메뉴 건너뛰기




Volumn 18, Issue 30, 2012, Pages 4619-4629

Protein-protein interactions: Network analysis and applications in drug discovery

Author keywords

Drug discovery; Interactome; Oncology; Protein protein interaction; Small molecule; Virology

Indexed keywords

AEG 40826; AT 406; CG 049090; CHETOMIN; GDC 0152; IMIDAZOLINE DERIVATIVE; ISOSORBIDE; LCL 161; NAVITOCLAX; OBATOCLAX; PFK 115584; RRD 251; SJ 172550; STX 0119; UNCLASSIFIED DRUG;

EID: 84866398910     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/138161212802651562     Document Type: Article
Times cited : (25)

References (158)
  • 1
    • 79956140184 scopus 로고    scopus 로고
    • Getting pharmaceutical R&D back on target
    • Bunnage ME. Getting pharmaceutical R&D back on target. Nat Chem Biol 2011; 7(6): 335-339.
    • (2011) Nat Chem Biol , vol.7 , Issue.6 , pp. 335-339
    • Bunnage, M.E.1
  • 4
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S, Thornton JM. Principles of protein-protein interactions. Proc Natl Acad Sci USA 1996; 93(1): 13-20.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.1 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 5
    • 34548779127 scopus 로고    scopus 로고
    • Hot spots--a review of the protein-protein interface determinant amino-acid residues
    • Moreira IS, Fernandes PA, Ramos MJ. Hot spots--a review of the protein-protein interface determinant amino-acid residues. Proteins 2007; 68(4): 803-812.
    • (2007) Proteins , vol.68 , Issue.4 , pp. 803-812
    • Moreira, I.S.1    Fernandes, P.A.2    Ramos, M.J.3
  • 6
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormonereceptor interface
    • Clackson T, Wells JA. A hot spot of binding energy in a hormonereceptor interface. Science 1995; 267(5196): 383-386.
    • (1995) Science , vol.267 , Issue.5196 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 7
    • 0037452709 scopus 로고    scopus 로고
    • Binding of small molecules to an adaptive protein-protein interface
    • Arkin MR, Randal M, DeLano WL, et al. Binding of small molecules to an adaptive protein-protein interface. Proc Natl Acad Sci USA 2003; 100(4): 1603-1608.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.4 , pp. 1603-1608
    • Arkin, M.R.1    Randal, M.2    Delano, W.L.3
  • 8
    • 2442705551 scopus 로고    scopus 로고
    • A mammalian genetic system to screen for small molecules capable of disrupting proteinprotein interactions
    • Zhao HF, Kiyota T, Chowdhury S, et al. A mammalian genetic system to screen for small molecules capable of disrupting proteinprotein interactions. Anal Chem 2004; 76(10): 2922-2927.
    • (2004) Anal Chem , vol.76 , Issue.10 , pp. 2922-2927
    • Zhao, H.F.1    Kiyota, T.2    Chowdhury, S.3
  • 9
    • 58149305794 scopus 로고    scopus 로고
    • An empirical framework for binary interactome mapping
    • Venkatesan K, Rual JF, Vazquez A, et al. An empirical framework for binary interactome mapping. Nat Methods 2009; 6(1): 83-90.
    • (2009) Nat Methods , vol.6 , Issue.1 , pp. 83-90
    • Venkatesan, K.1    Rual, J.F.2    Vazquez, A.3
  • 10
    • 44349113144 scopus 로고    scopus 로고
    • Estimating the size of the human interactome
    • Stumpf MP, Thorne T, de Silva E, et al. Estimating the size of the human interactome. Proc Natl Acad Sci USA 2008; 105(19): 6959-6964.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.19 , pp. 6959-6964
    • Stumpf, M.P.1    Thorne, T.2    de Silva, E.3
  • 11
    • 84877920920 scopus 로고    scopus 로고
    • DrugBank
    • DrugBank. http://www.drugbank.ca/.
  • 12
    • 84555190555 scopus 로고    scopus 로고
    • Targeting the proangiogenic VEGF-VEGFR protein-protein interface with druglike compounds by in silico and in vitro screening
    • Gautier B, Miteva MA, Goncalves V, et al. Targeting the proangiogenic VEGF-VEGFR protein-protein interface with druglike compounds by in silico and in vitro screening. Chem Biol 2011; 18(12): 1631-1639.
    • (2011) Chem Biol , vol.18 , Issue.12 , pp. 1631-1639
    • Gautier, B.1    Miteva, M.A.2    Goncalves, V.3
  • 13
    • 82255191693 scopus 로고    scopus 로고
    • Anti-VEGF and beyond: Shaping a new generation of anti-angiogenic therapies for cancer
    • Bertolini F, Marighetti P, Martin-Padura I, et al. Anti-VEGF and beyond: shaping a new generation of anti-angiogenic therapies for cancer. Drug Discov Today 2011; 16(23/24): 1052-1060.
    • (2011) Drug Discov Today , vol.16 , Issue.23-24 , pp. 1052-1060
    • Bertolini, F.1    Marighetti, P.2    Martin-Padura, I.3
  • 14
    • 80053025493 scopus 로고    scopus 로고
    • Allosteric Model of Maraviroc Binding to CC Chemokine Receptor 5 (CCR5)
    • Garcia-Perez J, Rueda P, Alcami J, et al. Allosteric Model of Maraviroc Binding to CC Chemokine Receptor 5 (CCR5). J Biol Chem 2011; 286(38): 33409-33421.
    • (2011) J Biol Chem , vol.286 , Issue.38 , pp. 33409-33421
    • Garcia-Perez, J.1    Rueda, P.2    Alcami, J.3
  • 15
    • 44949154279 scopus 로고    scopus 로고
    • Small molecular weight protein-protein interaction antagonists: An insurmountable challenge?
    • Domling A. Small molecular weight protein-protein interaction antagonists: an insurmountable challenge? Curr Opin Chem Biol 2008; 12(3): 281-291.
    • (2008) Curr Opin Chem Biol , vol.12 , Issue.3 , pp. 281-291
    • Domling, A.1
  • 16
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B, et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 2004; 303(5659): 844-848.
    • (2004) Science , vol.303 , Issue.5659 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 18
    • 77951224332 scopus 로고    scopus 로고
    • Identification and characterization of the first small molecule inhibitor of MDMX
    • Reed D, Shen Y, Shelat AA, et al. Identification and characterization of the first small molecule inhibitor of MDMX. J Biol Chem 2010; 285(14): 10786-10796.
    • (2010) J Biol Chem , vol.285 , Issue.14 , pp. 10786-10796
    • Reed, D.1    Shen, Y.2    Shelat, A.A.3
  • 19
    • 33847328289 scopus 로고    scopus 로고
    • The Bcl-2 apoptotic switch in cancer development and therapy
    • Adams JM, Cory S. The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 2007; 26(9): 1324-1337.
    • (2007) Oncogene , vol.26 , Issue.9 , pp. 1324-1337
    • Adams, J.M.1    Cory, S.2
  • 20
    • 60849086456 scopus 로고    scopus 로고
    • Bcl-2 inhibitors: Small molecules with a big impact on cancer therapy
    • Vogler M, Dinsdale D, Dyer MJ, Cohen GM. Bcl-2 inhibitors: small molecules with a big impact on cancer therapy. Cell Death Differ 2009; 16(3): 360-367.
    • (2009) Cell Death Differ , vol.16 , Issue.3 , pp. 360-367
    • Vogler, M.1    Dinsdale, D.2    Dyer, M.J.3    Cohen, G.M.4
  • 21
    • 84877920967 scopus 로고    scopus 로고
    • ClinicalTrials.gov
    • ClinicalTrials.gov. http://clinicaltrials.gov/ct2/home.
  • 22
    • 79960119761 scopus 로고    scopus 로고
    • Multiple BH3 mimetics antagonize antiapoptotic MCL1 protein by inducing the endoplasmic reticulum stress response and up-regulating BH3-only protein NOXA
    • Albershardt TC, Salerni BL, Soderquist RS, et al. Multiple BH3 mimetics antagonize antiapoptotic MCL1 protein by inducing the endoplasmic reticulum stress response and up-regulating BH3-only protein NOXA. J Biol Chem 2011; 286(28): 24882-24895.
    • (2011) J Biol Chem , vol.286 , Issue.28 , pp. 24882-24895
    • Albershardt, T.C.1    Salerni, B.L.2    Soderquist, R.S.3
  • 23
    • 76149118435 scopus 로고    scopus 로고
    • Small-molecule pan-IAP antagonists: A patent review
    • Flygare JA, Fairbrother WJ. Small-molecule pan-IAP antagonists: a patent review. Expert Opin Ther Pat 2010; 20(2): 251-267.
    • (2010) Expert Opin Ther Pat , vol.20 , Issue.2 , pp. 251-267
    • Flygare, J.A.1    Fairbrother, W.J.2
  • 24
    • 79958280454 scopus 로고    scopus 로고
    • Targeting the Wnt/beta-catenin signaling pathway in human cancers
    • Yao H, Ashihara E, Maekawa T. Targeting the Wnt/beta-catenin signaling pathway in human cancers. Expert Opin Ther Targets 2011; 15(7): 873-887.
    • (2011) Expert Opin Ther Targets , vol.15 , Issue.7 , pp. 873-887
    • Yao, H.1    Ashihara, E.2    Maekawa, T.3
  • 25
    • 4344587136 scopus 로고    scopus 로고
    • A small molecule inhibitor of beta-catenin/CREB-binding protein transcription [corrected]
    • Emami KH, Nguyen C, Ma H, et al. A small molecule inhibitor of beta-catenin/CREB-binding protein transcription [corrected]. Proc Natl Acad Sci USA 2004; 101(34): 12682-12687.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.34 , pp. 12682-12687
    • Emami, K.H.1    Nguyen, C.2    Ma, H.3
  • 26
    • 84862901143 scopus 로고    scopus 로고
    • Small-molecule modulators of c-Myc/Max and Max/Max interactions
    • Berg T. Small-molecule modulators of c-Myc/Max and Max/Max interactions. Curr Top Microbiol Immunol 2011; 348: 139-149.
    • (2011) Curr Top Microbiol Immunol , vol.348 , pp. 139-149
    • Berg, T.1
  • 27
    • 56249094537 scopus 로고    scopus 로고
    • Disrupting the Rb-Raf-1 interaction: A potential therapeutic target for cancer
    • Davis RK, Chellappan S. Disrupting the Rb-Raf-1 interaction: a potential therapeutic target for cancer. Drug News Perspect 2008; 21(6): 331-335.
    • (2008) Drug News Perspect , vol.21 , Issue.6 , pp. 331-335
    • Davis, R.K.1    Chellappan, S.2
  • 28
    • 45549105690 scopus 로고    scopus 로고
    • A small molecule disruptor of Rb/Raf-1 interaction inhibits cell proliferation, angiogenesis, and growth of human tumor xenografts in nude mice
    • Kinkade R, Dasgupta P, Carie A, et al. A small molecule disruptor of Rb/Raf-1 interaction inhibits cell proliferation, angiogenesis, and growth of human tumor xenografts in nude mice. Cancer Res 2008; 68(10): 3810-3818.
    • (2008) Cancer Res , vol.68 , Issue.10 , pp. 3810-3818
    • Kinkade, R.1    Dasgupta, P.2    Carie, A.3
  • 29
    • 70350271965 scopus 로고    scopus 로고
    • Epidithiodiketopiperazines block the interaction between hypoxia-inducible factor-1alpha (HIF-1alpha) and p300 by a zinc ejection mechanism
    • Cook KM, Hilton ST, Mecinovic J, Motherwell WB, Figg WD, Schofield CJ. Epidithiodiketopiperazines block the interaction between hypoxia-inducible factor-1alpha (HIF-1alpha) and p300 by a zinc ejection mechanism. J Biol Chem 2009; 284(39): 26831-26838.
    • (2009) J Biol Chem , vol.284 , Issue.39 , pp. 26831-26838
    • Cook, K.M.1    Hilton, S.T.2    Mecinovic, J.3    Motherwell, W.B.4    Figg, W.D.5    Schofield, C.J.6
  • 30
    • 3142622930 scopus 로고    scopus 로고
    • Small molecule blockade of transcriptional coactivation of the hypoxia-inducible factor pathway
    • Kung AL, Zabludoff SD, France DS, et al. Small molecule blockade of transcriptional coactivation of the hypoxia-inducible factor pathway. Cancer Cell 2004; 6(1): 33-43.
    • (2004) Cancer Cell , vol.6 , Issue.1 , pp. 33-43
    • Kung, A.L.1    Zabludoff, S.D.2    France, D.S.3
  • 31
    • 79955000497 scopus 로고    scopus 로고
    • Antitumor activity of a novel small molecule STAT3 inhibitor against a human lymphoma cell line with high STAT3 activation
    • Ashizawa T, Miyata H, Ishii H, et al. Antitumor activity of a novel small molecule STAT3 inhibitor against a human lymphoma cell line with high STAT3 activation. Int J Oncol 2011; 38(5): 1245-1252.
    • (2011) Int J Oncol , vol.38 , Issue.5 , pp. 1245-1252
    • Ashizawa, T.1    Miyata, H.2    Ishii, H.3
  • 32
    • 77953280591 scopus 로고    scopus 로고
    • Regression of castraterecurrent prostate cancer by a small-molecule inhibitor of the amino-terminus domain of the androgen receptor
    • Andersen RJ, Mawji NR, Wang J, et al. Regression of castraterecurrent prostate cancer by a small-molecule inhibitor of the amino-terminus domain of the androgen receptor. Cancer Cell 2010; 17(6): 535-546.
    • (2010) Cancer Cell , vol.17 , Issue.6 , pp. 535-546
    • Andersen, R.J.1    Mawji, N.R.2    Wang, J.3
  • 33
    • 33846449110 scopus 로고    scopus 로고
    • Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G
    • Moerke NJ, Aktas H, Chen H, et al. Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G. Cell 2007; 128(2): 257-267.
    • (2007) Cell , vol.128 , Issue.2 , pp. 257-267
    • Moerke, N.J.1    Aktas, H.2    Chen, H.3
  • 34
    • 79551648564 scopus 로고    scopus 로고
    • Reversing chemoresistance by small molecule inhibition of the translation initiation complex eIF4F
    • Cencic R, Hall DR, Robert F, et al. Reversing chemoresistance by small molecule inhibition of the translation initiation complex eIF4F. Proc Natl Acad Sci USA 2011; 108(3): 1046-1051.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.3 , pp. 1046-1051
    • Cencic, R.1    Hall, D.R.2    Robert, F.3
  • 35
    • 80053645046 scopus 로고    scopus 로고
    • Discovery and structural characterization of a small molecule 14-3-3 protein-protein interaction inhibitor
    • Zhao J, Du Y, Horton JR, et al. Discovery and structural characterization of a small molecule 14-3-3 protein-protein interaction inhibitor. Proc Natl Acad Sci USA 2011; 108(39): 16212-16216.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.39 , pp. 16212-16216
    • Zhao, J.1    Du, Y.2    Horton, J.R.3
  • 36
    • 84862896560 scopus 로고    scopus 로고
    • Small molecule inhibitors of the human papillomavirus E1-E2 interaction
    • White PW, Faucher AM, Goudreau N. Small molecule inhibitors of the human papillomavirus E1-E2 interaction. Curr Top Microbiol Immunol 2011; 348: 61-88.
    • (2011) Curr Top Microbiol Immunol , vol.348 , pp. 61-88
    • White, P.W.1    Faucher, A.M.2    Goudreau, N.3
  • 37
    • 0038035868 scopus 로고    scopus 로고
    • Inhibition of human papillomavirus DNA replication by small molecule antagonists of the E1-E2 protein interaction
    • White PW, Titolo S, Brault K, et al. Inhibition of human papillomavirus DNA replication by small molecule antagonists of the E1-E2 protein interaction. J Biol Chem 2003; 278(29): 26765-26772.
    • (2003) J Biol Chem , vol.278 , Issue.29 , pp. 26765-26772
    • White, P.W.1    Titolo, S.2    Brault, K.3
  • 38
    • 34250357662 scopus 로고    scopus 로고
    • The double bromodomain-containing chromatin adaptor Brd4 and transcriptional regulation
    • Wu SY, Chiang CM. The double bromodomain-containing chromatin adaptor Brd4 and transcriptional regulation. J Biol Chem 2007; 282(18): 13141-13145.
    • (2007) J Biol Chem , vol.282 , Issue.18 , pp. 13141-13145
    • Wu, S.Y.1    Chiang, C.M.2
  • 39
    • 77649248469 scopus 로고    scopus 로고
    • Genome-wide siRNA screen identifies SMCX, EP400, and Brd4 as E2-dependent regulators of human papillomavirus oncogene expression
    • Smith JA, White EA, Sowa ME, et al. Genome-wide siRNA screen identifies SMCX, EP400, and Brd4 as E2-dependent regulators of human papillomavirus oncogene expression. Proc Natl Acad Sci USA 2010; 107(8): 3752-3757.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.8 , pp. 3752-3757
    • Smith, J.A.1    White, E.A.2    Sowa, M.E.3
  • 40
    • 72849149501 scopus 로고    scopus 로고
    • Abrogation of the Brd4-positive transcription elongation factor B complex by papillomavirus E2 protein contributes to viral oncogene repression
    • Yan J, Li Q, Lievens S, Tavernier J, You J. Abrogation of the Brd4-positive transcription elongation factor B complex by papillomavirus E2 protein contributes to viral oncogene repression. J Virol 2010; 84(1): 76-87.
    • (2010) J Virol , vol.84 , Issue.1 , pp. 76-87
    • Yan, J.1    Li, Q.2    Lievens, S.3    Tavernier, J.4    You, J.5
  • 41
    • 77952553431 scopus 로고    scopus 로고
    • Rational design of smallmolecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication
    • Christ F, Voet A, Marchand A, et al. Rational design of smallmolecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication. Nat Chem Biol 2010; 6(6): 442-448.
    • (2010) Nat Chem Biol , vol.6 , Issue.6 , pp. 442-448
    • Christ, F.1    Voet, A.2    Marchand, A.3
  • 43
    • 53649086178 scopus 로고    scopus 로고
    • Small-molecule inhibition of HIV-1 Vif
    • 2008 Oct
    • Nathans R, Cao H, Sharova N, et al. Small-molecule inhibition of HIV-1 Vif. Nat Biotechnol 2008 Oct; 26(10): 1187-1192.
    • Nat Biotechnol , vol.26 , Issue.10 , pp. 1187-1192
    • Nathans, R.1    Cao, H.2    Sharova, N.3
  • 44
    • 77952781524 scopus 로고    scopus 로고
    • Small molecular compounds inhibit HIV-1 replication through specifically stabilizing APOBEC3G
    • Cen S, Peng ZG, Li XY, et al. Small molecular compounds inhibit HIV-1 replication through specifically stabilizing APOBEC3G. J Biol Chem 2010; 285(22): 16546-16552.
    • (2010) J Biol Chem , vol.285 , Issue.22 , pp. 16546-16552
    • Cen, S.1    Peng, Z.G.2    Li, X.Y.3
  • 45
    • 80052048025 scopus 로고    scopus 로고
    • Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication
    • Cencic R, Desforges M, Hall DR, et al. Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication. J Virol 2011; 85(13): 6381-6389.
    • (2011) J Virol , vol.85 , Issue.13 , pp. 6381-6389
    • Cencic, R.1    Desforges, M.2    Hall, D.R.3
  • 46
    • 46749097944 scopus 로고    scopus 로고
    • Therapeutic suppression of translation initiation modulates chemosensitivity in a mouse lymphoma model
    • Bordeleau ME, Robert F, Gerard B, et al. Therapeutic suppression of translation initiation modulates chemosensitivity in a mouse lymphoma model. J Clin Invest 2008; 118(7): 2651-2660.
    • (2008) J Clin Invest , vol.118 , Issue.7 , pp. 2651-2660
    • Bordeleau, M.E.1    Robert, F.2    Gerard, B.3
  • 47
    • 34848901974 scopus 로고    scopus 로고
    • Therapeutic suppression of translation initiation factor eIF4E expression reduces tumor growth without toxicity
    • Graff JR, Konicek BW, Vincent TM, et al. Therapeutic suppression of translation initiation factor eIF4E expression reduces tumor growth without toxicity. J Clin Invest 2007; 117(9): 2638-2648.
    • (2007) J Clin Invest , vol.117 , Issue.9 , pp. 2638-2648
    • Graff, J.R.1    Konicek, B.W.2    Vincent, T.M.3
  • 48
    • 78751477224 scopus 로고    scopus 로고
    • Challenges of antibacterial discovery
    • Silver LL. Challenges of antibacterial discovery. Clin Microbiol Rev 2011; 24(1): 71-109.
    • (2011) Clin Microbiol Rev , vol.24 , Issue.1 , pp. 71-109
    • Silver, L.L.1
  • 49
    • 79959740064 scopus 로고    scopus 로고
    • Antibiotics in the clinical pipeline in 2011
    • Butler MS, Cooper MA. Antibiotics in the clinical pipeline in 2011. J Antibiot (Tokyo) 2011; 64(6): 413-425.
    • (2011) J Antibiot (Tokyo) , vol.64 , Issue.6 , pp. 413-425
    • Butler, M.S.1    Cooper, M.A.2
  • 51
    • 31544454456 scopus 로고    scopus 로고
    • Novel synthetic molecules targeting the bacterial RNA polymerase assembly
    • Andre E, Bastide L, Michaux-Charachon S, et al. Novel synthetic molecules targeting the bacterial RNA polymerase assembly. J Antimicrob Chemother 2006; 57(2): 245-251.
    • (2006) J Antimicrob Chemother , vol.57 , Issue.2 , pp. 245-251
    • Andre, E.1    Bastide, L.2    Michaux-Charachon, S.3
  • 52
    • 78651300299 scopus 로고    scopus 로고
    • TAK-242 (resatorvid), a small-molecule inhibitor of Toll-like receptor (TLR) 4 signaling, binds selectively to TLR4 and interferes with interactions between TLR4 and its adaptor molecules
    • Matsunaga N, Tsuchimori N, Matsumoto T, Ii M. TAK-242 (resatorvid), a small-molecule inhibitor of Toll-like receptor (TLR) 4 signaling, binds selectively to TLR4 and interferes with interactions between TLR4 and its adaptor molecules. Mol Pharmacol 2011; 79(1): 34-41.
    • (2011) Mol Pharmacol , vol.79 , Issue.1 , pp. 34-41
    • Matsunaga, N.1    Tsuchimori, N.2    Matsumoto, T.3    Ii, M.4
  • 53
    • 0037153158 scopus 로고    scopus 로고
    • A central role for JNK in obesity and insulin resistance
    • Hirosumi J, Tuncman G, Chang L, et al. A central role for JNK in obesity and insulin resistance. Nature 2002; 420(6913): 333-336.
    • (2002) Nature , vol.420 , Issue.6913 , pp. 333-336
    • Hirosumi, J.1    Tuncman, G.2    Chang, L.3
  • 54
    • 7044230885 scopus 로고    scopus 로고
    • Possible novel therapy for diabetes with cell-permeable JNK-inhibitory peptide
    • Kaneto H, Nakatani Y, Miyatsuka T, et al. Possible novel therapy for diabetes with cell-permeable JNK-inhibitory peptide. Nat Med 2004; 10(10): 1128-1132.
    • (2004) Nat Med , vol.10 , Issue.10 , pp. 1128-1132
    • Kaneto, H.1    Nakatani, Y.2    Miyatsuka, T.3
  • 55
    • 66549126199 scopus 로고    scopus 로고
    • Identification of small-molecule inhibitors of the JIP-JNK interaction
    • Chen T, Kablaoui N, Little J, et al. Identification of small-molecule inhibitors of the JIP-JNK interaction. Biochem J 2009; 420(2): 283-294.
    • (2009) Biochem J , vol.420 , Issue.2 , pp. 283-294
    • Chen, T.1    Kablaoui, N.2    Little, J.3
  • 56
    • 55949100580 scopus 로고    scopus 로고
    • Identification of a new JNK inhibitor targeting the JNK-JIP interaction site
    • Stebbins JL, De SK, Machleidt T, et al. Identification of a new JNK inhibitor targeting the JNK-JIP interaction site. Proc Natl Acad Sci USA 2008; 105(43): 16809-16813.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.43 , pp. 16809-16813
    • Stebbins, J.L.1    De, S.K.2    Machleidt, T.3
  • 57
    • 79953164965 scopus 로고    scopus 로고
    • Functional regulation of cystic fibrosis transmembrane conductance regulator-containing macromolecular complexes: A small-molecule inhibitor approach
    • Zhang W, Penmatsa H, Ren A, et al. Functional regulation of cystic fibrosis transmembrane conductance regulator-containing macromolecular complexes: a small-molecule inhibitor approach. Biochem J 2011; 435(2): 451-462.
    • (2011) Biochem J , vol.435 , Issue.2 , pp. 451-462
    • Zhang, W.1    Penmatsa, H.2    Ren, A.3
  • 58
    • 69549118534 scopus 로고    scopus 로고
    • Disruption of nNOS-PSD95 protein-protein interaction inhibits acute thermal hyperalgesia and chronic mechanical allodynia in rodents
    • Florio SK, Loh C, Huang SM, et al. Disruption of nNOS-PSD95 protein-protein interaction inhibits acute thermal hyperalgesia and chronic mechanical allodynia in rodents. Br J Pharmacol 2009; 158(2): 494-506.
    • (2009) Br J Pharmacol , vol.158 , Issue.2 , pp. 494-506
    • Florio, S.K.1    Loh, C.2    Huang, S.M.3
  • 59
    • 78650947751 scopus 로고    scopus 로고
    • Discovery of modulators of proteinprotein interactions: Current approaches and limitations
    • Meireles LM, Mustata G. Discovery of modulators of proteinprotein interactions: current approaches and limitations. Curr Top Med Chem 2011; 11(3): 248-257.
    • (2011) Curr Top Med Chem , vol.11 , Issue.3 , pp. 248-257
    • Meireles, L.M.1    Mustata, G.2
  • 60
    • 51349160681 scopus 로고    scopus 로고
    • High-throughput screening assays to discover smallmolecule inhibitors of protein interactions
    • Colas P. High-throughput screening assays to discover smallmolecule inhibitors of protein interactions. Curr Drug Discov Technol 2008; 5(3): 190-199.
    • (2008) Curr Drug Discov Technol , vol.5 , Issue.3 , pp. 190-199
    • Colas, P.1
  • 61
    • 84877926996 scopus 로고    scopus 로고
    • The use of mammalian two-hybrids for high-throughput drug screening
    • submitted
    • Lievens S, Caligiuri M, Kley N, Tavernier J. The use of mammalian two-hybrids for high-throughput drug screening. Methods. submitted.
    • Methods
    • Lievens, S.1    Caligiuri, M.2    Kley, N.3    Tavernier, J.4
  • 62
    • 3342908718 scopus 로고    scopus 로고
    • Emerging classes of protein-protein interaction inhibitors and new tools for their development
    • Pagliaro L, Felding J, Audouze K, et al. Emerging classes of protein-protein interaction inhibitors and new tools for their development. Curr Opin Chem Biol 2004; 8(4): 442-449.
    • (2004) Curr Opin Chem Biol , vol.8 , Issue.4 , pp. 442-449
    • Pagliaro, L.1    Felding, J.2    Audouze, K.3
  • 63
    • 33645377497 scopus 로고    scopus 로고
    • Structure-based development of target-specific compound libraries
    • Orry AJ, Abagyan RA, Cavasotto CN. Structure-based development of target-specific compound libraries. Drug Discov Today 2006; 11(5-6): 261-266.
    • (2006) Drug Discov Today , vol.11 , Issue.5-6 , pp. 261-266
    • Orry, A.J.1    Abagyan, R.A.2    Cavasotto, C.N.3
  • 64
    • 77950839899 scopus 로고    scopus 로고
    • Designing focused chemical libraries enriched in protein-protein interaction inhibitors using machine-learning methods
    • Reynes C, Host H, Camproux AC, et al. Designing focused chemical libraries enriched in protein-protein interaction inhibitors using machine-learning methods. PLoS Comput Biol 2010; 6(3): e1000695.
    • (2010) PLoS Comput Biol , vol.6 , Issue.3
    • Reynes, C.1    Host, H.2    Camproux, A.C.3
  • 65
    • 77649233664 scopus 로고    scopus 로고
    • Rationalizing the chemical space of protein-protein interaction inhibitors
    • Sperandio O, Reynes CH, Camproux AC, Villoutreix BO. Rationalizing the chemical space of protein-protein interaction inhibitors. Drug Discov Today 2010; 15(5/6): 220-229.
    • (2010) Drug Discov Today , vol.15 , Issue.5-6 , pp. 220-229
    • Sperandio, O.1    Reynes, C.H.2    Camproux, A.C.3    Villoutreix, B.O.4
  • 66
    • 27144530248 scopus 로고    scopus 로고
    • Towards a proteome-scale map of the human protein-protein interaction network
    • Rual JF, Venkatesan K, Hao T, et al. Towards a proteome-scale map of the human protein-protein interaction network. Nature 2005; 437(7062): 1173-1178.
    • (2005) Nature , vol.437 , Issue.7062 , pp. 1173-1178
    • Rual, J.F.1    Venkatesan, K.2    Hao, T.3
  • 67
    • 25144498379 scopus 로고    scopus 로고
    • A human protein-protein interaction network: A resource for annotating the proteome
    • Stelzl U, Worm U, Lalowski M, et al. A human protein-protein interaction network: a resource for annotating the proteome. Cell 2005; 122(6): 957-968.
    • (2005) Cell , vol.122 , Issue.6 , pp. 957-968
    • Stelzl, U.1    Worm, U.2    Lalowski, M.3
  • 68
    • 33947219266 scopus 로고    scopus 로고
    • Large-scale mapping of human protein-protein interactions by mass spectrometry
    • Ewing RM, Chu P, Elisma F, et al. Large-scale mapping of human protein-protein interactions by mass spectrometry. Mol Syst Biol 2007; 3: 89.
    • (2007) Mol Syst Biol , vol.3 , pp. 89
    • Ewing, R.M.1    Chu, P.2    Elisma, F.3
  • 69
    • 0037245913 scopus 로고    scopus 로고
    • BIND: The Biomolecular Interaction Network Database
    • Bader GD, Betel D, Hogue CW. BIND: the Biomolecular Interaction Network Database. Nucleic Acids Res 2003; 31(1): 248-250.
    • (2003) Nucleic Acids Res , vol.31 , Issue.1 , pp. 248-250
    • Bader, G.D.1    Betel, D.2    Hogue, C.W.3
  • 71
    • 33846047770 scopus 로고    scopus 로고
    • IntAct--open source resource for molecular interaction data
    • Database issue
    • Kerrien S, Alam-Faruque Y, Aranda B, et al. IntAct--open source resource for molecular interaction data. Nucleic Acids Res 2007; 35(Database issue): D561-D565.
    • (2007) Nucleic Acids Res , vol.35
    • Kerrien, S.1    Alam-Faruque, Y.2    Aranda, B.3
  • 72
    • 33644877439 scopus 로고    scopus 로고
    • Human protein reference database--2006 update
    • Database issue
    • Mishra GR, Suresh M, Kumaran K, et al. Human protein reference database--2006 update. Nucleic Acids Res 2006; 34(Database issue): D411-D414.
    • (2006) Nucleic Acids Res , vol.34
    • Mishra, G.R.1    Suresh, M.2    Kumaran, K.3
  • 73
    • 20144387067 scopus 로고    scopus 로고
    • The MIPS mammalian protein-protein interaction database
    • Pagel P, Kovac S, Oesterheld M, et al. The MIPS mammalian protein-protein interaction database. Bioinformatics 2005; 21(6): 832-834.
    • (2005) Bioinformatics , vol.21 , Issue.6 , pp. 832-834
    • Pagel, P.1    Kovac, S.2    Oesterheld, M.3
  • 74
    • 33847064282 scopus 로고    scopus 로고
    • Comprehensive curation and analysis of global interaction networks in Saccharomyces cerevisiae
    • Reguly T, Breitkreutz A, Boucher L, et al. Comprehensive curation and analysis of global interaction networks in Saccharomyces cerevisiae. J Biol 2006; 5(4): 11.
    • (2006) J Biol , vol.5 , Issue.4 , pp. 11
    • Reguly, T.1    Breitkreutz, A.2    Boucher, L.3
  • 76
    • 58949087283 scopus 로고    scopus 로고
    • The interactome: Predicting the protein-protein interactions in cells
    • Plewczynski D, Ginalski K. The interactome: predicting the protein-protein interactions in cells. Cell Mol Biol Lett 2009; 14(1): 1-22.
    • (2009) Cell Mol Biol Lett , vol.14 , Issue.1 , pp. 1-22
    • Plewczynski, D.1    Ginalski, K.2
  • 78
    • 33645832196 scopus 로고    scopus 로고
    • PIANA: Protein interactions and network analysis
    • Aragues R, Jaeggi D, Oliva B. PIANA: protein interactions and network analysis. Bioinformatics 2006; 22(8): 1015-1017.
    • (2006) Bioinformatics , vol.22 , Issue.8 , pp. 1015-1017
    • Aragues, R.1    Jaeggi, D.2    Oliva, B.3
  • 79
    • 75249086155 scopus 로고    scopus 로고
    • NAViGaTOR: Network Analysis, Visualization and Graphing Toronto
    • Brown KR, Otasek D, Ali M, et al. NAViGaTOR: Network Analysis, Visualization and Graphing Toronto. Bioinformatics 2009; 25(24): 3327-3329.
    • (2009) Bioinformatics , vol.25 , Issue.24 , pp. 3327-3329
    • Brown, K.R.1    Otasek, D.2    Ali, M.3
  • 80
    • 67849122322 scopus 로고    scopus 로고
    • VisANT 3.5: Multi-scale network visualization, analysis and inference based on the gene ontology
    • Web Server issue
    • Hu Z, Hung JH, Wang Y, et al. VisANT 3.5: multi-scale network visualization, analysis and inference based on the gene ontology. Nucleic Acids Res 2009; 37(Web Server issue): W115-W121.
    • (2009) Nucleic Acids Res , vol.37
    • Hu, Z.1    Hung, J.H.2    Wang, Y.3
  • 81
    • 79952202448 scopus 로고    scopus 로고
    • Cytoscape: Software for visualization and analysis of biological networks
    • Kohl M, Wiese S, Warscheid B. Cytoscape: software for visualization and analysis of biological networks. Methods Mol Biol 2011; 696: 291-303.
    • (2011) Methods Mol Biol , vol.696 , pp. 291-303
    • Kohl, M.1    Wiese, S.2    Warscheid, B.3
  • 84
    • 84866383585 scopus 로고    scopus 로고
    • PINAT1.0: Protein interaction network analysis tool
    • Kushwaha SK, Shakya M. PINAT1.0: protein interaction network analysis tool. Bioinformation 2009; 3(10): 419-421.
    • (2009) Bioinformation , vol.3 , Issue.10 , pp. 419-421
    • Kushwaha, S.K.1    Shakya, M.2
  • 85
    • 75549087047 scopus 로고    scopus 로고
    • The IntAct molecular interaction database in 2010
    • Database issue
    • Aranda B, Achuthan P, Alam-Faruque Y, et al. The IntAct molecular interaction database in 2010. Nucleic Acids Res 2010; 38(Database issue): D525-D531.
    • (2010) Nucleic Acids Res , vol.38
    • Aranda, B.1    Achuthan, P.2    Alam-Faruque, Y.3
  • 88
    • 75549085083 scopus 로고    scopus 로고
    • Human Protein Reference Database and Human Proteinpedia as discovery tools for systems biology
    • Prasad TS, Kandasamy K, Pandey A. Human Protein Reference Database and Human Proteinpedia as discovery tools for systems biology. Methods Mol Biol 2009; 577: 67-79.
    • (2009) Methods Mol Biol , vol.577 , pp. 67-79
    • Prasad, T.S.1    Kandasamy, K.2    Pandey, A.3
  • 89
    • 65549102777 scopus 로고    scopus 로고
    • Protein-protein interaction databases: Keeping up with growing interactomes
    • Lehne B, Schlitt T. Protein-protein interaction databases: keeping up with growing interactomes. Hum Genomics 2009; 3(3): 291-297.
    • (2009) Hum Genomics , vol.3 , Issue.3 , pp. 291-297
    • Lehne, B.1    Schlitt, T.2
  • 90
    • 33746631391 scopus 로고    scopus 로고
    • Evolutionary and physiological importance of hub proteins
    • Batada NN, Hurst LD, Tyers M. Evolutionary and physiological importance of hub proteins. PLoS Comput Biol 2006; 2(7): e88.
    • (2006) PLoS Comput Biol , vol.2 , Issue.7
    • Batada, N.N.1    Hurst, L.D.2    Tyers, M.3
  • 91
    • 33644617753 scopus 로고    scopus 로고
    • Analysis of the human protein interactome and comparison with yeast, worm and fly interaction datasets
    • Gandhi TK, Zhong J, Mathivanan S, et al. Analysis of the human protein interactome and comparison with yeast, worm and fly interaction datasets. Nat Genet 2006; 38(3): 285-293.
    • (2006) Nat Genet , vol.38 , Issue.3 , pp. 285-293
    • Gandhi, T.K.1    Zhong, J.2    Mathivanan, S.3
  • 92
    • 0037161731 scopus 로고    scopus 로고
    • Comparative assessment of large-scale data sets of protein-protein interactions
    • von Mering C, Krause R, Snel B, et al. Comparative assessment of large-scale data sets of protein-protein interactions. Nature 2002; 417(6887): 399-403.
    • (2002) Nature , vol.417 , Issue.6887 , pp. 399-403
    • von Mering, C.1    Krause, R.2    Snel, B.3
  • 93
    • 58149242456 scopus 로고    scopus 로고
    • An experimentally derived confidence score for binary protein-protein interactions
    • Braun P, Tasan M, Dreze M, et al. An experimentally derived confidence score for binary protein-protein interactions. Nat Methods 2009; 6(1): 91-97.
    • (2009) Nat Methods , vol.6 , Issue.1 , pp. 91-97
    • Braun, P.1    Tasan, M.2    Dreze, M.3
  • 94
    • 58149213932 scopus 로고    scopus 로고
    • Literature-curated protein interaction datasets
    • Cusick ME, Yu H, Smolyar A, et al. Literature-curated protein interaction datasets. Nat Methods 2009; 6(1): 39-46.
    • (2009) Nat Methods , vol.6 , Issue.1 , pp. 39-46
    • Cusick, M.E.1    Yu, H.2    Smolyar, A.3
  • 95
    • 58149218155 scopus 로고    scopus 로고
    • Empirically controlled mapping of the Caenorhabditis elegans protein-protein interactome network
    • Simonis N, Rual JF, Carvunis AR, et al. Empirically controlled mapping of the Caenorhabditis elegans protein-protein interactome network. Nat Methods 2009; 6(1): 47-54.
    • (2009) Nat Methods , vol.6 , Issue.1 , pp. 47-54
    • Simonis, N.1    Rual, J.F.2    Carvunis, A.R.3
  • 96
    • 79952676403 scopus 로고    scopus 로고
    • Literature curation of protein interactions: Measuring agreement across major public databases
    • Turinsky AL, Razick S, Turner B, Donaldson IM, Wodak SJ. Literature curation of protein interactions: measuring agreement across major public databases. Database (Oxford) 2010; 2010: baq026.
    • (2010) Database (Oxford) , vol.2010
    • Turinsky, A.L.1    Razick, S.2    Turner, B.3    Donaldson, I.M.4    Wodak, S.J.5
  • 97
    • 34249107988 scopus 로고    scopus 로고
    • The minimum information required for reporting a molecular interaction experiment (MIMIx)
    • Orchard S, Salwinski L, Kerrien S, et al. The minimum information required for reporting a molecular interaction experiment (MIMIx). Nat Biotechnol 2007; 25(8): 894-898.
    • (2007) Nat Biotechnol , vol.25 , Issue.8 , pp. 894-898
    • Orchard, S.1    Salwinski, L.2    Kerrien, S.3
  • 98
    • 53349117774 scopus 로고    scopus 로고
    • High-quality binary protein interaction map of the yeast interactome network
    • Yu H, Braun P, Yildirim MA, et al. High-quality binary protein interaction map of the yeast interactome network. Science 2008; 322(5898): 104-110.
    • (2008) Science , vol.322 , Issue.5898 , pp. 104-110
    • Yu, H.1    Braun, P.2    Yildirim, M.A.3
  • 99
    • 76149105168 scopus 로고    scopus 로고
    • A P4-ATPase protein interaction network reveals a link between aminophospholipid transport and phosphoinositide metabolism
    • Puts CF, Lenoir G, Krijgsveld J, Williamson P, Holthuis JC. A P4-ATPase protein interaction network reveals a link between aminophospholipid transport and phosphoinositide metabolism. J Proteome Res 2010; 9(2): 833-842.
    • (2010) J Proteome Res , vol.9 , Issue.2 , pp. 833-842
    • Puts, C.F.1    Lenoir, G.2    Krijgsveld, J.3    Williamson, P.4    Holthuis, J.C.5
  • 100
    • 63049119068 scopus 로고    scopus 로고
    • Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry
    • Zhang H, Tang X, Munske GR, Tolic N, Anderson GA, Bruce JE. Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry. Mol Cell Proteomics 2009; 8(3): 409-420.
    • (2009) Mol Cell Proteomics , vol.8 , Issue.3 , pp. 409-420
    • Zhang, H.1    Tang, X.2    Munske, G.R.3    Tolic, N.4    Anderson, G.A.5    Bruce, J.E.6
  • 101
    • 77955381399 scopus 로고    scopus 로고
    • Probing native protein structures by chemical cross-linking, mass spectrometry, and bioinformatics
    • Leitner A, Walzthoeni T, Kahraman A, et al. Probing native protein structures by chemical cross-linking, mass spectrometry, and bioinformatics. Mol Cell Proteomics 2010; 9(8): 1634-1649.
    • (2010) Mol Cell Proteomics , vol.9 , Issue.8 , pp. 1634-1649
    • Leitner, A.1    Walzthoeni, T.2    Kahraman, A.3
  • 102
    • 41449110185 scopus 로고    scopus 로고
    • Identification of crosslinked peptides from large sequence databases
    • Rinner O, Seebacher J, Walzthoeni T, et al. Identification of crosslinked peptides from large sequence databases. Nat Methods 2008; 5(4): 315-318.
    • (2008) Nat Methods , vol.5 , Issue.4 , pp. 315-318
    • Rinner, O.1    Seebacher, J.2    Walzthoeni, T.3
  • 103
    • 40349092949 scopus 로고    scopus 로고
    • Probabilistic assembly of human protein interaction networks from label-free quantitative proteomics
    • Sardiu ME, Cai Y, Jin J, et al. Probabilistic assembly of human protein interaction networks from label-free quantitative proteomics. Proc Natl Acad Sci USA 2008; 105(5): 1454-1459.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.5 , pp. 1454-1459
    • Sardiu, M.E.1    Cai, Y.2    Jin, J.3
  • 104
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa ME, Bennett EJ, Gygi SP, Harper JW. Defining the human deubiquitinating enzyme interaction landscape. Cell 2009; 138(2): 389-403.
    • (2009) Cell , vol.138 , Issue.2 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 105
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends C, Sowa ME, Gygi SP, Harper JW. Network organization of the human autophagy system. Nature 2010; 466(7302): 68-76.
    • (2010) Nature , vol.466 , Issue.7302 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 106
    • 77951819088 scopus 로고    scopus 로고
    • Systematic analysis of human protein complexes identifies chromosome segregation proteins
    • 2010 Apr 30
    • Hutchins JR, Toyoda Y, Hegemann B, et al. Systematic analysis of human protein complexes identifies chromosome segregation proteins. Science 2010 Apr 30; 328(5978): 593-599.
    • Science , vol.328 , Issue.5978 , pp. 593-599
    • Hutchins, J.R.1    Toyoda, Y.2    Hegemann, B.3
  • 108
    • 79551523294 scopus 로고    scopus 로고
    • Interactive proteomics research technologies: Recent applications and advances
    • Petschnigg J, Snider J, Stagljar I. Interactive proteomics research technologies: recent applications and advances. Curr Opin Biotechnol 2011; 22(1): 50-58.
    • (2011) Curr Opin Biotechnol , vol.22 , Issue.1 , pp. 50-58
    • Petschnigg, J.1    Snider, J.2    Stagljar, I.3
  • 109
    • 77953124108 scopus 로고    scopus 로고
    • Strategies towards high-quality binary protein interactome maps
    • Lemmens I, Lievens S, Tavernier J. Strategies towards high-quality binary protein interactome maps. J Proteomics 2010; 73(8): 1415-1420.
    • (2010) J Proteomics , vol.73 , Issue.8 , pp. 1415-1420
    • Lemmens, I.1    Lievens, S.2    Tavernier, J.3
  • 110
    • 79957874673 scopus 로고    scopus 로고
    • Next-generation sequencing to generate interactome datasets
    • Yu H, Tardivo L, Tam S, et al. Next-generation sequencing to generate interactome datasets. Nat Methods 2011; 8(6): 478-480.
    • (2011) Nat Methods , vol.8 , Issue.6 , pp. 478-480
    • Yu, H.1    Tardivo, L.2    Tam, S.3
  • 111
    • 33747035889 scopus 로고    scopus 로고
    • Predicting disease genes using protein-protein interactions
    • Oti M, Snel B, Huynen MA, Brunner HG. Predicting disease genes using protein-protein interactions. J Med Genet 2006; 43(8): 691-698.
    • (2006) J Med Genet , vol.43 , Issue.8 , pp. 691-698
    • Oti, M.1    Snel, B.2    Huynen, M.A.3    Brunner, H.G.4
  • 112
    • 43249125341 scopus 로고    scopus 로고
    • Using protein complexes to predict phenotypic effects of gene mutation
    • Fraser HB, Plotkin JB. Using protein complexes to predict phenotypic effects of gene mutation. Genome Biol 2007; 8(11): R252.
    • (2007) Genome Biol , vol.8 , Issue.11
    • Fraser, H.B.1    Plotkin, J.B.2
  • 113
    • 41549139527 scopus 로고    scopus 로고
    • Walking the interactome for prioritization of candidate disease genes
    • Kohler S, Bauer S, Horn D, Robinson PN. Walking the interactome for prioritization of candidate disease genes. Am J Hum Genet 2008; 82(4): 949-958.
    • (2008) Am J Hum Genet , vol.82 , Issue.4 , pp. 949-958
    • Kohler, S.1    Bauer, S.2    Horn, D.3    Robinson, P.N.4
  • 114
    • 33947095027 scopus 로고    scopus 로고
    • A human phenomeinteractome network of protein complexes implicated in genetic disorders
    • Lage K, Karlberg EO, Storling ZM, et al. A human phenomeinteractome network of protein complexes implicated in genetic disorders. Nat Biotechnol 2007; 25(3): 309-316.
    • (2007) Nat Biotechnol , vol.25 , Issue.3 , pp. 309-316
    • Lage, K.1    Karlberg, E.O.2    Storling, Z.M.3
  • 115
    • 43249114206 scopus 로고    scopus 로고
    • Network-based global inference of human disease genes
    • Wu X, Jiang R, Zhang MQ, Li S. Network-based global inference of human disease genes. Mol Syst Biol 2008; 4: 189.
    • (2008) Mol Syst Biol , vol.4 , pp. 189
    • Wu, X.1    Jiang, R.2    Zhang, M.Q.3    Li, S.4
  • 116
    • 59649125020 scopus 로고    scopus 로고
    • A network-based method for predicting disease-causing genes
    • Karni S, Soreq H, Sharan R. A network-based method for predicting disease-causing genes. J Comput Biol 2009; 16(2): 181-189.
    • (2009) J Comput Biol , vol.16 , Issue.2 , pp. 181-189
    • Karni, S.1    Soreq, H.2    Sharan, R.3
  • 118
    • 34347326247 scopus 로고    scopus 로고
    • Network-based analysis of affected biological processes in type 2 diabetes models
    • Liu M, Liberzon A, Kong SW, et al. Network-based analysis of affected biological processes in type 2 diabetes models. PLoS Genet 2007; 3(6): e96.
    • (2007) PLoS Genet , vol.3 , Issue.6
    • Liu, M.1    Liberzon, A.2    Kong, S.W.3
  • 119
    • 77957745068 scopus 로고    scopus 로고
    • Gene regulatory network reveals oxidative stress as the underlying molecular mechanism of type 2 diabetes and hypertension
    • Jesmin J, Rashid MS, Jamil H, Hontecillas R, Bassaganya-Riera J. Gene regulatory network reveals oxidative stress as the underlying molecular mechanism of type 2 diabetes and hypertension. BMC Med Genomics 2010; 3(1): 45.
    • (2010) BMC Med Genomics , vol.3 , Issue.1 , pp. 45
    • Jesmin, J.1    Rashid, M.S.2    Jamil, H.3    Hontecillas, R.4    Bassaganya-Riera, J.5
  • 120
    • 61549115034 scopus 로고    scopus 로고
    • Diverse genome-wide association studies associate the IL12/IL23 pathway with Crohn Disease
    • Wang K, Zhang H, Kugathasan S, et al. Diverse genome-wide association studies associate the IL12/IL23 pathway with Crohn Disease. Am J Hum Genet 2009; 84(3): 399-405.
    • (2009) Am J Hum Genet , vol.84 , Issue.3 , pp. 399-405
    • Wang, K.1    Zhang, H.2    Kugathasan, S.3
  • 122
    • 35349024501 scopus 로고    scopus 로고
    • Network modeling links breast cancer susceptibility and centrosome dysfunction
    • Pujana MA, Han JD, Starita LM, et al. Network modeling links breast cancer susceptibility and centrosome dysfunction. Nat Genet 2007; 39(11): 1338-1349.
    • (2007) Nat Genet , vol.39 , Issue.11 , pp. 1338-1349
    • Pujana, M.A.1    Han, J.D.2    Starita, L.M.3
  • 123
  • 124
    • 39149143293 scopus 로고    scopus 로고
    • A systems biology approach to prediction of oncogenes and molecular perturbation targets in Bcell lymphomas
    • Mani KM, Lefebvre C, Wang K, et al. A systems biology approach to prediction of oncogenes and molecular perturbation targets in Bcell lymphomas. Mol Syst Biol 2008; 4: 169.
    • (2008) Mol Syst Biol , vol.4 , pp. 169
    • Mani, K.M.1    Lefebvre, C.2    Wang, K.3
  • 126
    • 77957694184 scopus 로고    scopus 로고
    • Identification of diagnostic subnetwork markers for cancer in human protein-protein interaction network
    • Su J, Yoon BJ, Dougherty ER. Identification of diagnostic subnetwork markers for cancer in human protein-protein interaction network. BMC Bioinformatics 2010; 11 Suppl 6: S8.
    • (2010) BMC Bioinformatics , vol.11 , Issue.SUPPL. 6
    • Su, J.1    Yoon, B.J.2    Dougherty, E.R.3
  • 127
    • 84873051678 scopus 로고    scopus 로고
    • Identification of coordinately dysregulated subnetworks in complex phenotypes
    • Chowdhury SA, Koyuturk M. Identification of coordinately dysregulated subnetworks in complex phenotypes. Pac Symp Biocomput 2010: 133-144.
    • (2010) Pac Symp Biocomput , pp. 133-144
    • Chowdhury, S.A.1    Koyuturk, M.2
  • 128
    • 66149156998 scopus 로고    scopus 로고
    • Discovery and scoring of protein interaction subnetworks discriminative of late stage human colon cancer
    • Nibbe RK, Markowitz S, Myeroff L, Ewing R, Chance MR. Discovery and scoring of protein interaction subnetworks discriminative of late stage human colon cancer. Mol Cell Proteomics 2009; 8(4): 827-845.
    • (2009) Mol Cell Proteomics , vol.8 , Issue.4 , pp. 827-845
    • Nibbe, R.K.1    Markowitz, S.2    Myeroff, L.3    Ewing, R.4    Chance, M.R.5
  • 129
    • 70349722912 scopus 로고    scopus 로고
    • Identification of novel hub genes associated with liver metastasis of gastric cancer
    • 2009 Dec 15
    • Chang W, Ma L, Lin L, et al. Identification of novel hub genes associated with liver metastasis of gastric cancer. Int J Cancer 2009 Dec 15; 125(12): 2844-2853.
    • Int J Cancer , vol.125 , Issue.12 , pp. 2844-2853
    • Chang, W.1    Ma, L.2    Lin, L.3
  • 130
    • 59849125136 scopus 로고    scopus 로고
    • Dynamic modularity in protein interaction networks predicts breast cancer outcome
    • 2009 Feb
    • Taylor IW, Linding R, Warde-Farley D, et al. Dynamic modularity in protein interaction networks predicts breast cancer outcome. Nat Biotechnol 2009 Feb; 27(2): 199-204.
    • Nat Biotechnol , vol.27 , Issue.2 , pp. 199-204
    • Taylor, I.W.1    Linding, R.2    Warde-Farley, D.3
  • 131
    • 79959392210 scopus 로고    scopus 로고
    • Optimally discriminative subnetwork markers predict response to chemotherapy
    • Dao P, Wang K, Collins C, Ester M, Lapuk A, Sahinalp SC. Optimally discriminative subnetwork markers predict response to chemotherapy. Bioinformatics 2011; 27(13): i205-i213.
    • (2011) Bioinformatics , vol.27 , Issue.13
    • Dao, P.1    Wang, K.2    Collins, C.3    Ester, M.4    Lapuk, A.5    Sahinalp, S.C.6
  • 132
    • 78651479105 scopus 로고    scopus 로고
    • Untangling the intracellular signalling network in cancer--a strategy for data integration in acute myeloid leukaemia
    • Jorgensen KM, Hjelle SM, Oye OK, et al. Untangling the intracellular signalling network in cancer--a strategy for data integration in acute myeloid leukaemia. J Proteomics 2011; 74(3): 269-281.
    • (2011) J Proteomics , vol.74 , Issue.3 , pp. 269-281
    • Jorgensen, K.M.1    Hjelle, S.M.2    Oye, O.K.3
  • 133
    • 79957561774 scopus 로고    scopus 로고
    • Quantitative proteomic and interaction network analysis of cisplatin resistance in HeLa cells
    • Chavez JD, Hoopmann MR, Weisbrod CR, Takara K, Bruce JE. Quantitative proteomic and interaction network analysis of cisplatin resistance in HeLa cells. PLoS One 2011; 6(5): e19892.
    • (2011) PLoS One , vol.6 , Issue.5
    • Chavez, J.D.1    Hoopmann, M.R.2    Weisbrod, C.R.3    Takara, K.4    Bruce, J.E.5
  • 134
    • 84455174502 scopus 로고    scopus 로고
    • Identification of genes involved in radioresistance of nasopharyngeal carcinoma by integrating gene ontology and protein-protein interaction networks
    • 2011 Aug 19
    • Guo Y, Zhu XD, Qu S, et al. Identification of genes involved in radioresistance of nasopharyngeal carcinoma by integrating gene ontology and protein-protein interaction networks. Int J Oncol 2011 Aug 19.
    • Int J Oncol
    • Guo, Y.1    Zhu, X.D.2    Qu, S.3
  • 135
    • 77957757417 scopus 로고    scopus 로고
    • A Myc network accounts for similarities between embryonic stem and cancer cell transcription programs
    • Kim J, Woo AJ, Chu J, et al. A Myc network accounts for similarities between embryonic stem and cancer cell transcription programs. Cell 2010; 143(2): 313-324.
    • (2010) Cell , vol.143 , Issue.2 , pp. 313-324
    • Kim, J.1    Woo, A.J.2    Chu, J.3
  • 136
    • 33646687963 scopus 로고    scopus 로고
    • A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration
    • Lim J, Hao T, Shaw C, et al. A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. Cell 2006; 125(4): 801-814.
    • (2006) Cell , vol.125 , Issue.4 , pp. 801-814
    • Lim, J.1    Hao, T.2    Shaw, C.3
  • 137
    • 4644231870 scopus 로고    scopus 로고
    • A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease
    • Goehler H, Lalowski M, Stelzl U, et al. A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease. Mol Cell 2004; 15(6): 853-865.
    • (2004) Mol Cell , vol.15 , Issue.6 , pp. 853-865
    • Goehler, H.1    Lalowski, M.2    Stelzl, U.3
  • 139
    • 1242338856 scopus 로고    scopus 로고
    • Huntingtin-protein interactions and the pathogenesis of Huntington's disease
    • Li SH, Li XJ. Huntingtin-protein interactions and the pathogenesis of Huntington's disease. Trends Genet 2004; 20(3): 146-154.
    • (2004) Trends Genet , vol.20 , Issue.3 , pp. 146-154
    • Li, S.H.1    Li, X.J.2
  • 140
    • 33845748185 scopus 로고    scopus 로고
    • Disrupted in Schizophrenia 1 Interactome: Evidence for the close connectivity of risk genes and a potential synaptic basis for schizophrenia
    • Camargo LM, Collura V, Rain JC, et al. Disrupted in Schizophrenia 1 Interactome: evidence for the close connectivity of risk genes and a potential synaptic basis for schizophrenia. Mol Psychiatry 2007; 12(1): 74-86.
    • (2007) Mol Psychiatry , vol.12 , Issue.1 , pp. 74-86
    • Camargo, L.M.1    Collura, V.2    Rain, J.C.3
  • 141
    • 37549004790 scopus 로고    scopus 로고
    • Suppression of neurodegeneration and increased neurotransmission caused by expanded full-length huntingtin accumulating in the cytoplasm
    • Romero E, Cha GH, Verstreken P, et al. Suppression of neurodegeneration and increased neurotransmission caused by expanded full-length huntingtin accumulating in the cytoplasm. Neuron 2008; 57(1): 27-40.
    • (2008) Neuron , vol.57 , Issue.1 , pp. 27-40
    • Romero, E.1    Cha, G.H.2    Verstreken, P.3
  • 142
    • 34250675300 scopus 로고    scopus 로고
    • Epstein-Barr virus and virus human protein interaction maps
    • Calderwood MA, Venkatesan K, Xing L, et al. Epstein-Barr virus and virus human protein interaction maps. Proc Natl Acad Sci USA 2007; 104(18): 7606-7611.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.18 , pp. 7606-7611
    • Calderwood, M.A.1    Venkatesan, K.2    Xing, L.3
  • 144
    • 68049131345 scopus 로고    scopus 로고
    • Connecting viral with cellular interactomes
    • Bailer SM, Haas J. Connecting viral with cellular interactomes. Curr Opin Microbiol 2009; 12(4): 453-459.
    • (2009) Curr Opin Microbiol , vol.12 , Issue.4 , pp. 453-459
    • Bailer, S.M.1    Haas, J.2
  • 145
    • 30844443758 scopus 로고    scopus 로고
    • Herpesviral protein networks and their interaction with the human proteome
    • Uetz P, Dong YA, Zeretzke C, et al. Herpesviral protein networks and their interaction with the human proteome. Science 2006; 311(5758): 239-242.
    • (2006) Science , vol.311 , Issue.5758 , pp. 239-242
    • Uetz, P.1    Dong, Y.A.2    Zeretzke, C.3
  • 146
    • 70349931825 scopus 로고    scopus 로고
    • Analysis of vaccinia virus-host protein-protein interactions: Validations of yeast two-hybrid screenings
    • Zhang L, Villa NY, Rahman MM, Smallwood S, Shattuck D, Neff C, et al. Analysis of vaccinia virus-host protein-protein interactions: validations of yeast two-hybrid screenings. J Proteome Res 2009; 8(9): 4311-4318.
    • (2009) J Proteome Res , vol.8 , Issue.9 , pp. 4311-4318
    • Zhang, L.1    Villa, N.Y.2    Rahman, M.M.3    Smallwood, S.4    Shattuck, D.5    Neff, C.6
  • 147
    • 72249103485 scopus 로고    scopus 로고
    • A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection
    • Shapira SD, Gat-Viks I, Shum BO, et al. A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection. Cell 2009; 139(7): 1255-1267.
    • (2009) Cell , vol.139 , Issue.7 , pp. 1255-1267
    • Shapira, S.D.1    Gat-Viks, I.2    Shum, B.O.3
  • 148
    • 83055173247 scopus 로고    scopus 로고
    • A physical interaction network of dengue virus and human proteins
    • 2011 Sep 12
    • Khadka S, Vangeloff AD, Zhang C, et al. A physical interaction network of dengue virus and human proteins. Mol Cell Proteomics 2011 Sep 12.
    • Mol Cell Proteomics
    • Khadka, S.1    Vangeloff, A.D.2    Zhang, C.3
  • 150
    • 78651501511 scopus 로고    scopus 로고
    • Purification and characterization of HIV-human protein complexes
    • Jager S, Gulbahce N, Cimermancic P, et al. Purification and characterization of HIV-human protein complexes. Methods 2011; 53(1): 13-19.
    • (2011) Methods , vol.53 , Issue.1 , pp. 13-19
    • Jager, S.1    Gulbahce, N.2    Cimermancic, P.3
  • 151
    • 83055163850 scopus 로고    scopus 로고
    • Proteomic analysis of virus-host interactions in an infectious context using recombinant viruses
    • 2011 Sep 12
    • Komarova AV, Combredet C, Meyniel-Schicklin L, et al. Proteomic analysis of virus-host interactions in an infectious context using recombinant viruses. Mol Cell Proteomics 2011 Sep 12.
    • Mol Cell Proteomics
    • Komarova, A.V.1    Combredet, C.2    Meyniel-Schicklin, L.3
  • 152
    • 40349106161 scopus 로고    scopus 로고
    • The landscape of human proteins interacting with viruses and other pathogens
    • Dyer MD, Murali TM, Sobral BW. The landscape of human proteins interacting with viruses and other pathogens. PLoS Pathog 2008; 4(2): e32.
    • (2008) PLoS Pathog , vol.4 , Issue.2
    • Dyer, M.D.1    Murali, T.M.2    Sobral, B.W.3
  • 153
    • 78651526843 scopus 로고    scopus 로고
    • When the human viral infectome and diseasome networks collide: Towards a systems biology platform for the aetiology of human diseases
    • Navratil V, de Chassey B, Combe CR, Lotteau V. When the human viral infectome and diseasome networks collide: towards a systems biology platform for the aetiology of human diseases. BMC Syst Biol 2011; 5: 13.
    • (2011) BMC Syst Biol , vol.5 , pp. 13
    • Navratil, V.1    de Chassey, B.2    Combe, C.R.3    Lotteau, V.4
  • 154
    • 65449115788 scopus 로고    scopus 로고
    • Targeting of immune signaling networks by bacterial pathogens
    • Brodsky IE, Medzhitov R. Targeting of immune signaling networks by bacterial pathogens. Nat Cell Biol 2009; 11(5): 521-526.
    • (2009) Nat Cell Biol , vol.11 , Issue.5 , pp. 521-526
    • Brodsky, I.E.1    Medzhitov, R.2
  • 155
    • 77957817012 scopus 로고    scopus 로고
    • The human-bacterial pathogen protein interaction networks of Bacillus anthracis, Francisella tularensis, and Yersinia pestis
    • Dyer MD, Neff C, Dufford M, et al. The human-bacterial pathogen protein interaction networks of Bacillus anthracis, Francisella tularensis, and Yersinia pestis. PLoS One 2010; 5(8): e12089.
    • (2010) PLoS One , vol.5 , Issue.8
    • Dyer, M.D.1    Neff, C.2    Dufford, M.3
  • 156
    • 80855129283 scopus 로고    scopus 로고
    • Insight into bacterial virulence mechanisms against host immune response via Y. pestis-human protein-protein interaction network
    • 2011 Sep 12
    • Yang H, Ke Y, Wang J, et al. Insight into bacterial virulence mechanisms against host immune response via Y. pestis-human protein-protein interaction network. Infect Immun 2011 Sep 12.
    • Infect Immun
    • Yang, H.1    Ke, Y.2    Wang, J.3
  • 157
    • 67650860423 scopus 로고    scopus 로고
    • The glyceraldehyde- 3-phosphate dehydrogenase and the small GTPase Rab 2 are crucial for Brucella replication
    • Fugier E, Salcedo SP, de Chastellier C, et al. The glyceraldehyde- 3-phosphate dehydrogenase and the small GTPase Rab 2 are crucial for Brucella replication. PLoS Pathog 2009; 5(6): e1000487.
    • (2009) PLoS Pathog , vol.5 , Issue.6
    • Fugier, E.1    Salcedo, S.P.2    de Chastellier, C.3
  • 158
    • 79959282083 scopus 로고    scopus 로고
    • Identification of a Brucella spp. secreted effector specifically interacting with human small GTPase Rab2
    • de Barsy M, Jamet A, Filopon D, et al. Identification of a Brucella spp. secreted effector specifically interacting with human small GTPase Rab2. Cell Microbiol 2011; 13(7): 1044-1058.
    • (2011) Cell Microbiol , vol.13 , Issue.7 , pp. 1044-1058
    • de Barsy, M.1    Jamet, A.2    Filopon, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.