Misassembly of full-length Disrupted-in-Schizophrenia 1 protein is linked to ... - Nature.com
Misassembly of full-length Disrupted-in-Schizophrenia 1 protein is linked to ... - Nature.com
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Misassembly of full-length Disrupted-in-Schizophrenia 1 protein is linked to ...
Nature.com
DISC1 protein pathology and its interaction with dopamine homeostasis is a novel cellular mechanism that is relevant for behavioral control and may have a role in mental illness. ..... (d) NMR analysis of ventricle size. The tgDISC1 rat (n=8) had a ...
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01-12-2016 04:01 PM
Solid-StateNMR of a Protein in a Precipitated Complexwith a Full-Length Antibody
Solid-StateNMR of a Protein in a Precipitated Complexwith a Full-Length Antibody
Jonathan M. Lamley, Dinu Iuga, Carl O?ster, Hans-Juergen Sass, Marco Rogowski, Andres Oss, Jaan Past, Andres Reinhold, Stephan Grzesiek, Ago Samoson and Jo?zef R. Lewandowski
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja5069992/20141118/images/medium/ja-2014-069992_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja5069992
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/iPedr9dmjv0
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11-20-2014 06:09 AM
[NMR paper] Solid-state NMR of a protein in a precipitated complex with a full-length antibody.
Solid-state NMR of a protein in a precipitated complex with a full-length antibody.
Solid-state NMR of a protein in a precipitated complex with a full-length antibody.
J Am Chem Soc. 2014 Nov 10;
Authors: Lamley JM, Iuga D, Oster C, Sass HJ, Rogowski M, Oss A, Past J, Reinhold A, Grzesiek S, Samoson A, Lewandowski JR
Abstract
NMR is a prime technique for characterizing atomic resolution structures and dynamics of biomolecular complexes but, for such systems, faces challenges of sensitivity and spectral resolution. We...
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11-11-2014 11:57 AM
Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR
Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus assembly and budding. While extensive structural information is known about the transmembrane helix and an adjacent amphipathic helix, the conformation of the N-terminal ectodomain and the C-terminal cytoplasmic tail remains largely unknown. Using two-dimensional (2D) magic-angle-spinning solid-state NMR, we have investigated the secondary structure and dynamics of full-length M2 (M2FL) and...
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10-07-2013 08:31 AM
[NMR paper] Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
Related Articles Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
FEBS J. 2013 Apr 20;
Authors: Renault M, García J, Cordeiro TN, Baldus M, Pons M
Abstract
Members of the histone-like nucleoid structuring protein (H-NS) family play roles both as architectural proteins and as modulators of gene expression in Gram-negative bacteria. The H-NS protein participates in modulatory processes...
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04-23-2013 08:37 PM
[NMR paper] Altered transition metal homeostasis in mice following manganese injections for manganese-enhanced magnetic resonance imaging.
Altered transition metal homeostasis in mice following manganese injections for manganese-enhanced magnetic resonance imaging.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Altered transition metal homeostasis in mice following manganese injections for manganese-enhanced magnetic resonance imaging.
Biometals. 2013 Feb;26(1):179-87
Authors: Moldovan N, Al-Ebraheem A, Miksys NA, Farquharson MJ, Bock NA
Abstract
In manganese-enhanced magnetic resonance...
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02-03-2013 10:19 AM
[NMR paper] NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima.
NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima.
Related Articles NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima.
J Biomol NMR. 2003 Feb;25(2):163-4
Authors: Ilin S, Hoskins A, Schwalbe H, Wöhnert J
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11-24-2010 09:01 PM
[NMR paper] NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231
NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).
FEBS Lett. 1997 Aug 18;413(2):282-8
Authors: Riek R, Hornemann S, Wider G, Glockshuber R, Wüthrich K
The recombinant murine prion protein, mPrP(23-231), was expressed in E. coli with uniform 15N-labeling. NMR experiments showed that the previously...