Related ArticlesProbing the intracellular glutathione redox potential by in-cell NMR spectroscopy.
Angew Chem Int Ed Engl. 2014 Jan 7;53(2):447-50
Authors: Rhieu SY, Urbas AA, Bearden DW, Marino JP, Lippa KA, Reipa V
Abstract
Non-invasive and real-time analysis of cellular redox processes has been greatly hampered by lack of suitable measurement techniques. Here we describe an in-cell nuclear magnetic resonance (NMR) based method for measuring the intracellular glutathione redox potential by direct and quantitative measurement of isotopically labeled glutathione introduced exogenously into living yeast. By using this approach, perturbations in the cellular glutathione redox homeostasis were also monitored as yeast cells were subjected to oxidative stress.
[NMR paper] Conformational analysis of oxidized peptide fragments of the C-terminal redox center in thioredoxin reductases by NMR spectroscopy.
Conformational analysis of oxidized peptide fragments of the C-terminal redox center in thioredoxin reductases by NMR spectroscopy.
Related Articles Conformational analysis of oxidized peptide fragments of the C-terminal redox center in thioredoxin reductases by NMR spectroscopy.
J Pept Sci. 2014 Mar 6;
Authors: Ruggles EL, Deker PB, Hondal RJ
Abstract
Vicinal disulfide rings (VDRs) occur when a disulfide bond forms between adjacent cysteine residues in a protein and results in a rare eight-membered ring structure. This eight-membered ring...
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[NMR paper] Detecting Intracellular Cysteine Redox States by in-Cell NMR Spectroscopy.
Detecting Intracellular Cysteine Redox States by in-Cell NMR Spectroscopy.
Related Articles Detecting Intracellular Cysteine Redox States by in-Cell NMR Spectroscopy.
Chembiochem. 2013 Jul 24;
Authors: Silvers R, Schwalbe H
Abstract
An in-cell perspective: Nowadays, in-cell NMR spectroscopy has proven to be a thrilling alternative for the investigation of biomacromolecules under physiological conditions at atomic resolution. A recent example demonstrating significant progress in in-cell NMR was published by the groups of Banci and Aricescu...
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[NMR paper] (1)H NMR spectroscopic studies on the characterization of renal cell lines and identification of novel potential markers of in vitro nephrotoxicity.
(1)H NMR spectroscopic studies on the characterization of renal cell lines and identification of novel potential markers of in vitro nephrotoxicity.
Related Articles (1)H NMR spectroscopic studies on the characterization of renal cell lines and identification of novel potential markers of in vitro nephrotoxicity.
Biomarkers. 1996;1(1):35-43
Authors: Anthony ML, McDowell PC, Gray TJ, Blackmore M, Nicholson JK
Abstract
Abstract Cell cultures are increasingly used in the evaluation of chemically-induced nephrotoxicity. The utili of renal cell...
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Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy
Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy
Abstract Cytochrome c (Cc) is a soluble electron carrier protein, transferring reducing equivalents between Cc reductase and Cc oxidase in eukaryotes. In this work, we assessed the structural differences between reduced and oxidized Cc in solution by paramagnetic NMR spectroscopy. First, we have obtained nearly-complete backbone NMR resonance assignments for iso-1-yeast Cc and horse Cc in both oxidation states. These were further used to derive pseudocontact shifts (PCSs) arising...
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Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Fabio Arnesano, Lucia Banci, Ivano Bertini, Isabella C. Felli, Maurizio Losacco and Giovanni Natile
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja207346p/aop/images/medium/ja-2011-07346p_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja207346p
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/9nWkAzWuq20
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Pb-207 NMR Spectroscopy Reveals that Pb(II) Coordinates with Glutathione (GSH) and Tris Cysteine Zinc Finger Proteins in a PbS(3) Coordination Environment.
Pb-207 NMR Spectroscopy Reveals that Pb(II) Coordinates with Glutathione (GSH) and Tris Cysteine Zinc Finger Proteins in a PbS(3) Coordination Environment.
Pb-207 NMR Spectroscopy Reveals that Pb(II) Coordinates with Glutathione (GSH) and Tris Cysteine Zinc Finger Proteins in a PbS(3) Coordination Environment.
J Inorg Biochem. 2011 Aug 1;105(8):1030-1034
Authors: Neupane KP, Pecoraro VL
(207)Pb NMR spectroscopy can be used to monitor the binding of Pb(II) to thiol rich biological small molecules such as glutathione and to zinc finger proteins. The...
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06-01-2011 02:30 PM
[NMR paper] Probing a CMP-Kdn synthetase by 1H, 31P, and STD NMR spectroscopy.
Probing a CMP-Kdn synthetase by 1H, 31P, and STD NMR spectroscopy.
Related Articles Probing a CMP-Kdn synthetase by 1H, 31P, and STD NMR spectroscopy.
Biochem Biophys Res Commun. 2005 Feb 11;327(2):565-70
Authors: Haselhorst T, Münster-Kühnel AK, Stolz A, Oschlies M, Tiralongo J, Kitajima K, Gerardy-Schahn R, von Itzstein M
CMP-Kdn synthetase catalyses the reaction of sialic acids (Sia) and cytidine-5'-triphosphate (CTP) to the corresponding activated sugar nucleotide CMP-Sia and pyrophosphate PP(i). STD NMR experiments of a recombinant...
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[NMR paper] Probing proteins in solution by (129)Xe NMR spectroscopy.
Probing proteins in solution by (129)Xe NMR spectroscopy.
Related Articles Probing proteins in solution by (129)Xe NMR spectroscopy.
J Magn Reson. 2001 Jun;150(2):167-74
Authors: Locci E, Dehouck Y, Casu M, Saba G, Lai A, Luhmer M, Reisse J, Bartik K
The interaction of xenon with different proteins in aqueous solution is investigated by (129)Xe NMR spectroscopy. Chemical shifts are measured in horse metmyoglobin, hen egg white lysozyme, and horse cytochrome c solutions as a function of xenon concentration. In these systems, xenon is in fast...