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Volumn 6, Issue 7, 2007, Pages 569-582

Universal strategies in research and drug discovery based on protein-fragment complementation assays

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ANTIDIABETIC AGENT; ANTIINFECTIVE AGENT; ANTIINFLAMMATORY AGENT; ANTINEOPLASTIC AGENT; CARDIOVASCULAR AGENT; CENTRAL NERVOUS SYSTEM AGENTS; CHAPERONE; CYAN FLUORESCENT PROTEIN; CYTOSKELETON PROTEIN; DESIGNED ANKYRIN REPEAT PROTEIN; ERYTHROPOIETIN RECEPTOR; G PROTEIN COUPLED RECEPTOR; GREEN FLUORESCENT PROTEIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; LEUCINE ZIPPER PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE INHIBITOR; SCAFFOLD PROTEIN; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN;

EID: 34347374044     PISSN: 14741776     EISSN: 14741784     Source Type: Journal    
DOI: 10.1038/nrd2311     Document Type: Review
Times cited : (277)

References (108)
  • 1
    • 0034677966 scopus 로고    scopus 로고
    • Drug discovery: A historical perspective
    • Drews, J. Drug discovery: A historical perspective. Science 287 1960-1964 (2000).
    • (2000) Science , vol.287 , pp. 1960-1964
    • Drews, J.1
  • 2
    • 10244219858 scopus 로고    scopus 로고
    • Accessing genetic information with high-density DNA arrays
    • Chee, M. et al. Accessing genetic information with high-density DNA arrays. Science 274, 610-614 (1996).
    • (1996) Science , vol.274 , pp. 610-614
    • Chee, M.1
  • 3
    • 18244370796 scopus 로고    scopus 로고
    • How molecular profiling could revolutionize drug discovery
    • Stoughton, R. B. & Friend, S. H. How molecular profiling could revolutionize drug discovery. Nature Rev. Drug Discov. 4, 345-350 (2005).
    • (2005) Nature Rev. Drug Discov , vol.4 , pp. 345-350
    • Stoughton, R.B.1    Friend, S.H.2
  • 4
    • 0031730097 scopus 로고    scopus 로고
    • Drug target validation and identification of secondary drug target effects using DNA microarrays
    • Marton, M. J. et al. Drug target validation and identification of secondary drug target effects using DNA microarrays. Nature Med. 4, 1293-1301 (1998).
    • (1998) Nature Med , vol.4 , pp. 1293-1301
    • Marton, M.J.1
  • 5
    • 0033592983 scopus 로고    scopus 로고
    • Rapamycin-modulated transcription defines the subset of nutrient-sensitive signaling pathways directly controlled by the Tor proteins
    • Hardwick, J. S., Kuruvilla, F. G., Tong, J. K., Shamji, A. F. & Schreiber, S. L. Rapamycin-modulated transcription defines the subset of nutrient-sensitive signaling pathways directly controlled by the Tor proteins. Proc. Natl Acad. Sci USA 96, 14866-14870 (1999).
    • (1999) Proc. Natl Acad. Sci USA , vol.96 , pp. 14866-14870
    • Hardwick, J.S.1    Kuruvilla, F.G.2    Tong, J.K.3    Shamji, A.F.4    Schreiber, S.L.5
  • 6
    • 0034616930 scopus 로고    scopus 로고
    • Functional discovery via a compendium of expression profiles
    • Hughes, T. R. et al. Functional discovery via a compendium of expression profiles. Cell 102, 109-126 (2000).
    • (2000) Cell , vol.102 , pp. 109-126
    • Hughes, T.R.1
  • 7
    • 0033048778 scopus 로고    scopus 로고
    • Genomic profiling of drug sensitivities via induced haploinsufficiency
    • Giaever, G. et al. Genomic profiling of drug sensitivities via induced haploinsufficiency. Nature Genet. 21, 278-283 (1999).
    • (1999) Nature Genet , vol.21 , pp. 278-283
    • Giaever, G.1
  • 8
    • 9144268287 scopus 로고    scopus 로고
    • Chemogenomic profiling: Identifying the functional interactions of small molecules in yeast
    • Giaever, G. et al. Chemogenomic profiling: Identifying the functional interactions of small molecules in yeast. Proc. Natl Acad. Sci. USA 101, 793-798 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 793-798
    • Giaever, G.1
  • 9
    • 0030667434 scopus 로고    scopus 로고
    • Integrating genetic approaches into the discovery of anticancer drugs
    • Hartwell, L. H., Szankasi, P., Roberts, C. J., Murray, A. W. & Friend, S. H. Integrating genetic approaches into the discovery of anticancer drugs. Science 278, 1064-1068 (1997).
    • (1997) Science , vol.278 , pp. 1064-1068
    • Hartwell, L.H.1    Szankasi, P.2    Roberts, C.J.3    Murray, A.W.4    Friend, S.H.5
  • 10
    • 0034312277 scopus 로고    scopus 로고
    • Requirement for Atr in phosphorylation of Chk1 and cell cycle regulation in response to DNA replication blocks and UV-damaged DNA in Xenopus egg extracts
    • Guo, Z., Kumagai, A., Wang, S. X. & Dunphy, W. G. Requirement for Atr in phosphorylation of Chk1 and cell cycle regulation in response to DNA replication blocks and UV-damaged DNA in Xenopus egg extracts. Genes Dev. 14, 2745-2756 (2000).
    • (2000) Genes Dev , vol.14 , pp. 2745-2756
    • Guo, Z.1    Kumagai, A.2    Wang, S.X.3    Dunphy, W.G.4
  • 11
    • 0037061492 scopus 로고    scopus 로고
    • Dissecting glucose signalling with diversity-oriented synthesis and small-molecule microarrays
    • Kuruvilla, F. G., Shamji, A. F., Sternson, S. M., Hergenrother, P. J. & Schreiber, S. L. Dissecting glucose signalling with diversity-oriented synthesis and small-molecule microarrays. Nature 416, 653-657 (2002).
    • (2002) Nature , vol.416 , pp. 653-657
    • Kuruvilla, F.G.1    Shamji, A.F.2    Sternson, S.M.3    Hergenrother, P.J.4    Schreiber, S.L.5
  • 12
    • 7044239645 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in plants using bimolecular fluorescence complementation
    • Bracha-Drori, K. et al. Detection of protein-protein interactions in plants using bimolecular fluorescence complementation. Plant J. 40, 419-427 (2004).
    • (2004) Plant J , vol.40 , pp. 419-427
    • Bracha-Drori, K.1
  • 13
    • 0347473810 scopus 로고    scopus 로고
    • Integration of chemical-genetic and genetic interaction data links bioactive compounds to cellular target pathways
    • Parsons, A. B. et al. Integration of chemical-genetic and genetic interaction data links bioactive compounds to cellular target pathways. Nature Biotech. 22, 62-69 (2004).
    • (2004) Nature Biotech , vol.22 , pp. 62-69
    • Parsons, A.B.1
  • 14
    • 33746753342 scopus 로고    scopus 로고
    • Exploring the mode-of-action of bioactive compounds by chemical-genetic profiling in yeast
    • Parsons, A. B. et al. Exploring the mode-of-action of bioactive compounds by chemical-genetic profiling in yeast. Cell 126, 611-625 (2006).
    • (2006) Cell , vol.126 , pp. 611-625
    • Parsons, A.B.1
  • 15
    • 0033518234 scopus 로고    scopus 로고
    • From molecular to modular cell biology
    • Hartwell, L. H., Hopfield, J. J., Leibler, S. & Murray, A. W. From molecular to modular cell biology. Nature 402 (Suppl. 6761), C47-C52. (1999).
    • (1999) Nature , vol.402 , Issue.SUPPL. 6761
    • Hartwell, L.H.1    Hopfield, J.J.2    Leibler, S.3    Murray, A.W.4
  • 16
    • 10744230485 scopus 로고    scopus 로고
    • Global mapping of the yeast genetic interaction network
    • Tong, A. H. et al. Global mapping of the yeast genetic interaction network. Science 303, 808-813 (2004).
    • (2004) Science , vol.303 , pp. 808-813
    • Tong, A.H.1
  • 17
    • 1842580761 scopus 로고    scopus 로고
    • Functional and topological characterization of protein interaction networks
    • Yook, S. H., Oltvai, Z. N. & Barabasi, A. L. Functional and topological characterization of protein interaction networks. Proteomics 4 928-942 (2004).
    • (2004) Proteomics , vol.4 , pp. 928-942
    • Yook, S.H.1    Oltvai, Z.N.2    Barabasi, A.L.3
  • 18
    • 0036699526 scopus 로고    scopus 로고
    • Revealing modular organization in the yeast transcriptional network
    • Ihmels, J. et al. Revealing modular organization in the yeast transcriptional network. Nature Genet. 31, 370-377 (2002).
    • (2002) Nature Genet , vol.31 , pp. 370-377
    • Ihmels, J.1
  • 19
    • 0037197886 scopus 로고    scopus 로고
    • The identification of functional modules from the genomic association of genes
    • Snel, B., Bork, P. & Huynen, M. A. The identification of functional modules from the genomic association of genes. Proc. Natl Acad. Sci. USA 99, 5890-5895 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5890-5895
    • Snel, B.1    Bork, P.2    Huynen, M.A.3
  • 20
    • 0037417817 scopus 로고    scopus 로고
    • Modular organization of cellular networks
    • Rives, A. W. & Galitski, T. Modular organization of cellular networks. Proc. Natl Acad. Sci. USA 100, 1128-1133 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1128-1133
    • Rives, A.W.1    Galitski, T.2
  • 21
    • 19344366383 scopus 로고    scopus 로고
    • Interaction networks in yeast define and enumerate the signaling steps of the vertebrate aryl hydrocarbon receptor
    • Yao, G., Craven, M., Drinkwater, N. & Bradfield, C. A. Interaction networks in yeast define and enumerate the signaling steps of the vertebrate aryl hydrocarbon receptor. PLoS Biol. 2, e65 (2004).
    • (2004) PLoS Biol , vol.2
    • Yao, G.1    Craven, M.2    Drinkwater, N.3    Bradfield, C.A.4
  • 22
    • 0028080090 scopus 로고
    • Split ubiquitin as a sensor of protein interactions in vivo
    • Johnsson, N. & Varshavsky, A. Split ubiquitin as a sensor of protein interactions in vivo. Proc. Natl Acad. Sci. USA 91, 10340-10344 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10340-10344
    • Johnsson, N.1    Varshavsky, A.2
  • 23
    • 0007188298 scopus 로고    scopus 로고
    • A protein complementation assay for detection of protein-protein interactions in vivo
    • Pelletier, J. N. & Michnick, S. W. A protein complementation assay for detection of protein-protein interactions in vivo. Protein Eng. 10, 89 (1997).
    • (1997) Protein Eng , vol.10 , pp. 89
    • Pelletier, J.N.1    Michnick, S.W.2
  • 24
    • 0032514623 scopus 로고    scopus 로고
    • Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments
    • Pelletier, J. N., Campbell-Valois, F. & Michnick, S. W. Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments. Proc. Natl Acad. Sci. USA 95, 12141-12146 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12141-12146
    • Pelletier, J.N.1    Campbell-Valois, F.2    Michnick, S.W.3
  • 26
    • 0033545844 scopus 로고    scopus 로고
    • Clonal selection and in vivo quantitation of protein interactions with protein fragment complementation assays
    • Remy, I. & Michnick, S. W. Clonal selection and in vivo quantitation of protein interactions with protein fragment complementation assays. Proc. Natl Acad. Sci. USA 96, 5394-5399 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 5394-5399
    • Remy, I.1    Michnick, S.W.2
  • 27
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy, I., Wilson, I. A. & Michnick, S. W. Erythropoietin receptor activation by a ligand-induced conformation change. Science 283 990-993 (1999).
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 28
    • 0034944377 scopus 로고    scopus 로고
    • Visualization of biochemical networks in living cells
    • Remy, I. & Michnick, S. W. Visualization of biochemical networks in living cells. Proc. Natl Acad. Sci. USA 98, 7678-7683 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7678-7683
    • Remy, I.1    Michnick, S.W.2
  • 29
    • 0035984722 scopus 로고    scopus 로고
    • β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein protein interactions
    • Galarneau, A., Primeau, M., Trudeau, L. E. & Michnick, S. W. β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein protein interactions. Nature Biotech. 20, 619-622 (2002).
    • (2002) Nature Biotech , vol.20 , pp. 619-622
    • Galarneau, A.1    Primeau, M.2    Trudeau, L.E.3    Michnick, S.W.4
  • 30
    • 0037069474 scopus 로고    scopus 로고
    • Time-lapse imaging of a dynamic phosphorylation-dependent protein-protein interaction in mammalian cells
    • Spotts, J. M., Dolmetsch, R. E. & Greenberg, M. E. Time-lapse imaging of a dynamic phosphorylation-dependent protein-protein interaction in mammalian cells. Proc. Natl Acad. Sci. USA 99, 15142-15147. (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 15142-15147
    • Spotts, J.M.1    Dolmetsch, R.E.2    Greenberg, M.E.3
  • 31
    • 0037133629 scopus 로고    scopus 로고
    • Protein-protein interactions monitored in mammalian cells via complementation of β-lactamase enzyme fragments
    • Wehrman, T., Kleaveland, B., Her, J. H., Balint, R. F. & Blau, H. M. Protein-protein interactions monitored in mammalian cells via complementation of β-lactamase enzyme fragments. Proc. Natl Acad. Sci. USA 99, 3469-3474 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3469-3474
    • Wehrman, T.1    Kleaveland, B.2    Her, J.H.3    Balint, R.F.4    Blau, H.M.5
  • 32
    • 0034647238 scopus 로고    scopus 로고
    • Antiparallel leucine zipper-directed protein reassembly: Application to the green fluorescent protein
    • Ghosh, I., Hamilton, A. D. & Regan, L. Antiparallel leucine zipper-directed protein reassembly: Application to the green fluorescent protein. J. Am. Chem. Soc. 122, 5658-5659 (2000).
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 5658-5659
    • Ghosh, I.1    Hamilton, A.D.2    Regan, L.3
  • 33
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C. D., Chinenov, Y. & Kerppola, T. K. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9, 789-798 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 34
    • 1542375250 scopus 로고    scopus 로고
    • cDNA library functional screening strategy based on fluorescent protein complementation assays to identify novel components of signaling pathways
    • Remy, I. & Michnick, S. A cDNA library functional screening strategy based on fluorescent protein complementation assays to identify novel components of signaling pathways. Methods 32, 381-388 (2004).
    • (2004) Methods , vol.32 , pp. 381-388
    • Remy, I.1    Michnick, S.A.2
  • 35
    • 0842304224 scopus 로고    scopus 로고
    • Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/ Akt
    • Remy, I. & Michnick, S. W. Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/ Akt. Mol. Cell. Biol. 24, 1493-1504 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 1493-1504
    • Remy, I.1    Michnick, S.W.2
  • 36
    • 2342647439 scopus 로고    scopus 로고
    • PKB/ Akt modulates TGF-β signalling through a direct interaction with Smad3
    • Remy, I., Montmarquette, A. & Michnick, S. W. PKB/ Akt modulates TGF-β signalling through a direct interaction with Smad3. Nature Cell Biol. 6, 358-365 (2004).
    • (2004) Nature Cell Biol , vol.6 , pp. 358-365
    • Remy, I.1    Montmarquette, A.2    Michnick, S.W.3
  • 37
    • 3242657478 scopus 로고    scopus 로고
    • Mapping biochemical networks with protein-fragment complementation assays
    • Remy, I. & Michnick, S. W. Mapping biochemical networks with protein-fragment complementation assays. Methods Mol. Biol. 261 411-426 (2004).
    • (2004) Methods Mol. Biol , vol.261 , pp. 411-426
    • Remy, I.1    Michnick, S.W.2
  • 38
    • 4344656346 scopus 로고    scopus 로고
    • Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals
    • Luker, K. E. et al. Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals. Proc. Natl Acad. Sci. USA 101, 12288-12293 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 12288-12293
    • Luker, K.E.1
  • 39
    • 0042476427 scopus 로고    scopus 로고
    • Locating a protein-protein interaction in living cells via split Renilla luciferase complementation
    • Kaihara, A., Kawai, Y., Sato, M., Ozawa, T. & Umezawa, Y. Locating a protein-protein interaction in living cells via split Renilla luciferase complementation. Anal. Chem. 75, 4176-4181 (2003).
    • (2003) Anal. Chem , vol.75 , pp. 4176-4181
    • Kaihara, A.1    Kawai, Y.2    Sato, M.3    Ozawa, T.4    Umezawa, Y.5
  • 40
    • 0037397074 scopus 로고    scopus 로고
    • Monitoring protein-protein interactions using split synthetic Renilla luciferase protein-fragment-assisted complementation
    • Paulmurugan, R. & Gambhir, S. S. Monitoring protein-protein interactions using split synthetic Renilla luciferase protein-fragment-assisted complementation. Anal. Chem. 75, 1584-1589. (2003).
    • (2003) Anal. Chem , vol.75 , pp. 1584-1589
    • Paulmurugan, R.1    Gambhir, S.S.2
  • 41
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive protein-protein interaction assay based on Gaussia luciferase
    • Remy, I. & Michnick, S. W. A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nature Methods 3, 977-979 (2006).
    • (2006) Nature Methods , vol.3 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 42
    • 0030738524 scopus 로고    scopus 로고
    • Monitoring protein-protein interactions in intact eukaryotic cells by β-galactosidase complementation
    • Rossi, F., Charlton, C. A. & Blau, H. M. Monitoring protein-protein interactions in intact eukaryotic cells by β-galactosidase complementation. Proc. Natl Acad. Sci. USA 94, 8405-8410 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 8405-8410
    • Rossi, F.1    Charlton, C.A.2    Blau, H.M.3
  • 43
    • 0034329620 scopus 로고    scopus 로고
    • A fluorescent indicator for detecting protein-protein interactions in vivo based on protein splicing
    • Ozawa, T., Nogami, S., Sato, M., Ohya, Y. & Umezawa, Y. A fluorescent indicator for detecting protein-protein interactions in vivo based on protein splicing. Anal. Chem. 72, 5151-5157 (2000).
    • (2000) Anal. Chem , vol.72 , pp. 5151-5157
    • Ozawa, T.1    Nogami, S.2    Sato, M.3    Ohya, Y.4    Umezawa, Y.5
  • 44
    • 0032977886 scopus 로고    scopus 로고
    • Pelletier, J. N., Arndt, K. M., Pluckthun, A. & Michnick, S. W. An in vivo library-versus-library selection of optimized protein-protein interactions. Nature Biotech. 17, 683-690 (1999).
    • Pelletier, J. N., Arndt, K. M., Pluckthun, A. & Michnick, S. W. An in vivo library-versus-library selection of optimized protein-protein interactions. Nature Biotech. 17, 683-690 (1999).
  • 45
    • 34347369882 scopus 로고    scopus 로고
    • Quantification of dynamic protein complexes using Renilla luciferase-fragment complementation applied to PKA activities in vivo
    • in the press
    • Stefan, E., Aquin, S., Berger, N. & Michnick, S. W. Quantification of dynamic protein complexes using Renilla luciferase-fragment complementation applied to PKA activities in vivo. Proc. Natl Acad. Sci. USA (in the press).
    • Proc. Natl Acad. Sci. USA
    • Stefan, E.1    Aquin, S.2    Berger, N.3    Michnick, S.W.4
  • 46
    • 11844252081 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: Scope and mechanism
    • Magliery, T. J. et al. Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: Scope and mechanism. J. Am. Chem. Soc. 127, 146-157 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 146-157
    • Magliery, T.J.1
  • 47
    • 18144394763 scopus 로고    scopus 로고
    • Capturing protein interactions in the secretory pathway of living cells
    • Nyfeler, B., Michnick, S. W. & Hauri, H. P. Capturing protein interactions in the secretory pathway of living cells. Proc. Natl Acad. Sci. USA 102, 6350-6355 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 6350-6355
    • Nyfeler, B.1    Michnick, S.W.2    Hauri, H.P.3
  • 48
    • 0034695427 scopus 로고    scopus 로고
    • A heterodimeric coiled-coil peptide pair selected in vivo from a designed library-versus-library ensemble
    • Arndt, K. M. et al. A heterodimeric coiled-coil peptide pair selected in vivo from a designed library-versus-library ensemble. J. Mol. Biol. 295, 627-639 (2000).
    • (2000) J. Mol. Biol , vol.295 , pp. 627-639
    • Arndt, K.M.1
  • 50
    • 33846012154 scopus 로고    scopus 로고
    • The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse
    • Campbell-Valois, F. X. & Michnick, S. W. The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559-1577 (2007).
    • (2007) J. Mol. Biol , vol.365 , pp. 1559-1577
    • Campbell-Valois, F.X.1    Michnick, S.W.2
  • 51
    • 33747354867 scopus 로고    scopus 로고
    • Massive sequence perturbation of the Raf Ras binding domain reveals relationships between sequence conservation, secondary structure propensity, hydrophobic core organization and stability
    • Campbell-Valois, F. X., Tarassov, K. & Michnick, S. W. Massive sequence perturbation of the Raf Ras binding domain reveals relationships between sequence conservation, secondary structure propensity, hydrophobic core organization and stability. J. Mol. Biol. 362, 151-171 (2006).
    • (2006) J. Mol. Biol , vol.362 , pp. 151-171
    • Campbell-Valois, F.X.1    Tarassov, K.2    Michnick, S.W.3
  • 52
    • 33646267001 scopus 로고    scopus 로고
    • Rapid selection of specific MAP kinase-binders from designed ankyrin repeat protein libraries
    • Amstutz, P., Koch, H., Binz, H. K., Deuber, S. A. & Pluckthun, A. Rapid selection of specific MAP kinase-binders from designed ankyrin repeat protein libraries. Protein Eng. Des. Sel. 19, 219-229 (2006).
    • (2006) Protein Eng. Des. Sel , vol.19 , pp. 219-229
    • Amstutz, P.1    Koch, H.2    Binz, H.K.3    Deuber, S.A.4    Pluckthun, A.5
  • 53
    • 33344463396 scopus 로고    scopus 로고
    • Direct selection of antibodies from complex libraries with the protein fragment complementation assay
    • Koch, H., Grafe, N., Schiess, R. & Pluckthun, A. Direct selection of antibodies from complex libraries with the protein fragment complementation assay. J. Mol. Biol. 357, 427-441 (2006).
    • (2006) J. Mol. Biol , vol.357 , pp. 427-441
    • Koch, H.1    Grafe, N.2    Schiess, R.3    Pluckthun, A.4
  • 54
    • 0027080589 scopus 로고
    • Crystal structure determination at 2.3 Å of recombinant human dihydrofolate reductase ternary complex with NADPH and methotrexate-γ-tetrazole
    • Cody, V., Luft, J. R., Ciszak, E., Kalman, T. I. & Freisheim, J. H. Crystal structure determination at 2.3 Å of recombinant human dihydrofolate reductase ternary complex with NADPH and methotrexate-γ-tetrazole. Anticancer Drug Design 7, 483-491 (1992).
    • (1992) Anticancer Drug Design , vol.7 , pp. 483-491
    • Cody, V.1    Luft, J.R.2    Ciszak, E.3    Kalman, T.I.4    Freisheim, J.H.5
  • 55
    • 0023514599 scopus 로고
    • Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system
    • Aruffo, A. & Seed, B. Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system. Proc. Natl Acad. Sci. USA 84, 8573-8577 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 8573-8577
    • Aruffo, A.1    Seed, B.2
  • 56
    • 0024976586 scopus 로고
    • Erythropoietin receptor and interleukin-2 receptor α-chain: A new receptor family
    • D'Andrea, A. D., Fasman, G. D. & Lodish, H. F. Erythropoietin receptor and interleukin-2 receptor α-chain: A new receptor family. Cell 58, 1023-1024 (1989).
    • (1989) Cell , vol.58 , pp. 1023-1024
    • D'Andrea, A.D.1    Fasman, G.D.2    Lodish, H.F.3
  • 57
    • 0027138212 scopus 로고
    • Expression cloning of a functional glycoprotein ligand for P-selectin
    • Sako, D. et al. Expression cloning of a functional glycoprotein ligand for P-selectin. Cell 75, 1179-1186 (1993).
    • (1993) Cell , vol.75 , pp. 1179-1186
    • Sako, D.1
  • 58
    • 0026537831 scopus 로고
    • Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/ threonine kinase
    • Lin, H. Y., Wang, X. F., Ng-Eaton, E., Weinberg, R. A. & Lodish, H. F. Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/ threonine kinase. Cell 68, 775-785 (1992).
    • (1992) Cell , vol.68 , pp. 775-785
    • Lin, H.Y.1    Wang, X.F.2    Ng-Eaton, E.3    Weinberg, R.A.4    Lodish, H.F.5
  • 59
    • 1542320541 scopus 로고    scopus 로고
    • The art and design of genetic screens: Mammalian culture cells
    • Grimm, S. The art and design of genetic screens: Mammalian culture cells. Nature Rev. Genet. 5, 179-189 (2004).
    • (2004) Nature Rev. Genet , vol.5 , pp. 179-189
    • Grimm, S.1
  • 60
    • 0034193568 scopus 로고    scopus 로고
    • Protein-protein interactions define specificity in signal transduction
    • Pawson, T. & Nash, P. Protein-protein interactions define specificity in signal transduction. Genes Dev. 14, 1027-1047 (2000).
    • (2000) Genes Dev , vol.14 , pp. 1027-1047
    • Pawson, T.1    Nash, P.2
  • 61
    • 0035967967 scopus 로고    scopus 로고
    • Signal transduction: Signaling specificity - a complex affair
    • Weston, C. R. & Davis, R. J. Signal transduction: Signaling specificity - a complex affair. Science 292, 2439-2440. (2001).
    • (2001) Science , vol.292 , pp. 2439-2440
    • Weston, C.R.1    Davis, R.J.2
  • 62
    • 0035836765 scopus 로고    scopus 로고
    • A comprehensive two-hybrid analysis to explore the yeast protein interactome
    • Ito, T. et al. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc. Natl Acad. Sci. USA 98, 4569-4574 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4569-4574
    • Ito, T.1
  • 63
    • 0033974688 scopus 로고    scopus 로고
    • Toward a protein-protein interaction map of the budding yeast: A comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteins
    • Ito, T. et al. Toward a protein-protein interaction map of the budding yeast: A comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteins. Proc. Natl Acad. Sci. USA 97, 1143-1147. (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1143-1147
    • Ito, T.1
  • 64
    • 0032983270 scopus 로고    scopus 로고
    • Progress and variations in two-hybrid and three-hybrid technologies
    • Drees, B. L. Progress and variations in two-hybrid and three-hybrid technologies. Curr. Opin. Chem. Biol. 3, 64-70 (1999).
    • (1999) Curr. Opin. Chem. Biol , vol.3 , pp. 64-70
    • Drees, B.L.1
  • 65
    • 0034614678 scopus 로고    scopus 로고
    • Protein interaction mapping in C. elegans using proteins involved in vulval development
    • Walhout, A. J. et al. Protein interaction mapping in C. elegans using proteins involved in vulval development. Science 287 116-122 (2000).
    • (2000) Science , vol.287 , pp. 116-122
    • Walhout, A.J.1
  • 66
    • 0033557224 scopus 로고    scopus 로고
    • Yeast forward and reverse 'n'-hybrid systems
    • Vidal, M. & Legrain, P. Yeast forward and reverse 'n'-hybrid systems. Nucleic Acids Res. 27, 919-929 (1999).
    • (1999) Nucleic Acids Res , vol.27 , pp. 919-929
    • Vidal, M.1    Legrain, P.2
  • 67
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S. & Song, O. A novel genetic system to detect protein-protein interactions. Nature 340, 245-246 (1989).
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 68
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz, P. et al. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403, 623-627 (2000).
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1
  • 69
    • 33750064552 scopus 로고    scopus 로고
    • A retrovirus-based protein complementation assay screen reveals functional AKT1-binding partners
    • Ding, Z. et al. A retrovirus-based protein complementation assay screen reveals functional AKT1-binding partners. Proc. Natl Acad. Sci. USA 103, 15014-15019 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 15014-15019
    • Ding, Z.1
  • 70
    • 33646893689 scopus 로고    scopus 로고
    • Identifying off-target effects and hidden phenotypes of drugs in human cells
    • Macdonald, M. L. et al. Identifying off-target effects and hidden phenotypes of drugs in human cells. Nature Chem. Biol. 2, 329-337 (2006).
    • (2006) Nature Chem. Biol , vol.2 , pp. 329-337
    • Macdonald, M.L.1
  • 71
    • 0037180571 scopus 로고    scopus 로고
    • Noninvasive imaging of protein-protein interactions in living subjects by using reporter protein complementation and reconstitution strategies
    • Paulmurugan, R., Umezawa, Y. & Gambhir, S. S. Noninvasive imaging of protein-protein interactions in living subjects by using reporter protein complementation and reconstitution strategies. Proc. Natl Acad. Sci. USA 99, 15608-15613. (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 15608-15613
    • Paulmurugan, R.1    Umezawa, Y.2    Gambhir, S.S.3
  • 72
    • 1542615075 scopus 로고    scopus 로고
    • Molecular imaging of drug-modulated protein-protein interactions in living subjects
    • Paulmurugan, R., Massoud, T. F., Huang, J. & Gambhir, S. S. Molecular imaging of drug-modulated protein-protein interactions in living subjects. Cancer Res. 64, 2113-2119 (2004).
    • (2004) Cancer Res , vol.64 , pp. 2113-2119
    • Paulmurugan, R.1    Massoud, T.F.2    Huang, J.3    Gambhir, S.S.4
  • 73
    • 9444222526 scopus 로고    scopus 로고
    • Molecular imaging of homodimeric protein-protein interactions in living subjects
    • Massoud, T. F., Paulmurugan, R. & Gambhir, S. S. Molecular imaging of homodimeric protein-protein interactions in living subjects. FASEB J. 18, 1105-1107 (2004).
    • (2004) FASEB J , vol.18 , pp. 1105-1107
    • Massoud, T.F.1    Paulmurugan, R.2    Gambhir, S.S.3
  • 74
    • 14744281422 scopus 로고    scopus 로고
    • Firefly luciferase enzyme fragment complementation for imaging in cells and living animals
    • Paulmurugan, R. & Gambhir, S. S. Firefly luciferase enzyme fragment complementation for imaging in cells and living animals. Anal. Chem. 77, 1295-1302 (2005).
    • (2005) Anal. Chem , vol.77 , pp. 1295-1302
    • Paulmurugan, R.1    Gambhir, S.S.2
  • 75
    • 33745223646 scopus 로고    scopus 로고
    • Finding function in novel targets: C. elegans as a model organism
    • Kaletta, T. & Hengartner, M. O. Finding function in novel targets: C. elegans as a model organism. Nature Rev. Drug Discov. 5, 387-398 (2006).
    • (2006) Nature Rev. Drug Discov , vol.5 , pp. 387-398
    • Kaletta, T.1    Hengartner, M.O.2
  • 76
    • 5344279061 scopus 로고    scopus 로고
    • Combinatorial marking of cells and organelles with reconstituted fluorescent proteins
    • Zhang, S., Ma, C. & Chalfie, M. Combinatorial marking of cells and organelles with reconstituted fluorescent proteins. Cell 119 137-144 (2004).
    • (2004) Cell , vol.119 , pp. 137-144
    • Zhang, S.1    Ma, C.2    Chalfie, M.3
  • 77
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire, A. et al. Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 391, 806-811 (1998).
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire, A.1
  • 78
    • 33244480581 scopus 로고    scopus 로고
    • Atypical membrane topology and heteromeric function of Drosophila odorant receptors in vivo
    • Benton, R., Sachse, S., Michnick, S. W. & Vosshall, L. B. Atypical membrane topology and heteromeric function of Drosophila odorant receptors in vivo. PLoS Biol. 4, e20 (2006).
    • (2006) PLoS Biol , vol.4
    • Benton, R.1    Sachse, S.2    Michnick, S.W.3    Vosshall, L.B.4
  • 79
    • 0028243532 scopus 로고
    • Ubiquitin-assisted dissection of protein transport across membranes
    • Johnsson, N. & Varshavsky, A. Ubiquitin-assisted dissection of protein transport across membranes. EMBO J. 13, 2686-2698 (1994).
    • (1994) EMBO J , vol.13 , pp. 2686-2698
    • Johnsson, N.1    Varshavsky, A.2
  • 80
    • 0032574840 scopus 로고    scopus 로고
    • A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo
    • Stagljar, I., Korostensky, C., Johnsson, N. & te Heesen, S. A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc. Natl Acad. Sci. USA 95, 5187-5192. (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5187-5192
    • Stagljar, I.1    Korostensky, C.2    Johnsson, N.3    te Heesen, S.4
  • 81
    • 0034610333 scopus 로고    scopus 로고
    • A new screen for protein interactions reveals that the Saccharomyces cerevisiae high mobility group proteins Nhp6A/B are involved in the regulation of the GAL1 promoter
    • Laser, H. et al. A new screen for protein interactions reveals that the Saccharomyces cerevisiae high mobility group proteins Nhp6A/B are involved in the regulation of the GAL1 promoter. Proc. Natl Acad. Sci. USA 97, 13732-13737 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13732-13737
    • Laser, H.1
  • 82
    • 34147167177 scopus 로고    scopus 로고
    • Mapping protein-protein interactions for the yeast ABC transporter Ycf1p by integrated split-ubiquitin membrane yeast two-hybrid analysis
    • Paumi, C. M. et al. Mapping protein-protein interactions for the yeast ABC transporter Ycf1p by integrated split-ubiquitin membrane yeast two-hybrid analysis. Mol. Cell 26, 15-25 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 15-25
    • Paumi, C.M.1
  • 83
    • 24744436626 scopus 로고    scopus 로고
    • Large-scale identification of yeast integral membrane protein interactions
    • Miller, J. P. et al. Large-scale identification of yeast integral membrane protein interactions. Proc. Natl Acad. Sci. USA 102 12123-12128 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 12123-12128
    • Miller, J.P.1
  • 84
    • 67349189383 scopus 로고
    • The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain
    • Anfinsen, C. B., Haber, E., Sela, M. & White Jr. F. H. The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain. Proc. Natl Acad. Sci. USA 47, 1309-1314 (1961).
    • (1961) Proc. Natl Acad. Sci. USA , vol.47 , pp. 1309-1314
    • Anfinsen, C.B.1    Haber, E.2    Sela, M.3    White Jr., F.H.4
  • 85
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C. B. Principles that govern the folding of protein chains. Science 181, 223-230 (1973).
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 86
    • 0015239247 scopus 로고
    • The synthesis of ribonuclease A
    • Gutte, B. & Merrifield, R. B. The synthesis of ribonuclease A. J. Biol. Chem. 246, 1922-1941 (1971).
    • (1971) J. Biol. Chem , vol.246 , pp. 1922-1941
    • Gutte, B.1    Merrifield, R.B.2
  • 87
    • 0000356227 scopus 로고
    • On the enzymatic activity of subtilisin-modified ribonuclease
    • Richards, F. M. On the enzymatic activity of subtilisin-modified ribonuclease. Proc. Natl Acad. Sci. USA 44, 162-166 (1958).
    • (1958) Proc. Natl Acad. Sci. USA , vol.44 , pp. 162-166
    • Richards, F.M.1
  • 88
    • 0015217635 scopus 로고
    • Simultaneous formation of two alternative enzymology active structures by complementation of two overlapping fragments of staphylococcal nuclease
    • Taniuchi, H. & Anfinsen, C. B. Simultaneous formation of two alternative enzymology active structures by complementation of two overlapping fragments of staphylococcal nuclease. J. Biol. Chem. 246, 2291-2301 (1971).
    • (1971) J. Biol. Chem , vol.246 , pp. 2291-2301
    • Taniuchi, H.1    Anfinsen, C.B.2
  • 90
    • 0030755307 scopus 로고    scopus 로고
    • Probing minimal independent folding units in dihydrofolate reductase by molecular dissection
    • Gegg, C. V., Bowers, K. E. & Matthews, C. R. Probing minimal independent folding units in dihydrofolate reductase by molecular dissection. Protein Sci. 6, 1885-1892 (1997).
    • (1997) Protein Sci , vol.6 , pp. 1885-1892
    • Gegg, C.V.1    Bowers, K.E.2    Matthews, C.R.3
  • 91
    • 0042268037 scopus 로고    scopus 로고
    • Dynamic visualization of expressed gene networks
    • Remy, I. & Michnick, S. W. Dynamic visualization of expressed gene networks. J. Cell. Physiol. 196, 419-429 (2003).
    • (2003) J. Cell. Physiol , vol.196 , pp. 419-429
    • Remy, I.1    Michnick, S.W.2
  • 93
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu, C. D. & Kerppola, T. K. Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nature Biotech. 21, 539-545 (2003).
    • (2003) Nature Biotech , vol.21 , pp. 539-545
    • Hu, C.D.1    Kerppola, T.K.2
  • 94
    • 33746435428 scopus 로고    scopus 로고
    • An improved mRFP1 adds red to bimolecular fluorescence complementation
    • Jach, G., Pesch, M., Richter, K., Frings, S. & Uhrig, J. F. An improved mRFP1 adds red to bimolecular fluorescence complementation. Nature Methods 3, 597-600 (2006).
    • (2006) Nature Methods , vol.3 , pp. 597-600
    • Jach, G.1    Pesch, M.2    Richter, K.3    Frings, S.4    Uhrig, J.F.5
  • 95
    • 33745234272 scopus 로고    scopus 로고
    • Analysis of G protein βγ dimer formation in live cells using multicolor bimolecular fluorescence complementation demonstrates preferences of β1 for particular γ subunits
    • Mervine, S. M., Yost, E. A., Sabo, J. L., Hynes, T. R. & Berlot, C. H. Analysis of G protein βγ dimer formation in live cells using multicolor bimolecular fluorescence complementation demonstrates preferences of β1 for particular γ subunits. Mol. Pharmacol. 70, 194-205 (2006).
    • (2006) Mol. Pharmacol , vol.70 , pp. 194-205
    • Mervine, S.M.1    Yost, E.A.2    Sabo, J.L.3    Hynes, T.R.4    Berlot, C.H.5
  • 96
    • 2442602269 scopus 로고    scopus 로고
    • Proximal, selective, and dynamic interactions between integrin αllbβ3 and protein tyrosine kinases in living cells
    • de Virgilio, M., Kiosses, W. B. & Shattil, S. J. Proximal, selective, and dynamic interactions between integrin αllbβ3 and protein tyrosine kinases in living cells. J. Cell Biol. 165, 305-311 (2004).
    • (2004) J. Cell Biol , vol.165 , pp. 305-311
    • de Virgilio, M.1    Kiosses, W.B.2    Shattil, S.J.3
  • 97
    • 6944227833 scopus 로고    scopus 로고
    • Ubiquitin-mediated fluorescence complementation reveals that Jun ubiquitinated by Itch/AIP4 is localized to lysosomes
    • Fang, D. & Kerppola, T. K. Ubiquitin-mediated fluorescence complementation reveals that Jun ubiquitinated by Itch/AIP4 is localized to lysosomes. Proc. Natl Acad. Sci. USA 101, 14782-14787 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 14782-14787
    • Fang, D.1    Kerppola, T.K.2
  • 98
    • 7044229949 scopus 로고    scopus 로고
    • Visualization of protein interactions in living plant cells using bimolecular fluorescence complementation
    • Walter, M. et al. Visualization of protein interactions in living plant cells using bimolecular fluorescence complementation. Plant J. 40, 428-438 (2004).
    • (2004) Plant J , vol.40 , pp. 428-438
    • Walter, M.1
  • 99
    • 2942559261 scopus 로고    scopus 로고
    • Visualization of Myc/Max/ Mad family dimers and the competition for dimerization in living cells
    • Grinberg, A. V., Hu, C. D. & Kerppola, T. K. Visualization of Myc/Max/ Mad family dimers and the competition for dimerization in living cells. Mol. Cell. Biol. 24, 4294-4308 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 4294-4308
    • Grinberg, A.V.1    Hu, C.D.2    Kerppola, T.K.3
  • 100
    • 6344237493 scopus 로고    scopus 로고
    • Live cell imaging of Gs and the β2-adrenergic receptor demonstrates that both alphas and β1γ7 internalize upon stimulation and exhibit similar trafficking patterns that differ from that of the β2-adrenergic receptor
    • Hynes, T. R., Mervine, S. M., Yost, E. A., Sabo, J. L. & Berlot, C. H. Live cell imaging of Gs and the β2-adrenergic receptor demonstrates that both alphas and β1γ7 internalize upon stimulation and exhibit similar trafficking patterns that differ from that of the β2-adrenergic receptor. J. Biol. Chem. 279, 44101-44112 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 44101-44112
    • Hynes, T.R.1    Mervine, S.M.2    Yost, E.A.3    Sabo, J.L.4    Berlot, C.H.5
  • 101
    • 23844476035 scopus 로고    scopus 로고
    • Novel fusion protein approach for efficient high-throughput screening of small molecule-mediating protein-protein interactions in cells and living animals
    • Paulmurugan, R. & Gambhir, S. S. Novel fusion protein approach for efficient high-throughput screening of small molecule-mediating protein-protein interactions in cells and living animals. Cancer Res. 65, 7413-7420 (2005).
    • (2005) Cancer Res , vol.65 , pp. 7413-7420
    • Paulmurugan, R.1    Gambhir, S.S.2
  • 102
    • 33748084743 scopus 로고    scopus 로고
    • Binding and stability determinants of the PPARγ nuclear receptor-coactivator interface as revealed by shotgun alanine scanning and in vivo selection
    • Phillips, K. J., Rosenbaum, D. M. & Liu, D. R. Binding and stability determinants of the PPARγ nuclear receptor-coactivator interface as revealed by shotgun alanine scanning and in vivo selection. J. Am. Chem. Soc. 128, 11298-11306 (2006).
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 11298-11306
    • Phillips, K.J.1    Rosenbaum, D.M.2    Liu, D.R.3
  • 103
    • 2642565358 scopus 로고    scopus 로고
    • Transforming a (β/ α)8-barrel enzyme into a split-protein sensor through directed evolution
    • Tafelmeyer, P., Johnsson, N. & Johnsson, K. Transforming a (β/ α)8-barrel enzyme into a split-protein sensor through directed evolution. Chem. Biol. 11, 681-689 (2004).
    • (2004) Chem. Biol , vol.11 , pp. 681-689
    • Tafelmeyer, P.1    Johnsson, N.2    Johnsson, K.3
  • 104
    • 25144503362 scopus 로고    scopus 로고
    • Enhanced catalytic efficiency of aminoglycoside phosphotransferase (3′)-IIa achieved through protein fragmentation and reassembly
    • Paschon, D. E., Patel, Z. S. & Ostermeier, M. Enhanced catalytic efficiency of aminoglycoside phosphotransferase (3′)-IIa achieved through protein fragmentation and reassembly. J. Mol. Biol. 353 26-37 (2005).
    • (2005) J. Mol. Biol , vol.353 , pp. 26-37
    • Paschon, D.E.1    Patel, Z.S.2    Ostermeier, M.3
  • 105
    • 0642365203 scopus 로고    scopus 로고
    • Regulation of Cre recombinase by ligand-induced complementation of inactive fragments
    • Jullien, N., Sampieri, F., Enjalbert, A. & Herman, J. P. Regulation of Cre recombinase by ligand-induced complementation of inactive fragments. Nucleic Acids Res. 31, e131 (2003).
    • (2003) Nucleic Acids Res , vol.31
    • Jullien, N.1    Sampieri, F.2    Enjalbert, A.3    Herman, J.P.4
  • 106
    • 3242715252 scopus 로고    scopus 로고
    • The split-ubiquitin membrane-based yeast two-hybrid system
    • Thaminy, S., Miller, J. & Stagljar, I. The split-ubiquitin membrane-based yeast two-hybrid system. Methods Mol. Biol. 261 297-312 (2004).
    • (2004) Methods Mol. Biol , vol.261 , pp. 297-312
    • Thaminy, S.1    Miller, J.2    Stagljar, I.3
  • 107
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova, G., Pidoux, J., Ullmann, A. & Ladant, D. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc. Natl Acad. Sci. USA 95, 5752-5756 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 108
    • 33751217186 scopus 로고    scopus 로고
    • Monitoring regulated protein-protein interactions using split TEV
    • Wehr, M. C. et al. Monitoring regulated protein-protein interactions using split TEV. Nature Methods 3, 985-993 (2006).
    • (2006) Nature Methods , vol.3 , pp. 985-993
    • Wehr, M.C.1


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