메뉴 건너뛰기




Volumn 3, Issue 11, 1996, Pages 887-893

Targeting signal transduction in the discovery of antiproliferative drugs

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0030294380     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(96)90177-5     Document Type: Review
Times cited : (26)

References (29)
  • 1
    • 0028968949 scopus 로고
    • Tyrosine kinase inhibition: An approach to drug development
    • Levitski, A. & Gazit, A. (1695). Tyrosine kinase inhibition: an approach to drug development. Science 267, 1782-1787.
    • (1695) Science , vol.267 , pp. 1782-1787
    • Levitski, A.1    Gazit, A.2
  • 2
    • 0026636883 scopus 로고
    • The regulation of transcription by phosphorylation
    • Hunter, T. & Karin, M. (1992). The regulation of transcription by phosphorylation. Cell 70, 375-387.
    • (1992) Cell , vol.70 , pp. 375-387
    • Hunter, T.1    Karin, M.2
  • 3
    • 0028915222 scopus 로고
    • Molecular foundations of cancer: New targets for intervention
    • Karp, J.E., & Broder, S. (1995). Molecular foundations of cancer: new targets for intervention. Nature Med. 1, 309-320.
    • (1995) Nature Med. , vol.1 , pp. 309-320
    • Karp, J.E.1    Broder, S.2
  • 4
    • 0028895654 scopus 로고
    • Molecular binding domains in signal transduction proteins
    • Cohen, G.B., Ren, R. & Baltimore, D. (1995). Molecular binding domains in signal transduction proteins. Cell 80, 237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 5
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang, Z., et al., & Cantley, L.C. (1993). SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767-778.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1    Cantley, L.C.2
  • 6
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • Feng, S., Chen, J.K., Yu, H., Simon, J.A., & Schreiber, S.L. (1994). Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266, 1241-1247.
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 7
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the comptexed and peptide-free forms
    • Waksman, G., Shoelson, S.E., Pant, N., Cowburn, D., & Kuriyan, J., (1993). Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the comptexed and peptide-free forms. Cell 72, 779-790.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 8
    • 12644277151 scopus 로고    scopus 로고
    • Design of peptidomimetic ligands for the pp60(Src) SH2 domain
    • in press
    • Plummer, M.S., et al., & Sawyer, T.K. (1996). Design of peptidomimetic ligands for the pp60(Src) SH2 domain. Bioorg. Med. Chem., in press.
    • (1996) Bioorg. Med. Chem.
    • Plummer, M.S.1    Sawyer, T.K.2
  • 9
    • 0028130221 scopus 로고
    • Peptide inhibitors of Src SH3-SH2-phosphoprotein interactions
    • Gilmer, T., et al., & Berman, J. (1994). Peptide inhibitors of Src SH3-SH2-phosphoprotein interactions. J. Biol. Chem. 269, 31711-31719.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31711-31719
    • Gilmer, T.1    Berman, J.2
  • 10
    • 0029953826 scopus 로고    scopus 로고
    • Hydrophobic D-amino acids in the design of peptide ligands for the pp60(Src) SH2 domain
    • Plummer, M.S., et al., & Sawyer, T.K. (1996). Hydrophobic D-amino acids in the design of peptide ligands for the pp60(Src) SH2 domain. Drug Design Discovery 13, 75-81.
    • (1996) Drug Design Discovery , vol.13 , pp. 75-81
    • Plummer, M.S.1    Sawyer, T.K.2
  • 11
  • 12
    • 0028675698 scopus 로고
    • NMR structure of the N-terminal SH3 domain of Grb2 and its complex with a proline-rich peptide from SOS
    • Goudreau, N., et al., & Roques, B.P. (1994). NMR structure of the N-terminal SH3 domain of Grb2 and its complex with a proline-rich peptide from SOS. Nature Struct Biol. 1, 898-907.
    • (1994) Nature Struct Biol. , vol.1 , pp. 898-907
    • Goudreau, N.1    Roques, B.P.2
  • 13
    • 15844398102 scopus 로고    scopus 로고
    • Structure basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode
    • Rahuel, J., et al., & Grutter, M.G. (1996). Structure basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode. Nature Struct. Biol. 3, 686-689.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 686-689
    • Rahuel, J.1    Grutter, M.G.2
  • 14
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski, M.S. & McCormick, F. (1993). Proteins regulating Ras and its relatives. Nature 366, 643-654.
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 15
    • 0027284950 scopus 로고
    • Protein prenylation: A mediator of protein-protein interactions
    • Marshall, C.J. (1993). Protein prenylation: a mediator of protein-protein interactions. Science 259, 1865-1866.
    • (1993) Science , vol.259 , pp. 1865-1866
    • Marshall, C.J.1
  • 16
    • 0027248872 scopus 로고
    • Selective inhibition of Ras-dependent transformation by a farnesyltransferase inhibitor
    • Kohl, N.E., et al., & Gibbs, J.B. (1993). Selective inhibition of Ras-dependent transformation by a farnesyltransferase inhibitor. Science 260, 1934-1937.
    • (1993) Science , vol.260 , pp. 1934-1937
    • Kohl, N.E.1    Gibbs, J.B.2
  • 17
    • 0027323459 scopus 로고
    • Benzodiazepine peptidomimetics are potent inhibitors of Ras farnesylation in animal cells
    • James, G.L., et al., & Marsters, Jr., J.C. (1993). Benzodiazepine peptidomimetics are potent inhibitors of Ras farnesylation in animal cells. Science 260, 1937-1942.
    • (1993) Science , vol.260 , pp. 1937-1942
    • James, G.L.1    Marsters Jr., J.C.2
  • 18
    • 0030034763 scopus 로고    scopus 로고
    • Potent, ceil active, non-thiol tetrapeptide inhibitors of farnesyltransferase
    • Hunt, J.T., et al., & Manne, V., J. (1996). Potent, ceil active, non-thiol tetrapeptide inhibitors of farnesyltransferase. Med. Chem. 39, 353-358.
    • (1996) Med. Chem. , vol.39 , pp. 353-358
    • Hunt, J.T.1    Manne, V.J.2
  • 19
    • 0028132044 scopus 로고
    • Peptidomimetic inhibitors of p21Ras farnesyltransferase: Hydrophobic functionalization leads to disruption of p21 Ras membrane association in whole cells
    • Qian, Y., Blaskovich, M.A., Seong, C.-M., Vogt, A., Hamilton, A.D., & Sebti, S.M. (1994). Peptidomimetic inhibitors of p21Ras farnesyltransferase: hydrophobic functionalization leads to disruption of p21 Ras membrane association in whole cells. Bioorg. Med. Chem. Lett. 21, 2579-2584.
    • (1994) Bioorg. Med. Chem. Lett. , vol.21 , pp. 2579-2584
    • Qian, Y.1    Blaskovich, M.A.2    Seong, C.-M.3    Vogt, A.4    Hamilton, A.D.5    Sebti, S.M.6
  • 20
    • 0028973293 scopus 로고
    • Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complsxes
    • Lerner, et al., & Sebti, S.M. (1995). Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complsxes. J. Biol. Chem. 270, 26802-26806.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26802-26806
    • Lerner1    Sebti, S.M.2
  • 21
    • 0027337248 scopus 로고
    • Normal and oncogenic p21Ras proteins bind to the amino terminal regulatory domain of c-Raf-1
    • Zhang, X-F, et al., & Avruch, J. (1993). Normal and oncogenic p21Ras proteins bind to the amino terminal regulatory domain of c-Raf-1. Nature 364, 308-313.
    • (1993) Nature , vol.364 , pp. 308-313
    • Zhang, X.-F.1    Avruch, J.2
  • 22
    • 0027043103 scopus 로고
    • Human T-cell mitogen activated protein kinase kinases are related to yeast signal transduction kinases
    • Seger, R., et al., & Krebs, E.G. (1992). Human T-cell mitogen activated protein kinase kinases are related to yeast signal transduction kinases. J. Biol. Chem. 267, 25628-25631.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25628-25631
    • Seger, R.1    Krebs, E.G.2
  • 23
    • 0025290163 scopus 로고
    • An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control
    • Boulton, T.G., et al., & Cobb, M.H. (1990). An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control. Science 249, 64-67.
    • (1990) Science , vol.249 , pp. 64-67
    • Boulton, T.G.1    Cobb, M.H.2
  • 24
    • 0027476773 scopus 로고
    • Pac-1: A mitogen induced nuclear protein tyrosine phosphatase
    • Kelly, K. (1993). Pac-1: a mitogen induced nuclear protein tyrosine phosphatase. Science 259, 1763-1766.
    • (1993) Science , vol.259 , pp. 1763-1766
    • Kelly, K.1
  • 25
    • 0028908158 scopus 로고
    • Nerve growth factor stimulates a novel protein kinase in PC-12 cells that phosphorylates and activates mitogen activated protein kinase kinase (MEK)
    • Pang, L., Zheng, C-F, Guan, K-L, & Saltiel, A.R. (1995), Nerve growth factor stimulates a novel protein kinase in PC-12 cells that phosphorylates and activates mitogen activated protein kinase kinase (MEK). Biochem. J. 307, 513-519.
    • (1995) Biochem. J. , vol.307 , pp. 513-519
    • Pang, L.1    Zheng, C.-F.2    Guan, K.-L.3    Saltiel, A.R.4
  • 27
    • 0028884033 scopus 로고
    • PD98059 is a specific inhibitor of the activation of mitogen activated protein kinase kinase in vitro and in vivo
    • Alessi, D.R., Cuenda, A., Cohen, P., Dudley, D.T., & Sattiel, A.R. (1995). PD98059 is a specific inhibitor of the activation of mitogen activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270, 27489-27494.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3    Dudley, D.T.4    Sattiel, A.R.5
  • 28
    • 0029131895 scopus 로고
    • Mitogen activated protein kinase kinase inhibition does not block the stimulation of glucose utilization by insulin
    • Lazar, D.F., et al., & Saltiel, A.R. (1995). Mitogen activated protein kinase kinase inhibition does not block the stimulation of glucose utilization by insulin, J. Biol. Chem. 270, 20801-20807.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20801-20807
    • Lazar, D.F.1    Saltiel, A.R.2
  • 29
    • 0029130317 scopus 로고
    • Desensitization of Ras activation by a feedback disassociation of the SOS-Grb2 complex
    • Waters, S.S., et al., & Pessin, J.E. (1995). Desensitization of Ras activation by a feedback disassociation of the SOS-Grb2 complex. J. Biol. Chem. 270, 20883-20886.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20883-20886
    • Waters, S.S.1    Pessin, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.