[NMR paper] Evidence for novel action at the cell binding site of human Angiogenin revealed by heteronuclear NMR spectroscopy, in silico and in vivo studies.
Evidence for novel action at the cell binding site of human Angiogenin revealed by heteronuclear NMR spectroscopy, in silico and in vivo studies.
Evidence for novel action at the cell binding site of human Angiogenin revealed by heteronuclear NMR spectroscopy, in silico and in vivo studies.
ChemMedChem. 2018 Jan 04;:
Authors: Chatzileontiadou DS, Tsika AC, Diamantopoulou Z, Delbé J, Badet J, Courty J, Skamnaki VT, Parmenopoulou V, Komiotis D, Hayes JM, Spyroulias GA, Leonidas DD
Abstract
A member of Ribonuclease A superfamily,...
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01-10-2018 12:45 PM
[NMR paper] Direct structural evidence of protein redox regulation obtained by in-cell NMR.
Direct structural evidence of protein redox regulation obtained by in-cell NMR.
Direct structural evidence of protein redox regulation obtained by in-cell NMR.
Biochim Biophys Acta. 2015 Nov 14;
Authors: Mercatelli E, Barbieri L, Luchinat E, Banci L
Abstract
The redox properties of cellular environments are critical to many functional processes, and are strictly controlled in all living organisms. The glutathione-glutathione disulfide (GSH-GSSG) couple is the most abundant intracellular redox couple. A GSH redox potential can be...
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11-22-2015 03:54 PM
Direct structural evidence of protein redox regulation obtained by in-cell NMR
Direct structural evidence of protein redox regulation obtained by in-cell NMR
Publication date: Available online 14 November 2015
Source:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research</br>
Author(s): Eleonora Mercatelli, Letizia Barbieri, Enrico Luchinat, Lucia Banci</br>
The redox properties of cellular environments are critical to many functional processes, and are strictly controlled in all living organisms. The glutathione-glutathione disulfide (GSH-GSSG) couple is the most abundant intracellular redox couple. A GSH redox potential can be...
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11-17-2015 02:57 PM
[NMR paper] Protein interaction patterns in different cellular environments are revealed by in-cell NMR.
Protein interaction patterns in different cellular environments are revealed by in-cell NMR.
Related Articles Protein interaction patterns in different cellular environments are revealed by in-cell NMR.
Sci Rep. 2015;5:14456
Authors: Barbieri L, Luchinat E, Banci L
Abstract
In-cell NMR allows obtaining atomic-level information on biological macromolecules in their physiological environment. Soluble proteins may interact with the cellular environment in different ways: either specifically, with their functional partners, or...
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09-26-2015 05:13 AM
[NMR paper] Probing the intracellular glutathione redox potential by in-cell NMR spectroscopy.
Probing the intracellular glutathione redox potential by in-cell NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Probing 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...
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10-24-2014 07:18 PM
[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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07-31-2013 12:00 PM
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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02-13-2012 02:34 AM
[Question from NMRWiki Q&A forum] How to check acquisition status of the NMR instrument remotely?
How to check acquisition status of the NMR instrument remotely?
Hello, does anyone know whether the instrument is busy or not by logging in remotely?
How do you do that on the platform that you are using?
Thanks.
BalancedRegulation of Redox Status of IntracellularThioredoxin Revealed by in-Cell NMR
Linear Mode
