[NMR paper] Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Chemistry. 2013 Aug 12;
Authors: Diana D, Smaldone G, De Antonellis P, Pirone L, Carotenuto M, Alonzi A, Di Gaetano S, Zollo M, Pedone EM, Fattorusso R
Abstract
Get well prune: The C-terminal third domain of h-prune is largely unfolded and involved in relevant protein-protein interactions, particularly with...
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08-14-2013 05:24 PM
[NMR paper] Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR an
Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.
Related Articles Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.
Biochemistry. 2004 Aug 17;43(32):10393-9
Authors: Lysek DA, Wüthrich K
Transmissible spongiform encephalopathies have been observed exclusively in organisms expressing the host-encoded prion protein (PrP). The function of the cellular isoform of PrP found in healthy organisms has so far not been identified,...
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11-24-2010 10:01 PM
[NMR paper] Solution NMR structure of the C-terminal domain of the human protein DEK.
Solution NMR structure of the C-terminal domain of the human protein DEK.
Related Articles Solution NMR structure of the C-terminal domain of the human protein DEK.
Protein Sci. 2004 Aug;13(8):2252-9
Authors: Devany M, Kotharu NP, Matsuo H
The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these...
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11-24-2010 09:51 PM
[NMR paper] The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA bindi
The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.
Related Articles The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.
J Mol Biol. 1999 Jul 9;290(2):495-504
Authors: Aihara H, Ito Y, Kurumizaka H, Yokoyama S, Shibata T
Human Rad51 protein (HsRad51) is a homolog of Escherichia coli RecA protein, and functions in DNA repair and recombination. In higher eukaryotes, Rad51 protein is essential for cell viability. The...
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11-18-2010 08:31 PM
[NMR paper] NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotei
NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments.
Related Articles NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments.
Protein Eng. 1998 Oct;11(10):847-53
Authors: McAlister MS, Davis B, Pfuhl M, Driscoll PC
CD5 is a type-I transmembrane glycoprotein found on thymocytes, T-cells and a subset of B-cells. The extracellular region consists of three domains belonging to the...
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11-17-2010 11:15 PM
[NMR paper] Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia col
Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
Biochemistry. 1997 Mar 4;36(9):2517-30
Authors: Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM
...
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08-22-2010 03:31 PM
[NMR paper] NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A pro
NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A protein.
EMBO J. 1994 Aug 15;13(16):3873-81
Authors: Howe PW, Nagai K, Neuhaus D, Varani G
The RNP domain is a very common motif found in hundreds of proteins, including many protein components of the RNA processing machinery. The 70-90...
The C-terminal domain of human Cdc37 studied by solution NMR
Linear Mode
