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
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 ...
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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[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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[NMR paper] 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.
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 Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR.
Protein Sci. 2013 Sep 10;
Authors: Liao SY, Fritzsching KJ, Hong M
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus...
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09-12-2013 11:02 PM
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 (TM) helix and an adjacent amphipathic helix (AH), the conformation of the N-terminal ectodomain and the C-terminal cytoplasmic tail remains largely unknown. Using 2D magic-angle-spinning (MAS) solid-state NMR, we have investigated the secondary structure and dynamics of full-length M2 (M2FL) and...
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09-10-2013 08:44 PM
[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] 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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[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...
Misassembly of full-length Disrupted-in-Schizophrenia 1 protein is linked to ... - Nature.com
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