[NMR paper] NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.
NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.
Related Articles NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.
Nat Commun. 2013;4:1890
Authors: Byeon IJ, Ahn J, Mitra M, Byeon CH, Hercík K, Hritz J, Charlton LM, Levin JG, Gronenborn AM
Abstract
Human APOBEC3A is a single-stranded DNA cytidine deaminase that restricts viral pathogens and endogenous retrotransposons, and has a role in the innate immune response. Furthermore, its...
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The NMR Structure of FliK, the Trigger for the Switch of Substrate Specificity in the Flagellar Type III Secretion Apparatus.
The NMR Structure of FliK, the Trigger for the Switch of Substrate Specificity in the Flagellar Type III Secretion Apparatus.
The NMR Structure of FliK, the Trigger for the Switch of Substrate Specificity in the Flagellar Type III Secretion Apparatus.
J Mol Biol. 2011 Apr 12;
Authors: Mizuno S, Amida H, Kobayashi N, Aizawa SI, Tate SI
The flagellar cytoplasmic protein FliK controls hook elongation by two successive events: by determining hook length and by stopping the supply of hook protein. These two distinct roles are assigned to different...
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[NMR paper] Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immuno
Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor.
Related Articles Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor.
J Biol Chem. 2000 May 26;275(21):16174-82
Authors: Gaul BS, Harrison ML, Geahlen RL, Burton RA, Post CB
The immunoreceptor tyrosine-based activation motif (ITAM) plays a central role...
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11-18-2010 09:15 PM
Arginine Kinase. Joint Crystallographic and NMR RDC Analyses link Substrate-Associate
Arginine Kinase. Joint Crystallographic and NMR RDC Analyses link Substrate-Associated Motions to Intrinsic Flexibility.
Related Articles Arginine Kinase. Joint Crystallographic and NMR RDC Analyses link Substrate-Associated Motions to Intrinsic Flexibility.
J Mol Biol. 2010 Nov 11;
Authors: Niu X, Brüschweiler-Li L, Davulcu O, Skalicky JJ, Brüschweiler R, Chapman MS
The phosphagen kinase family, including creatine and arginine kinases, catalyze the reversible transfer of a "high energy" phosphate between ATP and a phospho-guanidino substrate. They...
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Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.
Related Articles Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.
J Am Chem Soc. 2010 Aug 20;
Authors: Hu Y, Zhao E, Li H, Xia B, Jin C
The twin-arginine transport (Tat) system translocates folded proteins across the bacterial cytoplasmic or chloroplast thylakoid membrane of plants. The Tat system in most Gram-positive...
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[NMR paper] Partial purification and substrate specificity of heparan sulfate alpha-N-acetylgluco
Partial purification and substrate specificity of heparan sulfate alpha-N-acetylglucosaminyltransferase I: synthesis, NMR spectroscopic characterization and in vitro assays of two aryl tetrasaccharides.
Related Articles Partial purification and substrate specificity of heparan sulfate alpha-N-acetylglucosaminyltransferase I: synthesis, NMR spectroscopic characterization and in vitro assays of two aryl tetrasaccharides.
Glycobiology. 1997 Jul;7(5):587-95
Authors: Fritz TA, Agrawal PK, Esko JD, Krishna NR
Studies of heparan sulfate biosynthesis...
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[NMR paper] Partial purification and substrate specificity of heparan sulfate alpha-N-acetylgluco
Partial purification and substrate specificity of heparan sulfate alpha-N-acetylglucosaminyltransferase I: synthesis, NMR spectroscopic characterization and in vitro assays of two aryl tetrasaccharides.
Related Articles Partial purification and substrate specificity of heparan sulfate alpha-N-acetylglucosaminyltransferase I: synthesis, NMR spectroscopic characterization and in vitro assays of two aryl tetrasaccharides.
Glycobiology. 1997 Jul;7(5):587-95
Authors: Fritz TA, Agrawal PK, Esko JD, Krishna NR
Studies of heparan sulfate biosynthesis...
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Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis
Yunfei Hu et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1053785/aop/images/medium/ja-2010-053785_0001.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society
Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity
Linear Mode
