메뉴 건너뛰기




Volumn 4, Issue 4, 2012, Pages 1180-1211

Annotating cancer variants and anti-cancer therapeutics in Reactome

Author keywords

Cancer annotation; EGFR signaling; Network visualization; Pathway database; Pathway visualization

Indexed keywords

1 (1 CYANO 1 METHYLETHYL) 3 METHYL 8 (3 QUINOLINYL)IMIDAZO[4,5 C]QUINOLIN 2(1H,3H) ONE; 1 TERT BUTYL 3 [6 (3,5 DIMETHOXYPHENYL) 2 (4 DIETHYLAMINOBUTYLAMINO)PYRIDO[2,3 D]PYRIMIDIN 7 YL]UREA; 3 [4 METHYL 2 (2 OXO 3 INDOLINYLMETHYLIDENYL) 3 PYRROLYL]PROPIONIC ACID; AFATINIB; ALVESPIMYCIN; AZD 4547; BRIVANIB; BRIVANIB ALANINATE; BUPARLISIB; CANERTINIB; CETUXIMAB; DOVITINIB; EPIDERMAL GROWTH FACTOR RECEPTOR; ERLOTINIB; GEFITINIB; GELDANAMYCIN; HERBIMYCIN A; LAPATINIB; LENVATINIB; MASITINIB; MIDOSTAURIN; NERATINIB; PELITINIB; PROTEIN VARIANT; RABEPRAZOLE; RETASPIMYCIN; TANESPIMYCIN; VANDETANIB;

EID: 84871602426     PISSN: None     EISSN: 20726694     Source Type: Journal    
DOI: 10.3390/cancers4041180     Document Type: Article
Times cited : (237)

References (88)
  • 4
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenbery, D.; Nunez, G.; Milliman, C.; Schreiber, R.D.; Korsmeyer, S.J. Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 1990, 348, 334-336.
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenbery, D.1    Nunez, G.2    Milliman, C.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 5
    • 0025850767 scopus 로고
    • Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast
    • Lew, D.J.; Dulic, V.; Reed, S.I. Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast. Cell 1991, 66, 1197-1206.
    • (1991) Cell , vol.66 , pp. 1197-1206
    • Lew, D.J.1    Dulic, V.2    Reed, S.I.3
  • 13
    • 79951549584 scopus 로고    scopus 로고
    • Human and chicken TLR pathways: Manual curation and computer-based orthology analysis
    • Gillespie, M.; Shamovsky, V.; D'Eustachio, P. Human and chicken TLR pathways: Manual curation and computer-based orthology analysis. Mamm. Genome 2010, 22, 130-138.
    • (2010) Mamm. Genome , vol.22 , pp. 130-138
    • Gillespie, M.1    Shamovsky, V.2    D'Eustachio, P.3
  • 17
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the Universal Protein Resource (UniProt)
    • Consortium, T.U
    • Consortium, T.U. Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Res. 2012, 40, D71-D75.
    • (2012) Nucleic Acids Res , vol.40
  • 20
    • 75849158230 scopus 로고    scopus 로고
    • The Gene Ontology in 2010: Extensions and refinements
    • Consortium, G.O. The Gene Ontology in 2010: Extensions and refinements. Nucleic Acids Res. 2010, 38, D331-D335.
    • Nucleic Acids Res , vol.2010 , Issue.38
  • 21
    • 84871596718 scopus 로고    scopus 로고
    • Reactome-Signaling by EGFR. Available online, accessed on 20 September
    • Reactome-Signaling by EGFR. Available online: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_9417/ (accessed on 20 September 2012).
    • (2012)
  • 22
    • 84871579420 scopus 로고    scopus 로고
    • Reactome-Signaling by FGFR. Available online, accessed on 20 September
    • Reactome-Signaling by FGFR. Available online: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_9470/ (accessed on 20 September 2012).
    • (2012)
  • 23
    • 84871537675 scopus 로고    scopus 로고
    • Reactome-Signaling by NOTCH. Available online, accessed on 20 September
    • Reactome-Signaling by NOTCH. Available online: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_299/ (accessed on 20 September 2012).
    • (2012)
  • 24
    • 84871536323 scopus 로고    scopus 로고
    • Reactome-PIP3 Activates AKT Signaling. Available online, accessed on 20 September
    • Reactome-PIP3 Activates AKT Signaling. Available online: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_75829/ (accessed on 20 September 2012).
    • (2012)
  • 25
    • 84871557356 scopus 로고    scopus 로고
    • Reactome-RAF/MAP Kinase Cascade. Available online, accessed on 20 September
    • Reactome-RAF/MAP Kinase Cascade. Available online: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_634/ (accessed on 20 September 2012).
    • (2012)
  • 26
    • 84871571792 scopus 로고    scopus 로고
    • Reactome-Apoptosis. Available online, accessed on 20 September
    • Reactome-Apoptosis. Available online: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_578/ (accessed on 20 September 2012).
    • (2012)
  • 27
    • 84871560719 scopus 로고    scopus 로고
    • Reactome-Cell Cycle Checkpoints. Available online, accessed on 20 September
    • Reactome-Cell Cycle Checkpoints. Available online: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_1538/ (accessed on 20 September 2012).
    • (2012)
  • 28
    • 84871592666 scopus 로고    scopus 로고
    • Reactome-Mitotic G1-G1/S phases. Available online, accessed on 20 September
    • Reactome-Mitotic G1-G1/S phases. Available online: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=REACT_21267/ (accessed on 20 September 2012).
    • (2012)
  • 29
    • 0029974671 scopus 로고    scopus 로고
    • Activation of epidermal growth factor receptor by epidermal growth factor
    • Sherrill, J.M.; Kyte, J. Activation of epidermal growth factor receptor by epidermal growth factor. Biochemistry 1996, 35, 5705-5718.
    • (1996) Biochemistry , vol.35 , pp. 5705-5718
    • Sherrill, J.M.1    Kyte, J.2
  • 31
    • 48249158391 scopus 로고    scopus 로고
    • Structure-based view of epidermal growth factor receptor regulation
    • Ferguson, K.M. Structure-based view of epidermal growth factor receptor regulation. Annu. Rev. Biophys. 2008, 37, 353-373.
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 353-373
    • Ferguson, K.M.1
  • 32
    • 33344455174 scopus 로고    scopus 로고
    • Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction
    • Furdui, C.M.; Lew, E.D.; Schlessinger, J.; Anderson, K.S. Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction. Mol. Cell 2006, 21, 711-717.
    • (2006) Mol. Cell , vol.21 , pp. 711-717
    • Furdui, C.M.1    Lew, E.D.2    Schlessinger, J.3    Anderson, K.S.4
  • 33
    • 0035168141 scopus 로고    scopus 로고
    • Identification of tyrosine residues in constitutively activated fibroblast growth factor receptor 3 involved in mitogenesis, Stat activation, and phosphatidylinositol 3-kinase activation
    • Hart, K.C.; Robertson, S.C.; Donoghue, D.J. Identification of tyrosine residues in constitutively activated fibroblast growth factor receptor 3 involved in mitogenesis, Stat activation, and phosphatidylinositol 3-kinase activation. Mol. Biol. Cell 2001, 12, 931-942.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 931-942
    • Hart, K.C.1    Robertson, S.C.2    Donoghue, D.J.3
  • 34
    • 0030027488 scopus 로고    scopus 로고
    • Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction
    • Mohammadi, M.; Dikic, I.; Sorokin, A.; Burgess, W.H.; Jaye, M.; Schlessinger, J. Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction. Mol. Cell. Biol. 1996, 16, 977-989.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 977-989
    • Mohammadi, M.1    Dikic, I.2    Sorokin, A.3    Burgess, W.H.4    Jaye, M.5    Schlessinger, J.6
  • 35
    • 78951489049 scopus 로고    scopus 로고
    • Feedback regulation of EGFR signalling: Decision making by early and delayed loops
    • Avraham, R.; Yarden, Y. Feedback regulation of EGFR signalling: Decision making by early and delayed loops. Nat. Rev. Mol. Cell Biol. 2011, 12, 104-117.
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 104-117
    • Avraham, R.1    Yarden, Y.2
  • 36
    • 9444287030 scopus 로고    scopus 로고
    • Common and distinct elements in cellular signaling via EGF and FGF receptors
    • Schlessinger, J. Common and distinct elements in cellular signaling via EGF and FGF receptors. Science 2004, 306, 1506-1507.
    • (2004) Science , vol.306 , pp. 1506-1507
    • Schlessinger, J.1
  • 37
    • 0035933094 scopus 로고    scopus 로고
    • Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins
    • Ong, S.H.; Hadari, Y.R.; Gotoh, N.; Guy, G.R.; Schlessinger, J.; Lax, I. Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins. Proc. Natl. Acad. Sci. USA 2001, 98, 6074-6079.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6074-6079
    • Ong, S.H.1    Hadari, Y.R.2    Gotoh, N.3    Guy, G.R.4    Schlessinger, J.5    Lax, I.6
  • 38
    • 0033959896 scopus 로고    scopus 로고
    • A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling
    • Rodrigues, G.A.; Falasca, M.; Zhang, Z.; Ong, S.H.; Schlessinger, J. A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling. Mol. Cell. Biol. 2000, 20, 1448-1459.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 1448-1459
    • Rodrigues, G.A.1    Falasca, M.2    Zhang, Z.3    Ong, S.H.4    Schlessinger, J.5
  • 39
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • Manning, B.D.; Cantley, L.C. AKT/PKB signaling: Navigating downstream. Cell 2007, 129, 1261-1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 40
    • 80051488597 scopus 로고    scopus 로고
    • Dynamics of the phosphoinositide 3-kinase p110delta interaction with p85alpha and membranes reveals aspects of regulation distinct from p110alpha
    • Burke, J.E.; Vadas, O.; Berndt, A.; Finegan, T.; Perisic, O.; Williams, R.L. Dynamics of the phosphoinositide 3-kinase p110delta interaction with p85alpha and membranes reveals aspects of regulation distinct from p110alpha. Structure 2011, 19, 1127-1137.
    • (2011) Structure , vol.19 , pp. 1127-1137
    • Burke, J.E.1    Vadas, O.2    Berndt, A.3    Finegan, T.4    Perisic, O.5    Williams, R.L.6
  • 42
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama, T.; Dixon, J.E. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 1998, 273, 13375-13378.
    • (1998) J. Biol. Chem , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 43
    • 0036333737 scopus 로고    scopus 로고
    • Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B
    • Scheid, M.P.; Marignani, P.A.; Woodgett, J.R. Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B. Mol. Cell. Biol. 2002, 22, 6247-6260.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 6247-6260
    • Scheid, M.P.1    Marignani, P.A.2    Woodgett, J.R.3
  • 44
    • 79953038262 scopus 로고    scopus 로고
    • PTEN loss in the continuum of common cancers, rare syndromes and mouse models
    • Hollander, M.C.; Blumenthal, G.M.; Dennis, P.A. PTEN loss in the continuum of common cancers, rare syndromes and mouse models. Nat. Rev. Cancer 2011, 11, 289-301.
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 289-301
    • Hollander, M.C.1    Blumenthal, G.M.2    Dennis, P.A.3
  • 46
    • 0035895916 scopus 로고    scopus 로고
    • Glycosylation-induced conformational modification positively regulates receptor-receptor association: A study with an aberrant epidermal growth factor receptor (EGFRvIII/DeltaEGFR) expressed in cancer cells
    • Fernandes, H.; Cohen, S.; Bishayee, S. Glycosylation-induced conformational modification positively regulates receptor-receptor association: A study with an aberrant epidermal growth factor receptor (EGFRvIII/DeltaEGFR) expressed in cancer cells. J. Biol. Chem. 2001, 276, 5375-5383.
    • (2001) J. Biol. Chem , vol.276 , pp. 5375-5383
    • Fernandes, H.1    Cohen, S.2    Bishayee, S.3
  • 47
    • 79959713140 scopus 로고    scopus 로고
    • Fibroblast growth factors and their receptors in cancer
    • Wesche, J.; Haglund, K.; Haugsten, E.M. Fibroblast growth factors and their receptors in cancer. Biochem. J. 2011, 437, 199-213.
    • (2011) Biochem. J , vol.437 , pp. 199-213
    • Wesche, J.1    Haglund, K.2    Haugsten, E.M.3
  • 49
    • 75149170979 scopus 로고    scopus 로고
    • Fibroblast growth factor signalling: From development to cancer
    • Turner, N.; Grose, R. Fibroblast growth factor signalling: From development to cancer. Nat. Rev. Cancer 2010, 10, 116-129.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 116-129
    • Turner, N.1    Grose, R.2
  • 51
    • 0029764116 scopus 로고    scopus 로고
    • Ligand-independent activation of fibroblast growth factor receptors by point mutations in the extracellular, transmembrane, and kinase domains
    • Neilson, K.M.; Friesel, R. Ligand-independent activation of fibroblast growth factor receptors by point mutations in the extracellular, transmembrane, and kinase domains. J. Biol. Chem. 1996, 271, 25049-25057.
    • (1996) J. Biol. Chem , vol.271 , pp. 25049-25057
    • Neilson, K.M.1    Friesel, R.2
  • 52
    • 77957258073 scopus 로고    scopus 로고
    • Cancer-derived mutations in the regulatory subunit p85alpha of phosphoinositide 3-kinase function through the catalytic subunit p110alpha
    • Sun, M.; Hillmann, P.; Hofmann, B.T.; Hart, J.R.; Vogt, P.K. Cancer-derived mutations in the regulatory subunit p85alpha of phosphoinositide 3-kinase function through the catalytic subunit p110alpha. Proc. Natl. Acad. Sci. USA 2010, 107, 15547-15552.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 15547-15552
    • Sun, M.1    Hillmann, P.2    Hofmann, B.T.3    Hart, J.R.4    Vogt, P.K.5
  • 56
    • 29444449785 scopus 로고    scopus 로고
    • The oncogenic properties of mutant p110alpha and p110beta phosphatidylinositol 3-kinases in human mammary epithelial cells
    • Zhao, J.J.; Liu, Z.; Wang, L.; Shin, E.; Loda, M.F.; Roberts, T.M. The oncogenic properties of mutant p110alpha and p110beta phosphatidylinositol 3-kinases in human mammary epithelial cells. Proc. Natl. Acad. Sci. USA 2005, 102, 18443-18448.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18443-18448
    • Zhao, J.J.1    Liu, Z.2    Wang, L.3    Shin, E.4    Loda, M.F.5    Roberts, T.M.6
  • 59
    • 77958478674 scopus 로고    scopus 로고
    • Rational, biologically based treatment of EGFR-mutant non-small-cell lung cancer
    • Pao, W.; Chmielecki, J. Rational, biologically based treatment of EGFR-mutant non-small-cell lung cancer. Nat. Rev. Cancer 2010, 10, 760-774.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 760-774
    • Pao, W.1    Chmielecki, J.2
  • 60
    • 79955667838 scopus 로고    scopus 로고
    • Targeting mutant fibroblast growth factor receptors in cancer
    • Greulich, H.; Pollock, P.M. Targeting mutant fibroblast growth factor receptors in cancer. Trends Mol. Med. 2011, 17, 283-292.
    • (2011) Trends Mol. Med , vol.17 , pp. 283-292
    • Greulich, H.1    Pollock, P.M.2
  • 61
    • 68249093818 scopus 로고    scopus 로고
    • Targeting the phosphoinositide 3-kinase pathway in cancer
    • Liu, P.; Cheng, H.; Roberts, T.M.; Zhao, J.J. Targeting the phosphoinositide 3-kinase pathway in cancer. Nat. Rev. Drug Discov. 2009, 8, 627-644.
    • (2009) Nat. Rev. Drug Discov , vol.8 , pp. 627-644
    • Liu, P.1    Cheng, H.2    Roberts, T.M.3    Zhao, J.J.4
  • 63
    • 33847406095 scopus 로고    scopus 로고
    • Structures of lung cancer-derived EGFR mutants and inhibitor complexes: Mechanism of activation and insights into differential inhibitor sensitivity
    • Yun, C.H.; Boggon, T.J.; Li, Y.; Woo, M.S.; Greulich, H.; Meyerson, M.; Eck, M.J. Structures of lung cancer-derived EGFR mutants and inhibitor complexes: Mechanism of activation and insights into differential inhibitor sensitivity. Cancer Cell 2007, 11, 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    Eck, M.J.7
  • 64
    • 79958820962 scopus 로고    scopus 로고
    • PIK3R1 (p85alpha) is somatically mutated at high frequency in primary endometrial cancer
    • Urick, M.E.; Rudd, M.L.; Godwin, A.K.; Sgroi, D.; Merino, M.; Bell, D.W. PIK3R1 (p85alpha) is somatically mutated at high frequency in primary endometrial cancer. Cancer Res. 2011, 71, 4061-4067.
    • (2011) Cancer Res , vol.71 , pp. 4061-4067
    • Urick, M.E.1    Rudd, M.L.2    Godwin, A.K.3    Sgroi, D.4    Merino, M.5    Bell, D.W.6
  • 65
    • 0035895067 scopus 로고    scopus 로고
    • The t(8;22) in chronic myeloid leukemia fuses BCR to FGFR1: Transforming activity and specific inhibition of FGFR1 fusion proteins
    • Demiroglu, A.; Steer, E.J.; Heath, C.; Taylor, K.; Bentley, M.; Allen, S.L.; Koduru, P.; Brody, J.P.; Hawson, G.; Rodwell, R. et al. The t(8;22) in chronic myeloid leukemia fuses BCR to FGFR1: Transforming activity and specific inhibition of FGFR1 fusion proteins. Blood 2001, 98, 3778-3783.
    • (2001) Blood , vol.98 , pp. 3778-3783
    • Demiroglu, A.1    Steer, E.J.2    Heath, C.3    Taylor, K.4    Bentley, M.5    Allen, S.L.6    Koduru, P.7    Brody, J.P.8    Hawson, G.9    Rodwell, R.10
  • 70
    • 17444403242 scopus 로고    scopus 로고
    • Structural basis for inhibition of the epidermal growth factor receptor by cetuximab
    • Li, S.; Schmitz, K.R.; Jeffrey, P.D.; Wiltzius, J.J.; Kussie, P.; Ferguson, K.M. Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. Cancer Cell 2005, 7, 301-311.
    • (2005) Cancer Cell , vol.7 , pp. 301-311
    • Li, S.1    Schmitz, K.R.2    Jeffrey, P.D.3    Wiltzius, J.J.4    Kussie, P.5    Ferguson, K.M.6
  • 71
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C.E.; Russo, A.A.; Schneider, C.; Rosen, N.; Hartl, F.U.; Pavletich, N.P. Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent. Cell 1997, 89, 239-250.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 72
    • 77957331045 scopus 로고    scopus 로고
    • GP369, an FGFR2-IIIb-specific antibody, exhibits potent antitumor activity against human cancers driven by activated FGFR2 signaling
    • Bai, A.; Meetze, K.; Vo, N.Y.; Kollipara, S.; Mazsa, E.K.; Winston, W.M.; Weiler, S.; Poling, L.L.; Chen, T.; Ismail, N.S. et al. GP369, an FGFR2-IIIb-specific antibody, exhibits potent antitumor activity against human cancers driven by activated FGFR2 signaling. Cancer Res. 2010, 70, 7630-7639.
    • (2010) Cancer Res , vol.70 , pp. 7630-7639
    • Bai, A.1    Meetze, K.2    Vo, N.Y.3    Kollipara, S.4    Mazsa, E.K.5    Winston, W.M.6    Weiler, S.7    Poling, L.L.8    Chen, T.9    Ismail, N.S.10
  • 75
    • 61749093196 scopus 로고    scopus 로고
    • ChEMBL. An interview with John Overington, team leader, chemogenomics at the European Bioinformatics Institute Outstation of the European Molecular Biology Laboratory (EMBL-EBI). Interview by Wendy A
    • Overington, J. ChEMBL. An interview with John Overington, team leader, chemogenomics at the European Bioinformatics Institute Outstation of the European Molecular Biology Laboratory (EMBL-EBI). Interview by Wendy A. Warr. J. Comput. Aided Mol. Des. 2009, 23, 195-198.
    • (2009) Warr. J. Comput. Aided Mol. Des , vol.23 , pp. 195-198
    • Overington, J.1
  • 76
    • 9444266171 scopus 로고    scopus 로고
    • CellDesigner: A process diagram editor for gene-regulatory and biochemical networks
    • Funahashi, A.; Tanimura, N.; Morohashi, M.; Kitano, H. CellDesigner: A process diagram editor for gene-regulatory and biochemical networks. BioSilico 2003, 1, 159-162.
    • (2003) BioSilico , vol.1 , pp. 159-162
    • Funahashi, A.1    Tanimura, N.2    Morohashi, M.3    Kitano, H.4
  • 77
    • 70349581497 scopus 로고    scopus 로고
    • Cytoscape: A community-based framework for network modeling
    • Killcoyne, S.; Carter, G.W.; Smith, J.; Boyle, J. Cytoscape: A community-based framework for network modeling. Methods Mol. Biol. 2009, 563, 219-239.
    • (2009) Methods Mol. Biol , vol.563 , pp. 219-239
    • Killcoyne, S.1    Carter, G.W.2    Smith, J.3    Boyle, J.4
  • 78
    • 33645241830 scopus 로고    scopus 로고
    • VANTED: A system for advanced data analysis and visualization in the context of biological networks
    • Junker, B.H.; Klukas, C.; Schreiber, F. VANTED: A system for advanced data analysis and visualization in the context of biological networks. BMC Bioinformatics 2006, 7, 109.
    • (2006) BMC Bioinformatics , vol.7 , pp. 109
    • Junker, B.H.1    Klukas, C.2    Schreiber, F.3
  • 80
    • 84871542328 scopus 로고    scopus 로고
    • International Cancer Genome Consortium. Available online, accessed on 20 September
    • International Cancer Genome Consortium. Available online: http://www.icgc.org (accessed on 20 September 2012).
    • (2012)
  • 82
    • 75549090213 scopus 로고    scopus 로고
    • KEGG for representation and analysis of molecular networks involving diseases and drugs
    • Kanehisa, M.; Goto, S.; Furumichi, M.; Tanabe, M.; Hirakawa, M. KEGG for representation and analysis of molecular networks involving diseases and drugs. Nucleic Acids Res. 2010, 38, D355-D360.
    • (2010) Nucleic Acids Res , vol.38
    • Kanehisa, M.1    Goto, S.2    Furumichi, M.3    Tanabe, M.4    Hirakawa, M.5
  • 83
    • 75549084894 scopus 로고    scopus 로고
    • PANTHER version 7: Improved phylogenetic trees, orthologs and collaboration with the Gene Ontology Consortium
    • Mi, H.; Dong, Q.; Muruganujan, A.; Gaudet, P.; Lewis, S.; Thomas, P.D. PANTHER version 7: Improved phylogenetic trees, orthologs and collaboration with the Gene Ontology Consortium. Nucleic Acids Res. 2010, 38, D204-D210.
    • (2010) Nucleic Acids Res , vol.38
    • Mi, H.1    Dong, Q.2    Muruganujan, A.3    Gaudet, P.4    Lewis, S.5    Thomas, P.D.6
  • 88
    • 77952310528 scopus 로고    scopus 로고
    • A human functional protein interaction network and its application to cancer data analysis
    • Wu, G.; Feng, X.; Stein, L. A human functional protein interaction network and its application to cancer data analysis. Genome Biol. 2010, 11, R53.
    • (2010) Genome Biol , vol.11
    • Wu, G.1    Feng, X.2    Stein, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.