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Volumn 386, Issue 1, 2009, Pages 53-58

Quantitative determination of cyclic diguanosine monophosphate concentrations in nucleotide extracts of bacteria by matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry

Author keywords

c di GMP; HPLC; MALDI TOF; Quantification

Indexed keywords

BIOCHEMISTRY; CELL SIGNALING; ESCHERICHIA COLI; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PHYSIOLOGICAL MODELS; SALMONELLA;

EID: 58749088368     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.12.013     Document Type: Article
Times cited : (62)

References (22)
  • 1
    • 22644438480 scopus 로고    scopus 로고
    • C-di-GMP: the dawning of a novel bacterial signalling system
    • Römling U., Gomelsky M., and Galperin M.Y. C-di-GMP: the dawning of a novel bacterial signalling system. Mol. Microbiol. 57 (2005) 629-639
    • (2005) Mol. Microbiol. , vol.57 , pp. 629-639
    • Römling, U.1    Gomelsky, M.2    Galperin, M.Y.3
  • 2
    • 23944523895 scopus 로고    scopus 로고
    • A census of membrane-bound and intracellular signal transduction proteins in bacteria: bacterial IQ, extroverts, and introverts
    • Galperin M.Y. A census of membrane-bound and intracellular signal transduction proteins in bacteria: bacterial IQ, extroverts, and introverts. BMC Microbiol. 5 (2005) 35
    • (2005) BMC Microbiol. , vol.5 , pp. 35
    • Galperin, M.Y.1
  • 3
    • 1842451699 scopus 로고    scopus 로고
    • Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain
    • Paul R., Weiser S., Amiot N.C., Chan C., Schirmer T., Giese B., and Jenal U. Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain. Genes Dev. 18 (2004) 715-727
    • (2004) Genes Dev. , vol.18 , pp. 715-727
    • Paul, R.1    Weiser, S.2    Amiot, N.C.3    Chan, C.4    Schirmer, T.5    Giese, B.6    Jenal, U.7
  • 4
    • 21844451590 scopus 로고    scopus 로고
    • The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains
    • Schmidt A.J., Ryjenkov D.A., and Gomelsky M. The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J. Bacteriol. 187 (2005) 4774-4781
    • (2005) J. Bacteriol. , vol.187 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 6
    • 4344688129 scopus 로고    scopus 로고
    • GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility
    • Simm R., Morr M., Kader A., Nimtz M., and Römling U. GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility. Mol. Microbiol. 53 (2004) 1123-1134
    • (2004) Mol. Microbiol. , vol.53 , pp. 1123-1134
    • Simm, R.1    Morr, M.2    Kader, A.3    Nimtz, M.4    Römling, U.5
  • 7
    • 3843069972 scopus 로고    scopus 로고
    • Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation
    • Tischler A.D., and Camilli A. Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation. Mol. Microbiol. 53 (2004) 857-869
    • (2004) Mol. Microbiol. , vol.53 , pp. 857-869
    • Tischler, A.D.1    Camilli, A.2
  • 8
    • 0020443521 scopus 로고
    • Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography
    • Bochner B.R., and Ames B.N. Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography. J. Biol. Chem. 257 (1982) 9759-9769
    • (1982) J. Biol. Chem. , vol.257 , pp. 9759-9769
    • Bochner, B.R.1    Ames, B.N.2
  • 9
    • 0028170485 scopus 로고
    • Peptide sequence information derived by partial acid hydrolysis and matrix-assisted laser desorption/ionization mass spectrometry
    • Vorm O., and Roepstorff P. Peptide sequence information derived by partial acid hydrolysis and matrix-assisted laser desorption/ionization mass spectrometry. Biol. Mass Spectrom. 23 (1994) 734-740
    • (1994) Biol. Mass Spectrom. , vol.23 , pp. 734-740
    • Vorm, O.1    Roepstorff, P.2
  • 10
    • 0020491164 scopus 로고
    • RNA polymerase: linear competitive inhibition by bis-(3′ to 5′)-cyclic dinucleotides, NpNp
    • Hsu C.Y., and Dennis D. RNA polymerase: linear competitive inhibition by bis-(3′ to 5′)-cyclic dinucleotides, NpNp. Nucleic Acids Res. 10 (1982) 5637-5647
    • (1982) Nucleic Acids Res. , vol.10 , pp. 5637-5647
    • Hsu, C.Y.1    Dennis, D.2
  • 11
    • 4344668297 scopus 로고
    • Synthesis of ribonucleoside 3′, 5′-cyclic phosphorothioates using a modified hydroxybenzotriazole phosphotriester approach
    • de Vroom E., van der Marel G.A., and van Boom J.H. Synthesis of ribonucleoside 3′, 5′-cyclic phosphorothioates using a modified hydroxybenzotriazole phosphotriester approach. Recl. Trav. Chim. Pays-Bas 106 (1987) 577-580
    • (1987) Recl. Trav. Chim. Pays-Bas , vol.106 , pp. 577-580
    • de Vroom, E.1    van der Marel, G.A.2    van Boom, J.H.3
  • 12
    • 0031896213 scopus 로고    scopus 로고
    • Multicellular and aggregative behavior of Salmonella typhimurium strains is controlled by mutations in the agfD promoter
    • Römling U., Sierralta W.D., Eriksson K., and Normark S. Multicellular and aggregative behavior of Salmonella typhimurium strains is controlled by mutations in the agfD promoter. Mol. Microbiol. 28 (1998) 249-264
    • (1998) Mol. Microbiol. , vol.28 , pp. 249-264
    • Römling, U.1    Sierralta, W.D.2    Eriksson, K.3    Normark, S.4
  • 13
    • 33645894689 scopus 로고    scopus 로고
    • Cyclic di-GMP as a second messenger
    • Römling U., and Amikam D. Cyclic di-GMP as a second messenger. Curr. Opin. Microbiol. 9 (2006) 218-228
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 218-228
    • Römling, U.1    Amikam, D.2
  • 14
    • 33645819810 scopus 로고    scopus 로고
    • Hierarchical involvement of various GGDEF domain proteins in rdar morphotype development of Salmonella enterica serovar Typhimurium
    • Kader A., Simm R., Gerstel U., Morr M., and Römling U. Hierarchical involvement of various GGDEF domain proteins in rdar morphotype development of Salmonella enterica serovar Typhimurium. Mol. Microbiol. 60 (2006) 602-616
    • (2006) Mol. Microbiol. , vol.60 , pp. 602-616
    • Kader, A.1    Simm, R.2    Gerstel, U.3    Morr, M.4    Römling, U.5
  • 16
    • 43049087389 scopus 로고    scopus 로고
    • Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates
    • Witte G., Hartung S., Buttner K., and Hopfner K.P. Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates. Mol. Cell 30 (2008) 167-178
    • (2008) Mol. Cell , vol.30 , pp. 167-178
    • Witte, G.1    Hartung, S.2    Buttner, K.3    Hopfner, K.P.4
  • 17
    • 34247566143 scopus 로고    scopus 로고
    • Role of EAL-containing proteins in multicellular behavior of Salmonella enterica serovar Typhimurium
    • Simm R., Lusch A., Kader A., Andersson M., and Römling U. Role of EAL-containing proteins in multicellular behavior of Salmonella enterica serovar Typhimurium. J. Bacteriol. 189 (2007) 3613-3623
    • (2007) J. Bacteriol. , vol.189 , pp. 3613-3623
    • Simm, R.1    Lusch, A.2    Kader, A.3    Andersson, M.4    Römling, U.5
  • 19
    • 0015750359 scopus 로고
    • Purification and regulation of glucose-6-phosphate dehydrogenase from Bacillus licheniformis
    • Opheim D., and Bernlohr R.W. Purification and regulation of glucose-6-phosphate dehydrogenase from Bacillus licheniformis. J. Bacteriol. 116 (1973) 1150-1159
    • (1973) J. Bacteriol. , vol.116 , pp. 1150-1159
    • Opheim, D.1    Bernlohr, R.W.2
  • 20
    • 51649096200 scopus 로고    scopus 로고
    • The RNA binding protein CsrA controls c-di-GMP metabolism by directly regulating the expression of GGDEF proteins
    • Jonas K., Edwards A.N., Simm R., Romeo T., Römling U., and Melefors O. The RNA binding protein CsrA controls c-di-GMP metabolism by directly regulating the expression of GGDEF proteins. Mol. Microbiol. 70 (2008) 236-257
    • (2008) Mol. Microbiol. , vol.70 , pp. 236-257
    • Jonas, K.1    Edwards, A.N.2    Simm, R.3    Romeo, T.4    Römling, U.5    Melefors, O.6
  • 21
    • 34548428704 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa cupA-encoded fimbriae expression is regulated by a GGDEF and EAL domain-dependent modulation of the intracellular level of cyclic diguanylate
    • Meissner A., Wild V., Simm R., Rohde M., Erck C., Bredenbruch F., Morr M., Römling U., and Häussler S. Pseudomonas aeruginosa cupA-encoded fimbriae expression is regulated by a GGDEF and EAL domain-dependent modulation of the intracellular level of cyclic diguanylate. Environ. Microbiol. 9 (2007) 2475-2485
    • (2007) Environ. Microbiol. , vol.9 , pp. 2475-2485
    • Meissner, A.1    Wild, V.2    Simm, R.3    Rohde, M.4    Erck, C.5    Bredenbruch, F.6    Morr, M.7    Römling, U.8    Häussler, S.9
  • 22
    • 0031932327 scopus 로고    scopus 로고
    • Curli fibers are highly conserved between Salmonella typhimurium and Escherichia coli with respect to operon structure and regulation
    • Römling U., Bian Z., Hammar M., Sierralta W.D., and Normark S. Curli fibers are highly conserved between Salmonella typhimurium and Escherichia coli with respect to operon structure and regulation. J. Bacteriol. 180 (1998) 722-731
    • (1998) J. Bacteriol. , vol.180 , pp. 722-731
    • Römling, U.1    Bian, Z.2    Hammar, M.3    Sierralta, W.D.4    Normark, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.