메뉴 건너뛰기




Volumn 41, Issue 7, 2004, Pages 667-675

The glyceraldehyde-3-phosphate dehydrogenase homologue is differentially regulated in phases of Paracoccidioides brasiliensis: Molecular and phylogenetic analysis

Author keywords

Dimorphic transition; Paracoccidioides brasiliensis; PbGAPDH

Indexed keywords

COMPLEMENTARY DNA; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; PROTEOME;

EID: 2942558818     PISSN: 10871845     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fgb.2004.02.002     Document Type: Article
Times cited : (30)

References (40)
  • 2
    • 0022946198 scopus 로고
    • Sequences important for gene expression in filamentous fungi
    • Ballance D.J. Sequences important for gene expression in filamentous fungi. Yeast. 2:1986;229-236
    • (1986) Yeast , vol.2 , pp. 229-236
    • Ballance, D.J.1
  • 4
    • 0028125811 scopus 로고
    • Comparison of glyceraldehyde-3-phosphate dehydrogenase and 28S-ribosomal RNA gene expression as RNA loading controls for Northern blot analysis of cell lines of varying malignant potential
    • Bhatia P., Taylor W.R., Greenberg A.H., Wright J.A. Comparison of glyceraldehyde-3-phosphate dehydrogenase and 28S-ribosomal RNA gene expression as RNA loading controls for Northern blot analysis of cell lines of varying malignant potential. Anal. Biochem. 216:1994;223-226
    • (1994) Anal. Biochem. , vol.216 , pp. 223-226
    • Bhatia, P.1    Taylor, W.R.2    Greenberg, A.H.3    Wright, J.A.4
  • 7
    • 0032574738 scopus 로고    scopus 로고
    • Toward a resolution of the introns early/late debate: Only phase zero introns are correlated with the structure of ancient proteins
    • De Souza S.J., Long M., Klein R.J., Roy S., Gilbert W. Toward a resolution of the introns early/late debate: only phase zero introns are correlated with the structure of ancient proteins. Proc. Natl. Acad. Sci. USA. 95:1998;5094-5099
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5094-5099
    • De Souza, S.J.1    Long, M.2    Klein, R.J.3    Roy, S.4    Gilbert, W.5
  • 8
    • 0021760092 scopus 로고
    • A comprehensive set of sequences analysis programs for the VAX
    • Devereux J., Haeberli P., Smithies O. A comprehensive set of sequences analysis programs for the VAX. Nucleic Acids Res. 12:1984;387-395
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 10
    • 0002452677 scopus 로고
    • Contribuição para o estudo imunológico da blastomicose de Lutz
    • Fava-Neto C. Contribuição para o estudo imunológico da blastomicose de Lutz. Rev. Inst. Adolfo Lutz. 21:1961;99-194
    • (1961) Rev. Inst. Adolfo Lutz , vol.21 , pp. 99-194
    • Fava-Neto, C.1
  • 12
    • 0030789362 scopus 로고    scopus 로고
    • The glycolytic enzyme glyceraldeyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen
    • Gil-Navarro I., Gil M.L., Casanova M., O'Connor J.E., Martinez J.P., Gozalbo D. The glycolytic enzyme glyceraldeyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen. J. Bacteriol. 179:1997;4992-4999
    • (1997) J. Bacteriol. , vol.179 , pp. 4992-4999
    • Gil-Navarro, I.1    Gil, M.L.2    Casanova, M.3    O'Connor, J.E.4    Martinez, J.P.5    Gozalbo, D.6
  • 13
    • 0024358130 scopus 로고
    • The major parasite surface antigen associated with human resistence to schistosomiasis is a 37 kDa glyceraldehyde-3-P-dehydrogenase
    • Goudout-Crozel V., Caillol D., Djabali M., Dessein A.J. The major parasite surface antigen associated with human resistence to schistosomiasis is a 37. kDa glyceraldehyde-3-P-dehydrogenase J. Exp. Med. 170:1989;2065-2074
    • (1989) J. Exp. Med. , vol.170 , pp. 2065-2074
    • Goudout-Crozel, V.1    Caillol, D.2    Djabali, M.3    Dessein, A.J.4
  • 14
    • 0031896903 scopus 로고    scopus 로고
    • The cell wall-associated glyceraldehydes-3-phosphate dehydrogenase of Candida albicans is also a fibronectin and laminin binding protein
    • Gozalbo D., Gil-Navarro J., Azorin I., Renau-Piqueras J., Martinez J.P., Gil M.L. The cell wall-associated glyceraldehydes-3-phosphate dehydrogenase of Candida albicans is also a fibronectin and laminin binding protein. Infect. Immun. 66:1998;2052-2059
    • (1998) Infect. Immun. , vol.66 , pp. 2052-2059
    • Gozalbo, D.1    Gil-Navarro, J.2    Azorin, I.3    Renau-Piqueras, J.4    Martinez, J.P.5    Gil, M.L.6
  • 15
    • 0027971167 scopus 로고
    • Regulation of endothelial cell glyceraldehyde-3-phosphate dehydrogenase expression by hypoxia
    • Graven K.K., Troxler R.F., Kornfeld H., Panchenko M.V., Farber H.W. Regulation of endothelial cell glyceraldehyde-3-phosphate dehydrogenase expression by hypoxia. J. Biol. Chem. 269:1994;24446-24453
    • (1994) J. Biol. Chem. , vol.269 , pp. 24446-24453
    • Graven, K.K.1    Troxler, R.F.2    Kornfeld, H.3    Panchenko, M.V.4    Farber, H.W.5
  • 16
    • 0030715351 scopus 로고    scopus 로고
    • Molecular taxonomy and epidemiology of Blastomyces and Histoplasma capsulatum species
    • Guého E., Leclere M.C., Hoog G.S., Dupont B. Molecular taxonomy and epidemiology of Blastomyces and Histoplasma capsulatum species. Mycoses. 40:1997;69-81
    • (1997) Mycoses , vol.40 , pp. 69-81
    • Guého, E.1    Leclere, M.C.2    Hoog, G.S.3    Dupont, B.4
  • 17
    • 0036679346 scopus 로고    scopus 로고
    • Characterization of a chaperone ClpB homologue of Paracoccidioides brasiliensis
    • Jesuino R.S.A., Azevedo M.O., Felipe M.S.S., Pereira M., Soares C.M.A. Characterization of a chaperone ClpB homologue of Paracoccidioides brasiliensis. Yeast. 19:2002;963-972
    • (2002) Yeast , vol.19 , pp. 963-972
    • Jesuino, R.S.A.1    Azevedo, M.O.2    Felipe, M.S.S.3    Pereira, M.4    Soares, C.M.A.5
  • 18
    • 0028014282 scopus 로고
    • The Claviceps purpurea glyceraldehyde-3-phosphate dehydrogenase gene: Cloning, characterization, and use for the improvement of a dominant selection system
    • Jungehulsing U., Arntz C., Smit R., Tudzynski P. The Claviceps purpurea glyceraldehyde-3-phosphate dehydrogenase gene: cloning, characterization, and use for the improvement of a dominant selection system. Curr. Genet. 25:1994;101-106
    • (1994) Curr. Genet. , vol.25 , pp. 101-106
    • Jungehulsing, U.1    Arntz, C.2    Smit, R.3    Tudzynski, P.4
  • 19
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiation codon that modulates translation by eukaryotic ribosomes
    • Kozak M. Point mutations define a sequence flanking the AUG initiation codon that modulates translation by eukaryotic ribosomes. Cell. 44:1986;283-292
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0027264855 scopus 로고
    • Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3- phosphate dehydrogenase
    • McDonald L.J., Moss J. Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA. 90:1993;6238-6241
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6238-6241
    • McDonald, L.J.1    Moss, J.2
  • 22
    • 0032975361 scopus 로고    scopus 로고
    • The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase
    • Modun B., Williams P. The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase. Infect. Immun. 67:1999;1086-1092
    • (1999) Infect. Immun. , vol.67 , pp. 1086-1092
    • Modun, B.1    Williams, P.2
  • 23
    • 0034193246 scopus 로고    scopus 로고
    • The staphylococcal transferring receptor: A glycolytic enzyme with novel functions
    • Modun B., Morrissey J., Williams P. The staphylococcal transferring receptor: a glycolytic enzyme with novel functions. Trends Microbiol. 8:2000;231-236
    • (2000) Trends Microbiol. , vol.8 , pp. 231-236
    • Modun, B.1    Morrissey, J.2    Williams, P.3
  • 24
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrel P.H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:1975;4007-4021
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrel, P.H.1
  • 25
    • 0030661706 scopus 로고    scopus 로고
    • Regulation of the phosphorylation of human pharyngeal cell proteins by group a streptococcal surface dehydrogenase: Signal transduction between streptococci and pharyngeal cells
    • Pancholi V., Fischetti V.A. Regulation of the phosphorylation of human pharyngeal cell proteins by group A streptococcal surface dehydrogenase: signal transduction between streptococci and pharyngeal cells. J. Exp. Med. 186:1997;1633-1643
    • (1997) J. Exp. Med. , vol.186 , pp. 1633-1643
    • Pancholi, V.1    Fischetti, V.A.2
  • 26
    • 0347479351 scopus 로고    scopus 로고
    • Mycobacterium avium-superoxide dismutase binds to epithelial cell aldolase, glyceraldehydes-3-phosphate dehydrogenase and cyclophilin a
    • Reddy V.M., Suleman G.F. Mycobacterium avium-superoxide dismutase binds to epithelial cell aldolase, glyceraldehydes-3-phosphate dehydrogenase and cyclophilin A. Microb. Pathogen. 36:2004;67-74
    • (2004) Microb. Pathogen. , vol.36 , pp. 67-74
    • Reddy, V.M.1    Suleman, G.F.2
  • 28
    • 0026516216 scopus 로고
    • Sequence analysis of the gene coding for glyceraldehyde-3-phosphate dehydrogenase (gpd) of Podospora anserina: Use of homologous regulatory sequences to improve transformation efficiency
    • Ridder R., Osiewacz H.D. Sequence analysis of the gene coding for glyceraldehyde-3-phosphate dehydrogenase (gpd) of Podospora anserina: use of homologous regulatory sequences to improve transformation efficiency. Curr. Genet. 21:1992;207-213
    • (1992) Curr. Genet. , vol.21 , pp. 207-213
    • Ridder, R.1    Osiewacz, H.D.2
  • 29
    • 0032862380 scopus 로고    scopus 로고
    • Centripetal modules and ancient introns
    • Roy S.W., Nosaka M., Souza S.J., Gilbert W. Centripetal modules and ancient introns. Gene. 238:1999;85-91
    • (1999) Gene , vol.238 , pp. 85-91
    • Roy, S.W.1    Nosaka, M.2    Souza, S.J.3    Gilbert, W.4
  • 31
    • 0036301549 scopus 로고    scopus 로고
    • Paracoccidioides brasiliensis and paracoccidioidomycosis: Molecular approaches to morphogenesis, diagnosis, epidemiology taxonomy and genetics
    • San-Blas G., Niño-Vega G., Iturriaga T. Paracoccidioides brasiliensis and paracoccidioidomycosis: molecular approaches to morphogenesis, diagnosis, epidemiology taxonomy and genetics. Med. Mycol. 40:2002;225-242
    • (2002) Med. Mycol. , vol.40 , pp. 225-242
    • San-Blas, G.1    Niño-Vega, G.2    Iturriaga, T.3
  • 33
    • 0027016372 scopus 로고
    • In vivo excision properties of bacteriophage lambda ZAP expression vectors. Strategene Cloning Systems, la Jolla, California 92037
    • Short J.M., Sorge J.A. In vivo excision properties of bacteriophage lambda ZAP expression vectors. Strategene Cloning Systems, La Jolla, California 92037. Methods Enzymol. 216:1992;495-508
    • (1992) Methods Enzymol. , vol.216 , pp. 495-508
    • Short, J.M.1    Sorge, J.A.2
  • 34
    • 0028567277 scopus 로고
    • Phase transition and stage-specific protein synthesis in the dimorphic fungus Paracoccidioides brasiliensis
    • Silva S.P., Felipe M.S.S., Pereira M., Azevedo M.O., Soares C.M.A. Phase transition and stage-specific protein synthesis in the dimorphic fungus Paracoccidioides brasiliensis. Exp. Mycol. 18:1994;294-299
    • (1994) Exp. Mycol. , vol.18 , pp. 294-299
    • Silva, S.P.1    Felipe, M.S.S.2    Pereira, M.3    Azevedo, M.O.4    Soares, C.M.A.5
  • 35
    • 0027518424 scopus 로고
    • Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase
    • Singh R., Green M.R. Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science. 259:1993;365-368
    • (1993) Science , vol.259 , pp. 365-368
    • Singh, R.1    Green, M.R.2
  • 36
    • 0006312118 scopus 로고    scopus 로고
    • Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology
    • Sirover M.A. Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology. J. Cell. Biochem. 65:1997;1-8
    • (1997) J. Cell. Biochem. , vol.65 , pp. 1-8
    • Sirover, M.A.1
  • 37
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover M.A. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochem. Biophys. Acta. 1432:1999;159-184
    • (1999) Biochem. Biophys. Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 38
    • 0036275173 scopus 로고    scopus 로고
    • Transferrin-binding in Staphylococcus aureus: Involvement of a cell-wall anchored protein
    • Taylor M., Heinrichs D.E. Transferrin-binding in Staphylococcus aureus: involvement of a cell-wall anchored protein. Mol. Microbiol. 43:2002;1603-1614
    • (2002) Mol. Microbiol. , vol.43 , pp. 1603-1614
    • Taylor, M.1    Heinrichs, D.E.2
  • 39
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gilbson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:1997;4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gilbson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.