메뉴 건너뛰기




Volumn 45, Issue 5, 2008, Pages 597-604

Detection and localisation of protein-protein interactions in Saccharomyces cerevisiae using a split-GFP method

Author keywords

Biomolecular fluorescence complementation assay; Enhanced green fluorescent protein; Hapto GFP; Isocitrate dehydrogenase; Phosphofructokinase; Protein fragment complementation assay; Succinate dehydrogenase; TRAMP complex

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ENHANCED GREEN FLUORESCENT PROTEIN; IDH1P PROTEIN; IDH2P PROTEIN; MITOCHONDRIAL PROTEIN; MTR4P PROTEIN; PAP2P PROTEIN; SDH3P PROTEIN; SDH4P PROTEIN; UNCLASSIFIED DRUG;

EID: 41649087742     PISSN: 10871845     EISSN: 10960937     Source Type: Journal    
DOI: 10.1016/j.fgb.2008.01.003     Document Type: Article
Times cited : (15)

References (56)
  • 1
    • 34547628842 scopus 로고    scopus 로고
    • Detection of protein-protein interactions using protein-fragment complementation assays (PCA)
    • Barnard E., McFerran N.V., Nelson J., and Timson D.J. Detection of protein-protein interactions using protein-fragment complementation assays (PCA). Curr. Proteomics 4 (2007) 17-27
    • (2007) Curr. Proteomics , vol.4 , pp. 17-27
    • Barnard, E.1    McFerran, N.V.2    Nelson, J.3    Timson, D.J.4
  • 2
    • 0015221183 scopus 로고
    • Yeast diphosphopyridine nucleotide specific isocitrate dehydrogenase. Purification and some properties
    • Barnes L.D., Kuehn G.D., and Atkinson D.E. Yeast diphosphopyridine nucleotide specific isocitrate dehydrogenase. Purification and some properties. Biochemistry 10 (1971) 3939-3944
    • (1971) Biochemistry , vol.10 , pp. 3939-3944
    • Barnes, L.D.1    Kuehn, G.D.2    Atkinson, D.E.3
  • 3
    • 0027255909 scopus 로고
    • Elimination of false positives that arise in using the two-hybrid system
    • Bartel P., Chien C.T., Sternglanz R., and Fields S. Elimination of false positives that arise in using the two-hybrid system. BioTechniques 14 (1993) 920-924
    • (1993) BioTechniques , vol.14 , pp. 920-924
    • Bartel, P.1    Chien, C.T.2    Sternglanz, R.3    Fields, S.4
  • 5
    • 7044239645 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in plants using bimolecular fluorescence complementation
    • Bracha-Drori K., Shichrur K., Katz A., Oliva M., Angelovici R., Yalovsky S., and Ohad N. Detection of protein-protein interactions in plants using bimolecular fluorescence complementation. Plant J. 40 (2004) 419-427
    • (2004) Plant J. , vol.40 , pp. 419-427
    • Bracha-Drori, K.1    Shichrur, K.2    Katz, A.3    Oliva, M.4    Angelovici, R.5    Yalovsky, S.6    Ohad, N.7
  • 6
    • 14044251591 scopus 로고    scopus 로고
    • Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane
    • Campanella M.E., Chu H., and Low P.S. Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane. Proc. Natl. Acad. Sci. USA 102 (2005) 2402-2407
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2402-2407
    • Campanella, M.E.1    Chu, H.2    Low, P.S.3
  • 7
    • 0029393978 scopus 로고
    • Green fluorescent protein
    • Chalfie M. Green fluorescent protein. Photochem. Photobiol. 62 (1995) 651-656
    • (1995) Photochem. Photobiol. , vol.62 , pp. 651-656
    • Chalfie, M.1
  • 8
    • 0025940629 scopus 로고
    • The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest
    • Chien C.T., Bartel P.L., Sternglanz R., and Fields S. The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest. Proc. Natl. Acad. Sci. USA 88 (1991) 9578-9582
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9578-9582
    • Chien, C.T.1    Bartel, P.L.2    Sternglanz, R.3    Fields, S.4
  • 10
    • 0020481613 scopus 로고
    • Mutant studies of yeast phosphofructokinase
    • Clifton D., and Fraenkel D.G. Mutant studies of yeast phosphofructokinase. Biochemistry 21 (1982) 1935-1942
    • (1982) Biochemistry , vol.21 , pp. 1935-1942
    • Clifton, D.1    Fraenkel, D.G.2
  • 11
    • 0027465627 scopus 로고
    • Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein
    • Cody C.W., Prasher D.C., Westler W.M., Prendergast F.G., and Ward W.W. Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein. Biochemistry 32 (1993) 1212-1218
    • (1993) Biochemistry , vol.32 , pp. 1212-1218
    • Cody, C.W.1    Prasher, D.C.2    Westler, W.M.3    Prendergast, F.G.4    Ward, W.W.5
  • 12
    • 33947632303 scopus 로고    scopus 로고
    • Use of bimolecular fluorescence complementation to study in vivo interactions between Cdc42p and Rdi1p of Saccharomyces cerevisiae
    • Cole K.C., McLaughlin H.W., and Johnson D.I. Use of bimolecular fluorescence complementation to study in vivo interactions between Cdc42p and Rdi1p of Saccharomyces cerevisiae. Eukaryot. Cell. 6 (2007) 378-387
    • (2007) Eukaryot. Cell. , vol.6 , pp. 378-387
    • Cole, K.C.1    McLaughlin, H.W.2    Johnson, D.I.3
  • 13
    • 0026784538 scopus 로고
    • +-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae
    • +-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae. J. Biol. Chem. 267 (1992) 16417-16423
    • (1992) J. Biol. Chem. , vol.267 , pp. 16417-16423
    • Cupp, J.R.1    McAlister-Henn, L.2
  • 14
    • 0025841651 scopus 로고
    • +-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae
    • +-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae. J. Biol. Chem. 266 (1991) 22199-22205
    • (1991) J. Biol. Chem. , vol.266 , pp. 22199-22205
    • Cupp, J.R.1    McAlister-Henn, L.2
  • 15
    • 0032481316 scopus 로고    scopus 로고
    • Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3′ end formation of 58S rRNA in Saccharomyces cerevisiae
    • de la Cruz J., Kressler D., Tollervey D., and Linder P. Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3′ end formation of 58S rRNA in Saccharomyces cerevisiae. EMBO J. 17 (1998) 1128-1140
    • (1998) EMBO J. , vol.17 , pp. 1128-1140
    • de la Cruz, J.1    Kressler, D.2    Tollervey, D.3    Linder, P.4
  • 16
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S., and Song O. A novel genetic system to detect protein-protein interactions. Nature 340 (1989) 245-246
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 17
    • 0035984722 scopus 로고    scopus 로고
    • Beta-lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions
    • Galarneau A., Primeau M., Trudeau L.E., and Michnick S.W. Beta-lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions. Nat. Biotechnol. 20 (2002) 619-622
    • (2002) Nat. Biotechnol. , vol.20 , pp. 619-622
    • Galarneau, A.1    Primeau, M.2    Trudeau, L.E.3    Michnick, S.W.4
  • 19
    • 0034647238 scopus 로고    scopus 로고
    • Antiparallel leucine zipper-directed protein reassembly: application to the green fluorescent protein
    • Ghosh I., Hamilton A.D., and Regan L. Antiparallel leucine zipper-directed protein reassembly: application to the green fluorescent protein. J. Am. Chem. Soc. 122 (2000) 5658-5659
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5658-5659
    • Ghosh, I.1    Hamilton, A.D.2    Regan, L.3
  • 20
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • Gietz R.D., and Woods R.A. Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol. 350 (2002) 87-96
    • (2002) Methods Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 22
    • 0003293418 scopus 로고
    • On the Nature of the Function Expressive of the Law of Human Mortality, and on a New Mode of Determining the Value of Life Contingencies
    • Gompertz B. On the Nature of the Function Expressive of the Law of Human Mortality, and on a New Mode of Determining the Value of Life Contingencies. Phil. Trans. R. Soc. 115 (1825) 513-585
    • (1825) Phil. Trans. R. Soc. , vol.115 , pp. 513-585
    • Gompertz, B.1
  • 23
    • 0018668105 scopus 로고
    • The interaction of phosphofructokinase with erythrocyte membranes
    • Higashi T., Richards C.S., and Uyeda K. The interaction of phosphofructokinase with erythrocyte membranes. J. Biol. Chem. 254 (1979) 9542-9550
    • (1979) J. Biol. Chem. , vol.254 , pp. 9542-9550
    • Higashi, T.1    Richards, C.S.2    Uyeda, K.3
  • 24
    • 13644251429 scopus 로고    scopus 로고
    • Use of bimolecular fluorescence complementation to demonstrate transcription factor interaction in nuclei of living cells from the filamentous fungus Acremonium chrysogenum
    • Hoff B., and Kuck U. Use of bimolecular fluorescence complementation to demonstrate transcription factor interaction in nuclei of living cells from the filamentous fungus Acremonium chrysogenum. Curr. Genet. 47 (2005) 132-138
    • (2005) Curr. Genet. , vol.47 , pp. 132-138
    • Hoff, B.1    Kuck, U.2
  • 25
    • 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., and Kerppola T.K. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9 (2002) 789-798
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 26
    • 0028080090 scopus 로고
    • Split ubiquitin as a sensor of protein interactions in vivo
    • Johnsson N., and Varshavsky A. Split ubiquitin as a sensor of protein interactions in vivo. Proc. Natl. Acad. Sci. USA 91 (1994) 10340-10344
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10340-10344
    • Johnsson, N.1    Varshavsky, A.2
  • 27
    • 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., and Umezawa Y. Locating a protein-protein interaction in living cells via split Renilla luciferase complementation. Anal. Chem. 75 (2003) 4176-4181
    • (2003) Anal. Chem. , vol.75 , pp. 4176-4181
    • Kaihara, A.1    Kawai, Y.2    Sato, M.3    Ozawa, T.4    Umezawa, Y.5
  • 28
    • 0025280662 scopus 로고
    • Subunit structure, expression, and function of NAD(H)-specific isocitrate dehydrogenase in Saccharomyces cerevisiae
    • Keys D.A., and McAlister-Henn L. Subunit structure, expression, and function of NAD(H)-specific isocitrate dehydrogenase in Saccharomyces cerevisiae. J. Bacteriol. 172 (1990) 4280-4287
    • (1990) J. Bacteriol. , vol.172 , pp. 4280-4287
    • Keys, D.A.1    McAlister-Henn, L.2
  • 29
    • 0017759685 scopus 로고
    • Physicochemical parameters and subunit composition of yeast phosphofructokinase
    • Kopperschlager G., Bar J., Nissler K., and Hofmann E. Physicochemical parameters and subunit composition of yeast phosphofructokinase. Eur. J. Biochem. 81 (1977) 317-325
    • (1977) Eur. J. Biochem. , vol.81 , pp. 317-325
    • Kopperschlager, G.1    Bar, J.2    Nissler, K.3    Hofmann, E.4
  • 31
    • 0013458648 scopus 로고    scopus 로고
    • Analysis of protein-protein proximities using the split-ubiquitin system
    • Lehming N. Analysis of protein-protein proximities using the split-ubiquitin system. Brief Funct. Genomic Proteomic 1 (2002) 230-238
    • (2002) Brief Funct. Genomic Proteomic , vol.1 , pp. 230-238
    • Lehming, N.1
  • 32
    • 0029760875 scopus 로고    scopus 로고
    • A DEAD-box-family protein is required for nucleocytoplasmic transport of yeast mRNA
    • Liang S., Hitomi M., Hu Y.H., Liu Y., and Tartakoff A.M. A DEAD-box-family protein is required for nucleocytoplasmic transport of yeast mRNA. Mol. Cell. Biol. 16 (1996) 5139-5146
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5139-5146
    • Liang, S.1    Hitomi, M.2    Hu, Y.H.3    Liu, Y.4    Tartakoff, A.M.5
  • 33
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine M.S., McKenzie III A., Demarini D.J., Shah N.G., Wach A., Brachat A., Philippsen P., and Pringle J.R. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14 (1998) 953-961
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 34
    • 11844252081 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism
    • Magliery T.J., Wilson C.G., Pan W., Mishler D., Ghosh I., Hamilton A.D., and Regan L. Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism. J. Am. Chem. Soc. 127 (2005) 146-157
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 146-157
    • Magliery, T.J.1    Wilson, C.G.2    Pan, W.3    Mishler, D.4    Ghosh, I.5    Hamilton, A.D.6    Regan, L.7
  • 36
    • 0344687406 scopus 로고    scopus 로고
    • Protein fragment complementation strategies for biochemical network mapping
    • Michnick S.W. Protein fragment complementation strategies for biochemical network mapping. Curr. Opin. Biotechnol. 14 (2003) 610-617
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 610-617
    • Michnick, S.W.1
  • 37
    • 34247525991 scopus 로고    scopus 로고
    • Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case
    • Morell M., Espargaro A., Aviles F.X., and Ventura S. Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case. Proteomics 7 (2007) 1023-1036
    • (2007) Proteomics , vol.7 , pp. 1023-1036
    • Morell, M.1    Espargaro, A.2    Aviles, F.X.3    Ventura, S.4
  • 38
    • 33947248700 scopus 로고    scopus 로고
    • A split enhanced green fluorescent protein-based reporter in yeast two-hybrid system
    • Park K., Yi S.Y., Lee C.S., Kim K.E., Pai H.S., Seol D.W., Chung B.H., and Kim M. A split enhanced green fluorescent protein-based reporter in yeast two-hybrid system. Protein J. 26 (2007) 107-116
    • (2007) Protein J. , vol.26 , pp. 107-116
    • Park, K.1    Yi, S.Y.2    Lee, C.S.3    Kim, K.E.4    Pai, H.S.5    Seol, D.W.6    Chung, B.H.7    Kim, M.8
  • 39
    • 0032514623 scopus 로고    scopus 로고
    • Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments
    • Pelletier J.N., Campbell-Valois F.X., and Michnick S.W. Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments. Proc. Natl. Acad. Sci. USA 95 (1998) 12141-12146
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12141-12146
    • Pelletier, J.N.1    Campbell-Valois, F.X.2    Michnick, S.W.3
  • 41
    • 1542375250 scopus 로고    scopus 로고
    • A cDNA library functional screening strategy based on fluorescent protein complementation assays to identify novel components of signaling pathways
    • Remy I., and Michnick S.W. A cDNA library functional screening strategy based on fluorescent protein complementation assays to identify novel components of signaling pathways. Methods 32 (2004) 381-388
    • (2004) Methods , vol.32 , pp. 381-388
    • Remy, I.1    Michnick, S.W.2
  • 42
    • 0842304224 scopus 로고    scopus 로고
    • Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt
    • Remy I., and Michnick S.W. Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt. Mol. Cell. Biol. 24 (2004) 1493-1504
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1493-1504
    • Remy, I.1    Michnick, S.W.2
  • 43
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G., Shevchenko A., Rutz B., Wilm M., Mann M., and Seraphin B. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17 (1999) 1030-1032
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 44
    • 0030738524 scopus 로고    scopus 로고
    • Monitoring protein-protein interactions in intact eukaryotic cells by beta-galactosidase complementation
    • Rossi F., Charlton C.A., and Blau H.M. Monitoring protein-protein interactions in intact eukaryotic cells by beta-galactosidase complementation. Proc. Natl. Acad. Sci. USA 94 (1997) 8405-8410
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8405-8410
    • Rossi, F.1    Charlton, C.A.2    Blau, H.M.3
  • 45
    • 4143070653 scopus 로고    scopus 로고
    • What's in a picture? The temptation of image manipulation
    • Rossner M., and Yamada K.M. What's in a picture? The temptation of image manipulation. J. Cell. Biol. 166 (2004) 11-15
    • (2004) J. Cell. Biol. , vol.166 , pp. 11-15
    • Rossner, M.1    Yamada, K.M.2
  • 46
    • 0037416207 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations
    • Sekar R.B., and Periasamy A. Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations. J. Cell Biol. 160 (2003) 629-633
    • (2003) J. Cell Biol. , vol.160 , pp. 629-633
    • Sekar, R.B.1    Periasamy, A.2
  • 47
    • 0033960424 scopus 로고    scopus 로고
    • Approaches to detecting false positives in yeast two-hybrid systems
    • Serebriiskii I., Estojak J., Berman M., and Golemis E.A. Approaches to detecting false positives in yeast two-hybrid systems. BioTechniques 28 (2000) 328-336
    • (2000) BioTechniques , vol.28 , pp. 328-336
    • Serebriiskii, I.1    Estojak, J.2    Berman, M.3    Golemis, E.A.4
  • 48
    • 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., and 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 (1998) 5187-5192
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5187-5192
    • Stagljar, I.1    Korostensky, C.2    Johnsson, N.3    te Heesen, S.4
  • 49
    • 34548680957 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation analysis system for in vivo detection of protein-protein interaction in Saccharomyces cerevisiae
    • Sung M.K., and Huh W.K. Bimolecular fluorescence complementation analysis system for in vivo detection of protein-protein interaction in Saccharomyces cerevisiae. Yeast 24 (2007) 767-775
    • (2007) Yeast , vol.24 , pp. 767-775
    • Sung, M.K.1    Huh, W.K.2
  • 50
    • 0035442412 scopus 로고    scopus 로고
    • The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo
    • Truong K., and Ikura M. The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo. Curr. Opin. Struct. Biol. 11 (2001) 573-578
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 573-578
    • Truong, K.1    Ikura, M.2
  • 53
    • 0032957639 scopus 로고    scopus 로고
    • Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange site-directed mutagenesis
    • Wang W., and Malcolm B.A. Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange site-directed mutagenesis. BioTechniques 26 (1999) 680-682
    • (1999) BioTechniques , vol.26 , pp. 680-682
    • Wang, W.1    Malcolm, B.A.2
  • 54
    • 0035227656 scopus 로고    scopus 로고
    • High-efficiency transformation of plasmid DNA into yeast
    • Woods R.A., and Gietz R.D. High-efficiency transformation of plasmid DNA into yeast. Methods Mol. Biol. 177 (2001) 85-97
    • (2001) Methods Mol. Biol. , vol.177 , pp. 85-97
    • Woods, R.A.1    Gietz, R.D.2
  • 55
    • 0029739903 scopus 로고    scopus 로고
    • Quantitation of putative activator-target affinities predicts transcriptional activating potentials
    • Wu Y., Reece R.J., and Ptashne M. Quantitation of putative activator-target affinities predicts transcriptional activating potentials. EMBO J. 15 (1996) 3951-3963
    • (1996) EMBO J. , vol.15 , pp. 3951-3963
    • Wu, Y.1    Reece, R.J.2    Ptashne, M.3
  • 56
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang F., Moss L.G., and Phillips Jr. G.N. The molecular structure of green fluorescent protein. Nat. Biotechnol. 14 (1996) 1246-1251
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.