • 48
    • 84883017405 scopus 로고    scopus 로고
    • The preclinical profile of crizotinib for the treatment of non-small-cell lung cancer and other neoplastic disorders
    • R. Roskoski Jr. The preclinical profile of crizotinib for the treatment of non-small-cell lung cancer and other neoplastic disorders Expert. Opin. Drug Discov. 8 2013 1165 1179
    • (2013) Expert. Opin. Drug Discov. , vol.8 , pp. 1165-1179
    • Roskoski, R.1
  • 49
    • 34547638047 scopus 로고    scopus 로고
    • Identification of the transforming EML4-ALK fusion gene in non-small-cell lung cancer
    • M. Soda, Y.L. Choi, M. Enomoto, S. Takada, Y. Yamashita, S. Ishikawa, and et al. Identification of the transforming EML4-ALK fusion gene in non-small-cell lung cancer Nature 448 2007 561 566
    • (2007) Nature , vol.448 , pp. 561-566
    • Soda, M.1    Choi, Y.L.2    Enomoto, M.3    Takada, S.4    Yamashita, Y.5    Ishikawa, S.6
  • 50
    • 36849065315 scopus 로고    scopus 로고
    • Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer
    • K. Rikova, A. Guo, Q. Zeng, A. Possemato, J. Yu, H. Haack, and et al. Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer Cell 131 2007 1190 1203
    • (2007) Cell , vol.131 , pp. 1190-1203
    • Rikova, K.1    Guo, A.2    Zeng, Q.3    Possemato, A.4    Yu, J.5    Haack, H.6
  • 51
    • 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, M. Tran-Dubé, H. Shen, M. Nambu, P.P. Kung, M. Pairish, and et al. 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    Tran-Dubé, M.2    Shen, H.3    Nambu, M.4    Kung, P.P.5    Pairish, M.6
  • 53
    • 84938342028 scopus 로고    scopus 로고
    • A historical overview of protein kinases and their targeted small molecule inhibitors
    • R. Roskoski Jr. A historical overview of protein kinases and their targeted small molecule inhibitors Pharmacol. Res. 100 2015 1 23
    • (2015) Pharmacol. Res. , vol.100 , pp. 1-23
    • Roskoski, R.1
  • 54
    • 84940190644 scopus 로고    scopus 로고
    • Treating patients with ALK-positive non-small cell lung cancer: Latest evidence and management strategy
    • B.C. Liao, C.C. Lin, J.Y. Shih, and J.C. Yang Treating patients with ALK-positive non-small cell lung cancer: latest evidence and management strategy Ther. Adv. Med. Oncol. 7 2015 274 290
    • (2015) Ther. Adv. Med. Oncol. , vol.7 , pp. 274-290
    • Liao, B.C.1    Lin, C.C.2    Shih, J.Y.3    Yang, J.C.4
  • 55
    • 84903466222 scopus 로고    scopus 로고
    • The ALK inhibitor ceritinib overcomes crizotinib resistance in non-small cell lung cancer
    • L. Friboulet, N. Li, R. Katayama, C.C. Lee, J.F. Gainor, A.S. Crystal, and et al. 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    Li, N.2    Katayama, R.3    Lee, C.C.4    Gainor, J.F.5    Crystal, A.S.6
  • 56
    • 77950684805 scopus 로고    scopus 로고
    • Preclinical characterization of the selective JAK1/2 inhibitor INCB018424: Therapeutic implications for the treatment of myeloproliferative neoplasms
    • A. Quintás-Cardama, K. Vaddi, P. Liu, T. Manshouri, J. Li, P.A. Scherle, and et al. Preclinical characterization of the selective JAK1/2 inhibitor INCB018424: therapeutic implications for the treatment of myeloproliferative neoplasms Blood 115 2010 3109 3117
    • (2010) Blood , vol.115 , pp. 3109-3117
    • Quintás-Cardama, A.1    Vaddi, K.2    Liu, P.3    Manshouri, T.4    Li, J.5    Scherle, P.A.6
  • 57
    • 84947812154 scopus 로고    scopus 로고
    • Polycythemia vera: An appraisal of the biology and management 10 years after the discovery of JAK2 V617F
    • pii: JCO.2015.61.6474
    • B.L. Stein, S.T. Oh, D. Berenzon, G.S. Hobbs, M. Kremyanskaya, R.K. Rampal, C.N. Abboud, and et al. Polycythemia vera: an appraisal of the biology and management 10 years after the discovery of JAK2 V617F J. Clin. Oncol. 2015 pii: JCO.2015.61.6474
    • (2015) J. Clin. Oncol.
    • Stein, B.L.1    Oh, S.T.2    Berenzon, D.3    Hobbs, G.S.4    Kremyanskaya, M.5    Rampal, R.K.6    Abboud, C.N.7
  • 58
    • 84907082111 scopus 로고    scopus 로고
    • C-Src binds to the cancer drug ruxolitinib with an active conformation
    • Y. Duan, L. Chen, Y. Chen, and X.G. Fan c-Src binds to the cancer drug ruxolitinib with an active conformation PLoS One 9 2014 e106225
    • (2014) PLoS One , vol.9 , pp. e106225
    • Duan, Y.1    Chen, L.2    Chen, Y.3    Fan, X.G.4
  • 61
    • 66249118670 scopus 로고    scopus 로고
    • Vandetanib (ZD6474), a dual inhibitor of vascular endothelial growth factor receptor (VEGFR) and epidermal growth factor receptor (EGFR) tyrosine kinases: Current status and future directions
    • A. Morabito, M.C. Piccirillo, F. Falasconi, G. De Feo, A. Del Giudice, J. Bryce, and et al. Vandetanib (ZD6474), a dual inhibitor of vascular endothelial growth factor receptor (VEGFR) and epidermal growth factor receptor (EGFR) tyrosine kinases: current status and future directions Oncologist 14 2009 378 390
    • (2009) Oncologist , vol.14 , pp. 378-390
    • Morabito, A.1    Piccirillo, M.C.2    Falasconi, F.3    De Feo, G.4    Del Giudice, A.5    Bryce, J.6
  • 62
    • 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
  • 63
    • 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, A. Patny, I.K. Leung, B. Korniski, T.L. Emmons, T. Hall, and et al. 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    Patny, A.2    Leung, I.K.3    Korniski, B.4    Emmons, T.L.5    Hall, T.6
  • 64
    • 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, R.S. Bamert, O. Patel, C. Wang, P.M. Walden, A.F. Wilks, and et al. 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    Bamert, R.S.2    Patel, O.3    Wang, C.4    Walden, P.M.5    Wilks, A.F.6
  • 65
    • 84908473540 scopus 로고    scopus 로고
    • Cyclin-dependent kinases
    • M. Malumbres Cyclin-dependent kinases Genome Biol. 15 2014 122
    • (2014) Genome Biol. , vol.15 , pp. 122
    • Malumbres, M.1
  • 66
    • 84905699926 scopus 로고    scopus 로고
    • Palbociclib: An evidence-based review of its potential in the treatment of breast cancer
    • K.A. Cadoo, A. Gucalp, and T.A. Traina Palbociclib: an evidence-based review of its potential in the treatment of breast cancer Breast Cancer (Dove Med. Press) 6 2014 123 133
    • (2014) Breast Cancer (Dove Med. Press) , vol.6 , pp. 123-133
    • Cadoo, K.A.1    Gucalp, A.2    Traina, T.A.3
  • 67
    • 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
  • 68
    • 84923102615 scopus 로고    scopus 로고
    • Src protein-tyrosine kinase structure, mechanism, and small molecule inhibitors
    • R. Roskoski Jr. Src protein-tyrosine kinase structure, mechanism, and small molecule inhibitors Pharmacol. Res. 94 2015 9 25
    • (2015) Pharmacol. Res. , vol.94 , pp. 9-25
    • Roskoski, R.1
  • 69
    • 80052483131 scopus 로고    scopus 로고
    • Inhibition of Src family kinases and receptor tyrosine kinases by dasatinib: Possible combinations in solid tumors
    • J.C. Montero, S. Seoane, A. Ocaña, and A. Pandiella Inhibition of Src family kinases and receptor tyrosine kinases by dasatinib: possible combinations in solid tumors Clin. Cancer Res. 17 2011 5546 5552
    • (2011) Clin. Cancer Res. , vol.17 , pp. 5546-5552
    • Montero, J.C.1    Seoane, S.2    Ocaña, A.3    Pandiella, A.4
  • 70
    • 84901218392 scopus 로고    scopus 로고
    • The anti-apoptotic form of tyrosine kinase Lyn that is generated by proteolysis is degraded by the N-end rule pathway
    • M.A. Eldeeb, and R.P. Fahlman The anti-apoptotic form of tyrosine kinase Lyn that is generated by proteolysis is degraded by the N-end rule pathway Oncotarget 5 2014 2714 2722
    • (2014) Oncotarget , vol.5 , pp. 2714-2722
    • Eldeeb, M.A.1    Fahlman, R.P.2
  • 71
    • 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.T. Truesdale, O.B. McDonald, D. Yuan, A. Hassell, S.H. Dickerson, and et al. 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    Truesdale, A.T.2    McDonald, O.B.3    Yuan, D.4    Hassell, A.5    Dickerson, S.H.6
  • 72
    • 84862294189 scopus 로고    scopus 로고
    • ERK1/2 MAP kinases: Structure, function, and regulation
    • R. Roskoski Jr. ERK1/2 MAP kinases: structure, function, and regulation Pharmacol. Res. 66 2012 105 143
    • (2012) Pharmacol. Res. , vol.66 , pp. 105-143
    • Roskoski, R.1
  • 73
    • 77956513286 scopus 로고    scopus 로고
    • Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF -mutant melanoma
    • G. Bollag, P. Hirth, J. Tsai, J. Zhang, P.N. Ibrahim, H. Cho, and et al. 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    Hirth, P.2    Tsai, J.3    Zhang, J.4    Ibrahim, P.N.5    Cho, H.6
  • 75
  • 76
    • 33947370773 scopus 로고    scopus 로고
    • Vascular endothelial growth factor (VEGF) signaling in tumor progression
    • R. Roskoski Jr. Vascular endothelial growth factor (VEGF) signaling in tumor progression Crit. Rev. Oncol. Hematol. 62 2007 179 213
    • (2007) Crit. Rev. Oncol. Hematol. , vol.62 , pp. 179-213
    • Roskoski, R.1
  • 78
    • 84870005636 scopus 로고    scopus 로고
    • Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain
    • J.H. Park, Y. Liu, M.A. Lemmon, and R. Radhakrishnan Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain Biochem. J. 448 2012 417 423
    • (2012) Biochem. J. , vol.448 , pp. 417-423
    • Park, J.H.1    Liu, Y.2    Lemmon, M.A.3    Radhakrishnan, R.4
  • 81
    • 84903208494 scopus 로고    scopus 로고
    • Exploration of type II binding mode: A privileged approach for kinase inhibitor focused drug discovery?
    • Z. Zhao, H. Wu, L. Wang, Y. Liu, S. Knapp, Q. Liu, and N.S. Gray 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    Wu, H.2    Wang, L.3    Liu, Y.4    Knapp, S.5    Liu, Q.6    Gray, N.S.7
  • 82
    • 27744551009 scopus 로고    scopus 로고
    • Structure and regulation of Kit protein-tyrosine kinase-the stem cell factor receptor
    • R. Roskoski Jr. Structure and regulation of Kit protein-tyrosine kinase-the stem cell factor receptor Biochem. Biophys. Res. Commun. 338 2005 1307 1315
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 1307-1315
    • Roskoski, R.1
  • 83
    • 25844507795 scopus 로고    scopus 로고
    • Signaling by Kit protein-tyrosine kinase-the stem cell factor receptor
    • R. Roskoski Jr. Signaling by Kit protein-tyrosine kinase-the stem cell factor receptor Biochem. Biophys. Res. Commun. 337 2005 1 13
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 1-13
    • Roskoski, R.1
  • 84
    • 2942542387 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition and STI-571 inhibition of c-Kit tyrosine kinase
    • C.D. Mol, D.R. Dougan, T.R. Schneider, R.J. Skene, M.L. Kraus, D.N. Scheibe, and et al. Structural basis for the autoinhibition and STI-571 inhibition of c-Kit tyrosine kinase J. Biol. Chem. 279 2004 31655 31663
    • (2004) J. Biol. Chem. , vol.279 , pp. 31655-31663
    • Mol, C.D.1    Dougan, D.R.2    Schneider, T.R.3    Skene, R.J.4    Kraus, M.L.5    Scheibe, D.N.6
  • 86
    • 12144289677 scopus 로고    scopus 로고
    • Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF
    • P.T. Wan, M.J. Garnett, S.M. Roe, S. Lee, D. Niculescu-Duvaz, V.M. Good, and et al. 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.1    Garnett, M.J.2    Roe, S.M.3    Lee, S.4    Niculescu-Duvaz, D.5    Good, V.M.6
  • 87
    • 80052034056 scopus 로고    scopus 로고
    • The structure of CDK8/CycC implicates specificity in the CDK/cyclin family and reveals interaction with a deep pocket binder
    • E.V. Schneider, J. Böttcher, M. Blaesse, L. Neumann, R. Huber, and K. Maskos The structure of CDK8/CycC implicates specificity in the CDK/cyclin family and reveals interaction with a deep pocket binder J. Mol. Biol. 412 2011 251 266
    • (2011) J. Mol. Biol. , vol.412 , pp. 251-266
    • Schneider, E.V.1    Böttcher, J.2    Blaesse, M.3    Neumann, L.4    Huber, R.5    Maskos, K.6
  • 88
    • 84867816311 scopus 로고    scopus 로고
    • Molecular conformations, interactions, and properties associated with drug efficiency and clinical performance among VEGFR TK inhibitors
    • M. McTigue, B.W. Murray, J.H. Chen, Y.L. Deng, J. Solowiej, and R.S. Kania 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    Murray, B.W.2    Chen, J.H.3    Deng, Y.L.4    Solowiej, J.5    Kania, R.S.6
  • 90
    • 78650159009 scopus 로고    scopus 로고
    • Structural mechanism of the Pan-BCR-ABL inhibitor ponatinib (AP24534): Lessons for overcoming kinase inhibitor resistance
    • T. Zhou, L. Commodore, W.S. Huang, Y. Wang, M. Thomas, J. Keats, and et al. Structural mechanism of the Pan-BCR-ABL inhibitor ponatinib (AP24534): lessons for overcoming kinase inhibitor resistance Chem. Biol. Drug Des. 77 2011 1 11
    • (2011) Chem. Biol. Drug Des. , vol.77 , pp. 1-11
    • Zhou, T.1    Commodore, L.2    Huang, W.S.3    Wang, Y.4    Thomas, M.5    Keats, J.6
  • 92
    • 84916911952 scopus 로고    scopus 로고
    • Ponatinib inhibits polyclonal drug-resistant KIT oncoproteins and shows therapeutic potential in heavily pretreated gastrointestinal stromal tumor (GIST) patients
    • A.P. Garner, J.M. Gozgit, R. Anjum, S. Vodala, A. Schrock, T. Zhou, and et al. Ponatinib inhibits polyclonal drug-resistant KIT oncoproteins and shows therapeutic potential in heavily pretreated gastrointestinal stromal tumor (GIST) patients Clin. Cancer Res. 20 2014 5745 5755
    • (2014) Clin. Cancer Res. , vol.20 , pp. 5745-5755
    • Garner, A.P.1    Gozgit, J.M.2    Anjum, R.3    Vodala, S.4    Schrock, A.5    Zhou, T.6
  • 93
    • 60849113175 scopus 로고    scopus 로고
    • KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients
    • K.S. Gajiwala, J.C. Wu, J. Christensen, G.D. Deshmukh, W. Diehl, J.P. DiNitto, and et al. KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients Proc. Natl. Acad. Sci. U. S. A. 106 2009 1542 1547
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 1542-1547
    • Gajiwala, K.S.1    Wu, J.C.2    Christensen, J.3    Deshmukh, G.D.4    Diehl, W.5    DiNitto, J.P.6
  • 94
    • 84942327021 scopus 로고    scopus 로고
    • Evidence for its therapeutic potential in idiopathic pulmonary fibrosis
    • M. Inomata, Y. Nishioka, and Azuma A. Nintedanib evidence for its therapeutic potential in idiopathic pulmonary fibrosis Core Evid. 10 2015 89 98
    • (2015) Core Evid. , vol.10 , pp. 89-98
    • Inomata, M.1    Nishioka, Y.2    Nintedanib, A.A.3
  • 95
    • 66449098872 scopus 로고    scopus 로고
    • VEGF ameliorates pulmonary hypertension through inhibition of endothelial apoptosis in experimental lung fibrosis in rats
    • L. Farkas, D. Farkas, K. Ask, A. Möller, J. Gauldie, P. Margetts, and et al. VEGF ameliorates pulmonary hypertension through inhibition of endothelial apoptosis in experimental lung fibrosis in rats J. Clin. Invest. 119 2009 1298 1311
    • (2009) J. Clin. Invest. , vol.119 , pp. 1298-1311
    • Farkas, L.1    Farkas, D.2    Ask, K.3    Möller, A.4    Gauldie, J.5    Margetts, P.6
  • 96
    • 49649123154 scopus 로고    scopus 로고
    • BIBF 1120: Triple angiokinase inhibitor with sustained receptor blockade and good antitumor efficacy
    • F. Hilberg, G.J. Roth, M. Krssak, S. Kautschitsch, W. Sommergruber, U. Tontsch-Grunt, and et al. BIBF 1120: triple angiokinase inhibitor with sustained receptor blockade and good antitumor efficacy Cancer Res. 68 2008 4774 4782
    • (2008) Cancer Res. , vol.68 , pp. 4774-4782
    • Hilberg, F.1    Roth, G.J.2    Krssak, M.3    Kautschitsch, S.4    Sommergruber, W.5    Tontsch-Grunt, U.6
  • 99
    • 79951722555 scopus 로고    scopus 로고
    • Discovery of TAK-733, a potent and selective MEK allosteric site inhibitor for the treatment of cancer
    • Q. Dong, D.R. Dougan, X. Gong, P. Halkowycz, B. Jin, T. Kanouni, and et al. 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    Dougan, D.R.2    Gong, X.3    Halkowycz, P.4    Jin, B.5    Kanouni, T.6
  • 100
    • 80053576891 scopus 로고    scopus 로고
    • Protein kinase biochemistry and drug discovery
    • P.A. Schwartz, and B.W. Murray Protein kinase biochemistry and drug discovery Bioorg. Chem. 39 2011 192 210
    • (2011) Bioorg. Chem. , vol.39 , pp. 192-210
    • Schwartz, P.A.1    Murray, B.W.2
  • 101
    • 84867621201 scopus 로고    scopus 로고
    • Target binding properties and cellular activity of afatinib (BIBW 2992), an irreversible ERBB family blocker
    • F. Solca, G. Dahl, A. Zoephel, G. Bader, M. Sanderson, C. Klein, and et al. 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    Dahl, G.2    Zoephel, A.3    Bader, G.4    Sanderson, M.5    Klein, C.6
  • 102
    • 33748325882 scopus 로고    scopus 로고
    • Drug-target residence time and its implications for lead optimization
    • R.A. Copeland, D.L. Pompliano, and T.D. Meek Drug-target residence time and its implications for lead optimization Nat. Rev. Drug. Discov. 5 2006 730 739
    • (2006) Nat. Rev. Drug. Discov. , vol.5 , pp. 730-739
    • Copeland, R.A.1    Pompliano, D.L.2    Meek, T.D.3
  • 103
    • 44049103958 scopus 로고    scopus 로고
    • Residence time of receptor-ligand complexes and its effect on biological function
    • Erratum in: Biochemistry 2008; 47: 8465
    • P.J. Tummino, and R.A. Copeland Residence time of receptor-ligand complexes and its effect on biological function Biochemistry 47 2008 5481 5492 Erratum in: Biochemistry 2008; 47: 8465
    • (2008) Biochemistry , vol.47 , pp. 5481-5492
    • Tummino, P.J.1    Copeland, R.A.2
  • 104
    • 80052462704 scopus 로고    scopus 로고
    • Conformational adaptation in drug-target interactions and residence time
    • R.A. Copeland Conformational adaptation in drug-target interactions and residence time Future Med. Chem. 3 2011 1491 1501
    • (2011) Future Med. Chem. , vol.3 , pp. 1491-1501
    • Copeland, R.A.1
  • 105
    • 79952375489 scopus 로고    scopus 로고
    • HTS reporter displacement assay for fragment screening and fragment evolution toward leads with optimized binding kinetics, binding selectivity, and thermodynamic signature
    • L. Neumann, K. von König, and D. Ullmann HTS reporter displacement assay for fragment screening and fragment evolution toward leads with optimized binding kinetics, binding selectivity, and thermodynamic signature Methods Enzymol. 493 2011 299 320
    • (2011) Methods Enzymol. , vol.493 , pp. 299-320
    • Neumann, L.1    Von König, K.2    Ullmann, D.3
  • 106
    • 84941803293 scopus 로고
    • The ABC of protein kinase conformations
    • H. Möbitz The ABC of protein kinase conformations Biochim. Biophys. Acta 2015 1854 1555 1566
    • (1854) Biochim. Biophys. Acta , vol.2015 , pp. 1555-1566
    • Möbitz, H.1
  • 108
    • 84872515516 scopus 로고    scopus 로고
    • Kinase drug discovery - What's next in the field?
    • P. Cohen, and D.R. Alessi Kinase drug discovery - what's next in the field? ACS Chem. Biol. 8 2013 96 104
    • (2013) ACS Chem. Biol. , vol.8 , pp. 96-104
    • Cohen, P.1    Alessi, D.R.2
  • 109
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.