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Volumn 12, Issue 7, 2005, Pages 847-855

Ligand-regulated peptides: A general approach for modulating protein-peptide interactions with small molecules

Author keywords

[No Author keywords available]

Indexed keywords

5' AMP ACTIVATED PROTEIN KINASE; 5'-AMP-ACTIVATED PROTEIN KINASE; FK 506 BINDING PROTEIN; GLUTATHIONE TRANSFERASE; LIGAND; MULTIENZYME COMPLEX; PEPTIDE; PEPTIDE LIBRARY; PROTEIN KINASE P60; PROTEIN SERINE THREONINE KINASE; RETINOBLASTOMA PROTEIN;

EID: 22544454196     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2005.05.021     Document Type: Article
Times cited : (8)

References (57)
  • 1
    • 0035491607 scopus 로고    scopus 로고
    • Conditional control of gene expression in the mouse
    • M. Lewandoski Conditional control of gene expression in the mouse Nat. Rev. Genet. 2 2001 743 755
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 743-755
    • Lewandoski, M.1
  • 2
    • 0036956875 scopus 로고    scopus 로고
    • Studying gene function in eukaryotes by conditional gene inactivation
    • M. Gossen, and H. Bujard Studying gene function in eukaryotes by conditional gene inactivation Annu. Rev. Genet. 36 2002 153 173
    • (2002) Annu. Rev. Genet. , vol.36 , pp. 153-173
    • Gossen, M.1    Bujard, H.2
  • 3
    • 0037062951 scopus 로고    scopus 로고
    • RNA interference
    • G.J. Hannon RNA interference Nature 418 2002 244 251
    • (2002) Nature , vol.418 , pp. 244-251
    • Hannon, G.J.1
  • 4
    • 0037416141 scopus 로고    scopus 로고
    • The small-molecule approach to biology
    • S.L. Schreiber The small-molecule approach to biology Chem. Eng. News 81 2003 51 61
    • (2003) Chem. Eng. News , vol.81 , pp. 51-61
    • Schreiber, S.L.1
  • 5
    • 0029876415 scopus 로고    scopus 로고
    • Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2
    • P. Colas, B. Cohen, T. Jessen, I. Grishina, J. McCoy, and R. Brent Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2 Nature 380 1996 548 550
    • (1996) Nature , vol.380 , pp. 548-550
    • Colas, P.1    Cohen, B.2    Jessen, T.3    Grishina, I.4    McCoy, J.5    Brent, R.6
  • 6
    • 0036843787 scopus 로고    scopus 로고
    • In vivo-applied functional RNAs as tools in proteomics and genomics research
    • M. Famulok, and S. Verma In vivo-applied functional RNAs as tools in proteomics and genomics research Trends Biotechnol. 20 2002 462 466
    • (2002) Trends Biotechnol. , vol.20 , pp. 462-466
    • Famulok, M.1    Verma, S.2
  • 9
    • 0030296634 scopus 로고    scopus 로고
    • Three-part inventions: Intracellular signaling and induced proximity
    • G.R. Crabtree, and S.L. Schreiber Three-part inventions: Intracellular signaling and induced proximity Trends Biochem. Sci. 21 1996 418 422
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 418-422
    • Crabtree, G.R.1    Schreiber, S.L.2
  • 10
    • 0023665149 scopus 로고
    • A mutation that alters the nucleotide specificity of elongation factor-Tu, a Gtp regulatory protein
    • Y.W. Hwang, and D.L. Miller A mutation that alters the nucleotide specificity of elongation factor-Tu, a Gtp regulatory protein J. Biol. Chem. 262 1987 13081 13085
    • (1987) J. Biol. Chem. , vol.262 , pp. 13081-13085
    • Hwang, Y.W.1    Miller, D.L.2
  • 12
    • 0030887842 scopus 로고    scopus 로고
    • Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates
    • K. Shah, Y. Liu, C. Deirmengian, and K.M. Shokat Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates Proc. Natl. Acad. Sci. USA 94 1997 3565 3570
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3565-3570
    • Shah, K.1    Liu, Y.2    Deirmengian, C.3    Shokat, K.M.4
  • 13
    • 0037101904 scopus 로고    scopus 로고
    • Novel chemical genetic approaches to the discovery of signal transduction inhibitors
    • K. Shokat, and M. Velleca Novel chemical genetic approaches to the discovery of signal transduction inhibitors Drug Discov. Today 7 2002 872 879
    • (2002) Drug Discov. Today , vol.7 , pp. 872-879
    • Shokat, K.1    Velleca, M.2
  • 14
    • 0034787013 scopus 로고    scopus 로고
    • Tools for dissecting signaling pathways in vivo: Receptors activated solely by synthetic ligands
    • K. Scearce-Levie, P. Coward, C.H. Redfern, and B.R. Conklin Tools for dissecting signaling pathways in vivo: Receptors activated solely by synthetic ligands Methods Enzymol. 343 2002 232 248
    • (2002) Methods Enzymol. , vol.343 , pp. 232-248
    • Scearce-Levie, K.1    Coward, P.2    Redfern, C.H.3    Conklin, B.R.4
  • 15
    • 0023789310 scopus 로고
    • A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptor
    • D. Picard, S.J. Salser, and K.R. Yamamoto A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptor Cell 54 1988 1073 1080
    • (1988) Cell , vol.54 , pp. 1073-1080
    • Picard, D.1    Salser, S.J.2    Yamamoto, K.R.3
  • 16
    • 0026485739 scopus 로고
    • Acetylcholine-receptor channel structure probed in cysteine-substitution mutants
    • M.H. Akabas, D.A. Stauffer, M. Xu, and A. Karlin Acetylcholine-receptor channel structure probed in cysteine-substitution mutants Science 258 1992 307 310
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 17
    • 0035313222 scopus 로고    scopus 로고
    • Cysteine mutants as chemical sensors for ligand-receptor interactions
    • B. Foucaud, P. Ferret, T. Grutter, and M. Goeldner Cysteine mutants as chemical sensors for ligand-receptor interactions Trends Pharmacol. Sci. 22 2001 170 173
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 170-173
    • Foucaud, B.1    Ferret, P.2    Grutter, T.3    Goeldner, M.4
  • 18
    • 0038143609 scopus 로고    scopus 로고
    • Selective inhibition of engineered receptors via proximity-accelerated alkylation
    • K. Levitsky, C.J. Ciolli, and P.J. Belshaw Selective inhibition of engineered receptors via proximity-accelerated alkylation Org. Lett. 5 2003 693 696
    • (2003) Org. Lett. , vol.5 , pp. 693-696
    • Levitsky, K.1    Ciolli, C.J.2    Belshaw, P.J.3
  • 19
    • 0035925207 scopus 로고    scopus 로고
    • A subtype-selective thyromimetic designed to bind a mutant thyroid hormone receptor implicated in resistance to thyroid hormone
    • H.F. Ye, K.E. O'Reilly, and J.T. Koh A subtype-selective thyromimetic designed to bind a mutant thyroid hormone receptor implicated in resistance to thyroid hormone J. Am. Chem. Soc. 123 2001 1521 1522
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1521-1522
    • Ye, H.F.1    O'Reilly, K.E.2    Koh, J.T.3
  • 20
    • 0001474784 scopus 로고    scopus 로고
    • Rational design of vitamin D-3 analogues which selectively restore activity to a vitamin D receptor mutant associated with rickets
    • S.L. Swann, J.J. Bergh, M.C. Farach-Carson, and J.T. Koh Rational design of vitamin D-3 analogues which selectively restore activity to a vitamin D receptor mutant associated with rickets Org. Lett. 4 2002 3863 3866
    • (2002) Org. Lett. , vol.4 , pp. 3863-3866
    • Swann, S.L.1    Bergh, J.J.2    Farach-Carson, M.C.3    Koh, J.T.4
  • 21
    • 0023666091 scopus 로고
    • The inducible Iac operator-repressor system is functional in mammalian-cells
    • M.C.T. Hu, and N. Davidson The inducible Iac operator-repressor system is functional in mammalian-cells Cell 48 1987 555 566
    • (1987) Cell , vol.48 , pp. 555-566
    • Hu, M.C.T.1    Davidson, N.2
  • 23
    • 0030013607 scopus 로고    scopus 로고
    • Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins
    • P.J. Belshaw, S.N. Ho, G.R. Crabtree, and S.L. Schreiber Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins Proc. Natl. Acad. Sci. USA 93 1996 4604 4607
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4604-4607
    • Belshaw, P.J.1    Ho, S.N.2    Crabtree, G.R.3    Schreiber, S.L.4
  • 24
    • 1842298127 scopus 로고    scopus 로고
    • Selective targeting and inhibition of yeast RNA polymerase II by RNA aptamers
    • M. Thomas, S. Chedin, C. Carles, M. Riva, M. Famulok, and A. Sentenac Selective targeting and inhibition of yeast RNA polymerase II by RNA aptamers J. Biol. Chem. 272 1997 27980 27986
    • (1997) J. Biol. Chem. , vol.272 , pp. 27980-27986
    • Thomas, M.1    Chedin, S.2    Carles, C.3    Riva, M.4    Famulok, M.5    Sentenac, A.6
  • 25
    • 0031691987 scopus 로고    scopus 로고
    • Controlling gene expression using synthetic ligands
    • V.M. Rivera Controlling gene expression using synthetic ligands Methods 14 1998 421 429
    • (1998) Methods , vol.14 , pp. 421-429
    • Rivera, V.M.1
  • 26
    • 0032500736 scopus 로고    scopus 로고
    • Controlling gene expression in living cells through small molecule-RNA interactions
    • G. Werstuck, and M.R. Green Controlling gene expression in living cells through small molecule-RNA interactions Science 282 1998 296 298
    • (1998) Science , vol.282 , pp. 296-298
    • Werstuck, G.1    Green, M.R.2
  • 27
    • 0032799637 scopus 로고    scopus 로고
    • Antiprogestin regulable gene switch for induction of gene expression in vivo
    • Y.L. Wang, S.Y. Tsai, and B.W. O'Malley Antiprogestin regulable gene switch for induction of gene expression in vivo Methods Enzymol. 306 1999 281 294
    • (1999) Methods Enzymol. , vol.306 , pp. 281-294
    • Wang, Y.L.1    Tsai, S.Y.2    O'Malley, B.W.3
  • 28
    • 4344646564 scopus 로고    scopus 로고
    • Engineering a ligand-dependent RNA transcriptional activator
    • A.R. Buskirk, A. Landrigan, and D.R. Liu Engineering a ligand-dependent RNA transcriptional activator Chem. Biol. 11 2004 1157 1163
    • (2004) Chem. Biol. , vol.11 , pp. 1157-1163
    • Buskirk, A.R.1    Landrigan, A.2    Liu, D.R.3
  • 30
    • 0036669759 scopus 로고    scopus 로고
    • Controlling protein activity with ligand-regulated RNA aptamers
    • M. Vuyisich, and P.A. Beal Controlling protein activity with ligand-regulated RNA aptamers Chem. Biol. 9 2002 907 913
    • (2002) Chem. Biol. , vol.9 , pp. 907-913
    • Vuyisich, M.1    Beal, P.A.2
  • 32
    • 11144330098 scopus 로고    scopus 로고
    • Natural and engineered nucleic acids as tools to explore biology
    • R.R. Breaker Natural and engineered nucleic acids as tools to explore biology Nature 432 2004 838 845
    • (2004) Nature , vol.432 , pp. 838-845
    • Breaker, R.R.1
  • 34
    • 3342931068 scopus 로고    scopus 로고
    • A mechanism-based cross-linker for the identification of kinase-substrate pairs
    • D.J. Maly, J.A. Allen, and K.M. Shokat A mechanism-based cross-linker for the identification of kinase-substrate pairs J. Am. Chem. Soc. 126 2004 9160 9161
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9160-9161
    • Maly, D.J.1    Allen, J.A.2    Shokat, K.M.3
  • 35
    • 0024442393 scopus 로고
    • A cytosolic binding-protein for the immunosuppressant Fk506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
    • J.J. Siekierka, S.H.Y. Hung, M. Poe, C.S. Lin, and N.H. Sigal A cytosolic binding-protein for the immunosuppressant Fk506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin Nature 341 1989 755 757
    • (1989) Nature , vol.341 , pp. 755-757
    • Siekierka, J.J.1    Hung, S.H.Y.2    Poe, M.3    Lin, C.S.4    Sigal, N.H.5
  • 36
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant Fk506 is a cis-trans peptidyl-prolyl isomerase
    • M.W. Harding, A. Galat, D.E. Uehling, and S.L. Schreiber A receptor for the immunosuppressant Fk506 is a cis-trans peptidyl-prolyl isomerase Nature 341 1989 758 760
    • (1989) Nature , vol.341 , pp. 758-760
    • Harding, M.W.1    Galat, A.2    Uehling, D.E.3    Schreiber, S.L.4
  • 37
    • 0029055145 scopus 로고
    • Identification of an 11-kDa Fkbp12-rapamycin-binding domain within the 289-kDa Fkbp12-rapamycin-associated protein and characterization of a critical serine residue
    • J. Chen, X.F. Zheng, E.J. Brown, and S.L. Schreiber Identification of an 11-kDa Fkbp12-rapamycin-binding domain within the 289-kDa Fkbp12-rapamycin- associated protein and characterization of a critical serine residue Proc. Natl. Acad. Sci. USA 92 1995 4947 4951
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4947-4951
    • Chen, J.1    Zheng, X.F.2    Brown, E.J.3    Schreiber, S.L.4
  • 38
    • 0025776523 scopus 로고
    • Targets for cell-cycle arrest by the immunosuppressant rapamycin in yeast
    • J. Heitman, N.R. Movva, and M.N. Hall Targets for cell-cycle arrest by the immunosuppressant rapamycin in yeast Science 253 1991 905 909
    • (1991) Science , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 39
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP
    • J.W. Choi, J. Chen, S.L. Schreiber, and J. Clardy Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP Science 273 1996 239 242
    • (1996) Science , vol.273 , pp. 239-242
    • Choi, J.W.1    Chen, J.2    Schreiber, S.L.3    Clardy, J.4
  • 40
    • 0642365203 scopus 로고    scopus 로고
    • Regulation of Cre recombinase by ligand-induced complementation of inactive fragments
    • N. Jullien, F. Sampieri, A. Enjalbert, and J.P. Herman Regulation of Cre recombinase by ligand-induced complementation of inactive fragments Nucleic Acids Res. 31 2003 e131
    • (2003) Nucleic Acids Res. , vol.31 , pp. 131
    • Jullien, N.1    Sampieri, F.2    Enjalbert, A.3    Herman, J.P.4
  • 41
    • 2642601106 scopus 로고    scopus 로고
    • Structure of the retinoblastoma tumor-suppressor pocket domain bound to a peptide from HPV E7
    • J. Lee, A.A. Russo, and N.P. Pavletich Structure of the retinoblastoma tumor-suppressor pocket domain bound to a peptide from HPV E7 Nature 391 1998 859 865
    • (1998) Nature , vol.391 , pp. 859-865
    • Lee, J.1    Russo, A.A.2    Pavletich, N.P.3
  • 44
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • S. Feng, J.K. Chen, H. Yu, J.A. Simon, and S.L. Schreiber Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions Science 266 1994 1241 1247
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 45
    • 0035958959 scopus 로고    scopus 로고
    • Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions
    • P. Pellicena, and W.T. Miller Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions J. Biol. Chem. 276 2001 28190 28196
    • (2001) J. Biol. Chem. , vol.276 , pp. 28190-28196
    • Pellicena, P.1    Miller, W.T.2
  • 46
    • 0028593398 scopus 로고
    • Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of Gp41 from HIV
    • K. Lim, J.X. Ho, K. Keeling, G.L. Gilliland, X.H. Ji, F. Ruker, and D.C. Carter Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of Gp41 from HIV Protein Sci. 3 1994 2233 2244
    • (1994) Protein Sci. , vol.3 , pp. 2233-2244
    • Lim, K.1    Ho, J.X.2    Keeling, K.3    Gilliland, G.L.4    Ji, X.H.5    Ruker, F.6    Carter, D.C.7
  • 47
    • 0030878873 scopus 로고    scopus 로고
    • Inducible gene expression and protein translocation using nontoxic ligands identified by a mammalian three-hybrid screen
    • S.D. Liberles, S.T. Diver, D.J. Austin, and S.L. Schreiber Inducible gene expression and protein translocation using nontoxic ligands identified by a mammalian three-hybrid screen Proc. Natl. Acad. Sci. USA 94 1997 7825 7830
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7825-7830
    • Liberles, S.D.1    Diver, S.T.2    Austin, D.J.3    Schreiber, S.L.4
  • 48
    • 0036169663 scopus 로고    scopus 로고
    • A system for small-molecule control of conditionally replication- competent adenoviral vectors
    • H. Chong, A. Ruchatz, T. Clackson, V.M. Rivera, and R.G. Vile A system for small-molecule control of conditionally replication-competent adenoviral vectors Mol. Ther. 5 2002 195 203
    • (2002) Mol. Ther. , vol.5 , pp. 195-203
    • Chong, H.1    Ruchatz, A.2    Clackson, T.3    Rivera, V.M.4    Vile, R.G.5
  • 49
    • 0030853257 scopus 로고    scopus 로고
    • Effect of nitrogen source on biosynthesis of rapamycin by Streptomyces hygroscopicus
    • M.S. Lee, I. Kojima, and A.L. Demain Effect of nitrogen source on biosynthesis of rapamycin by Streptomyces hygroscopicus J. Ind. Microbiol. Biotechnol. 19 1997 83 86
    • (1997) J. Ind. Microbiol. Biotechnol. , vol.19 , pp. 83-86
    • Lee, M.S.1    Kojima, I.2    Demain, A.L.3
  • 50
    • 0023245677 scopus 로고
    • FK-506, a novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics
    • T. Kino, H. Hatanaka, M. Hashimoto, M. Nishiyama, T. Goto, M. Okuhara, M. Kohsaka, H. Aoki, and H. Imanaka FK-506, a novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics J. Antibiot. (Tokyo) 40 1987 1249 1255
    • (1987) J. Antibiot. (Tokyo) , vol.40 , pp. 1249-1255
    • Kino, T.1    Hatanaka, H.2    Hashimoto, M.3    Nishiyama, M.4    Goto, T.5    Okuhara, M.6    Kohsaka, M.7    Aoki, H.8    Imanaka, H.9
  • 51
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • P. James, J. Halladay, and E.A. Craig Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast Genetics 144 1996 1425 1436
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 52
    • 0028825698 scopus 로고
    • TOR mutations confer rapamycin resistance by preventing interaction with FKBP12-rapamycin
    • M.C. Lorenz, and J. Heitman TOR mutations confer rapamycin resistance by preventing interaction with FKBP12-rapamycin J. Biol. Chem. 270 1995 27531 27537
    • (1995) J. Biol. Chem. , vol.270 , pp. 27531-27537
    • Lorenz, M.C.1    Heitman, J.2
  • 53
    • 0028598672 scopus 로고
    • Rapt1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex
    • M.I. Chiu, H. Katz, and V. Berlin Rapt1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex Proc. Natl. Acad. Sci. USA 91 1994 12574 12578
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12574-12578
    • Chiu, M.I.1    Katz, H.2    Berlin, V.3
  • 54
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae
    • A. Wach PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae Yeast 12 1996 259 265
    • (1996) Yeast , vol.12 , pp. 259-265
    • Wach, A.1
  • 55
    • 22544478681 scopus 로고    scopus 로고
    • Peptide aptamers: Dominant "genetic" agents for forward and reverse analysis of cellular processes
    • F.M. Ausubel R. Brent R.E. Kingston D.D. Moore J.G. Seidman J.A. Smith K. Struhl:John Wiley and Sons, Inc. New York
    • C.R. Geyer Peptide aptamers: Dominant "genetic" agents for forward and reverse analysis of cellular processes F.M. Ausubel R. Brent R.E. Kingston D.D. Moore J.G. Seidman J.A. Smith K. Struhl Current Protocols in Molecular Biology 2000:John Wiley and Sons, Inc. New York 24.24.21 24.24.25
    • (2000) Current Protocols in Molecular Biology , pp. 242421-242425
    • Geyer, C.R.1
  • 56
    • 0035224505 scopus 로고    scopus 로고
    • Yeast two hybrid vectors and strains
    • P.N. MacDonald Humana Press Inc. Clifton, NJ
    • P. James Yeast two hybrid vectors and strains P.N. MacDonald Two Hybrid Systems: Methods and Protocols, Volume 177 2001 Humana Press Inc. Clifton, NJ 41 84
    • (2001) Two Hybrid Systems: Methods and Protocols, Volume 177 , pp. 41-84
    • James, P.1
  • 57
    • 0035224754 scopus 로고    scopus 로고
    • Strategies for rescuing plasmid DNA from yeast two-hybrid colonies
    • P.N. MacDonald Humana Press Inc. Clifton, NJ
    • A. Byrd, and R. St-Arnaud Strategies for rescuing plasmid DNA from yeast two-hybrid colonies P.N. MacDonald Two Hybrid Systems: Methods and Protocols, Volume 177 2001 Humana Press Inc. Clifton, NJ 107 122
    • (2001) Two Hybrid Systems: Methods and Protocols, Volume 177 , pp. 107-122
    • Byrd, A.1    St-Arnaud, R.2


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