Related ArticlesNMR-based metabolomics reveals the metabolite profiles of Vibrio parahaemolyticus under ferric iron stimulation.
J Microbiol. 2017 Aug;55(8):628-634
Authors: Zhou J, Lu C, Zhang D, Ma C, Su X
Abstract
Vibrio parahaemolyticus is a halophilic bacterium endemic to coastal areas, and its pathogenicity has caused widespread seafood poisoning. In our previous research, the protein expression of V. parahaemolyticus in Fe(3+) medium was determined using isobaric tags for relative and absolute quantitation (iTRAQ). Here, nuclear magnetic resonance (NMR) was used to detect changes in the V. parahaemolyticus metabolome. NMR spectra were obtained using methanol-water extracts of intracellular metabolites from V. parahaemolyticus under various culture conditions, and 62 metabolites were identified, including serine, arginine, alanine, ornithine, tryptophan, glutamine, malate, NAD(+), NADP(+), oxypurinol, xanthosine, dCTP, uracil, thymine, hypoxanthine, and betaine. Among these, 21 metabolites were up-regulated after the stimulation of the cells by ferric iron, and 9 metabolites were down-regulated. These metabolites are involved in amino acid and protein synthesis, energy metabolism, DNA and RNA synthesis and osmolality. Based on these results, we conclude that Fe(3+) influences the metabolite profiles of V. parahaemolyticus.
[NMR paper] 1H-NMR-Based Metabolomic Study for Identifying Serum Profiles Associated with the Response to Etanercept in Patients with Rheumatoid Arthritis.
1H-NMR-Based Metabolomic Study for Identifying Serum Profiles Associated with the Response to Etanercept in Patients with Rheumatoid Arthritis.
1H-NMR-Based Metabolomic Study for Identifying Serum Profiles Associated with the Response to Etanercept in Patients with Rheumatoid Arthritis.
PLoS One. 2015;10(11):e0138537
Authors: Priori R, Casadei L, Valerio M, Scrivo R, Valesini G, Manetti C
Abstract
OBJECTIVE: A considerable proportion of patients with rheumatoid arthritis (RA) do not have a satisfactory response to biological...
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11-13-2015 11:33 AM
[NMR paper] 1H-NMR metabolite profiles of different strains of Plasmodium falciparum.
1H-NMR metabolite profiles of different strains of Plasmodium falciparum.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-highwire.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles 1H-NMR metabolite profiles of different strains of Plasmodium falciparum.
Biosci Rep. 2014;34(6):e00150
Authors: Teng R, Lehane AM, Winterberg M, Shafik SH, Summers RL, Martin RE, van Schalkwyk DA,...
[NMR paper] Aqueous and lipid NMR metabolomic profiles of the earthworm Aporrectodea caliginosa show potential as an indicator species for environmental metabolomics.
Aqueous and lipid NMR metabolomic profiles of the earthworm Aporrectodea caliginosa show potential as an indicator species for environmental metabolomics.
Related Articles Aqueous and lipid NMR metabolomic profiles of the earthworm Aporrectodea caliginosa show potential as an indicator species for environmental metabolomics.
Environ Toxicol Chem. 2014 Jul 4;
Authors: Brown JN, Samuelsson L, Bernardi G, Gooneratne R, Larsson DJ
Abstract
The common pasture earthworm Aporrectodea caliginosa has often been neglected in environmental...
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[NMR paper] NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae.
NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae.
J Biol Chem. 2013 Oct 18;288(42):30597-606
Authors: Nedielkov R,...
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Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Proteins. 2011 Oct;79(10):2988-91
Authors: Aramini JM, Rossi P, Fischer M, Xiao R, Acton TB, Montelione GT
Abstract
Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri,...
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09-10-2011 06:51 PM
Nuclear magnetic resonance (NMR)-based drug metabolite profiling.
Nuclear magnetic resonance (NMR)-based drug metabolite profiling.
Nuclear magnetic resonance (NMR)-based drug metabolite profiling.
Methods Mol Biol. 2011;708:299-319
Authors: Lenz EM
The identification of drug metabolites in biofluids such as urine, plasma and bile is an important step in drug discovery and development. Proton nuclear magnetic resonance ((1)H-NMR) spectroscopy can provide detailed information regarding the structural transformation of a compound as a consequence of metabolism. However, successful identification of drug...
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04-09-2011 10:57 AM
[NMR paper] 13C NMR signal detection of iron-bound cyanide ions in ferric cyanide complexes of he
13C NMR signal detection of iron-bound cyanide ions in ferric cyanide complexes of heme proteins.
Related Articles 13C NMR signal detection of iron-bound cyanide ions in ferric cyanide complexes of heme proteins.
J Am Chem Soc. 2002 May 29;124(21):5936-7
Authors: Fujii H
13CN ion appears to have the greatest potential to probe the heme environment of the ferric heme proteins; however, a resonance of the iron-bound (13)CN ion in ferric heme proteins has not yet been located. We show here the first detection of (13)C NMR signals of the...
NMR-based metabolomics reveals the metabolite profiles of Vibrio parahaemolyticus under ferric iron stimulation.
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