메뉴 건너뛰기




Volumn 365, Issue 4, 2007, Pages 945-957

Ligand-regulated Peptide Aptamers that Inhibit the 5′-AMP-activated Protein Kinase

Author keywords

AMPK; ligand regulated peptide aptamers; peptide aptamer; pseudosubstrate; substrate inhibition

Indexed keywords

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; APTAMER; HYBRID PROTEIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE ALPHA1; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE ALPHA2; LIGAND REGULATED PEPTIDE; RAPAMYCIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 33845772308     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.07.035     Document Type: Article
Times cited : (9)

References (59)
  • 1
    • 7244245762 scopus 로고    scopus 로고
    • Finishing the euchromatic sequence of the human genome
    • International Human Genome Sequencing Consortium
    • International Human Genome Sequencing Consortium. Finishing the euchromatic sequence of the human genome. Nature 431 (2004) 931-945
    • (2004) Nature , vol.431 , pp. 931-945
  • 2
    • 0036956875 scopus 로고    scopus 로고
    • Studying gene function in eukaryotes by conditional gene inactivation
    • Gossen M., and Bujard H. 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
    • Hannon G.J. 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
    • Schreiber S.L. 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
    • 0031197176 scopus 로고    scopus 로고
    • Controlling mammalian gene expression with small molecules
    • Clackson T. Controlling mammalian gene expression with small molecules. Curr. Opin. Chem. Biol. 1 (1997) 210-218
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 210-218
    • Clackson, T.1
  • 6
    • 0030878873 scopus 로고    scopus 로고
    • Inducible gene expression and protein translocation using nontoxic ligands identified by a mammalian three-hybrid screen
    • Liberles S.D., Diver S.T., Austin D.J., and Schreiber S.L. 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
  • 7
    • 0041854719 scopus 로고    scopus 로고
    • Conditional protein splicing: a new tool to control protein structure and function in vitro and in vivo
    • Mootz H.D., Blum E.S., Tyszkiewicz A.B., and Muir T.W. Conditional protein splicing: a new tool to control protein structure and function in vitro and in vivo. J. Am. Chem. Soc. 125 (2003) 10561-10569
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10561-10569
    • Mootz, H.D.1    Blum, E.S.2    Tyszkiewicz, A.B.3    Muir, T.W.4
  • 8
    • 0034603114 scopus 로고    scopus 로고
    • Regulation of protein secretion through controlled aggregation in the endoplasmic reticulum
    • Rivera V.M., Wang X.R., Wardwell S., Courage N.L., Volchuk A., and Keenan T. Regulation of protein secretion through controlled aggregation in the endoplasmic reticulum. Science 287 (2000) 826-830
    • (2000) Science , vol.287 , pp. 826-830
    • Rivera, V.M.1    Wang, X.R.2    Wardwell, S.3    Courage, N.L.4    Volchuk, A.5    Keenan, T.6
  • 9
    • 0035902475 scopus 로고    scopus 로고
    • Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation
    • Sakamoto K.M., Kim K.B., Kumagai A., Mercurio F., Crews C.M., and Deshaies R.J. Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation. Proc. Natl Acad. Sci. USA 98 (2001) 8554-8559
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8554-8559
    • Sakamoto, K.M.1    Kim, K.B.2    Kumagai, A.3    Mercurio, F.4    Crews, C.M.5    Deshaies, R.J.6
  • 13
    • 0036008086 scopus 로고    scopus 로고
    • Engineering selectivity and discrimination into ligand-receptor interfaces
    • Koh J.T. Engineering selectivity and discrimination into ligand-receptor interfaces. Chem. Biol. 9 (2002) 17-23
    • (2002) Chem. Biol. , vol.9 , pp. 17-23
    • Koh, J.T.1
  • 14
    • 3342931068 scopus 로고    scopus 로고
    • A mechanism-based cross-linker for the identification of kinase-substrate pairs
    • Maly D.J., Allen J.A., and Shokat K.M. 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
  • 15
    • 0035006293 scopus 로고    scopus 로고
    • Selective regulation of gene expression by an orthogonal estrogen receptor-ligand pair created by polar-group exchange
    • Shi Y.H., and Koh J.T. Selective regulation of gene expression by an orthogonal estrogen receptor-ligand pair created by polar-group exchange. Chem. Biol. 8 (2001) 501-510
    • (2001) Chem. Biol. , vol.8 , pp. 501-510
    • Shi, Y.H.1    Koh, J.T.2
  • 16
    • 22544454196 scopus 로고    scopus 로고
    • Ligand-regulated peptides: a general approach for modulating protein-peptide interactions with small molecules
    • Binkowski B.F., Miller R.A., and Belshaw P.J. Ligand-regulated peptides: a general approach for modulating protein-peptide interactions with small molecules. Chem. Biol. 12 (2005) 847-855
    • (2005) Chem. Biol. , vol.12 , pp. 847-855
    • Binkowski, B.F.1    Miller, R.A.2    Belshaw, P.J.3
  • 17
    • 4344646564 scopus 로고    scopus 로고
    • Engineering a ligand-dependent RNA transcriptional activator
    • Buskirk A.R., Landrigan A., and Liu D.R. 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
  • 18
    • 14144254396 scopus 로고    scopus 로고
    • Creating small-molecule-dependent switches to modulate biological functions
    • Buskirk A.R., and Liu D.R. Creating small-molecule-dependent switches to modulate biological functions. Chem. Biol. 12 (2005) 151-161
    • (2005) Chem. Biol. , vol.12 , pp. 151-161
    • Buskirk, A.R.1    Liu, D.R.2
  • 20
    • 0036669759 scopus 로고    scopus 로고
    • Controlling protein activity with ligand-regulated RNA aptamers
    • Vuyisich M., and Beal P.A. 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
  • 21
    • 0032500736 scopus 로고    scopus 로고
    • Controlling gene expression in living cells through small molecule-RNA interactions
    • Werstuck G., and Green M.R. 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
  • 24
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R., et al. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403 (2000) 623-627
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3    Mansfield, T.A.4    Judson, R.S.5    Knight, J.R.6
  • 25
    • 0029876415 scopus 로고    scopus 로고
    • Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2
    • Colas P., Cohen B., Jessen T., Grishina I., McCoy J., and Brent R. 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
  • 26
    • 0032564350 scopus 로고    scopus 로고
    • An artificial cell-cycle inhibitor isolated from a combinatorial library
    • Cohen B.A., Colas P., and Brent R. An artificial cell-cycle inhibitor isolated from a combinatorial library. Proc. Natl Acad. Sci. USA 95 (1998) 14272-14277
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14272-14277
    • Cohen, B.A.1    Colas, P.2    Brent, R.3
  • 27
    • 0033614968 scopus 로고    scopus 로고
    • Inhibition of mammalian cell proliferation by genetically selected peptide aptamers that functionally antagonize E2F activity
    • Fabbrizio E., Le Cam L., Polanowska J., Kaczorek M., Lamb N., Brent R., and Sardet C. Inhibition of mammalian cell proliferation by genetically selected peptide aptamers that functionally antagonize E2F activity. Oncogene 18 (1999) 4357-4363
    • (1999) Oncogene , vol.18 , pp. 4357-4363
    • Fabbrizio, E.1    Le Cam, L.2    Polanowska, J.3    Kaczorek, M.4    Lamb, N.5    Brent, R.6    Sardet, C.7
  • 28
    • 0037420409 scopus 로고    scopus 로고
    • Inhibition of an activated Ras protein with genetically selected peptide aptamers
    • Kurtz S.E., Esposito K., Tang W., and Menzel R. Inhibition of an activated Ras protein with genetically selected peptide aptamers. Biotechnol. Bioeng. 82 (2003) 38-46
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 38-46
    • Kurtz, S.E.1    Esposito, K.2    Tang, W.3    Menzel, R.4
  • 29
    • 0034612296 scopus 로고    scopus 로고
    • Induction of apoptosis in human papillomaviruspositive cancer cells by peptide aptamers targeting the viral E6 oncoprotein
    • Butz K., Denk C., Ullmann A., Scheffner M., and Hoppe-Seyler F. Induction of apoptosis in human papillomaviruspositive cancer cells by peptide aptamers targeting the viral E6 oncoprotein. Proc. Natl Acad. Sci. USA 97 (2000) 6693-6697
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6693-6697
    • Butz, K.1    Denk, C.2    Ullmann, A.3    Scheffner, M.4    Hoppe-Seyler, F.5
  • 30
    • 0032518204 scopus 로고    scopus 로고
    • Green fluorescent protein as a scaffold for intracellular presentation of peptides
    • Abedi M.R., Caponigro G., and Kamb A. Green fluorescent protein as a scaffold for intracellular presentation of peptides. Nucl. Acids Res. 26 (1998) 623-630
    • (1998) Nucl. Acids Res. , vol.26 , pp. 623-630
    • Abedi, M.R.1    Caponigro, G.2    Kamb, A.3
  • 32
    • 24944581684 scopus 로고    scopus 로고
    • Design and validation of a neutral protein scaffold for the presentation of peptide aptamers
    • Woodman R., Yeh J.T., Laurenson S., and Ko Ferrigno P. Design and validation of a neutral protein scaffold for the presentation of peptide aptamers. J. Mol. Biol. 352 (2005) 1118-1133
    • (2005) J. Mol. Biol. , vol.352 , pp. 1118-1133
    • Woodman, R.1    Yeh, J.T.2    Laurenson, S.3    Ko Ferrigno, P.4
  • 33
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • Binz H.K., Amstutz P., and Pluckthun A. Engineering novel binding proteins from nonimmunoglobulin domains. Nature Biotechnol. 23 (2005) 1257-1268
    • (2005) Nature Biotechnol. , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Pluckthun, A.3
  • 34
    • 10744225311 scopus 로고    scopus 로고
    • Cellular localization and antiproliferative effect of peptides discovered from a functional screen of a retrovirally delivered random peptide library
    • Hitoshi Y., Gururaja T., Pearsall D.M., Lang W., Sharma P., Huang B., et al. Cellular localization and antiproliferative effect of peptides discovered from a functional screen of a retrovirally delivered random peptide library. Chem. Biol. 10 (2003) 975-987
    • (2003) Chem. Biol. , vol.10 , pp. 975-987
    • Hitoshi, Y.1    Gururaja, T.2    Pearsall, D.M.3    Lang, W.4    Sharma, P.5    Huang, B.6
  • 35
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP
    • Choi J.W., Chen J., Schreiber S.L., and Clardy J. 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
  • 36
    • 0035542970 scopus 로고    scopus 로고
    • AMP-activated protein kinase: the energy charge hypothesis revisited
    • Hardie D.G., and Hawley S.A. AMP-activated protein kinase: the energy charge hypothesis revisited. Bioessays 23 (2001) 1112-1119
    • (2001) Bioessays , vol.23 , pp. 1112-1119
    • Hardie, D.G.1    Hawley, S.A.2
  • 37
    • 0023896220 scopus 로고
    • The low activity of acetyl-CoA carboxylase in basal and glucagon-stimulated hepatocytes is due to phosphorylation by the AMP-activated protein kinase and not cyclic AMP-dependent protein kinase
    • Sim A.T., and Hardie D.G. The low activity of acetyl-CoA carboxylase in basal and glucagon-stimulated hepatocytes is due to phosphorylation by the AMP-activated protein kinase and not cyclic AMP-dependent protein kinase. FEBS Letters 233 (1988) 294-298
    • (1988) FEBS Letters , vol.233 , pp. 294-298
    • Sim, A.T.1    Hardie, D.G.2
  • 38
    • 0024786438 scopus 로고
    • Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl-CoA reductase kinase activities
    • Carling D., Clarke P.R., Zammit V.A., and Hardie D.G. Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl-CoA reductase kinase activities. Eur. J. Biochem. 186 (1989) 129-136
    • (1989) Eur. J. Biochem. , vol.186 , pp. 129-136
    • Carling, D.1    Clarke, P.R.2    Zammit, V.A.3    Hardie, D.G.4
  • 39
    • 9444287616 scopus 로고    scopus 로고
    • The alpha2-5′AMP-activated protein kinase is a site 2 glycogen synthase kinase in skeletal muscle and is responsive to glucose loading
    • Jorgensen S.B., Nielsen J.N., Birk J.B., Olsen G.S., Viollet B., Andreelli F., et al. The alpha2-5′AMP-activated protein kinase is a site 2 glycogen synthase kinase in skeletal muscle and is responsive to glucose loading. Diabetes 53 (2004) 3074-3081
    • (2004) Diabetes , vol.53 , pp. 3074-3081
    • Jorgensen, S.B.1    Nielsen, J.N.2    Birk, J.B.3    Olsen, G.S.4    Viollet, B.5    Andreelli, F.6
  • 40
    • 0037025356 scopus 로고    scopus 로고
    • AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling
    • Bolster D.R., Crozier S.J., Kimball S.R., and Jefferson L.S. AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. J. Biol. Chem. 277 (2002) 23977-23980
    • (2002) J. Biol. Chem. , vol.277 , pp. 23977-23980
    • Bolster, D.R.1    Crozier, S.J.2    Kimball, S.R.3    Jefferson, L.S.4
  • 41
    • 0037163076 scopus 로고    scopus 로고
    • The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase
    • Marsin A.S., Bouzin C., Bertrand L., and Hue L. The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase. J. Biol. Chem. 277 (2002) 30778-30783
    • (2002) J. Biol. Chem. , vol.277 , pp. 30778-30783
    • Marsin, A.S.1    Bouzin, C.2    Bertrand, L.3    Hue, L.4
  • 42
    • 0032765396 scopus 로고    scopus 로고
    • 5′ AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle
    • Kurth-Kraczek E.J., Hirshman M.F., Goodyear L.J., and Winder W.W. 5′ AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle. Diabetes 48 (1999) 1667-1671
    • (1999) Diabetes , vol.48 , pp. 1667-1671
    • Kurth-Kraczek, E.J.1    Hirshman, M.F.2    Goodyear, L.J.3    Winder, W.W.4
  • 43
    • 0034654362 scopus 로고    scopus 로고
    • Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding
    • Cheung P.C., Salt I.P., Davies S.P., Hardie D.G., and Carling D. Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding. Biochem. J. 346 (2000) 659-669
    • (2000) Biochem. J. , vol.346 , pp. 659-669
    • Cheung, P.C.1    Salt, I.P.2    Davies, S.P.3    Hardie, D.G.4    Carling, D.5
  • 44
    • 17144362480 scopus 로고    scopus 로고
    • AMP-activated protein kinase beta subunit tethers alpha and gamma subunits via its C-terminal sequence (186-270)
    • Iseli T.J., Walter M., van Denderen B.J., Katsis F., Witters L.A., Kemp B.E., et al. AMP-activated protein kinase beta subunit tethers alpha and gamma subunits via its C-terminal sequence (186-270). J. Biol. Chem. 280 (2005) 13395-13400
    • (2005) J. Biol. Chem. , vol.280 , pp. 13395-13400
    • Iseli, T.J.1    Walter, M.2    van Denderen, B.J.3    Katsis, F.4    Witters, L.A.5    Kemp, B.E.6
  • 45
    • 0024839973 scopus 로고
    • Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic-AMP-dependent protein kinase, studied using a specific and sensitive peptide assay
    • Davies S.P., Carling D., and Hardie D.G. Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic-AMP-dependent protein kinase, studied using a specific and sensitive peptide assay. Eur. J. Biochem. 186 (1989) 123-128
    • (1989) Eur. J. Biochem. , vol.186 , pp. 123-128
    • Davies, S.P.1    Carling, D.2    Hardie, D.G.3
  • 46
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell? Annu
    • Hardie D.G., Carling D., and Carlson M. The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell? Annu. Rev. Biochem. 67 (1998) 821-855
    • (1998) Rev. Biochem. , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 48
    • 27144548462 scopus 로고    scopus 로고
    • Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1
    • Rudolph M.J., Amodeo G.A., Bai Y., and Tong L. Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1. Biochem. Biophys. Res. Commun. 337 (2005) 1224-1228
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 1224-1228
    • Rudolph, M.J.1    Amodeo, G.A.2    Bai, Y.3    Tong, L.4
  • 49
    • 16844385435 scopus 로고    scopus 로고
    • Characterization of the FKBP.rapamycin.FRB ternary complex
    • Banaszynski L.A., Liu C.W., and Wandless T.J. Characterization of the FKBP.rapamycin.FRB ternary complex. J. Am. Chem. Soc. 127 (2005) 4715-4721
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4715-4721
    • Banaszynski, L.A.1    Liu, C.W.2    Wandless, T.J.3
  • 50
    • 0028942747 scopus 로고
    • Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I
    • Dale S., Wilson W.A., Edelman A.M., and Hardie D.G. Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I. FEBS Letters 361 (1995) 191-195
    • (1995) FEBS Letters , vol.361 , pp. 191-195
    • Dale, S.1    Wilson, W.A.2    Edelman, A.M.3    Hardie, D.G.4
  • 51
    • 0032853242 scopus 로고    scopus 로고
    • In vitro selection of functional nucleic acids
    • Wilson D.S., and Szostak J.W. In vitro selection of functional nucleic acids. Annu. Rev. Biochem. 68 (1999) 611-647
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 611-647
    • Wilson, D.S.1    Szostak, J.W.2
  • 52
    • 0036290846 scopus 로고    scopus 로고
    • Protein kinase substrate recognition studied using the recombinant catalytic domain of AMP-activated protein kinase and a model substrate
    • Scott J.W., Norman D.G., Hawley S.A., Kontogiannis L., and Hardie D.G. Protein kinase substrate recognition studied using the recombinant catalytic domain of AMP-activated protein kinase and a model substrate. J. Mol. Biol. 317 (2002) 309-323
    • (2002) J. Mol. Biol. , vol.317 , pp. 309-323
    • Scott, J.W.1    Norman, D.G.2    Hawley, S.A.3    Kontogiannis, L.4    Hardie, D.G.5
  • 53
    • 0029883316 scopus 로고    scopus 로고
    • G. Van den Berghe, Stimulation of rat liver AMP-activated protein kinase by AMP analogues
    • Henin N., and Vincent M.F. G. Van den Berghe, Stimulation of rat liver AMP-activated protein kinase by AMP analogues. Biochim. Biophys. Acta 1290 (1996) 197-203
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 197-203
    • Henin, N.1    Vincent, M.F.2
  • 54
    • 0013863538 scopus 로고
    • The interpretation of non-hyperbolic rate curves for two-substrate enzymes. A possible mechanism for phosphofructokinase
    • Ferdinand W. The interpretation of non-hyperbolic rate curves for two-substrate enzymes. A possible mechanism for phosphofructokinase. Biochem. J. 98 (1966) 278-283
    • (1966) Biochem. J. , vol.98 , pp. 278-283
    • Ferdinand, W.1
  • 55
    • 0030779872 scopus 로고    scopus 로고
    • Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX
    • McCafferty D.G., Lessard I.A., and Walsh C.T. Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX. Biochemistry 36 (1997) 10498-10505
    • (1997) Biochemistry , vol.36 , pp. 10498-10505
    • McCafferty, D.G.1    Lessard, I.A.2    Walsh, C.T.3
  • 56
    • 0029999325 scopus 로고    scopus 로고
    • Hypermutagenic PCR involving all four transitions and a sizeable proportion of transversions
    • Vartanian J.P., Henry M., and Wain-Hobson S. Hypermutagenic PCR involving all four transitions and a sizeable proportion of transversions. Nucl. Acids Res. 24 (1996) 2627-2631
    • (1996) Nucl. Acids Res. , vol.24 , pp. 2627-2631
    • Vartanian, J.P.1    Henry, M.2    Wain-Hobson, S.3
  • 57
    • 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
  • 58
    • 0033648637 scopus 로고    scopus 로고
    • Analysis of the role of the AMP-activated protein kinase in the response to cellular stress
    • Hardie D.G., Salt I.P., and Davies S.P. Analysis of the role of the AMP-activated protein kinase in the response to cellular stress. Methods Mol. Biol. 99 (2000) 63-74
    • (2000) Methods Mol. Biol. , vol.99 , pp. 63-74
    • Hardie, D.G.1    Salt, I.P.2    Davies, S.P.3
  • 59
    • 0027440990 scopus 로고
    • Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides
    • Weekes J., Ball K.L., Caudwell F.B., and Hardie D.G. Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides. FEBS Letters 334 (1993) 335-339
    • (1993) FEBS Letters , vol.334 , pp. 335-339
    • Weekes, J.1    Ball, K.L.2    Caudwell, F.B.3    Hardie, D.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.