Determination of the Lithium Binding Site in Inositol Monophosphatase, the Putative Target for Lithium Therapy, by Magic-Angle-Spinning Solid-State NMR
Determination of the Lithium Binding Site in Inositol Monophosphatase, the Putative Target for Lithium Therapy, by Magic-Angle-Spinning Solid-State NMR
Anat Haimovich, Uzi Eliav and Amir Goldbourt
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja211794x/aop/images/medium/ja-2011-11794x_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja211794x
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Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Proteins. 2011 Oct;79(10):2988-91
Authors: Aramini JM, Rossi P, Fischer M, Xiao R, Acton TB, Montelione GT
Abstract
Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri,...
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09-10-2011 06:51 PM
1H NMR-based metabolic profiling reveals inherent biological variation in yeast and nematode model systems
1H NMR-based metabolic profiling reveals inherent biological variation in yeast and nematode model systems
Abstract The application of metabolomics to human and animal model systems is poised to provide great insight into our understanding of disease etiology and the metabolic changes that are associated with these conditions. However, metabolomic studies have also revealed that there is significant, inherent biological variation in human samples and even in samples from animal model systems where the animals are housed under carefully controlled conditions. This inherent biological...
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03-03-2011 02:06 AM
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
Chemistry. 2011 Feb 1;17(5):1547-1560
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-),...
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01-27-2011 02:52 PM
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
Chemistry. 2011 Jan 5;
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-), with the broadly...
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01-06-2011 11:21 AM
[NMR paper] Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation p
Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli.
Related Articles Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli.
J Mol Biol. 2003 Mar 21;327(2):521-36
Authors: Huang YJ, Swapna GV, Rajan PK, Ke H, Xia B, Shukla K, Inouye M, Montelione GT
Ribosome-binding factor A (RbfA) from Escherichia coli is a cold-shock adaptation protein. It is essential for efficient processing of 16S rRNA and is suspected to interact with...
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11-24-2010 09:01 PM
[NMR paper] Yeast heat shock transcription factor N-terminal activation domains are unstructured
Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.
Protein Sci. 1996 Feb;5(2):262-9...
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08-22-2010 02:27 PM
[NMR paper] Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arg
Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arginine residues are crucial for binding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arginine residues are crucial for binding.
Biochem J. 1995 Dec 1;312 ( Pt 2):357-65
Authors: Mayo KH, Ilyina E, Roongta V, Dundas M, Joseph J, Lai CK, Maione T, Daly TJ
Native platelet factor-4 (PF4) is an...
Solution NMR Structureof Yeast Succinate DehydrogenaseFlavinylation Factor Sdh5 Reveals a Putative Sdh1 Binding Site
Linear Mode
