메뉴 건너뛰기




Volumn 11, Issue 1, 2001, Pages 84-97

Molecular interaction maps as information organizers and simulation guides

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0038027881     PISSN: 10541500     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.1338126     Document Type: Review
Times cited : (68)

References (46)
  • 1
    • 0032776303 scopus 로고    scopus 로고
    • Molecular interaction map of the mammalian cell cycle control and DNA repair systems
    • K. W. Kohn, " Molecular interaction map of the mammalian cell cycle control and DNA repair systems, " Mol. Biol. Cell 10, 2703 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2703
    • Kohn, K.W.1
  • 2
    • 0032568043 scopus 로고    scopus 로고
    • Functional capabilities of molecular network components controlling the mammalian G1/S cell cycle phase transition
    • K. W. Kohn, " Functional capabilities of molecular network components controlling the mammalian G1/S cell cycle phase transition, " Oncogene 16, 1065 (1998).
    • (1998) Oncogene , vol.16 , pp. 1065
    • Kohn, K.W.1
  • 3
    • 0031804503 scopus 로고    scopus 로고
    • Signaling complexes: Biophysical constraints on intracellular communication
    • D. Bray, " Signaling complexes: Biophysical constraints on intracellular communication, " Annu. Rev. Biophys. Biomol. Struct. 27, 59 (1998).
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 59
    • Bray, D.1
  • 4
    • 0034193568 scopus 로고    scopus 로고
    • Protein-protein interactions define specificity in signal transduction
    • T. Pawson and P. Nash, " Protein-protein interactions define specificity in signal transduction, " Genes Dev. 14, 1027 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 1027
    • Pawson, T.1    Nash, P.2
  • 5
    • 0033515888 scopus 로고    scopus 로고
    • Complexity in biological signaling systems
    • G. Wang, U. S. Bhalla, and R. Iyengar, " Complexity in biological signaling systems, " Science 284, 92 (1999).
    • (1999) Science , vol.284 , pp. 92
    • Wang, G.1    Bhalla, U.S.2    Iyengar, R.3
  • 6
    • 0031443249 scopus 로고    scopus 로고
    • Computer-based analysis of the binding steps in protein complex formation
    • D. Bray and S. Lay, " Computer-based analysis of the binding steps in protein complex formation, " Proc. Natl. Acad. Sci. U.S.A. 94, 13493 (1997).
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13493
    • Bray, D.1    Lay, S.2
  • 7
    • 0032492834 scopus 로고    scopus 로고
    • Predicting temporal fluctuations in an intracellular signalling pathway
    • C. J. Morton-Firth and D. Bray, " Predicting temporal fluctuations in an intracellular signalling pathway, " J. Theor. Biol. 192, 117 (1998).
    • (1998) J. Theor. Biol. , vol.192 , pp. 117
    • Morton-Firth, C.J.1    Bray, D.2
  • 8
    • 0033083733 scopus 로고    scopus 로고
    • It's a noisy business! Genetic regulation at the nanomolar scale
    • H. H. McAdams and A. Arkin, " It's a noisy business! Genetic regulation at the nanomolar scale, " Trends Genet. 15, 65 (1999).
    • (1999) Trends Genet. , vol.15 , pp. 65
    • McAdams, H.H.1    Arkin, A.2
  • 9
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • P. H. Kussie, S. Gorina, V. Marechal et al., " Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain, " Science 274, 948 (1996).
    • (1996) Science , vol.274 , pp. 948
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3
  • 10
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • T. Pawson and J. D. Scott, " Signaling through scaffold, anchoring, and adaptor proteins, " Science 278, 2075 (1997).
    • (1997) Science , vol.278 , pp. 2075
    • Pawson, T.1    Scott, J.D.2
  • 11
    • 0032422785 scopus 로고    scopus 로고
    • Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals
    • A. J. Whitmarsh and R. J. Davis, " Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals, " Trends Biochem. Sci. 23, 481 (1998).
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 481
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 12
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • W. Xu, A. Doshi, M. Lei et al., " Crystal structures of c-Src reveal features of its autoinhibitory mechanism, " Molec. Cell 3, 629 (1999).
    • (1999) Molec. Cell , vol.3 , pp. 629
    • Xu, W.1    Doshi, A.2    Lei, M.3
  • 13
    • 0034072765 scopus 로고    scopus 로고
    • Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src
    • S. Gonfloni, A. Weijland, J. Kretzschmar et al., " Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src, " Nat. Struct. Biol. 7, 281 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 281
    • Gonfloni, S.1    Weijland, A.2    Kretzschmar, J.3
  • 14
    • 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 et al., " Mechanism of biological synergy between cellular Src and epidermal growth factor receptor, " Proc. Natl. Acad. Sci. U.S.A. 96, 1415 (1999).
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1415
    • Tice, D.A.1    Biscardi, J.S.2    Nickles, A.L.3
  • 15
    • 0034161405 scopus 로고    scopus 로고
    • A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
    • X.-M. Zheng, R. J. Resnick, and D. Shalloway, " A phosphotyrosine displacement mechanism for activation of Src by PTPalpha, " EMBO J. 19, 964 (2000).
    • (2000) EMBO J. , vol.19 , pp. 964
    • Zheng, X.-M.1    Resnick, R.J.2    Shalloway, D.3
  • 16
    • 0034720153 scopus 로고    scopus 로고
    • Molecular switches in lipid rafts
    • L. A. Cary and J. A. Cooper, " Molecular switches in lipid rafts, " Nature (London) 404, 945 (2000).
    • (2000) Nature (London) , vol.404 , pp. 945
    • Cary, L.A.1    Cooper, J.A.2
  • 17
    • 0034720166 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases
    • M. Kawabuchi, Y. Satomi, T. Takao et al., " Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases, " Nature (London) 404, 999 (2000).
    • (2000) Nature (London) , vol.404 , pp. 999
    • Kawabuchi, M.1    Satomi, Y.2    Takao, T.3
  • 18
    • 0034703099 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl-terminal Src kinase, Csk
    • S. Takeuchi, Y. Takayama, A. Ogawa et al., " Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl-terminal Src kinase, Csk, " J. Biol. Chem. 275, 29183 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 29183
    • Takeuchi, S.1    Takayama, Y.2    Ogawa, A.3
  • 19
    • 0032933797 scopus 로고    scopus 로고
    • C-Src, receptor tyrosine kinases, and human cancer
    • J. S. Biscardi, D. A. Tice, and S. J. Parsons, " c-Src, receptor tyrosine kinases, and human cancer, " Adv. Cancer Res. 76, 61 (1999).
    • (1999) Adv. Cancer Res. , vol.76 , pp. 61
    • Biscardi, J.S.1    Tice, D.A.2    Parsons, S.J.3
  • 20
    • 0032146274 scopus 로고    scopus 로고
    • The regulation of E2F by pRB-family proteins (Review)
    • N. Dyson, " The regulation of E2F by pRB-family proteins (Review), " Genes Dev. 12, 2245 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 2245
    • Dyson, N.1
  • 21
    • 0000589398 scopus 로고    scopus 로고
    • Implications of transcription factor E2F in regulation of DNA replication
    • K. Ohtani, " Implications of transcription factor E2F in regulation of DNA replication, " Front. Biosci. 4, d793 (1999).
    • (1999) Front. Biosci. , vol.4 , pp. 793
    • Ohtani, K.1
  • 22
    • 0037998134 scopus 로고    scopus 로고
    • The E2F transcription factors: Key regulators of cell proliferation
    • H. Muller and K. Helin, " The E2F transcription factors: Key regulators of cell proliferation, " Biochim. Biophys. Acta 1470, M1 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1470 , pp. 1
    • Muller, H.1    Helin, K.2
  • 23
    • 0033988256 scopus 로고    scopus 로고
    • E2F is required to prevent inappropriate S-phase entry of mammalian cells
    • S. He, B. L. Cook, B. E. Deverman et al., " E2F is required to prevent inappropriate S-phase entry of mammalian cells, " Mol. Cell. Biol. 20, 363 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 363
    • He, S.1    Cook, B.L.2    Deverman, B.E.3
  • 24
    • 0034646630 scopus 로고    scopus 로고
    • E2F family members are differentially regulated by reversible acetylation
    • G. Marzio, C. Wagener, I. Gutierrez et al., " E2F family members are differentially regulated by reversible acetylation, " J. Biol. Chem. 275, 10887 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 10887
    • Marzio, G.1    Wagener, C.2    Gutierrez, I.3
  • 25
    • 0029926303 scopus 로고    scopus 로고
    • Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F
    • J. Karlseder, H. Rotheneder, and E. Wintersberger, " Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F, " Mol. Cell. Biol. 16, 1659 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1659
    • Karlseder, J.1    Rotheneder, H.2    Wintersberger, E.3
  • 26
    • 0029981560 scopus 로고    scopus 로고
    • Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction
    • S-Y. Lin, A. R. Black, D. Kostic et al., " Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction, " Mol. Cell. Biol. 16, 1668 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1668
    • Lin, S.-Y.1    Black, A.R.2    Kostic, D.3
  • 27
    • 0031816342 scopus 로고    scopus 로고
    • Inhibition of cyclin D1 kinase activity is associated with E2F-mediated inhibition of cyclin D1 promoter activity through E2F and Sp1
    • G. Watanabe, C. Albanese, R. J. Lee et al., " Inhibition of cyclin D1 kinase activity is associated with E2F-mediated inhibition of cyclin D1 promoter activity through E2F and Sp1, " Mol. Cell. Biol. 18, 3212 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3212
    • Watanabe, G.1    Albanese, C.2    Lee, R.J.3
  • 28
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • R. X. Luo, A. A. Postigo, and D. C. Dean, " Rb interacts with histone deacetylase to repress transcription, " Cell 92, 463 (1998).
    • (1998) Cell , vol.92 , pp. 463
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 29
    • 0032484989 scopus 로고    scopus 로고
    • Retinoblastoma protein recruits histone deacetylase to repress transcription
    • A. Brehm, E. A. Miska, D. J. McCanee et al., " Retinoblastoma protein recruits histone deacetylase to repress transcription, " Nature (London) 391, 597 (1998).
    • (1998) Nature (London) , vol.391 , pp. 597
    • Brehm, A.1    Miska, E.A.2    McCanee, D.J.3
  • 30
    • 0034175616 scopus 로고    scopus 로고
    • Analysis of promoter binding by the E2F and pRB families in vivo: Distinct E2F proteins mediate activation and repression
    • Y. Takahashi, J. B. Rayman, and B. D. Dynlacht, " Analysis of promoter binding by the E2F and pRB families in vivo: Distinct E2F proteins mediate activation and repression, " Genes Dev. 14, 804 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 804
    • Takahashi, Y.1    Rayman, J.B.2    Dynlacht, B.D.3
  • 31
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • S. R. Datta, A. Brunet, and M. E. Greenberg, " Cellular survival: A play in three Akts, " Genes Dev. 13, 2905 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2905
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 32
    • 0032863163 scopus 로고    scopus 로고
    • All along the watchtower: On the regulation apoptosis regulators
    • B. Fadeel, B. Zhivotovsky, and S. Orrenius, " All along the watchtower: On the regulation apoptosis regulators, " FASEB J. 13, 1647 (1999).
    • (1999) FASEB J. , vol.13 , pp. 1647
    • Fadeel, B.1    Zhivotovsky, B.2    Orrenius, S.3
  • 33
    • 0033018109 scopus 로고    scopus 로고
    • Mechanism of protein kinase B activation by insulin/insulin-like growth factor-1 reavealed by specific inhibitors of phosphoinositide-3-kinase - Significance for diabetes and cancer
    • I. Galetic, M. Andjelkovic, R. Meier et al., " Mechanism of protein kinase B activation by insulin/insulin-like growth factor-1 reavealed by specific inhibitors of phosphoinositide-3-kinase - Significance for diabetes and cancer, " Pharmacol. Therap. 82, 409 (1999).
    • (1999) Pharmacol. Therap. , vol.82 , pp. 409
    • Galetic, I.1    Andjelkovic, M.2    Meier, R.3
  • 34
    • 0034614598 scopus 로고    scopus 로고
    • Genomic biology
    • R. Brent, " Genomic biology, " Cell 100, 169 (2000).
    • (2000) Cell , vol.100 , pp. 169
    • Brent, R.1
  • 35
    • 0033043389 scopus 로고    scopus 로고
    • Domain swapping used to investigate the mechanism of protein kinase B regulation by 3-phosphoinositide-dependent protein kinase 1 and Ser473 kinase
    • M. Andjelkovic, S-M. Maira, P. Cron et al., " Domain swapping used to investigate the mechanism of protein kinase B regulation by 3-phosphoinositide-dependent protein kinase 1 and Ser473 kinase, " Mol. Cell. Biol. 19, 5061 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5061
    • Andjelkovic, M.1    Maira, S.-M.2    Cron, P.3
  • 36
    • 0032474838 scopus 로고    scopus 로고
    • A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
    • G. Tzivion, Z. Luo, and J. Avruch, " A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity, " Nature (London) 394, 88 (1998).
    • (1998) Nature (London) , vol.394 , pp. 88
    • Tzivion, G.1    Luo, Z.2    Avruch, J.3
  • 37
    • 0033860695 scopus 로고    scopus 로고
    • The EGF receptor: A nexus for trafficking and signaling
    • G. Carpenter, " The EGF receptor: A nexus for trafficking and signaling, " BioEssays 22, 697 (2000).
    • (2000) BioEssays , vol.22 , pp. 697
    • Carpenter, G.1
  • 38
    • 0032881288 scopus 로고    scopus 로고
    • Akt/PKB and other D3 phosphoinositide-regulated kinases: Kinase activation by phosphoinositide-dependent phosphorylation
    • T. O. Chan, S. E. Rittenhouse, and P. N. Tsichlis, " Akt/PKB and other D3 phosphoinositide-regulated kinases: Kinase activation by phosphoinositide-dependent phosphorylation, " Annu. Rev. Biochem. 68, 965 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 965
    • Chan, T.O.1    Rittenhouse, S.E.2    Tsichlis, P.N.3
  • 39
    • 0033605718 scopus 로고    scopus 로고
    • The role of phosphoinositide 3-kinase lipid products in cell function
    • L. E. Rameh and L. C. Cantley, " The role of phosphoinositide 3-kinase lipid products in cell function, " J. Biol. Chem. 274, 8347 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 8347
    • Rameh, L.E.1    Cantley, L.C.2
  • 40
    • 0033537926 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphate kinases, a multifaceted family of signaling enzymes
    • R. A. Anderson, I. V. Boronenkov, S. D. Doughman et al., " Phosphatidylinositol phosphate kinases, a multifaceted family of signaling enzymes, " J. Biol. Chem. 274, 9907 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 9907
    • Anderson, R.A.1    Boronenkov, I.V.2    Doughman, S.D.3
  • 41
    • 0032407241 scopus 로고    scopus 로고
    • Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation, and membrane trafficking
    • T. F. J. Martin, " Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation, and membrane trafficking, " Annu. Rev. Cell Dev. Biol. 14, 231 (1998).
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 231
    • Martin, T.F.J.1
  • 42
    • 0034705455 scopus 로고    scopus 로고
    • Autophosphorylation of type I phosphatidylinositol phosphate kinase regulates its lipid kinase activity
    • Published electronically on 20 April 2000 as manuscript M000426200
    • T. Itoh et al., "Autophosphorylation of type I phosphatidylinositol phosphate kinase regulates its lipid kinase activity," J. Biol. Chem. (Published electronically on 20 April 2000 as manuscript M000426200) (2000).
    • (2000) J. Biol. Chem.
    • Itoh, T.1
  • 44
    • 0032929762 scopus 로고    scopus 로고
    • Signalling through phosphoinositide 3-kinases: The lipids take centre stage
    • S. J. Leevers, B. Vanhaesebroeck, and M. D. Waterfield, " Signalling through phosphoinositide 3-kinases: The lipids take centre stage, " Curr. Opin. Cell Biol. 11, 219 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 219
    • Leevers, S.J.1    Vanhaesebroeck, B.2    Waterfield, M.D.3
  • 45
    • 0032545343 scopus 로고    scopus 로고
    • The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells
    • M. F. Aman, T. D. Lamkin, H. Okada et al., " The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells, " J. Biol. Chem. 273, 33922 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 33922
    • Aman, M.F.1    Lamkin, T.D.2    Okada, H.3
  • 46
    • 0033587047 scopus 로고    scopus 로고
    • PDGF induces an early and a late wave of PI 3-kinase activity, and only the late wave is required for progression through G1
    • S. M. Jones, R. Klinghoffer, G. D. Prestwich et al., " PDGF induces an early and a late wave of PI 3-kinase activity, and only the late wave is required for progression through G1, " Curr. Biol. 9, 512 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 512
    • Jones, S.M.1    Klinghoffer, R.2    Prestwich, G.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.