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Oncol Res. 1993;5(3):119-26
Authors: Rasmussen J, Hansen LL, Friche E, Jaroszewski JW
Steady-state 31P NMR spectra of wild type EHR2 Ehrlich ascites tumor cells and multidrug resistant EHR2/DNR+ cells, immobilized in agarose threads, and continuously perfused with medium, showed temperature-dependent differences in the levels of intracellular phosphate metabolites. At 37 degrees C, the EHR2/DNR+ cells contained four times more phosphocreatine (PCr) than the EHR2 cells. At 20 degrees C, the EHR2 cells contained 80% more of phosphodiesters (PDE), the levels of PCr being equal. The quantitative metabolite level data are based on T1 relaxation times data and are normalized for the protein content of the cells. Perfusion of the cells with azide, an inhibitor of mitochondrial respiration, had no effect on the ATP level, and caused no changes in glucose consumption and lactate production. Azide perfusion, combined with glucose depletion, caused rapid drop in the ATP content, which was reestablished after renewed perfusion with glucose. Similarly, perfusion with 2,4-dinitrophenol, an uncoupler of the respiration chain, had no effect on the phosphate metabolites. These results demonstrate that aerobic glycolysis is the main route by which glucose is metabolised under the conditions used (glucose concentration in medium 2 g/L). Rates of uptake and phosphorylation of 2-deoxy-D-glucose were measured by following the formation of intracellular [6-13C]2-deoxy-D-glucose-6-phosphate by 13C NMR; at 37 degrees C the observed rates for EHR2 and EHR2/DNR+ cells were equal, about 10 nmol/(min x mg protein), whereas at 20 degrees C the wild type cells produced the 6-phosphate at an approximately twice the rate found for the resistant cells [about 4 and 2 nmol/(min x mg protein), respectively].(ABSTRACT TRUNCATED AT 250 WORDS)
An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.
An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.
An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.
Proteins. 2011 May 16;
Authors: Gayen S, Li Q, Chen AS, Nguyen TH, Huang Q, Hill J, Kang C
The human Ether-à-go-go Related Gene (hERG) potassium channel plays an important role in the heart by controlling the rapid delayed rectifier current. The N-terminal 135 residues (NTD) contain a Per-Arnt-Sim (PAS) domain and an N-terminal amphipathic helix....
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[NMR paper] Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cel
Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cells are modulated by rafts.
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Cancer Cell Int. 2005 Feb 9;5(1):2
Authors: Mannechez A, Reungpatthanaphong P, de Certaines JD, Leray G, Le Moyec L
BACKGROUND: Most cancer cells are characterized by mobile lipids visible on proton NMR (1H-NMR), these being comprised mainly of methyl and methylene signals from lipid acyl chains....
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[NMR paper] Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for
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FEBS Lett. 2004 Jun 18;568(1-3):117-21
Authors: Mason AJ, Siarheyeva A, Haase W, Lorch M, van Veen H, Glaubitz C
The ABC transporter LmrA in Lactococcus lactis confers resistance to a wide range of antibiotics and cytotoxic drugs and is a functional homologue of P-glycoprotein. Recently, solid-state NMR...
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[NMR paper] Study of electrostatic potential surface distribution of wild-type plastocyanin Synec
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Biopolymers. 2003 Oct;70(2):212-20
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Plastocyanin is a small (approximately 10 kDa), type I blue copper protein that works as an electron donor to photosystem I from cytochrome f in both chloroplast systems and in some...
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[NMR paper] 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
Biophys J. 1994 Jun;66(6):2111-26
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[NMR paper] 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
Biophys J. 1994 Jun;66(6):2111-26
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[NMR paper] Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
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Eur J Biochem. 1991 Aug 15;200(1):139-48
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Recording of good quality NMR spectra of the single-stranded DNA binding protein gene V of the...
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[NMR paper] Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
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Eur J Biochem. 1991 Aug 15;200(1):139-48
Authors: Folkers PJ, Stassen AP, van Duynhoven JP, Harmsen BJ, Konings RN, Hilbers CW
Recording of good quality NMR spectra of the single-stranded DNA binding protein gene V of the...