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Volumn 34, Issue 6 SUPPL., 2003, Pages

Novel protein kinase inhibitors: SMART drug design technology

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; BCR ABL PROTEIN; C TERMINAL SRC KINASE; COLONY STIMULATING FACTOR RECEPTOR; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE 1; CYCLIN DEPENDENT KINASE 2; EPIDERMAL GROWTH FACTOR RECEPTOR; FIBROBLAST GROWTH FACTOR RECEPTOR; HEMATOPOIETIC CELL KINASE; I KAPPA B; INSULIN RECEPTOR; JANUS KINASE; MITOGEN ACTIVATED PROTEIN KINASE; NERVE GROWTH FACTOR RECEPTOR; PHOSPHOINOSITOL 3 KINASE; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEIN; PROTEIN KINASE B; PROTEIN KINASE C; PROTEIN KINASE FYN; PROTEIN KINASE INHIBITOR; PROTEIN KINASE LCK; PROTEIN KINASE P60; PROTEIN TYROSINE KINASE; SOMATOMEDIN RECEPTOR; TRANSFORMING GROWTH FACTOR RECEPTOR; UNCLASSIFIED DRUG; UNINDEXED DRUG; VASCULOTROPIN RECEPTOR; ENZYME INHIBITOR;

EID: 0642367580     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/sawyerjun03revised     Document Type: Review
Times cited : (16)

References (98)
  • 2
    • 0037150728 scopus 로고    scopus 로고
    • Src in cancer: Deregulation and consequences for cell behaviour
    • Frame, M.C. 2002. Src in cancer: deregulation and consequences for cell behaviour. Biochim. Biophys. Acta 1602:114-130.
    • (2002) Biochim. Biophys. Acta , vol.1602 , pp. 114-130
    • Frame, M.C.1
  • 3
    • 0037519563 scopus 로고    scopus 로고
    • Cancer metastasis: Therapeutic targets and drug discovery
    • In press
    • Sawyer, T.K. Cancer metastasis: therapeutic targets and drug discovery. Expert Opin. Investig. Drugs (In press).
    • Expert Opin. Investig. Drugs
    • Sawyer, T.K.1
  • 4
    • 0001182421 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Structural determinants for target specificity
    • McMahon, G., L. Sun, C. Liang, and C. Tang. 1998. Protein kinase inhibitors: structural determinants for target specificity. Curr. Opin. Drug Discov. Devel. 1:131-146.
    • (1998) Curr. Opin. Drug Discov. Devel , vol.1 , pp. 131-146
    • McMahon, G.1    Sun, L.2    Liang, C.3    Tang, C.4
  • 5
    • 85017325712 scopus 로고    scopus 로고
    • Tyrosine kinases in diseases. Overview of kinase inhibitors as therapeutic agents and current drugs in clinical trials
    • Strawn, L.M. and L.K. Shawver. 1998. Tyrosine kinases in diseases. Overview of kinase inhibitors as therapeutic agents and current drugs in clinical trials. Exp. Opin. Invest. Drugs 7:533-573.
    • (1998) Exp. Opin. Invest. Drugs , vol.7 , pp. 533-573
    • Strawn, L.M.1    Shawver, L.K.2
  • 6
    • 0031731295 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors in cancer treatment (part II)
    • Traxler, P. 1998. Tyrosine kinase inhibitors in cancer treatment (part II). Exp. Opin. Ther. Patents 8:1599-1628.
    • (1998) Exp. Opin. Ther. Patents , vol.8 , pp. 1599-1628
    • Traxler, P.1
  • 7
    • 0031887743 scopus 로고    scopus 로고
    • Protein kinase inhibitors: The tyrosine-specific kinases
    • Lawrence, D.S. and J. Niu. 1998. Protein kinase inhibitors: the tyrosine-specific kinases. Pharmacol. Ther. 77:81-114.
    • (1998) Pharmacol. Ther. , vol.77 , pp. 81-114
    • Lawrence, D.S.1    Niu, J.2
  • 8
    • 0032830412 scopus 로고    scopus 로고
    • The rationale and strategy used to develop a series of highly potent, irreversible, inhibitors of the epidermal growth factor receptor family of tyrosine kinases
    • Bridges, A.J. 1999. The rationale and strategy used to develop a series of highly potent, irreversible, inhibitors of the epidermal growth factor receptor family of tyrosine kinases. Curr. Med. Chem. 6:825-843.
    • (1999) Curr. Med. Chem. , vol.6 , pp. 825-843
    • Bridges, A.J.1
  • 9
    • 0032854118 scopus 로고    scopus 로고
    • The structure-based design of ATP-site directed protein kinases
    • Toledo, L.M., N.B. Lydon, and D. Elbaum. 1999. The structure-based design of ATP-site directed protein kinases. Curr. Med. Chem. 6:775-805.
    • (1999) Curr. Med. Chem. , vol.6 , pp. 775-805
    • Toledo, L.M.1    Lydon, N.B.2    Elbaum, D.3
  • 10
    • 0032773425 scopus 로고    scopus 로고
    • Recent advances in protein kinase inhibition: Current molecular scaffolds used for inhibitor synthesis
    • Stover, D.R., N.B. Lydon, and J.J. Nunes. 1999. Recent advances in protein kinase inhibition: current molecular scaffolds used for inhibitor synthesis. Curr. Opin. Drug Discov. Devel. 2:274-285.
    • (1999) Curr. Opin. Drug Discov. Devel , vol.2 , pp. 274-285
    • Stover, D.R.1    Lydon, N.B.2    Nunes, J.J.3
  • 11
    • 0034048844 scopus 로고    scopus 로고
    • Kinase inhibitors in cancer therapy
    • Sedlacek, H.H. 2000. Kinase inhibitors in cancer therapy. Drugs 59:435-476.
    • (2000) Drugs , vol.59 , pp. 435-476
    • Sedlacek, H.H.1
  • 12
    • 0034199806 scopus 로고    scopus 로고
    • The role of oncogenic kinases in human cancer
    • Tsatsanis, C. and D.A. Spanidos. 2000. The role of oncogenic kinases in human cancer. Int. J. Mol. Med. 5:583-590.
    • (2000) Int. J. Mol. Med. , vol.5 , pp. 583-590
    • Tsatsanis, C.1    Spanidos, D.A.2
  • 14
    • 0035117012 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Emerging pharmacophores 1997-2000
    • Dumas, J. 2001. Protein kinase inhibitors: emerging pharmacophores 1997-2000. Exp. Opin. Ther. Patents 11:405-429.
    • (2001) Exp. Opin. Ther. Patents , vol.11 , pp. 405-429
    • Dumas, J.1
  • 16
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases-the major drug targets of the twenty-first century?
    • Cohen, P. 2002. Protein kinases - the major drug targets of the twenty-first century? Nat. Rev. Drug Discov. 1:309-315.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 309-315
    • Cohen, P.1
  • 19
    • 0036372416 scopus 로고    scopus 로고
    • Targeting protein kinases for bone disease: Discovery and development of Src inhibitors
    • Metcalf, C.A., III, M.R. van Schravendijk, D.C. Dalgarno, and T.K. Sawyer. 2002. Targeting protein kinases for bone disease: discovery and development of Src inhibitors. Curr. Pharm. Des. 8:2049-2075.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 2049-2075
    • Metcalf C.A. III1    Van Schravendijk, M.R.2    Dalgarno, D.C.3    Sawyer, T.K.4
  • 20
    • 0037392444 scopus 로고    scopus 로고
    • Issues and progress with protein kinase inhibitors for cancer treatment
    • Dancey, J. and E.A. Sausville. 2003. Issues and progress with protein kinase inhibitors for cancer treatment. Nat. Rev. Drug Discov. 2:296-313.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 296-313
    • Dancey, J.1    Sausville, E.A.2
  • 21
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • International Human Genome Consortium. 2001. Initial sequencing and analysis of the human genome. Nature 409:860-921.
    • (2001) Nature , vol.409 , pp. 860-921
  • 22
  • 24
    • 0037434853 scopus 로고    scopus 로고
    • Imatinib mesylate - The new gold standard for treatment of chronic myeloid leukemia
    • Peggs K. and S. Mackinnon. 2003. Imatinib mesylate - the new gold standard for treatment of chronic myeloid leukemia. N. Engl. J. Med. 348:1048-1050.
    • (2003) N. Engl. J. Med. , vol.348 , pp. 1048-1050
    • Peggs, K.1    Mackinnon, S.2
  • 25
    • 0037254419 scopus 로고    scopus 로고
    • Imatinib alone and in combination for chronic myeloid leukemia
    • Druker, B.J. 2003. Imatinib alone and in combination for chronic myeloid leukemia. Semin. Hematol. 40:50-58.
    • (2003) Semin. Hematol. , vol.40 , pp. 50-58
    • Druker, B.J.1
  • 26
    • 0036989987 scopus 로고    scopus 로고
    • Imatinib for relapsed BCR/ABL positive leukemias
    • Ottmann, O.G., B. Wassmann, and D. Hoelzer. 2002. Imatinib for relapsed BCR/ABL positive leukemias. Ann. Hematol. 81(Supp12):S36-S37.
    • (2002) Ann. Hematol. , vol.81 , Issue.SUPPL. 2
    • Ottmann, O.G.1    Wassmann, B.2    Hoelzer, D.3
  • 27
    • 0037109014 scopus 로고    scopus 로고
    • ZD1839 (Iressa): An orally active inhibitor of epidermal growth factor signaling with potential for cancer therapy
    • Wakeling, A.E., S.P. Guy, J.R. Woodburn, S.E. Ashton, B.J. Curry, A.J. Barker, and ICH. Gibson. 2002. ZD1839 (Iressa): an orally active inhibitor of epidermal growth factor signaling with potential for cancer therapy. Cancer Res. 62:49-54.
    • (2002) Cancer Res. , vol.62 , pp. 49-54
    • Wakeling, A.E.1    Guy, S.P.2    Woodburn, J.R.3    Ashton, S.E.4    Curry, B.J.5    Barker, A.J.6    Gibson, I.C.H.7
  • 28
    • 0036667387 scopus 로고    scopus 로고
    • Epidermal growth factor receptor tyrosine kinase inhibitors
    • Wakeling, A.E. 2002. Epidermal growth factor receptor tyrosine kinase inhibitors. Curr. Opin. Pharmacol. 2:382-387.
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 382-387
    • Wakeling, A.E.1
  • 30
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas, S.M. and J.S. Brugge. 1997. Cellular functions regulated by Src family kinases. Annu. Rev. Cell. Dev. Biol. 13:513-609.
    • (1997) Annu. Rev. Cell. Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 31
    • 0032933797 scopus 로고    scopus 로고
    • c-Src, receptor tyrosine kinases, and human cancer
    • Biscardi, J.S., D.A. Tice, and S.J. Parsons. 1999. c-Src, receptor tyrosine kinases, and human cancer. Adv. Cancer Res. 76:61-119.
    • (1999) Adv. Cancer Res. , vol.76 , pp. 61-119
    • Biscardi, J.S.1    Tice, D.A.2    Parsons, S.J.3
  • 32
    • 0034424220 scopus 로고    scopus 로고
    • Src inhibitors: Drugs for the treatment of osteoporosis, cancer or both?
    • Susa, M., M. Missbach, and J. Green. 2000. Src inhibitors: drugs for the treatment of osteoporosis, cancer or both? Trends Pharmacol. Sci. 21:489-495.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 489-495
    • Susa, M.1    Missbach, M.2    Green, J.3
  • 33
    • 0000328787 scopus 로고    scopus 로고
    • Tyrosine kinase Src inhibitors: Potential therapeutic applications
    • Susa, M. and A. Teti. 2000. Tyrosine kinase Src inhibitors: potential therapeutic applications. Drug News Perspect. 13:169-175.
    • (2000) Drug News Perspect. , vol.13 , pp. 169-175
    • Susa, M.1    Teti, A.2
  • 34
    • 0026023289 scopus 로고
    • Targeted disruption of the c-Src proto-oncogene leads to osteopetrosis in mice
    • Soriano, P., C. Montgomery, R. Geske, and A. Bradley. 1991. Targeted disruption of the c-Src proto-oncogene leads to osteopetrosis in mice. Cell 64:693-702.
    • (1991) Cell , vol.64 , pp. 693-702
    • Soriano, P.1    Montgomery, C.2    Geske, R.3    Bradley, A.4
  • 35
    • 0027318189 scopus 로고
    • Osteopetrosis in Srcdeficient mice is due to an autonomous defect of osteoclasts
    • Lowe, C., T. Yoneda, B.F. Boyce, H. Chen, et al. 1993. Osteopetrosis in Srcdeficient mice is due to an autonomous defect of osteoclasts. Proc. Natl. Acad. Sci. USA 90:4485-4489.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4485-4489
    • Lowe, C.1    Yoneda, T.2    Boyce, B.F.3    Chen, H.4
  • 36
    • 0030856131 scopus 로고    scopus 로고
    • Rescue of osteoclast function by transgenic expression of kinase-deficient Src in src-/- mutant mice
    • Schwartzberg, P.L., L. Xing, O. Hoffmann, et al. 1997. Rescue of osteoclast function by transgenic expression of kinase-deficient Src in src-/- mutant mice. Genes Dev. 11:2835-2844.
    • (1997) Genes Dev. , vol.11 , pp. 2835-2844
    • Schwartzberg, P.L.1    Xing, L.2    Hoffmann, O.3
  • 37
    • 0034676060 scopus 로고    scopus 로고
    • Decreased c-Src expression enhances osteoblast differentiation and bone formation
    • Marzia, M., N.A. Sims, S. Voit, S. Migliacco, et al. 2000. Decreased c-Src expression enhances osteoblast differentiation and bone formation. J. Cell Biol. 151:311-320.
    • (2000) J. Cell Biol. , vol.151 , pp. 311-320
    • Marzia, M.1    Sims, N.A.2    Voit, S.3    Migliacco, S.4
  • 38
    • 0033766934 scopus 로고    scopus 로고
    • Progressive increase in bone mass and development of odontomas in aging osteopetrotic csrc-deficient mice
    • Amling, M., I. Neff, M. Priemel, A.F. Schilling, et al. 2000. Progressive increase in bone mass and development of odontomas in aging osteopetrotic csrc-deficient mice. Bone 27:603-610.
    • (2000) Bone , vol.27 , pp. 603-610
    • Amling, M.1    Neff, I.2    Priemel, M.3    Schilling, A.F.4
  • 39
    • 0029786988 scopus 로고    scopus 로고
    • Knockouts of Src-family kinases: Stiff bones, wimpy T cells, and bad memories
    • Lowell, C.A. and P. Soriano. 1996. Knockouts of Src-family kinases: stiff bones, wimpy T cells, and bad memories. Genes Dev. 10:1845-1857.
    • (1996) Genes Dev. , vol.10 , pp. 1845-1857
    • Lowell, C.A.1    Soriano, P.2
  • 40
    • 0035866364 scopus 로고    scopus 로고
    • The COOH-terminal Src kinase Csk is a tumor antigen in human carcinoma
    • Benistant, C., J.-F. Bourgaux, H. Chapuis, N. Mottet, et al. 2001. The COOH-terminal Src kinase Csk is a tumor antigen in human carcinoma. Cancer Res. 61:1415-1420.
    • (2001) Cancer Res. , vol.61 , pp. 1415-1420
    • Benistant, C.1    Bourgaux, J.-F.2    Chapuis, H.3    Mottet, N.4
  • 41
    • 0034731372 scopus 로고    scopus 로고
    • Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines
    • Bjorge, J.D., A. Pang, and D.J. Fujita. 2000. Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines. J. Biol. Chem. 275:41439-41446.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41439-41446
    • Bjorge, J.D.1    Pang, A.2    Fujita, D.J.3
  • 42
    • 0024478058 scopus 로고
    • pp60c-src tyrosine kinase, myristylation, and modulatory domains are required for enhanced mitogenic responsiveness to epidermal growth factor seen in cells overexpressing c-Src
    • Wilson, L.K., D.K. Luttrell, J.T. Parsons, and S.J. Parsons. 1989. pp60c-src tyrosine kinase, myristylation, and modulatory domains are required for enhanced mitogenic responsiveness to epidermal growth factor seen in cells overexpressing c-Src. Mol. Cell. Biol. 9:1536-1544.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1536-1544
    • Wilson, L.K.1    Luttrell, D.K.2    Parsons, J.T.3    Parsons, S.J.4
  • 43
    • 0029121267 scopus 로고
    • Potentiation of epidermal growth factor receptor-mediated oncogenesis by c-Src: Implications for the etiology of multiple human cancers
    • Maa, M.-C., T.H. Leu, D.J. McCarley, R.C. Schatzman, and S.J. Parsons. 1995. Potentiation of epidermal growth factor receptor-mediated oncogenesis by c-Src: implications for the etiology of multiple human cancers. Proc. Natl. Acad. Sci. USA 92:6981-6985.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6981-6985
    • Maa, M.-C.1    Leu, T.H.2    McCarley, D.J.3    Schatzman, R.C.4    Parsons, S.J.5
  • 44
    • 6844259884 scopus 로고    scopus 로고
    • Activation of c-Src by receptor tyrosine kinases in human colon cancer cells with high metastatic potential
    • Mao, W., R. Irby, D. Coppola, L. Fu, et al. 1997. Activation of c-Src by receptor tyrosine kinases in human colon cancer cells with high metastatic potential. Oncogene 15:3083-3090.
    • (1997) Oncogene , vol.15 , pp. 3083-3090
    • Mao, W.1    Irby, R.2    Coppola, D.3    Fu, L.4
  • 45
    • 0031953831 scopus 로고    scopus 로고
    • STAT3 activation by Src induces specific gene regulation and is required for cell transformation
    • Turkson, J., T Bowman, R. Garci, E. Caldenhove, et al. 1998. STAT3 activation by Src induces specific gene regulation and is required for cell transformation. Mol. Cell. Biol. 18:2545-2552.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2545-2552
    • Turkson, J.1    Bowman, T.2    Garci, R.3    Caldenhove, E.4
  • 46
    • 0030970723 scopus 로고    scopus 로고
    • Decreased tumorigenicity of a human colon carcinoma cell line by an antisense expression vector specific for c-Src
    • Staley, C.A., N.U. Parikh, and G.E. Gallick. 1997. Decreased tumorigenicity of a human colon carcinoma cell line by an antisense expression vector specific for c-Src. Cell Growth Differ. 8:269-274.
    • (1997) Cell Growth Differ. , vol.8 , pp. 269-274
    • Staley, C.A.1    Parikh, N.U.2    Gallick, G.E.3
  • 47
    • 0031985127 scopus 로고    scopus 로고
    • Downregulation of vascular endothelial growth factor in a human colon carcinoma cell line transfected with an antisense expression vector specific for c-Src
    • Ellis, L.M., C.A. Staley, W. Liu, R.Y. Fleming, et al. 1998. Downregulation of vascular endothelial growth factor in a human colon carcinoma cell line transfected with an antisense expression vector specific for c-Src. J. Biol. Chem. 273:1052-1057.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1052-1057
    • Ellis, L.M.1    Staley, C.A.2    Liu, W.3    Fleming, R.Y.4
  • 48
    • 0032932248 scopus 로고    scopus 로고
    • Activating SRC mutation in a subset of advanced human colon cancers
    • Irby, R.B., W. Mao, D. Coppola, J. Kang, et al. 1999. Activating SRC mutation in a subset of advanced human colon cancers. Nat. Genet. 21:187-190.
    • (1999) Nat. Genet. , vol.21 , pp. 187-190
    • Irby, R.B.1    Mao, W.2    Coppola, D.3    Kang, J.4
  • 49
    • 0033521886 scopus 로고    scopus 로고
    • Activation of Src in human breast tumor cell lines: Elevated levels of phosphotyrosine phosphatase activity that preferentially recognizes the Src carboxy terminal negative regulatory tyrosine 530
    • Egan, C., A. Pang, D. Durda, H.-C. Cheng, et al. 1999. Activation of Src in human breast tumor cell lines: elevated levels of phosphotyrosine phosphatase activity that preferentially recognizes the Src carboxy terminal negative regulatory tyrosine 530. Oncogene 18:1227-1237.
    • (1999) Oncogene , vol.18 , pp. 1227-1237
    • Egan, C.1    Pang, A.2    Durda, D.3    Cheng, H.-C.4
  • 50
    • 0030474489 scopus 로고    scopus 로고
    • c-Src protein expression is increased in human breast cancer. An immunohistochemical and biochemical analysis
    • Verbeek, B.S., T.M. Vroom, S.S. Adriaansen-Slot, A.E. Ottenhoff-Kalif, et al. 1996. c-Src protein expression is increased in human breast cancer. An immunohistochemical and biochemical analysis. J. Pathol. 180:383-388.
    • (1996) J. Pathol. , vol.180 , pp. 383-388
    • Verbeek, B.S.1    Vroom, T.M.2    Adriaansen-Slot, S.S.3    Ottenhoff-Kalif, A.E.4
  • 51
    • 0027469402 scopus 로고
    • Increase in activity and level of pp60c-src in progressive stages of human colorectal cancer
    • Talamonti, M.S., M.S. Roh, S.A. Curley, and G.E. Gallick. 1993. Increase in activity and level of pp60c-src in progressive stages of human colorectal cancer. J. Clin. Invest. 91:3-60.
    • (1993) J. Clin. Invest. , vol.91 , pp. 3-60
    • Talamonti, M.S.1    Roh, M.S.2    Curley, S.A.3    Gallick, G.E.4
  • 52
    • 0032054511 scopus 로고    scopus 로고
    • Overexpression of c-Src in areas of hyperproliferation in head and neck cancer, premalignant lesions and benign mucosal disorders
    • Van Oijen, M.G., C.T. Rijkseng, F.W. ten Broek, and P.J. Slootweg. 1998. Overexpression of c-Src in areas of hyperproliferation in head and neck cancer, premalignant lesions and benign mucosal disorders. J. Oral Pathol. Med. 27:147-152.
    • (1998) J. Oral Pathol. Med. , vol.27 , pp. 147-152
    • Van Oijen, M.G.1    Rijkseng, C.T.2    Ten Broek, F.W.3    Slootweg, P.J.4
  • 53
  • 54
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction
    • Cohen, G.B., R. Ren, and D. Baltimore. 1995. Modular binding domains in signal transduction. Cell 80.237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 55
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. 1995. Protein modules and signalling networks. Nature 373:573-580
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 56
    • 0031418201 scopus 로고    scopus 로고
    • SH3 domains and drug design: Ligands, structure, and biological function
    • Dalgarno, D.C., M.C. Botfield, and R.J. Rickles. 1997. SH3 domains and drug design: ligands, structure, and biological function. Biopolymers (Peptide Sci.) 43:383-400.
    • (1997) Biopolymers (Peptide Sci.) , vol.43 , pp. 383-400
    • Dalgarno, D.C.1    Botfield, M.C.2    Rickles, R.J.3
  • 58
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Xu, W., A. Doshi, M. Lei, M. Eck, and S.C. Harrison. 1999. Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol. Cell 3:629-636.
    • (1999) Mol. Cell , vol.3 , pp. 629-636
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.4    Harrison, S.C.5
  • 59
    • 0033152210 scopus 로고    scopus 로고
    • Structural analysis of the lymphocyte-specific Lck in complex with non-selective and Src family-selective kinase inhibitors
    • Zhu, X., J.L. Kim, J.R. Newcomb, P.E. Rose, D.R. Stover, et al. 1999. Structural analysis of the lymphocyte-specific Lck in complex with non-selective and Src family-selective kinase inhibitors. Structure 7:651-661.
    • (1999) Structure , vol.7 , pp. 651-661
    • Zhu, X.1    Kim, J.L.2    Newcomb, J.R.3    Rose, P.E.4    Stover, D.R.5
  • 60
    • 0033063429 scopus 로고    scopus 로고
    • Crystal structure of Hck in complex with Src family-selective tyrosine kinase inhibitor
    • Schindler, T., F. Sichieri, A. Pico, A. Gazit, et al. 1999. Crystal structure of Hck in complex with Src family-selective tyrosine kinase inhibitor. Mol. Cell 3:639-648.
    • (1999) Mol. Cell , vol.3 , pp. 639-648
    • Schindler, T.1    Sichieri, F.2    Pico, A.3    Gazit, A.4
  • 62
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard, S.R. 1997. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16:5572-5581.
    • (1997) EMBO J. , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 63
    • 0030945871 scopus 로고    scopus 로고
    • Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors
    • Mohammadi, M., G. McMahon, L. Sun, PC. Tang, et al. 1997. Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors. Science 276:955-960.
    • (1997) Science , vol.276 , pp. 955-960
    • Mohammadi, M.1    McMahon, G.2    Sun, L.3    Tang, P.C.4
  • 64
    • 0033103867 scopus 로고    scopus 로고
    • Crystal structure of the kinase domain of human vascular endothelial growth factor receptor 2: A key enzyme in angiogenesis
    • McTigue, M.A., J.A. Wilkersham, C. Pinko, R.E. Showalter, et al. 1999. Crystal structure of the kinase domain of human vascular endothelial growth factor receptor 2: a key enzyme in angiogenesis. Structure Fold. Des. 7:319-330.
    • (1999) Structure Fold. Des. , vol.7 , pp. 319-330
    • McTigue, M.A.1    Wilkersham, J.A.2    Pinko, C.3    Showalter, R.E.4
  • 65
    • 0032563315 scopus 로고    scopus 로고
    • Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors
    • Gray, N.S., L. Wodicka, A.-M. Thunnissen, T.C. Norman, S. Kwon, et al. 1998. Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors. Science 281:533-538.
    • (1998) Science , vol.281 , pp. 533-538
    • Gray, N.S.1    Wodicka, L.2    Thunnissen, A.-M.3    Norman, T.C.4    Kwon, S.5
  • 66
    • 0034611620 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibition by new C-2 alkynylated purine derivatives and molecular structure of a CDK2-inhibitor complex
    • Legravend, M., P. Tunnah, M. Noble, P. Ducrot, et al. 2002. Cyclin-dependent kinase inhibition by new C-2 alkynylated purine derivatives and molecular structure of a CDK2-inhibitor complex. J. Med. Chem. 43:1282-1292.
    • (2002) J. Med. Chem. , vol.43 , pp. 1282-1292
    • Legravend, M.1    Tunnah, P.2    Noble, M.3    Ducrot, P.4
  • 67
    • 0035865934 scopus 로고    scopus 로고
    • Crystal structure of human cyclin-dependent kinase 2 in complex with the adenine-derived inhibitor H717
    • Dreyer, M.K., D.R. Borcherding, J.A. Dumont, N.P. Peet, et al. 2001. Crystal structure of human cyclin-dependent kinase 2 in complex with the adenine-derived inhibitor H717. J. Med. Chem. 44:524-530.
    • (2001) J. Med. Chem. , vol.44 , pp. 524-530
    • Dreyer, M.K.1    Borcherding, D.R.2    Dumont, J.A.3    Peet, N.P.4
  • 68
    • 0034665713 scopus 로고    scopus 로고
    • Structural mechanism for STI-571 inhibition of Abelson tyrosine kinase
    • Schindler, T., W. Bommann, P. Pellicena, W.T. Miller, et al. 2002. Structural mechanism for STI-571 inhibition of Abelson tyrosine kinase. Science 289:1938-1942.
    • (2002) Science , vol.289 , pp. 1938-1942
    • Schindler, T.1    Bommann, W.2    Pellicena, P.3    Miller, W.T.4
  • 69
    • 0030887842 scopus 로고    scopus 로고
    • Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label is direct substrates
    • Shah, K., Y. Liu, C. Deirmengian, and K.M. Shokat. 1997. Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label is direct substrates. Proc. Natl. Acad. Sci. USA 94:3565-3570.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3565-3570
    • Shah, K.1    Liu, Y.2    Deirmengian, C.3    Shokat, K.M.4
  • 70
    • 0032568055 scopus 로고    scopus 로고
    • Design of allele-specific inhibitors to probe protein kinase signaling
    • Bishop, A.C., K. Shah, Y. Liu, L Witucki, et al. 1998. Design of allele-specific inhibitors to probe protein kinase signaling. Curr. Biol. 8:257-266.
    • (1998) Curr. Biol. , vol.8 , pp. 257-266
    • Bishop, A.C.1    Shah, K.2    Liu, Y.3    Witucki, L.4
  • 71
    • 0033518610 scopus 로고    scopus 로고
    • Generation of monospecific nanomolar tyrosine kinase inhibitors via a chemical genomics approach
    • Bishop, A.C., C.-Y. Kung, K. Shah, L. Witucki, et al. 1999. Generation of monospecific nanomolar tyrosine kinase inhibitors via a chemical genomics approach. J. Am. Chem. Soc. 121:627-631.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 627-631
    • Bishop, A.C.1    Kung, C.-Y.2    Shah, K.3    Witucki, L.4
  • 73
    • 0036776168 scopus 로고    scopus 로고
    • A novel pathway regulating the mammalian target of rapamycin (mTOR) signaling
    • Chen, J. and Y. Fang. 2002. A novel pathway regulating the mammalian target of rapamycin (mTOR) signaling. Biochem. Pharmacol. 64:1071-1077.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1071-1077
    • Chen, J.1    Fang, Y.2
  • 74
    • 0036225178 scopus 로고    scopus 로고
    • Inhibitors of mammalian target of rapamycin as novel antitumor agents: From bench to clinic
    • Huang, S. and P.J. Houghton. 2002. Inhibitors of mammalian target of rapamycin as novel antitumor agents: from bench to clinic. Curr. Opin. Investig. Drugs 3:295-304.
    • (2002) Curr. Opin. Investig. Drugs , vol.3 , pp. 295-304
    • Huang, S.1    Houghton, P.J.2
  • 76
    • 0037519507 scopus 로고    scopus 로고
    • Discovery of potent and selective Src inhibitors and their development as antitumor and antimetastatic agents
    • Metcalf, C., III, Y. Wang, W. Shakespeare, R. Sundaramoorthi, T. Keenan, D. Dalgarno, et al. 2003. Discovery of potent and selective Src inhibitors and their development as antitumor and antimetastatic agents. Proc. AACR 44:A1716.
    • (2003) Proc. AACR , vol.44
    • Metcalf C. III1    Wang, Y.2    Shakespeare, W.3    Sundaramoorthi, R.4    Keenan, T.5    Dalgarno, D.6
  • 77
    • 0030029143 scopus 로고    scopus 로고
    • Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor
    • Hanke, J.H., J.P. Gardner, R.L. Dow, P.S. Changelian, et al. 1996. Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. J. Biol. Chem. 271:695-701.
    • (1996) J. Biol. Chem. , vol.271 , pp. 695-701
    • Hanke, J.H.1    Gardner, J.P.2    Dow, R.L.3    Changelian, P.S.4
  • 78
    • 0032904762 scopus 로고    scopus 로고
    • A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo
    • Missbach, M., M. Jeschke, J. Feyer, K. Muller, et al. 1999. A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo. Bone 24:437-449.
    • (1999) Bone , vol.24 , pp. 437-449
    • Missbach, M.1    Jeschke, M.2    Feyer, J.3    Muller, K.4
  • 79
    • 0002957883 scopus 로고    scopus 로고
    • Tyrosine kinase Src inhibitor CGP 76030 suppresses rapid bone loss induced by retinoic acid in rats
    • Kneissel, M., R. Gamse, M. Missbach, L. Wilder, et al. 1999. Tyrosine kinase Src inhibitor CGP 76030 suppresses rapid bone loss induced by retinoic acid in rats. Calcif. Tissue Int. 64(Suppl 1):S75.
    • (1999) Calcif. Tissue Int. , vol.64 , Issue.SUPPL. 1
    • Kneissel, M.1    Gamse, R.2    Missbach, M.3    Wilder, L.4
  • 80
    • 14444281388 scopus 로고    scopus 로고
    • Structure-activity relationships for a novel series of pyrido[2,3-d]pyrimidine tyrosine kinase inhibitors
    • Hamby, J.M., C.J.C. Connolly, M.C. Schroeder, R.T. Winters, et al. 1997. Structure-activity relationships for a novel series of pyrido[2,3-d]pyrimidine tyrosine kinase inhibitors. J. Med. Chem. 40.2296-2303.
    • (1997) J. Med. Chem. , vol.40 , pp. 2296-2303
    • Hamby, J.M.1    Connolly, C.J.C.2    Schroeder, M.C.3    Winters, R.T.4
  • 82
    • 0034308176 scopus 로고    scopus 로고
    • Biochemical and cellular effects of c-Src kinase-selective pyrido[2,3-d]pyrimidine tyrosine kinase inhibitors
    • Kraker, A.J., B.G. Hartl, A.M. Amar, M.R. Barvian, et al. 2000. Biochemical and cellular effects of c-Src kinase-selective pyrido[2,3-d]pyrimidine tyrosine kinase inhibitors. Biochem. Pharmacol. 60:885-898.
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 885-898
    • Kraker, A.J.1    Hartl, B.G.2    Amar, A.M.3    Barvian, M.R.4
  • 83
    • 0034613645 scopus 로고    scopus 로고
    • Inhibitors of Src tyrosine kinase: The preparation and structure-activity relationship of 4-anilino-3-cyanoquinolines and 4-anilinoquinazolines
    • Wang, Y.D., K. Miller, D.H. Boschelli, F. Ye, et al. 2000. Inhibitors of Src tyrosine kinase: the preparation and structure-activity relationship of 4-anilino-3-cyanoquinolines and 4-anilinoquinazolines. Bioorg. Med. Chem. Lett. 10:2477-2480.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 2477-2480
    • Wang, Y.D.1    Miller, K.2    Boschelli, D.H.3    Ye, F.4
  • 84
    • 0035282974 scopus 로고    scopus 로고
    • Synthesis and Src kinase inhibitory activity of a series of 4-phenylamino-3-quinolinecarbonitriles
    • Boschelli, D.H., Y.D. Wang, F. Ye, B. Wu, et al. 2001. Synthesis and Src kinase inhibitory activity of a series of 4-phenylamino-3-quinolinecarbonitriles. J. Med. Chem. 44:822-833.
    • (2001) J. Med. Chem. , vol.44 , pp. 822-833
    • Boschelli, D.H.1    Wang, Y.D.2    Ye, F.3    Wu, B.4
  • 85
    • 0034458943 scopus 로고    scopus 로고
    • SU6656, a selective Src family kinase inhibitor used to probe growth factor signaling
    • Blake, R.A., M.A. Broome, X. Liu, J. Wu, et al. 2000. SU6656, a selective Src family kinase inhibitor used to probe growth factor signaling. Mol. Cell. Biol. 20:9018-9027.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 9018-9027
    • Blake, R.A.1    Broome, M.A.2    Liu, X.3    Wu, J.4
  • 86
    • 0031026055 scopus 로고    scopus 로고
    • Potent and selective inhibitors of the Abl-kinase: Phenylaminopyrimidine (PAP) derivatives
    • Zimmerman, J., E. Buchdunger, H. Mett, T. Meyer, and N.B. Lydon. 1997. Potent and selective inhibitors of the Abl-kinase: phenylaminopyrimidine (PAP) derivatives. Bioorg. Med. Chem. Lett. 7:187-192.
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 187-192
    • Zimmerman, J.1    Buchdunger, E.2    Mett, H.3    Meyer, T.4    Lydon, N.B.5
  • 87
    • 0027336839 scopus 로고
    • Herbimycin A, a pp60c-src tyrosine kinase inhibitor, inhibits osteoclastic bone resorption in vitro and hypercalcemia in vivo
    • Yoneda, T., C. Lowe, C.-H. Lee, G. Gutierra, et al. 1993. Herbimycin A, a pp60c-src tyrosine kinase inhibitor, inhibits osteoclastic bone resorption in vitro and hypercalcemia in vivo. J. Clin. Invest. 91:2791-2795.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2791-2795
    • Yoneda, T.1    Lowe, C.2    Lee, C.-H.3    Gutierra, G.4
  • 88
    • 0034646370 scopus 로고    scopus 로고
    • Combinatorial target-guided ligand assembly: Identification of potent subtype-selective c-Src inhibitors
    • Maly, D.J., I.C. Choong, and J.A. Ellman. 2000. Combinatorial target-guided ligand assembly: identification of potent subtype-selective c-Src inhibitors. Proc. Natl. Acad. Sci. USA 97:2419-2424.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2419-2424
    • Maly, D.J.1    Choong, I.C.2    Ellman, J.A.3
  • 89
    • 0032543527 scopus 로고    scopus 로고
    • Discovery of a novel series of potent and selective substrate-based inhibitors of pp60c-src protein tyrosine kinase: Conformational and topographical constraints in peptide design
    • Alfaro-Lopez, J., W. Yuan, B.C. Phan, J. Kamath, et al. 1998. Discovery of a novel series of potent and selective substrate-based inhibitors of pp60c-src protein tyrosine kinase: conformational and topographical constraints in peptide design. J. Med. Chem. 41:2252-2260.
    • (1998) J. Med. Chem. , vol.41 , pp. 2252-2260
    • Alfaro-Lopez, J.1    Yuan, W.2    Phan, B.C.3    Kamath, J.4
  • 90
    • 0038533533 scopus 로고    scopus 로고
    • Development of a novel bone-targeted Src tyrosine kinase inhibitor AP23451 having potent activity in an animal model of osteolytic bone metastasis
    • Shakespeare, W., Y. Wang, C. Metcalf, R. Sundaramoorthi, T. Keenan, R. Bohacek, et al. 2003. Development of a novel bone-targeted Src tyrosine kinase inhibitor AP23451 having potent activity in an animal model of osteolytic bone metastasis. Proc. AACR 44:A3871.
    • (2003) Proc. AACR , vol.44
    • Shakespeare, W.1    Wang, Y.2    Metcalf, C.3    Sundaramoorthi, R.4    Keenan, T.5    Bohacek, R.6
  • 91
    • 0030220960 scopus 로고    scopus 로고
    • Molecular basis for the binding of SH3 ligands with non-peptide elements identified by combinatorial synthesis
    • Feng, S., T.M. Kapoor, F. Shirai, A.P. Combs, and S.L. Schreiber. 1996. Molecular basis for the binding of SH3 ligands with non-peptide elements identified by combinatorial synthesis. Chem. Biol. 3:661-670.
    • (1996) Chem. Biol. , vol.3 , pp. 661-670
    • Feng, S.1    Kapoor, T.M.2    Shirai, F.3    Combs, A.P.4    Schreiber, S.L.5
  • 92
    • 12944281813 scopus 로고    scopus 로고
    • Structurebased design of an osteoclast-selective, nonpeptide Src homology 2 inhibitor with in vivo antiresorptive activity
    • Shakespeare, W.C., M. Yang, R. Bohacek, F. Cerasoli, et al. 2000. Structurebased design of an osteoclast-selective, nonpeptide Src homology 2 inhibitor with in vivo antiresorptive activity. Proc. Natl. Acad. Sci. USA 97:9373-9378.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9373-9378
    • Shakespeare, W.C.1    Yang, M.2    Bohacek, R.3    Cerasoli, F.4
  • 93
    • 0034687218 scopus 로고    scopus 로고
    • Structure-based design of novel bicyclic inhibitors for the Src SH2 domain
    • Shakespeare, W.C., R.S. Bohacek, M.D. Azimiora, K.J. Macek, et al. 2000. Structure-based design of novel bicyclic inhibitors for the Src SH2 domain. J. Med. Chem. 43:3815-3819.
    • (2000) J. Med. Chem. , vol.43 , pp. 3815-3819
    • Shakespeare, W.C.1    Bohacek, R.S.2    Azimiora, M.D.3    Macek, K.J.4
  • 94
    • 0035283021 scopus 로고    scopus 로고
    • X-ray structure of citrate bound to Src SH2 leads to high-affinity, bone-targeted Src SH2 inhibitor
    • Bohacek, R.S., D.C. Dalgarno, M. Hatada, V.A. Jacobsen, et al. 2001. X-ray structure of citrate bound to Src SH2 leads to high-affinity, bone-targeted Src SH2 inhibitor. J. Med. Chem. 44:660-663.
    • (2001) J. Med. Chem. , vol.44 , pp. 660-663
    • Bohacek, R.S.1    Dalgarno, D.C.2    Hatada, M.3    Jacobsen, V.A.4
  • 97
    • 12444257367 scopus 로고    scopus 로고
    • Bone-targeted pyrido[2,3-d]pyrimidin-7-ones: Potent inhibitors of Src tyrosine kinase as novel antiresorptive agents
    • In press
    • Vu, C., G.P. Luke, N. Kawahata, W.C. Shakespeare, Y. Wang, R. Sundaramoorthi, et al. Bone-targeted pyrido[2,3-d]pyrimidin-7-ones: potent inhibitors of Src tyrosine kinase as novel antiresorptive agents. Bioorg. Med. Chem. Lett. (In press).
    • Bioorg. Med. Chem. Lett.
    • Vu, C.1    Luke, G.P.2    Kawahata, N.3    Shakespeare, W.C.4    Wang, Y.5    Sundaramoorthi, R.6


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