UK scientists have used NMR for the first time to develop a 3D picture of a herpes virus protein interacting with a key part of the human cellular machinery. The study improves our understanding of how the virus hijacks human cells and could eventually lead to new targets for drug therapy.
NMR reveals novel mechanisms of protein activity regulation.
NMR reveals novel mechanisms of protein activity regulation.
NMR reveals novel mechanisms of protein activity regulation.
Protein Sci. 2011 Mar 14;
Authors: Kalodimos CG
NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide site-resolved information about the conformation entropy of binding, as well as about energetically excited...
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03-16-2011 04:15 PM
Herpes hitches a ride on cellular protein - LabnewsOnline
Herpes hitches a ride on cellular protein - LabnewsOnline
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Herpes hitches a ride on cellular protein
LabnewsOnline
Using NMR, the team from the University of Manchester were able to produce images of a herpes protein interacting with a mouse cellular protein. ...
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02-04-2011 07:12 PM
Herpes 3D: NMR reveals viral protein hijacking - spectroscopyNOW.com
Herpes 3D: NMR reveals viral protein hijacking - spectroscopyNOW.com
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Herpes 3D: NMR reveals viral protein hijacking
spectroscopyNOW.com
UK scientists have used solution-state NMR spectroscopy for the first time to develop a 3D picture of a herpes virus protein interacting with a key part of ...
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01-15-2011 02:09 AM
[NMR paper] NMR assignment of the apo and peptide-bound SH2 domain from the Rous sarcoma viral protein Src.
NMR assignment of the apo and peptide-bound SH2 domain from the Rous sarcoma viral protein Src.
Related Articles NMR assignment of the apo and peptide-bound SH2 domain from the Rous sarcoma viral protein Src.
J Biomol NMR. 2005 Aug;32(4):339
Authors: Taylor JD, Fawaz RR, Ababou A, Williams MA, Ladbury JE
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[NMR paper] NMR structures of anti-HIV D-peptides derived from the N-terminus of viral chemokine vMIP-II.
NMR structures of anti-HIV D-peptides derived from the N-terminus of viral chemokine vMIP-II.
Related Articles NMR structures of anti-HIV D-peptides derived from the N-terminus of viral chemokine vMIP-II.
Biochem Biophys Res Commun. 2005 Sep 30;335(3):651-8
Authors: Mori M, Liu D, Kumar S, Huang Z
The viral macrophage inflammatory protein-II (vMIP-II) encoded by Kaposi's sarcoma-associated herpesvirus has unique biological activities in that it blocks the cell entry by several different human immunodeficiency virus type 1 (HIV-1) strains via...
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[NMR paper] The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of co
The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.
Related Articles The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.
Nat Struct Biol. 2000 Apr;7(4):329-35
Authors: Varani L, Gunderson SI, Mattaj IW, Kay LE, Neuhaus D, Varani G
The status of the poly(A) tail at the 3'-end of mRNAs controls the expression of numerous genes in response to...
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11-18-2010 09:15 PM
[NMR paper] NMR studies of a viral protein that mimics the regulators of complement activation.
NMR studies of a viral protein that mimics the regulators of complement activation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of a viral protein that mimics the regulators of complement activation.
J Mol Biol. 1997 Sep 19;272(2):253-65
Authors: Wiles AP, Shaw G, Bright J, Perczel A, Campbell ID, Barlow PN
Vaccinia virus complement control protein (VCP) is a 243-residue protein that is similar in sequence to the regulators of complement activation; its...
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08-22-2010 05:08 PM
[NMR paper] Computer-aided assignment of the 1H-NMR spectrum of the viral-protein-genome-linked p
Computer-aided assignment of the 1H-NMR spectrum of the viral-protein-genome-linked polypeptide from cowpea mosaic virus.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Computer-aided assignment of the 1H-NMR spectrum of the viral-protein-genome-linked polypeptide from cowpea mosaic virus.
Eur J Biochem. 1990 Jul 5;190(3):583-91
Authors: van de Ven FJ, Lycksell PO, van Kammen A, Hilbers CW
The 1H-NMR spectrum of the...
Herpes 3D: NMR reveals viral protein hijacking
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