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Volumn 2, Issue 6, 2005, Pages 427-433

Reverse MAPPIT: Screening for protein-protein interaction modifiers in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE RECEPTOR; ERYTHROPOIETIN RECEPTOR; FK 506 BINDING PROTEIN; GROWTH FACTOR RECEPTOR; POLYPEPTIDE; PROTEIN MDM2; PROTEIN P53; SUPPRESSOR OF CYTOKINE SIGNALING;

EID: 21444437387     PISSN: 15487091     EISSN: None     Source Type: Journal    
DOI: 10.1038/nmeth760     Document Type: Article
Times cited : (49)

References (37)
  • 1
    • 0025986843 scopus 로고
    • Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide
    • Zhang, Z.Y., Poorman, R.A., Maggiora, L.L., Heinrikson, R.L. & Kezdy, F.J. Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide. J. Biol. Chem. 266, 15591-15594 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 15591-15594
    • Zhang, Z.Y.1    Poorman, R.A.2    Maggiora, L.L.3    Heinrikson, R.L.4    Kezdy, F.J.5
  • 2
    • 10244237616 scopus 로고    scopus 로고
    • Peptidomimetic inhibitors of herpes simplex virus ribonucleotide reductase with improved in vivo antiviral activity
    • Moss, N. et al. Peptidomimetic inhibitors of herpes simplex virus ribonucleotide reductase with improved in vivo antiviral activity. J. Med. Chem. 39, 4173-4180 (1996).
    • (1996) J. Med. Chem. , vol.39 , pp. 4173-4180
    • Moss, N.1
  • 3
    • 0033565287 scopus 로고    scopus 로고
    • A novel Lyn-binding peptide inhibitor blocks eosinophil differentiation, survival, and airway eosinophilic inflammation
    • Adachi, T., Stafford, S., Sur, S. & Alam, R. A novel Lyn-binding peptide inhibitor blocks eosinophil differentiation, survival, and airway eosinophilic inflammation. J. Immunol. 163, 939-946 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 939-946
    • Adachi, T.1    Stafford, S.2    Sur, S.3    Alam, R.4
  • 5
    • 0037069343 scopus 로고    scopus 로고
    • Suppression of bone resorption by madindoline A, a novel nonpeptide antagonist to gp130
    • Hayashi, M. et al. Suppression of bone resorption by madindoline A, a novel nonpeptide antagonist to gp130. Proc. Natl. Acad. Sci. USA 99, 14728-14733 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14728-14733
    • Hayashi, M.1
  • 6
    • 0036785514 scopus 로고    scopus 로고
    • Biological activity of a novel nonpeptide antagonist to the interleukin-6 receptor 20S, 21-epoxy-resibufogenin-3-formate
    • Hayashi, M. et al. Biological activity of a novel nonpeptide antagonist to the interleukin-6 receptor 20S, 21-epoxy-resibufogenin-3-formate. J. Pharmacol. Exp. Ther. 303, 104-109 (2002).
    • (2002) J. Pharmacol. Exp. Ther. , vol.303 , pp. 104-109
    • Hayashi, M.1
  • 7
    • 0034948339 scopus 로고    scopus 로고
    • Statins selectively inhibit leukocyte function antigen-1 by binding to a novel regulatory integrin site
    • Weitz-Schmidt, G. et al. Statins selectively inhibit leukocyte function antigen-1 by binding to a novel regulatory integrin site. Nat. Med. 7, 687-692 (2001).
    • (2001) Nat. Med. , vol.7 , pp. 687-692
    • Weitz-Schmidt, G.1
  • 8
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev, L.T. et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 303, 844-848 (2004).
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1
  • 9
    • 1642512639 scopus 로고    scopus 로고
    • Small-molecule antagonists of the oncogenic Tcf/β-catenin protein complex
    • Lepourcelet, M. et al. Small-molecule antagonists of the oncogenic Tcf/β-catenin protein complex. Cancer Cell 5, 91-102 (2004).
    • (2004) Cancer Cell , vol.5 , pp. 91-102
    • Lepourcelet, M.1
  • 10
    • 0037212039 scopus 로고    scopus 로고
    • Small molecule antagonists of proteins
    • Gadek, T.R. & Nicholas, J.B. Small molecule antagonists of proteins. Biochem. Pharmacol. 65, 1-8 (2003).
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 1-8
    • Gadek, T.R.1    Nicholas, J.B.2
  • 11
    • 0344837844 scopus 로고    scopus 로고
    • Luminescence resonance energy transfer-based high-throughput screening assay for inhibitors of essential protein-protein interactions in bacterial RNA polymerase
    • Bergendahl, V., Heyduk, T. & Burgess, R.R. Luminescence resonance energy transfer-based high-throughput screening assay for inhibitors of essential protein-protein interactions in bacterial RNA polymerase. Appl. Environ. Microbiol. 69, 1492-1498 (2003).
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1492-1498
    • Bergendahl, V.1    Heyduk, T.2    Burgess, R.R.3
  • 12
    • 2442705551 scopus 로고    scopus 로고
    • A mammalian genetic system to screen for small molecules capable of disrupting protein-protein interactions
    • Zhao, H.F. et al. A mammalian genetic system to screen for small molecules capable of disrupting protein-protein interactions. Anal. Chem. 76, 2922-2927 (2004).
    • (2004) Anal. Chem. , vol.76 , pp. 2922-2927
    • Zhao, H.F.1
  • 13
    • 0037195142 scopus 로고    scopus 로고
    • Inhibitors of Ras/Raf-1 interaction identified by two-hybrid screening revert Ras-dependent transformation phenotypes in human cancer cells
    • Kato-Stankiewicz, J. et al. Inhibitors of Ras/Raf-1 interaction identified by two-hybrid screening revert Ras-dependent transformation phenotypes in human cancer cells. Proc. Natl. Acad. Sci. USA 99, 14398-14403 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14398-14403
    • Kato-Stankiewicz, J.1
  • 14
    • 0031472251 scopus 로고    scopus 로고
    • A yeast genetic system for selecting small molecule inhibitors of protein-protein interactions in nanodroplets
    • Huang, J. & Schreiber, S.L. A yeast genetic system for selecting small molecule inhibitors of protein-protein interactions in nanodroplets. Proc. Natl. Acad. Sci. USA 94, 13396-13401 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13396-13401
    • Huang, J.1    Schreiber, S.L.2
  • 15
    • 0029840668 scopus 로고    scopus 로고
    • Genetic characterization of a mammalian protein-protein interaction domain by using a yeast reverse two-hybrid system
    • Vidal, M., Braun, P., Chen, E., Boeke, J.D. & Harlow, E. Genetic characterization of a mammalian protein-protein interaction domain by using a yeast reverse two-hybrid system. Proc. Natl. Acad. Sci. USA 93, 10321-10326 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10321-10326
    • Vidal, M.1    Braun, P.2    Chen, E.3    Boeke, J.D.4    Harlow, E.5
  • 16
    • 0033896165 scopus 로고    scopus 로고
    • Genetic selection for dissociative inhibitors of designated protein-protein interactions
    • Park, S.H. & Raines, R.T. Genetic selection for dissociative inhibitors of designated protein-protein interactions. Nat. Biotechnol. 18, 847-851 (2000).
    • (2000) Nat. Biotechnol. , vol.18 , pp. 847-851
    • Park, S.H.1    Raines, R.T.2
  • 17
    • 0035199166 scopus 로고    scopus 로고
    • Design and application of a cytokine receptor-based interaction trap
    • Eyckerman, S. et al. Design and application of a cytokine receptor-based interaction trap. Nat. Cell Biol. 3, 1114-1119 (2001).
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1114-1119
    • Eyckerman, S.1
  • 18
    • 0034801684 scopus 로고    scopus 로고
    • SOCS proteins: Negative regulators of cytokine signaling
    • Krebs, D.L. & Hilton, D.J. SOCS proteins: negative regulators of cytokine signaling. Stem Cells 19, 378-387 (2001).
    • (2001) Stem Cells , vol.19 , pp. 378-387
    • Krebs, D.L.1    Hilton, D.J.2
  • 19
    • 0029014206 scopus 로고
    • A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors
    • Yoshimura, A. et al. A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors. EMBO J. 14, 2816-2826 (1995).
    • (1995) EMBO J. , vol.14 , pp. 2816-2826
    • Yoshimura, A.1
  • 20
    • 0029776030 scopus 로고    scopus 로고
    • The full-length leptin receptor has signaling capabilities of interleukin 6-type cytokine receptors
    • Baumann, H. et al. The full-length leptin receptor has signaling capabilities of interleukin 6-type cytokine receptors. Proc. Natl. Acad. Sci. USA 93, 8374-8378 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8374-8378
    • Baumann, H.1
  • 21
    • 0034548763 scopus 로고    scopus 로고
    • Identification of the Y985 and Y1077 motifs as SOCS3 recruitment sites in the murine leptin receptor
    • Eyckerman, S., Broekaert, D., Verhee, A., Vandekerckhove, J. & Tavernier, J. Identification of the Y985 and Y1077 motifs as SOCS3 recruitment sites in the murine leptin receptor. FEBS Lett. 486, 33-37 (2000).
    • (2000) FEBS Lett. , vol.486 , pp. 33-37
    • Eyckerman, S.1    Broekaert, D.2    Verhee, A.3    Vandekerckhove, J.4    Tavernier, J.5
  • 22
    • 13044263097 scopus 로고    scopus 로고
    • The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation
    • Zhang, J.G. et al. The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation. Proc. Natl. Acad. Sci. USA 96, 2071-2076 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2071-2076
    • Zhang, J.G.1
  • 23
    • 0032014178 scopus 로고    scopus 로고
    • Identification of SOCS-3 as a potential mediator of central leptin resistance
    • Bjorbaek, C., Elmquist, J.K., Frantz, J.D., Shoelson, S.E. & Flier, J.S. Identification of SOCS-3 as a potential mediator of central leptin resistance. Mol. Cell 1, 619-625 (1998).
    • (1998) Mol. Cell , vol.1 , pp. 619-625
    • Bjorbaek, C.1    Elmquist, J.K.2    Frantz, J.D.3    Shoelson, S.E.4    Flier, J.S.5
  • 24
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGF β receptor in complex with FKBP12
    • Huse, M., Chen, Y.G., Massague, J. & Kuriyan, J. Crystal structure of the cytoplasmic domain of the type I TGF β receptor in complex with FKBP12. Cell 96, 425-436 (1999).
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massague, J.3    Kuriyan, J.4
  • 25
    • 0028108801 scopus 로고
    • Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12
    • Wang, T., Donahoe, P.K. & Zervos, A.S. Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12. Science 265, 674-676 (1994).
    • (1994) Science , vol.265 , pp. 674-676
    • Wang, T.1    Donahoe, P.K.2    Zervos, A.S.3
  • 26
    • 0036230536 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B: A potential leptin resistance factor of obesity
    • Cook, W.S. & Unger, R.H. Protein tyrosine phosphatase 1B: a potential leptin resistance factor of obesity. Dev. Cell 2, 385-387 (2002).
    • (2002) Dev. Cell , vol.2 , pp. 385-387
    • Cook, W.S.1    Unger, R.H.2
  • 27
    • 0036318564 scopus 로고    scopus 로고
    • Identification of a nuclear Stat1 protein tyrosine phosphatase
    • ten Hoeve, J. et al. Identification of a nuclear Stat1 protein tyrosine phosphatase. Mol. Cell. Biol. 22, 5662-5668 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5662-5668
    • ten Hoeve, J.1
  • 28
    • 0030725378 scopus 로고    scopus 로고
    • Specific inhibition of Stat3 signal transduction by PIAS3
    • Chung, C. D. et al. Specific inhibition of Stat3 signal transduction by PIAS3. Science 278, 1803-1805 (1997).
    • (1997) Science , vol.278 , pp. 1803-1805
    • Chung, C.D.1
  • 29
    • 0030926004 scopus 로고    scopus 로고
    • Mechanism of TGFbeta receptor inhibition by FKBP12
    • Chen, Y.G., Liu, F. & Massague, J. Mechanism of TGFbeta receptor inhibition by FKBP12. EMBO J. 16, 3866-3876 (1997).
    • (1997) EMBO J. , vol.16 , pp. 3866-3876
    • Chen, Y.G.1    Liu, F.2    Massague, J.3
  • 30
    • 0029836237 scopus 로고    scopus 로고
    • FKBP-12 recognition is dispensable for signal generation by type I transforming growth factor-βreceptors
    • Charng, M.J., Kinnunen, P., Hawker, J., Brand, T. & Schneider, M.D. FKBP-12 recognition is dispensable for signal generation by type I transforming growth factor-βreceptors. J. Biol. Chem. 271, 22941-22944 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 22941-22944
    • Charng, M.J.1    Kinnunen, P.2    Hawker, J.3    Brand, T.4    Schneider, M.D.5
  • 31
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A.A. & Thorn, K.S. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280, 1-9 (1998).
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 32
    • 0037388679 scopus 로고    scopus 로고
    • Protein-protein interactions as a target for drugs in proteomics
    • Archakov, A.I. et al. Protein-protein interactions as a target for drugs in proteomics. Proteomics 3, 380-391 (2003).
    • (2003) Proteomics , vol.3 , pp. 380-391
    • Archakov, A.I.1
  • 33
    • 0037452709 scopus 로고    scopus 로고
    • Binding of small molecules to an adaptive protein-protein interface
    • Arkin, M.R. et al. Binding of small molecules to an adaptive protein-protein interface. Proc. Natl. Acad. Sci. USA 100, 1603-1608 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1603-1608
    • Arkin, M.R.1
  • 34
    • 0033198152 scopus 로고    scopus 로고
    • Prospects for drug screening using the reverse two-hybrid system
    • Vidal, M. & Endoh, H. Prospects for drug screening using the reverse two-hybrid system. Trends Biotechnol. 17, 374-381 (1999).
    • (1999) Trends Biotechnol. , vol.17 , pp. 374-381
    • Vidal, M.1    Endoh, H.2
  • 35
    • 0024348798 scopus 로고
    • The yeast gene ERG6 is required for normal membrane function but is not essential for biosynthesis of the cell-cycle-sparking sterol
    • Gaber, R.F., Copple, D.M., Kennedy, B.K., Vidal, M. & Bard, M. The yeast gene ERG6 is required for normal membrane function but is not essential for biosynthesis of the cell-cycle-sparking sterol. Mol. Cell. Biol. 9, 3447-3456 (1989).
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3447-3456
    • Gaber, R.F.1    Copple, D.M.2    Kennedy, B.K.3    Vidal, M.4    Bard, M.5
  • 36
    • 0032736383 scopus 로고    scopus 로고
    • Analysis of Tyr to Phe and fa/fa leptin receptor mutations in the PC12 cell line
    • Eyckerman, S. et al. Analysis of Tyr to Phe and fa/fa leptin receptor mutations in the PC12 cell line. Eur. Cytokine Netw. 10, 549-556 (1999).
    • (1999) Eur. Cytokine Netw. , vol.10 , pp. 549-556
    • Eyckerman, S.1
  • 37
    • 0242317457 scopus 로고    scopus 로고
    • Heteromeric MAPPIT: A novel strategy to study modification-dependent protein-protein interactions in mammalian cells
    • Lemmens, I. et al. Heteromeric MAPPIT: a novel strategy to study modification-dependent protein-protein interactions in mammalian cells. Nucleic Acids Res. 31, e75 (2003).
    • (2003) Nucleic Acids Res. , vol.31
    • Lemmens, I.1


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