[NMR paper] The assessment of the quality of the graft in an animal model for lung transplantation using the metabolomics 1H high-resolution magic angle spinning NMR spectroscopy.
The assessment of the quality of the graft in an animal model for lung transplantation using the metabolomics 1H high-resolution magic angle spinning NMR spectroscopy.
Related ArticlesThe assessment of the quality of the graft in an animal model for lung transplantation using the metabolomics 1H high-resolution magic angle spinning NMR spectroscopy.
Magn Reson Med. 2012 Oct;68(4):1026-38
Authors: Benahmed MA, Santelmo N, Elbayed K, Frossard N, Noll E, Canuet M, Pottecher J, Diemunsch P, Piotto M, Massard G, Namer IJ
Abstract
Standards are needed to control the quality of the lungs from nonheart-beating donors as potential grafts. This was here assessed using the metabolomics 1H high-resolution magic angle spinning NMR spectroscopy. Selective perfusion of the porcine bilung block was set up 30 min after cardiac arrest with cold Perfadex®. Lung alterations were analyzed at 3, 6, and 8 h of cold ischemia as compared to baseline and to nonperfused lung. Metabolomics analysis of lung biopsies allowed identification of 35 metabolites. Levels of the majority of the metabolites increased over time at 4°C without perfusion, indicating cellular degradation, whereas levels of glutathione decreased. When lung was perfused at 4°C, levels of the majority of the metabolites remained stable, including levels of glutathione. Levels of uracil by contrast showed a reverse profile, as its signal increased over time in the absence of perfusion while being totally absent in perfused samples. Our results showed glutathione and uracil as potential biomarkers for the quality of the lung. The metabolomics 1H high-resolution magic angle spinning NMR spectroscopy can be efficiently applied for the assessment of the quality of the lung as an original technique characterized by a rapid assessment of intact biopsy samples without extraction and can be implemented in hospital environment.
[NMR paper] Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Acc Chem Res. 2013 Feb 13;
Authors: Yan S, Suiter CL, Hou G, Zhang H, Polenova T
Abstract
In living organisms, biological molecules often organize into multicomponent complexes. Such assemblies consist of various proteins and carry out essential functions, ranging from cell division, transport, and energy transduction to catalysis, signaling, and viral...
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02-14-2013 02:37 PM
[NMR paper] Magic angle spinning nuclear magnetic resonance spectroscopy of g protein-coupled receptors.
Magic angle spinning nuclear magnetic resonance spectroscopy of g protein-coupled receptors.
Related Articles Magic angle spinning nuclear magnetic resonance spectroscopy of g protein-coupled receptors.
Methods Enzymol. 2013;522:365-89
Authors: Goncalves J, Eilers M, South K, Opefi CA, Laissue P, Reeves PJ, Smith SO
Abstract
G protein-coupled receptors (GPCRs) represent the largest family of membrane receptors and mediate a diversity of cellular processes. These receptors have a common seven-transmembrane helix structure, yet have evolved...
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02-05-2013 09:51 PM
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Biochim Biophys Acta. 2011 Aug 3;
Authors: Gustavsson M, Traaseth NJ, Veglia G
In this paper, we analyzed the ground and excited states of phospholamban (PLN), a membrane protein that regulates sarcoplasmic reticulum calcium ATPase (SERCA), in different membrane mimetic environments....
[NMR paper] High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments.
High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments.
Related Articles High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments.
J Am Chem Soc. 2005 Jul 27;127(29):10138-9
Authors: Sillen A, Wieruszeski JM, Leroy A, Younes AB, Landrieu I, Lippens G
HRMAS NMR of tau paired helical fragments assembled with heparin show an intensity decrease for those amino acids that are incorporated into the rigid core...
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12-01-2010 06:56 PM
[NMR paper] Magic angle spinning solid-state NMR spectroscopy for structural studies of protein i
Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
Related Articles Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
J Am Chem Soc. 2004 Dec 22;126(50):16608-20
Authors: Marulanda D, Tasayco ML, McDermott A, Cataldi M, Arriaran V,...
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11-24-2010 10:03 PM
[NMR paper] Evidence of secondary structure by high-resolution magic angle spinning NMR spectrosc
Evidence of secondary structure by high-resolution magic angle spinning NMR spectroscopy of a bioactive peptide bound to different solid supports.
Related Articles Evidence of secondary structure by high-resolution magic angle spinning NMR spectroscopy of a bioactive peptide bound to different solid supports.
J Am Chem Soc. 2001 May 9;123(18):4130-8
Authors: Furrer J, Piotto M, Bourdonneau M, Limal D, Guichard G, Elbayed K, Raya J, Briand JP, Bianco A
The structure of the 19-amino acid peptide epitope, corresponding to the 141-159 sequence of...
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11-19-2010 08:32 PM
[NMR paper] High-resolution magic angle spinning 1H NMR spectroscopic studies on intact rat renal
High-resolution magic angle spinning 1H NMR spectroscopic studies on intact rat renal cortex and medulla.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles High-resolution magic angle spinning 1H NMR spectroscopic studies on intact rat renal cortex and medulla.
Magn Reson Med. 1999 Jun;41(6):1108-18
Authors: Garrod S, Humpfer E, Spraul M, Connor SC, Polley S, Connelly J, Lindon JC, Nicholson JK, Holmes E
High-resolution magic angle...