메뉴 건너뛰기




Volumn 33, Issue 2, 2012, Pages 109-118

Yeast two-hybrid methods and their applications in drug discovery

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ANTINEOPLASTIC AGENT; CALCIUM CHANNEL N TYPE; FK 506 BINDING PROTEIN; MAX PROTEIN; MYC PROTEIN; NAVITOCLAX; NUTLIN 3; POTASSIUM CHANNEL KV1.1; RAF PROTEIN; RAS PROTEIN; ROSCOVITINE; SHAL POTASSIUM CHANNEL; TRANSCRIPTION FACTOR NRF2; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 84856511126     PISSN: 01656147     EISSN: 18733735     Source Type: Journal    
DOI: 10.1016/j.tips.2011.10.008     Document Type: Review
Times cited : (75)

References (93)
  • 1
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • DOI 10.1038/340245a0
    • S. Fields, and O. Song A novel genetic system to detect protein-protein interactions Nature 340 1989 245 246 (Pubitemid 19171591)
    • (1989) Nature , vol.340 , Issue.6230 , pp. 245-246
    • Fields, S.1    Song, O.-K.2
  • 2
    • 73249138144 scopus 로고    scopus 로고
    • Interactive learning: Lessons from two hybrids over two decades
    • S. Fields Interactive learning: lessons from two hybrids over two decades Proteomics 9 2009 5209 5213
    • (2009) Proteomics , vol.9 , pp. 5209-5213
    • Fields, S.1
  • 3
    • 43249097241 scopus 로고    scopus 로고
    • Resolving the network of cell signaling pathways using the evolving yeast two-hybrid system
    • DOI 10.2144/000112797
    • V. Ratushny, and E. Golemis Resolving the network of cell signaling pathways using the evolving yeast two-hybrid system Biotechniques 44 2008 655 662 (Pubitemid 351656285)
    • (2008) BioTechniques , vol.44 , Issue.5 , pp. 655-662
    • Ratushny, V.1    Golemis, E.A.2
  • 4
    • 49549084138 scopus 로고    scopus 로고
    • Two-hybrid technologies in proteomics research
    • B. Suter Two-hybrid technologies in proteomics research Curr. Opin. Biotechnol. 19 2008 316 323
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 316-323
    • Suter, B.1
  • 5
    • 85028113437 scopus 로고    scopus 로고
    • Translating p53 into the clinic
    • C.F. Cheok Translating p53 into the clinic Nat. Rev. Clin. Oncol. 8 2011 25 37
    • (2011) Nat. Rev. Clin. Oncol. , vol.8 , pp. 25-37
    • Cheok, C.F.1
  • 6
    • 57049136656 scopus 로고    scopus 로고
    • RAS: Target for cancer therapy
    • N. Saxena RAS: target for cancer therapy Cancer Invest. 26 2008 948 955
    • (2008) Cancer Invest. , vol.26 , pp. 948-955
    • Saxena, N.1
  • 7
    • 80051802020 scopus 로고    scopus 로고
    • Raf kinases in cancer - Roles and therapeutic opportunities
    • G. Maurer Raf kinases in cancer - roles and therapeutic opportunities Oncogene 30 2011 3477 3488
    • (2011) Oncogene , vol.30 , pp. 3477-3488
    • Maurer, G.1
  • 11
    • 27144530248 scopus 로고    scopus 로고
    • Towards a proteome-scale map of the human protein-protein interaction network
    • J.F. Rual Towards a proteome-scale map of the human protein-protein interaction network Nature 437 2005 1173 1178
    • (2005) Nature , vol.437 , pp. 1173-1178
    • Rual, J.F.1
  • 14
    • 35148862429 scopus 로고    scopus 로고
    • Analysis of intraviral protein-protein interactions of the SARS coronavirus ORFeome
    • A. von Brunn Analysis of intraviral protein-protein interactions of the SARS coronavirus ORFeome PLoS ONE 2 2007 e459
    • (2007) PLoS ONE , vol.2 , pp. 459
    • Von Brunn, A.1
  • 16
    • 77949440090 scopus 로고    scopus 로고
    • Improving the yeast two-hybrid system with permutated fusions proteins: The Varicella Zoster virus interactome
    • T. Stellberger Improving the yeast two-hybrid system with permutated fusions proteins: the Varicella Zoster virus interactome Proteome Sci. 8 2010 8
    • (2010) Proteome Sci. , vol.8 , pp. 8
    • Stellberger, T.1
  • 17
    • 38549161592 scopus 로고    scopus 로고
    • A proteome-wide protein interaction map for Campylobacter jejuni
    • J.R. Parrish A proteome-wide protein interaction map for Campylobacter jejuni Genome Biol. 8 2007 R130
    • (2007) Genome Biol. , vol.8 , pp. 130
    • Parrish, J.R.1
  • 18
    • 48249128882 scopus 로고    scopus 로고
    • The binary protein interactome of Treponema pallidum - The syphilis spirochete
    • B. Titz The binary protein interactome of Treponema pallidum - the syphilis spirochete PLoS ONE 3 2008 e2292
    • (2008) PLoS ONE , vol.3 , pp. 2292
    • Titz, B.1
  • 19
    • 70449568301 scopus 로고    scopus 로고
    • A protein-protein interaction map of the Trypanosoma brucei paraflagellar rod
    • S. Lacomble A protein-protein interaction map of the Trypanosoma brucei paraflagellar rod PLoS ONE 4 2009 e7685
    • (2009) PLoS ONE , vol.4 , pp. 7685
    • Lacomble, S.1
  • 20
    • 55549117151 scopus 로고    scopus 로고
    • Hepatitis C virus infection protein network
    • B. de Chassey Hepatitis C virus infection protein network Mol. Syst. Biol. 4 2008 230
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 230
    • De Chassey, B.1
  • 21
    • 72249103485 scopus 로고    scopus 로고
    • A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection
    • S.D. Shapira A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection Cell 139 2009 1255 1267
    • (2009) Cell , vol.139 , pp. 1255-1267
    • Shapira, S.D.1
  • 22
    • 83055173247 scopus 로고    scopus 로고
    • A physical interaction network of dengue virus and human proteins
    • 10.1074/mcp.M111.012187
    • S. Khadka A physical interaction network of dengue virus and human proteins Mol. Cell. Proteomics 2011 10.1074/mcp.M111.012187
    • (2011) Mol. Cell. Proteomics
    • Khadka, S.1
  • 23
    • 79952151929 scopus 로고    scopus 로고
    • Comparison of the mechanisms of drug resistance among HIV, Hepatitis B, and Hepatitis C
    • S. Margeridon-Thermet, and R.W. Shafer Comparison of the mechanisms of drug resistance among HIV, Hepatitis B, and Hepatitis C Viruses 2 2010 2696 2739
    • (2010) Viruses , vol.2 , pp. 2696-2739
    • Margeridon-Thermet, S.1    Shafer, R.W.2
  • 24
    • 78649712445 scopus 로고    scopus 로고
    • The continuing crisis in antibiotic resistance
    • G.L. French The continuing crisis in antibiotic resistance Int. J. Antimicrob. Agents 36 Suppl. 3 2010 S3 S7
    • (2010) Int. J. Antimicrob. Agents , vol.36 , Issue.SUPPL. 3
    • French, G.L.1
  • 25
    • 79551517793 scopus 로고    scopus 로고
    • Recent advances in charting protein-protein interaction: Mass spectrometry-based approaches
    • A.C. Gavin Recent advances in charting protein-protein interaction: mass spectrometry-based approaches Curr. Opin. Biotechnol. 22 2011 42 49
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 42-49
    • Gavin, A.C.1
  • 26
    • 79952674000 scopus 로고    scopus 로고
    • Interactome networks and human disease
    • M. Vidal Interactome networks and human disease Cell 144 2011 986 998
    • (2011) Cell , vol.144 , pp. 986-998
    • Vidal, M.1
  • 27
    • 33748706765 scopus 로고    scopus 로고
    • Global topological features of cancer proteins in the human interactome
    • DOI 10.1093/bioinformatics/btl390
    • P.F. Jonsson, and P.A. Bates Global topological features of cancer proteins in the human interactome Bioinformatics 22 2006 2291 2297 (Pubitemid 44390886)
    • (2006) Bioinformatics , vol.22 , Issue.18 , pp. 2291-2297
    • Jonsson, P.F.1    Bates, P.A.2
  • 28
    • 72849142731 scopus 로고    scopus 로고
    • Edgetic perturbation models of human inherited disorders
    • Q. Zhong Edgetic perturbation models of human inherited disorders Mol. Syst. Biol. 5 2009 321
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 321
    • Zhong, Q.1
  • 29
    • 0028971677 scopus 로고
    • P16 proteins from melanoma-prone families are deficient in binding to Cdk4
    • A. Reymond, and R. Brent p16 proteins from melanoma-prone families are deficient in binding to Cdk4 Oncogene 11 1995 1173 1178
    • (1995) Oncogene , vol.11 , pp. 1173-1178
    • Reymond, A.1    Brent, R.2
  • 30
    • 33749248536 scopus 로고    scopus 로고
    • Decompartmentalizing target validation - Thinking outside the pipeline boxes
    • DOI 10.1007/s00109-006-0080-2
    • R. Hooft van Huijsduijnen, and C. Rommel Decompartmentalizing target validation-thinking outside the pipeline boxes J. Mol. Med. (Berl.) 84 2006 802 813 (Pubitemid 44478864)
    • (2006) Journal of Molecular Medicine , vol.84 , Issue.10 , pp. 802-813
    • Hooft Van Huijsduijnen, R.1    Rommel, C.2
  • 31
    • 79953249834 scopus 로고    scopus 로고
    • High drug attrition rates - Where are we going wrong?
    • L. Hutchinson, and R. Kirk High drug attrition rates - where are we going wrong? Nat. Rev. Clin. Oncol. 8 2011 189 190
    • (2011) Nat. Rev. Clin. Oncol. , vol.8 , pp. 189-190
    • Hutchinson, L.1    Kirk, R.2
  • 32
    • 33846676987 scopus 로고    scopus 로고
    • Chemical Genetics: Where Genetics and Pharmacology Meet
    • DOI 10.1016/j.cell.2007.01.021, PII S0092867407001195
    • Z.A. Knight, and K.M. Shokat Chemical genetics: where genetics and pharmacology meet Cell 128 2007 425 430 (Pubitemid 46198904)
    • (2007) Cell , vol.128 , Issue.3 , pp. 425-430
    • Knight, Z.A.1    Shokat, K.M.2
  • 33
    • 79960503652 scopus 로고    scopus 로고
    • Chemical genetics
    • C.J. O'Connor Chemical genetics Chem. Soc. Rev. 40 2011 4332 4345
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 4332-4345
    • O'Connor, C.J.1
  • 34
    • 84862192766 scopus 로고    scopus 로고
    • ChEMBL: A large-scale bioactivity database for drug discovery
    • 10.1093/nar/gkr777
    • A. Gaulton ChEMBL: a large-scale bioactivity database for drug discovery Nucleic Acids Res. 2011 10.1093/nar/gkr777
    • (2011) Nucleic Acids Res.
    • Gaulton, A.1
  • 35
    • 41149117550 scopus 로고    scopus 로고
    • The eleven-year switch of peptide aptamers
    • P. Colas The eleven-year switch of peptide aptamers J. Biol. 7 2008 2
    • (2008) J. Biol. , vol.7 , pp. 2
    • Colas, P.1
  • 37
    • 66349096574 scopus 로고    scopus 로고
    • Targeting LMO2 with a peptide aptamer establishes a necessary function in overt T-cell neoplasia
    • A. Appert Targeting LMO2 with a peptide aptamer establishes a necessary function in overt T-cell neoplasia Cancer Res. 69 2009 4784 4790
    • (2009) Cancer Res. , vol.69 , pp. 4784-4790
    • Appert, A.1
  • 38
    • 78751478982 scopus 로고    scopus 로고
    • Peptides and aptamers targeting HSP70: A novel approach for anticancer chemotherapy
    • A.L. Rerole Peptides and aptamers targeting HSP70: a novel approach for anticancer chemotherapy Cancer Res. 71 2011 484 495
    • (2011) Cancer Res. , vol.71 , pp. 484-495
    • Rerole, A.L.1
  • 39
    • 80052049395 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 27 (HspB1) tumorigenic functions by peptide aptamers
    • B. Gibert Inhibition of heat shock protein 27 (HspB1) tumorigenic functions by peptide aptamers Oncogene 30 2011 3672 3681
    • (2011) Oncogene , vol.30 , pp. 3672-3681
    • Gibert, B.1
  • 40
    • 38349050571 scopus 로고    scopus 로고
    • A comparative analysis of perturbations caused by a gene knock-out, a dominant negative allele, and a set of peptide aptamers
    • N. Abed A comparative analysis of perturbations caused by a gene knock-out, a dominant negative allele, and a set of peptide aptamers Mol. Cell. Proteomics 6 2007 2110 2121
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2110-2121
    • Abed, N.1
  • 41
    • 51449104047 scopus 로고    scopus 로고
    • A RasGAP SH3 peptide aptamer inhibits RasGAP-Aurora interaction and induces caspase-independent tumor cell death
    • P. Pamonsinlapatham A RasGAP SH3 peptide aptamer inhibits RasGAP-Aurora interaction and induces caspase-independent tumor cell death PLoS ONE 3 2008 e2902
    • (2008) PLoS ONE , vol.3 , pp. 2902
    • Pamonsinlapatham, P.1
  • 43
    • 34147120254 scopus 로고    scopus 로고
    • An antiproliferative genetic screening identifies a peptide aptamer that targets calcineurin and up-regulates its activity
    • B. de Chassey An antiproliferative genetic screening identifies a peptide aptamer that targets calcineurin and up-regulates its activity Mol. Cell. Proteomics 6 2007 451 459
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 451-459
    • De Chassey, B.1
  • 44
    • 38449115445 scopus 로고    scopus 로고
    • Intracellular antibodies (intrabodies) and their therapeutic potential
    • A.S. Lo Intracellular antibodies (intrabodies) and their therapeutic potential Handb. Exp. Pharmacol. 2008 343 373
    • (2008) Handb. Exp. Pharmacol. , pp. 343-373
    • Lo, A.S.1
  • 45
    • 77955744034 scopus 로고    scopus 로고
    • Characterization of single chain antibody targets through yeast two hybrid
    • O. Vielemeyer Characterization of single chain antibody targets through yeast two hybrid BMC Biotechnol. 10 2010 59
    • (2010) BMC Biotechnol. , vol.10 , pp. 59
    • Vielemeyer, O.1
  • 46
    • 77952562129 scopus 로고    scopus 로고
    • Isolation of peptides blocking the function of anti-apoptotic Livin protein
    • I. Crnkovic-Mertens Isolation of peptides blocking the function of anti-apoptotic Livin protein Cell. Mol. Life Sci. 67 2010 1895 1905
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 1895-1905
    • Crnkovic-Mertens, I.1
  • 47
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • DOI 10.1038/nature06526, PII NATURE06526
    • J.A. Wells, and C.L. McClendon Reaching for high-hanging fruit in drug discovery at protein-protein interfaces Nature 450 2007 1001 1009 (Pubitemid 350273630)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 48
    • 50249154886 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions
    • T. Berg Small-molecule inhibitors of protein-protein interactions Curr. Opin. Drug Discov. Dev. 11 2008 666 674
    • (2008) Curr. Opin. Drug Discov. Dev. , vol.11 , pp. 666-674
    • Berg, T.1
  • 49
    • 78049365170 scopus 로고    scopus 로고
    • A phase IIa study of ABT-263 in patients with relapsed small-cell lung cancer (SCLC)
    • C.M. Rudin A phase IIa study of ABT-263 in patients with relapsed small-cell lung cancer (SCLC) J. Clin. Oncol. 28 2010 7046
    • (2010) J. Clin. Oncol. , vol.28 , pp. 7046
    • Rudin, C.M.1
  • 50
    • 79953655080 scopus 로고    scopus 로고
    • Recent advances in the therapeutic perspectives of Nutlin-3
    • P. Secchiero Recent advances in the therapeutic perspectives of Nutlin-3 Curr. Pharm. Des. 17 2011 569 577
    • (2011) Curr. Pharm. Des. , vol.17 , pp. 569-577
    • Secchiero, P.1
  • 51
    • 51349160681 scopus 로고    scopus 로고
    • High-throughput screening assays to discover small-molecule inhibitors of protein interactions
    • P. Colas High-throughput screening assays to discover small-molecule inhibitors of protein interactions Curr. Drug Discov. Technol. 5 2008 190 199
    • (2008) Curr. Drug Discov. Technol. , vol.5 , pp. 190-199
    • Colas, P.1
  • 53
    • 0142057146 scopus 로고    scopus 로고
    • Low molecular weight inhibitors of Myc-Max interaction and function
    • DOI 10.1038/sj.onc.1206641
    • X. Yin Low molecular weight inhibitors of Myc-Max interaction and function Oncogene 22 2003 6151 6159 (Pubitemid 37281644)
    • (2003) Oncogene , vol.22 , Issue.40 , pp. 6151-6159
    • Yin, X.1    Giap, C.2    Lazo, J.S.3    Prochownik, E.V.4
  • 54
    • 3242668951 scopus 로고    scopus 로고
    • A dual luciferase multiplexed high-throughput screening platform for protein-protein interactions
    • B.W. Nieuwenhuijsen A dual luciferase multiplexed high-throughput screening platform for protein-protein interactions J. Biomol. Screen. 8 2003 676 684
    • (2003) J. Biomol. Screen. , vol.8 , pp. 676-684
    • Nieuwenhuijsen, B.W.1
  • 55
    • 77649320940 scopus 로고    scopus 로고
    • Peptide aptamers for small molecule drug discovery
    • C. Bardou Peptide aptamers for small molecule drug discovery Methods Mol. Biol. 535 2009 373 388
    • (2009) Methods Mol. Biol. , vol.535 , pp. 373-388
    • Bardou, C.1
  • 59
    • 8444238625 scopus 로고    scopus 로고
    • Quenching accumulation of toxic galactose-1-phosphate as a system to select disruption of protein-protein interactions in vivo
    • T. Gunde Quenching accumulation of toxic galactose-1-phosphate as a system to select disruption of protein-protein interactions in vivo Biotechniques 37 2004 844 852 (Pubitemid 39488465)
    • (2004) BioTechniques , vol.37 , Issue.5 , pp. 844-852
    • Gunde, T.1    Tanner, S.2    Auf Der Maur, A.3    Petrascheck, M.4    Barberis, A.5
  • 60
    • 34250674950 scopus 로고    scopus 로고
    • Identification of protein interaction antagonists using the repressed transactivator two-hybrid system
    • DOI 10.2144/000112434
    • P.B. Joshi Identification of protein interaction antagonists using the repressed transactivator two-hybrid system Biotechniques 42 2007 635 644 (Pubitemid 46932738)
    • (2007) BioTechniques , vol.42 , Issue.5 , pp. 635-644
    • Joshi, P.B.1    Hirst, M.2    Malcolm, T.3    Parent, J.4    Mitchell, D.5    Lund, K.6    Sadowski, I.7
  • 61
    • 0036051171 scopus 로고    scopus 로고
    • A novel natural product compound enhances cAMP-regulated chloride conductance of cells expressing CFTRΔF508
    • A.V. deCarvalho A novel natural product compound enhances cAMP-regulated chloride conductance of cells expressing CFTRΔF508 Mol. Med. 8 2002 75 87
    • (2002) Mol. Med. , vol.8 , pp. 75-87
    • Decarvalho, A.V.1
  • 62
    • 70350678893 scopus 로고    scopus 로고
    • The natural product Aristolactam AIIIa as a new ligand targeting the polo-box domain of polo-like kinase 1 potently inhibits cancer cell proliferation
    • L. Li The natural product Aristolactam AIIIa as a new ligand targeting the polo-box domain of polo-like kinase 1 potently inhibits cancer cell proliferation Acta Pharmacol. Sin. 30 2009 1443 1453
    • (2009) Acta Pharmacol. Sin. , vol.30 , pp. 1443-1453
    • Li, L.1
  • 63
    • 0031453678 scopus 로고    scopus 로고
    • Understanding gene and allele function with two-hybrid methods
    • DOI 10.1146/annurev.genet.31.1.663
    • R. Brent, and R.L. Finley Jr. Understanding gene and allele function with two-hybrid methods Annu. Rev. Genet. 31 1997 663 704 (Pubitemid 28023723)
    • (1997) Annual Review of Genetics , vol.31 , pp. 663-704
    • Brent, R.1    Finley Jr., R.L.2
  • 64
    • 79959952716 scopus 로고    scopus 로고
    • First BRET-based screening assay performed in budding yeast leads to the discovery of CDK5/p25 interaction inhibitors
    • C. Corbel First BRET-based screening assay performed in budding yeast leads to the discovery of CDK5/p25 interaction inhibitors Biotechnol. J. 6 2011 860 870
    • (2011) Biotechnol. J. , vol.6 , pp. 860-870
    • Corbel, C.1
  • 66
    • 0034600324 scopus 로고    scopus 로고
    • Dexamethasone-methotrexate: An efficient chemical inducer of protein dimerization in vivo [18]
    • DOI 10.1021/ja9941532
    • H. Lin Dexamethasone-methotrexate: an efficient chemical inducer of protein dimerization in vivo J. Am. Chem. Soc. 122 2000 4247 4248 (Pubitemid 30304874)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.17 , pp. 4247-4248
    • Lin, H.1    Abida, W.M.2    Sauer, R.T.3    Cornish, V.W.4
  • 68
    • 82755160878 scopus 로고    scopus 로고
    • Recent developments in engineering and delivery of protein and antibody therapeutics
    • L.A. Fernandez, and S. Muyldermans Recent developments in engineering and delivery of protein and antibody therapeutics Curr. Opin. Biotechnol. 22 2011 1 4
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 1-4
    • Fernandez, L.A.1    Muyldermans, S.2
  • 69
    • 40349111099 scopus 로고    scopus 로고
    • Monomeric recombinant peptide aptamers are required for efficient intracellular uptake and target inhibition
    • DOI 10.1158/1541-7786.MCR-07-0245
    • C. Borghouts Monomeric recombinant peptide aptamers are required for efficient intracellular uptake and target inhibition Mol. Cancer Res. 6 2008 267 281 (Pubitemid 351342415)
    • (2008) Molecular Cancer Research , vol.6 , Issue.2 , pp. 267-281
    • Borghouts, C.1    Kunz, C.2    Delis, N.3    Groner, B.4
  • 70
    • 0034610373 scopus 로고    scopus 로고
    • Targeted modification and transportation of cellular proteins
    • P. Colas Targeted modification and transportation of cellular proteins Proc. Natl. Acad. Sci. U.S.A. 97 2000 13720 13725
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13720-13725
    • Colas, P.1
  • 71
    • 0029876415 scopus 로고    scopus 로고
    • Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2
    • DOI 10.1038/380548a0
    • P. Colas Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2 Nature 380 1996 548 550 (Pubitemid 26110646)
    • (1996) Nature , vol.380 , Issue.6574 , pp. 548-550
    • Colas, P.1    Cohen, B.2    Jessen, T.3    Grishina, I.4    McCoy, J.5    Brent, R.6
  • 72
    • 46249130022 scopus 로고    scopus 로고
    • A novel druglike spleen tyrosine kinase binder prevents anaphylactic shock when administered orally
    • E. Mazuc A novel druglike spleen tyrosine kinase binder prevents anaphylactic shock when administered orally J. Allergy Clin. Immunol. 122 2008 188 194
    • (2008) J. Allergy Clin. Immunol. , vol.122 , pp. 188-194
    • Mazuc, E.1
  • 73
    • 79959913133 scopus 로고    scopus 로고
    • Protein microarrays: Novel developments and applications
    • L. Berrade Protein microarrays: novel developments and applications Pharm. Res. 28 2011 1480 1499
    • (2011) Pharm. Res. , vol.28 , pp. 1480-1499
    • Berrade, L.1
  • 74
    • 79551529098 scopus 로고    scopus 로고
    • Development of peptide aptamer microarrays for detection of HPV16 oncoproteins in cell extracts
    • S. Laurenson Development of peptide aptamer microarrays for detection of HPV16 oncoproteins in cell extracts Anal. Biochem. 410 2011 161 170
    • (2011) Anal. Biochem. , vol.410 , pp. 161-170
    • Laurenson, S.1
  • 75
    • 77951795521 scopus 로고    scopus 로고
    • Label-free sub-picomolar protein detection with field-effect transistors
    • P. Estrela Label-free sub-picomolar protein detection with field-effect transistors Anal. Chem. 82 2010 3531 3536
    • (2010) Anal. Chem. , vol.82 , pp. 3531-3536
    • Estrela, P.1
  • 76
    • 58149234807 scopus 로고    scopus 로고
    • Cost-effective strategies for completing the interactome
    • A.S. Schwartz Cost-effective strategies for completing the interactome Nat. Methods 6 2009 55 61
    • (2009) Nat. Methods , vol.6 , pp. 55-61
    • Schwartz, A.S.1
  • 77
    • 79957874673 scopus 로고    scopus 로고
    • Next-generation sequencing to generate interactome datasets
    • H. Yu Next-generation sequencing to generate interactome datasets Nat. Methods 8 2011 478 480
    • (2011) Nat. Methods , vol.8 , pp. 478-480
    • Yu, H.1
  • 78
    • 77649182705 scopus 로고    scopus 로고
    • Unveiling the role of network and systems biology in drug discovery
    • A. Pujol Unveiling the role of network and systems biology in drug discovery Trends Pharmacol. Sci. 31 2010 115 123
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 115-123
    • Pujol, A.1
  • 79
    • 58849145512 scopus 로고    scopus 로고
    • Predicting druggable binding sites at the protein-protein interface
    • J.C. Fuller Predicting druggable binding sites at the protein-protein interface Drug Discov. Today 14 2009 155 161
    • (2009) Drug Discov. Today , vol.14 , pp. 155-161
    • Fuller, J.C.1
  • 80
    • 70349739403 scopus 로고    scopus 로고
    • Assessing the druggability of protein-protein interactions by a supervised machine-learning method
    • N. Sugaya, and K. Ikeda Assessing the druggability of protein-protein interactions by a supervised machine-learning method BMC Bioinform. 10 2009 263
    • (2009) BMC Bioinform. , vol.10 , pp. 263
    • Sugaya, N.1    Ikeda, K.2
  • 81
    • 77949743743 scopus 로고    scopus 로고
    • Atomic analysis of protein-protein interfaces with known inhibitors: The 2P2I database
    • R. Bourgeas Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database PLoS ONE 5 2010 e9598
    • (2010) PLoS ONE , vol.5 , pp. 9598
    • Bourgeas, R.1
  • 82
    • 77649233664 scopus 로고    scopus 로고
    • Rationalizing the chemical space of protein-protein interaction inhibitors
    • O. Sperandio Rationalizing the chemical space of protein-protein interaction inhibitors Drug Discov. Today 15 2010 220 229
    • (2010) Drug Discov. Today , vol.15 , pp. 220-229
    • Sperandio, O.1
  • 83
    • 79960990847 scopus 로고    scopus 로고
    • Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2P2I)
    • X. Morelli Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2P2I) Curr. Opin. Chem. Biol. 15 2011 475 481
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 475-481
    • Morelli, X.1
  • 84
    • 0022328481 scopus 로고
    • A eukaryotic transcriptional activator bearing the DNA specificity of a prokaryotic repressor
    • R. Brent, and M. Ptashne A eukaryotic transcriptional activator bearing the DNA specificity of a prokaryotic repressor Cell 43 1985 729 736
    • (1985) Cell , vol.43 , pp. 729-736
    • Brent, R.1    Ptashne, M.2
  • 85
    • 0025940629 scopus 로고
    • The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest
    • C.T. Chien The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest Proc. Natl. Acad. Sci. U.S.A. 88 1991 9578 9582
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9578-9582
    • Chien, C.T.1
  • 86
    • 77953124108 scopus 로고    scopus 로고
    • Strategies towards high-quality binary protein interactome maps
    • I. Lemmens Strategies towards high-quality binary protein interactome maps J. Proteomics 73 2010 1415 1420
    • (2010) J. Proteomics , vol.73 , pp. 1415-1420
    • Lemmens, I.1
  • 87
    • 53349117774 scopus 로고    scopus 로고
    • High-quality binary protein interaction map of the yeast interactome network
    • H. Yu High-quality binary protein interaction map of the yeast interactome network Science 322 2008 104 110
    • (2008) Science , vol.322 , pp. 104-110
    • Yu, H.1
  • 88
    • 58149242456 scopus 로고    scopus 로고
    • An experimentally derived confidence score for binary protein-protein interactions
    • P. Braun An experimentally derived confidence score for binary protein-protein interactions Nat. Methods 6 2009 91 97
    • (2009) Nat. Methods , vol.6 , pp. 91-97
    • Braun, P.1
  • 89
    • 58049215468 scopus 로고    scopus 로고
    • Combining multiple positive training sets to generate confidence scores for protein-protein interactions
    • J. Yu, and R.L. Finley Jr. Combining multiple positive training sets to generate confidence scores for protein-protein interactions Bioinformatics 25 2009 105 111
    • (2009) Bioinformatics , vol.25 , pp. 105-111
    • Yu, J.1    Finley, Jr.R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.