메뉴 건너뛰기




Volumn 5, Issue 12, 2009, Pages 920-928

Moonlighting proteins Hal3 and Vhs3 form a heteromeric PPCDC with Ykl088w in yeast CoA biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

COENZYME A; FLAVOPROTEIN; HAL3 PROTEIN; MONOMER; PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE; PHOSPHOPROTEIN PHOSPHATASE; PPZ1 PROTEIN PHOSPHATASE; UNCLASSIFIED DRUG; VHS3 PROTEIN; YKL088W PROTEIN; CARBOXYLYASE; CELL CYCLE PROTEIN; PHOSPHOPANTOTHENOYL CYSTEINE DECARBOXYLASE; PHOSPHOPANTOTHENOYL-CYSTEINE DECARBOXYLASE; PPZ1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SIS2 PROTEIN, S CEREVISIAE; VHS3 PROTEIN, S CEREVISIAE;

EID: 73549091964     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.243     Document Type: Article
Times cited : (50)

References (50)
  • 1
    • 0035234935 scopus 로고    scopus 로고
    • The biosynthesis of coenzyme A in bacteria
    • Begley, T.P., Kinsland, C. & Strauss, E. The biosynthesis of coenzyme A in bacteria. Vitam. Horm. 61, 157-171 (2001).
    • (2001) Vitam. Horm. , vol.61 , pp. 157-171
    • Begley, T.P.1    Kinsland, C.2    Strauss, E.3
  • 2
    • 34547102510 scopus 로고    scopus 로고
    • The ubiquitous carrier protein-a window to metabolite biosynthesis
    • Mercer, A.C. & Burkart, M.D. The ubiquitous carrier protein-a window to metabolite biosynthesis. Nat. Prod. Rep. 24, 750-773 (2007).
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 750-773
    • Mercer, A.C.1    Burkart, M.D.2
  • 3
    • 0037077259 scopus 로고    scopus 로고
    • Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics
    • Daugherty, M. et al. Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics. J. Biol. Chem. 277, 21431-21439 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 21431-21439
    • Daugherty, M.1
  • 4
    • 0141643343 scopus 로고    scopus 로고
    • 4′-phosphopantetheine and coenzyme A biosynthesis in plants
    • Kupke, T., Hernandez-Acosta, P. & Culianez-Macia, F.A. 4′-phosphopantetheine and coenzyme A biosynthesis in plants. J. Biol. Chem. 278, 38229-38237 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 38229-38237
    • Kupke, T.1    Hernandez-Acosta, P.2    Culianez-Macia, F.A.3
  • 5
    • 27144524216 scopus 로고    scopus 로고
    • Automatic detection of subsystem/ pathway variants in genome analysis
    • Ye, Y., Osterman, A., Overbeek, R. & Godzik, A. Automatic detection of subsystem/ pathway variants in genome analysis. Bioinformatics 21 Suppl 1: i478-i486 (2005).
    • (2005) Bioinformatics , vol.21 , Issue.SUPPL. 1
    • Ye, Y.1    Osterman, A.2    Overbeek, R.3    Godzik, A.4
  • 6
    • 0037398732 scopus 로고    scopus 로고
    • Missing genes in metabolic pathways: A comparative genomics approach
    • Osterman, A. & Overbeek, R. Missing genes in metabolic pathways: a comparative genomics approach. Curr. Opin. Chem. Biol. 7, 238-251 (2003).
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 238-251
    • Osterman, A.1    Overbeek, R.2
  • 7
    • 0035377354 scopus 로고    scopus 로고
    • Arabidopsis thaliana flavoprotein AtHAL3a catalyzes the decarboxylation of 4′-Phosphopantothenoylcysteine to 4′-phosphopantetheine, a key step in coenzyme A biosynthesis
    • Kupke, T., Hernandez-Acosta, P., Steinbacher, S. & Culianez-Macia, F.A. Arabidopsis thaliana flavoprotein AtHAL3a catalyzes the decarboxylation of 4′-Phosphopantothenoylcysteine to 4′-phosphopantetheine, a key step in coenzyme A biosynthesis. J. Biol. Chem. 276, 19190-19196 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 19190-19196
    • Kupke, T.1    Hernandez-Acosta, P.2    Steinbacher, S.3    Culianez-Macia, F.A.4
  • 8
    • 0035957936 scopus 로고    scopus 로고
    • Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria
    • Strauss, E., Kinsland, C., Ge, Y., McLafferty, F.W. & Begley, T.P. Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria. J. Biol. Chem. 276, 13513-13516 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 13513-13516
    • Strauss, E.1    Kinsland, C.2    Ge, Y.3    McLafferty, F.W.4    Begley, T.P.5
  • 9
    • 0037036420 scopus 로고    scopus 로고
    • Molecular characterization of the Arabidopsis thaliana flavoprotein AtHAL3a reveals the general reaction mechanism of ′- phosphopantothenoylcysteine decarboxylases
    • Hernandez-Acosta, P., Schmid, D.G., Jung, G., Culianez-Macia, F.A. & Kupke, T. Molecular characterization of the Arabidopsis thaliana flavoprotein AtHAL3a reveals the general reaction mechanism of 4′- phosphopantothenoylcysteine decarboxylases. J. Biol. Chem. 277, 20490-20498 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 20490-20498
    • Hernandez-Acosta, P.1    Schmid, D.G.2    Jung, G.3    Culianez-Macia, F.A.4    Kupke, T.5
  • 10
    • 0037436377 scopus 로고    scopus 로고
    • Crystal structure of the plant PPC decarboxylase AtHAL3a complexed with an ene-thiol reaction intermediate
    • Steinbacher, S. et al. Crystal structure of the plant PPC decarboxylase AtHAL3a complexed with an ene-thiol reaction intermediate. J. Mol. Biol. 327, 193-202 (2003).
    • (2003) J. Mol. Biol. , vol.327 , pp. 193-202
    • Steinbacher, S.1
  • 11
    • 10644288567 scopus 로고    scopus 로고
    • Mechanistic studies on phosphopantothenoylcysteine decarboxylase: Trapping of an enethiolate intermediate with a mechanism-based inactivating agent
    • Strauss, E., Zhai, H., Brand, L.A., McLafferty, F.W. & Begley, T.P. Mechanistic studies on phosphopantothenoylcysteine decarboxylase: trapping of an enethiolate intermediate with a mechanism-based inactivating agent. Biochemistry 43, 15520-15533 (2004).
    • (2004) Biochemistry , vol.43 , pp. 15520-15533
    • Strauss, E.1    Zhai, H.2    Brand, L.A.3    McLafferty, F.W.4    Begley, T.P.5
  • 12
    • 0029166109 scopus 로고
    • Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3
    • Ferrando, A., Kron, S.J., Rios, G., Fink, G.R. & Serrano, R. Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3. Mol. Cell. Biol. 15, 5470-5481 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5470-5481
    • Ferrando, A.1    Kron, S.J.2    Rios, G.3    Fink, G.R.4    Serrano, R.5
  • 13
    • 0028800585 scopus 로고
    • Overexpression of SIS2, which contains an extremely acidic region, increases the expression of SWI4, CLN1 and CLN2 in sit4 mutants
    • Di Como, C.J., Bose, R. & Arndt, K.T. Overexpression of SIS2, which contains an extremely acidic region, increases the expression of SWI4, CLN1 and CLN2 in sit4 mutants. Genetics 139, 95-107 (1995).
    • (1995) Genetics , vol.139 , pp. 95-107
    • Di Como, C.J.1    Bose, R.2    Arndt, K.T.3
  • 14
    • 0036183665 scopus 로고    scopus 로고
    • Novel protein phosphatases in yeast
    • Ariño, J. Novel protein phosphatases in yeast. Eur. J. Biochem. 269, 1072-1077 (2002).
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1072-1077
    • Ariño, J.1
  • 15
    • 0032560472 scopus 로고    scopus 로고
    • The yeast halotolerance determinant Hal3p is an inhibitory subunit of the Ppz1p Ser/Thr protein phosphatase
    • de Nadal, E. et al. The yeast halotolerance determinant Hal3p is an inhibitory subunit of the Ppz1p Ser/Thr protein phosphatase. Proc. Natl. Acad. Sci. USA 95, 7357-7362 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7357-7362
    • De Nadal, E.1
  • 16
    • 0029019792 scopus 로고
    • The PPZ protein phosphatases are important determinants of salt tolerance in yeast cells
    • Posas, F., Camps, M. & Ariño, J. The PPZ protein phosphatases are important determinants of salt tolerance in yeast cells. J. Biol. Chem. 270, 13036-13041 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 13036-13041
    • Posas, F.1    Camps, M.2    Ariño, J.3
  • 17
    • 0036500159 scopus 로고    scopus 로고
    • The Ppz protein phosphatases are key regulators of K+ and pH homeostasis: Implications for salt tolerance, cell wall integrity and cell cycle progression
    • Yenush, L., Mulet, J.M., Ariño, J. & Serrano, R. The Ppz protein phosphatases are key regulators of K+ and pH homeostasis: implications for salt tolerance, cell wall integrity and cell cycle progression. EMBO J. 21, 920-929 (2002).
    • (2002) EMBO J , vol.21 , pp. 920-929
    • Yenush, L.1    Mulet, J.M.2    Ariño, J.3    Serrano, R.4
  • 18
    • 0142153872 scopus 로고    scopus 로고
    • Regulation of ENA1 Na(+)-ATPase gene expression by the Ppz1 protein phosphatase is mediated by the calcineurin pathway.
    • Ruiz, A., Yenush, L. & Ariño, J. Regulation of ENA1 Na(+)-ATPase gene expression by the Ppz1 protein phosphatase is mediated by the calcineurin pathway. Eukaryot. Cell 2, 937-948 (2003).
    • (2003) Eukaryot. Cell , vol.2 , pp. 937-948
    • Ruiz, A.1    Yenush, L.2    Ariño, J.3
  • 19
    • 0027219432 scopus 로고
    • A pair of functionally redundant yeast genes (PPZ1 and PPZ2) encoding type 1-related protein phosphatases function within the PKC1-mediated pathway
    • Lee, K.S., Hines, L.K. & Levin, D.E. A pair of functionally redundant yeast genes (PPZ1 and PPZ2) encoding type 1-related protein phosphatases function within the PKC1-mediated pathway. Mol. Cell. Biol. 13, 5843-5853 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5843-5853
    • Lee, K.S.1    Hines, L.K.2    Levin, D.E.3
  • 20
    • 1242277786 scopus 로고    scopus 로고
    • Response of the Saccharomyces cerevisiae Mpk1 mitogen-activated protein kinase pathway to increases in internal turgor pressure caused by loss of Ppz protein phosphatases
    • Merchan, S., Bernal, D., Serrano, R. & Yenush, L. Response of the Saccharomyces cerevisiae Mpk1 mitogen-activated protein kinase pathway to increases in internal turgor pressure caused by loss of Ppz protein phosphatases. Eukaryot. Cell 3, 100-107 (2004).
    • (2004) Eukaryot. Cell , vol.3 , pp. 100-107
    • Merchan, S.1    Bernal, D.2    Serrano, R.3    Yenush, L.4
  • 21
    • 0033019059 scopus 로고    scopus 로고
    • The yeast ser/thr phosphatases sit4 and ppz1 play opposite roles in regulation of the cell cycle
    • Clotet, J., Gari, E., Aldea, M. & Ariño, J. The yeast ser/thr phosphatases sit4 and ppz1 play opposite roles in regulation of the cell cycle. Mol. Cell. Biol. 19, 2408-2415 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2408-2415
    • Clotet, J.1    Gari, E.2    Aldea, M.3    Ariño, J.4
  • 22
    • 0037472529 scopus 로고    scopus 로고
    • Identification of multicopy suppressors of cell cycle arrest at the G1-S transition in Saccharomyces cerevisiae.
    • Munoz, I., Simon, E., Casals, N., Clotet, J. & Ariño, J. Identification of multicopy suppressors of cell cycle arrest at the G1-S transition in Saccharomyces cerevisiae. Yeast 20, 157-169 (2003).
    • (2003) Yeast , vol.20 , pp. 157-169
    • Munoz, I.1    Simon, E.2    Casals, N.3    Clotet, J.4    Ariño, J.5
  • 23
    • 4544345613 scopus 로고    scopus 로고
    • Functional characterization of the Saccharomyces cerevisiae VHS3 gene: A regulatory subunit of the Ppz1 protein phosphatase with novel, phosphataseunrelated functions
    • Ruiz, A. et al. Functional characterization of the Saccharomyces cerevisiae VHS3 gene: a regulatory subunit of the Ppz1 protein phosphatase with novel, phosphataseunrelated functions. J. Biol. Chem. 279, 34421-34430 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 34421-34430
    • Ruiz, A.1
  • 24
    • 0037173615 scopus 로고    scopus 로고
    • Functional profiling of the Saccharomyces cerevisiae genome
    • Giaever, G. et al. Functional profiling of the Saccharomyces cerevisiae genome. Nature 418, 387-391 (2002).
    • (2002) Nature , vol.418 , pp. 387-391
    • Giaever, G.1
  • 25
    • 0033401081 scopus 로고    scopus 로고
    • Arabidopsis thaliana AtHAL3: A flavoprotein related to salt and osmotic tolerance and plant growth
    • Espinosa-Ruiz, A., Belles, J.M., Serrano, R. & Culianez-Macia, F.A. Arabidopsis thaliana AtHAL3: a flavoprotein related to salt and osmotic tolerance and plant growth. Plant J. 20, 529-539 (1999).
    • (1999) Plant J , vol.20 , pp. 529-539
    • Espinosa-Ruiz, A.1    Belles, J.M.2    Serrano, R.3    Culianez-Macia, F.A.4
  • 26
    • 0034665046 scopus 로고    scopus 로고
    • The X-ray structure of the FMN-binding protein AtHal3 provides the structural basis for the activity of a regulatory subunit involved in signal transduction
    • Albert, A. et al. The X-ray structure of the FMN-binding protein AtHal3 provides the structural basis for the activity of a regulatory subunit involved in signal transduction. Structure 8, 961-969 (2000).
    • (2000) Structure , vol.8 , pp. 961-969
    • Albert, A.1
  • 27
    • 0034811831 scopus 로고    scopus 로고
    • Mechanistic studies on phosphopantothenoylcysteine decarboxylase
    • Strauss, E. & Begley, T.P. Mechanistic studies on phosphopantothenoylcysteine decarboxylase. J. Am. Chem. Soc. 123, 6449-6450 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6449-6450
    • Strauss, E.1    Begley, T.P.2
  • 28
    • 0037325586 scopus 로고    scopus 로고
    • Stereochemical studies on phosphopantothenoylcysteine decarboxylase from Escherichia coli
    • Strauss, E. & Begley, T.P. Stereochemical studies on phosphopantothenoylcysteine decarboxylase from Escherichia coli. Bioorg. Med. Chem. Lett. 13, 339-342 (2003).
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 339-342
    • Strauss, E.1    Begley, T.P.2
  • 29
    • 33646825686 scopus 로고    scopus 로고
    • 4′-phosphopantetheine biosynthesis in Archaea
    • Kupke, T. & Schwarz, W. 4′-phosphopantetheine biosynthesis in Archaea. J. Biol. Chem. 281, 5435-5444 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 5435-5444
    • Kupke, T.1    Schwarz, W.2
  • 30
    • 0035805492 scopus 로고    scopus 로고
    • A role for the Ppz Ser/Thr protein phosphatases in the regulation of translation elongation factor 1Balpha
    • de Nadal, E., Fadden, R.P., Ruiz, A., Haystead, T. & Ariño, J. A role for the Ppz Ser/Thr protein phosphatases in the regulation of translation elongation factor 1Balpha. J. Biol. Chem. 276, 14829-14834 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 14829-14834
    • De Nadal, E.1    Fadden, R.P.2    Ruiz, A.3    Haystead, T.4    Ariño, J.5
  • 31
    • 0028331458 scopus 로고
    • NHP6A and NHP6B, which encode HMG1-like proteins, are candidates for downstream components of the yeast SLT2 mitogen-activated protein kinase pathway
    • Costigan, C., Kolodrubetz, D. & Snyder, M. NHP6A and NHP6B, which encode HMG1-like proteins, are candidates for downstream components of the yeast SLT2 mitogen-activated protein kinase pathway. Mol. Cell. Biol. 14, 2391-2403 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2391-2403
    • Costigan, C.1    Kolodrubetz, D.2    Snyder, M.3
  • 32
    • 33644555054 scopus 로고    scopus 로고
    • Proteome survey reveals modularity of the yeast cell machinery
    • Gavin, A.C. et al. Proteome survey reveals modularity of the yeast cell machinery. Nature 440, 631-636 (2006).
    • (2006) Nature , vol.440 , pp. 631-636
    • Gavin, A.C.1
  • 33
    • 0027483798 scopus 로고
    • MIF2 is required for mitotic spindle integrity during anaphase spindle elongation in Saccharomyces cerevisiae
    • DOI 10.1083/jcb.123.2.387
    • Brown, M.T., Goetsch, L. & Hartwell, L.H. MIF2 is required for mitotic spindle integrity during anaphase spindle elongation in Saccharomyces cerevisiae. J. Cell Biol. 123, 387-403 (1993). (Pubitemid 23313963)
    • (1993) Journal of Cell Biology , vol.123 , Issue.2 , pp. 387-403
    • Brown, M.T.1    Goetsch, L.2    Hartwell, L.H.3
  • 34
    • 0034644779 scopus 로고    scopus 로고
    • Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals a function for bacterial Dfp proteins in coenzyme A biosynthesis
    • Kupke, T. et al. Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals a function for bacterial Dfp proteins in coenzyme A biosynthesis. J. Biol. Chem. 275, 31838-31846 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 31838-31846
    • Kupke, T.1
  • 35
    • 9144257235 scopus 로고    scopus 로고
    • Assigning function to yeast proteins by integration of technologies
    • Hazbun, T.R. et al. Assigning function to yeast proteins by integration of technologies. Mol. Cell 12, 1353-1365 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1353-1365
    • Hazbun, T.R.1
  • 36
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • Krogan, N.J. et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440, 637-643 (2006).
    • (2006) Nature , vol.440 , pp. 637-643
    • Krogan, N.J.1
  • 37
    • 34147121646 scopus 로고    scopus 로고
    • Toward a comprehensive atlas of the physical interactome of Saccharomyces cerevisiae
    • Collins, S.R. et al. Toward a comprehensive atlas of the physical interactome of Saccharomyces cerevisiae. Mol. Cell. Proteomics 6, 439-450 (2007).
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 439-450
    • Collins, S.R.1
  • 38
    • 0022353123 scopus 로고
    • Dfp Gene of Escherichia coli K-12 a locus affecting DNA synthesis codes for a flavoprotein
    • Spitzer, E.D. & Weiss, B. dfp Gene of Escherichia coli K-12, a locus affecting DNA synthesis, codes for a flavoprotein. J. Bacteriol. 164, 994-1003 (1985).
    • (1985) J. Bacteriol. , vol.164 , pp. 994-1003
    • Spitzer, E.D.1    Weiss, B.2
  • 39
    • 0023959445 scopus 로고
    • Beta-Alanine auxotrophy associated with dfp a locus affecting DNA synthesis in Escherichia coli
    • Spitzer, E.D., Jimenez-Billini, H.E. & Weiss, B. beta-Alanine auxotrophy associated with dfp, a locus affecting DNA synthesis in Escherichia coli. J. Bacteriol. 170, 872-876 (1988).
    • (1988) J. Bacteriol. , vol.170 , pp. 872-876
    • Spitzer, E.D.1    Jimenez-Billini, H.E.2    Weiss, B.3
  • 40
    • 33745736295 scopus 로고    scopus 로고
    • Yeasts illustrate the molecular mechanisms of eukaryotic genome evolution
    • Dujon, B. Yeasts illustrate the molecular mechanisms of eukaryotic genome evolution. Trends Genet. 22, 375-387 (2006).
    • (2006) Trends Genet , vol.22 , pp. 375-387
    • Dujon, B.1
  • 41
    • 5644250569 scopus 로고    scopus 로고
    • Functional characterization of the yeast Ppz1 phosphatase inhibitory subunit Hal3: A mutagenesis study
    • Munoz, I. et al. Functional characterization of the yeast Ppz1 phosphatase inhibitory subunit Hal3: a mutagenesis study. J. Biol. Chem. 279, 42619-42627 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 42619-42627
    • Munoz, I.1
  • 42
    • 0031405029 scopus 로고    scopus 로고
    • The coenzyme A-synthesizing protein complex and its proposed role in CoA biosynthesis in bakers' yeast
    • Bucovaz, E.T., Macleod, R.M., Morrison, J.C. & Whybrew, W.D. The coenzyme A-synthesizing protein complex and its proposed role in CoA biosynthesis in bakers' yeast. Biochimie 79, 787-798 (1997).
    • (1997) Biochimie , vol.79 , pp. 787-798
    • Bucovaz, E.T.1    MacLeod, R.M.2    Morrison, J.C.3    Whybrew, W.D.4
  • 43
    • 0018974651 scopus 로고
    • Coenzyme A-synthesizing protein complex of Saccharomyces cerevisiae
    • Bucovaz, E.T. et al. Coenzyme A-synthesizing protein complex of Saccharomyces cerevisiae. Mol. Cell. Biochem. 30, 7-26 (1980).
    • (1980) Mol. Cell. Biochem. , vol.30 , pp. 7-26
    • Bucovaz, E.T.1
  • 44
    • 67349203977 scopus 로고    scopus 로고
    • Genetic analysis of coenzyme A biosynthesis in the yeast Saccharomyces cerevisiae: Identification of a conditional mutation in the pantothenate kinase gene CAB1
    • Olzhausen, J., Schubbe, S. & Schuller, H.J. Genetic analysis of coenzyme A biosynthesis in the yeast Saccharomyces cerevisiae: identification of a conditional mutation in the pantothenate kinase gene CAB1. Curr. Genet. 55, 163-173 (2009).
    • (2009) Curr. Genet. , vol.55 , pp. 163-173
    • Olzhausen, J.1    Schubbe, S.2    Schuller, H.J.3
  • 47
    • 0038429941 scopus 로고    scopus 로고
    • Growth and manipulation of yeast
    • (eds. Ausubel, F.M. et al.) 13.2.10-13.2.12 (John Wiley & Sons, New York
    • Treco, D.A. & Winston, F. Growth and manipulation of yeast. in Current Protocols in Molecular Biology (eds. Ausubel, F.M. et al.) 13.2.10-13.2.12 (John Wiley & Sons, New York, 1998).
    • (1998) Current Protocols in Molecular Biology
    • Treco, D.A.1    Winston, F.2
  • 48
    • 0346850852 scopus 로고    scopus 로고
    • Molecular characterization of Ypi1, a novel Saccharomyces cerevisiae type 1 protein phosphatase inhibitor
    • Garcia-Gimeno, M.A., Munoz, I., Ariño, J. & Sanz, P. Molecular characterization of Ypi1, a novel Saccharomyces cerevisiae type 1 protein phosphatase inhibitor. J. Biol. Chem. 278, 47744-47752 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 47744-47752
    • Garcia-Gimeno, M.A.1    Munoz, I.2    Ariño, J.3    Sanz, P.4
  • 49
    • 0000817381 scopus 로고
    • A simple and accurate spectrophotometric assay for phosphoenolpyruvate carboxylase activity
    • Meyer, C.R., Rustin, P. & Wedding, R.T. A simple and accurate spectrophotometric assay for phosphoenolpyruvate carboxylase activity. Plant Physiol. 86, 325-328 (1988).
    • (1988) Plant Physiol , vol.86 , pp. 325-328
    • Meyer, C.R.1    Rustin, P.2    Wedding, R.T.3
  • 50
    • 0034525575 scopus 로고    scopus 로고
    • PhyloDraw: A phylogenetic tree drawing system
    • Choi, J.H., Jung, H.Y., Kim, H.S. & Cho, H.G. PhyloDraw: a phylogenetic tree drawing system. Bioinformatics 16, 1056-1058 (2000).
    • (2000) Bioinformatics , vol.16 , pp. 1056-1058
    • Choi, J.H.1    Jung, H.Y.2    Kim, H.S.3    Cho, H.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.