Magnaporthe (physiology) < Magnetic Resonance Spectroscopy (MeSH) < Magnetic Resonance Spectroscopy (methods)

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List of bibliographic references indexed by Magnetic Resonance Spectroscopy (MeSH)

Number of relevant bibliographic references: 38.
[20-40] [0 - 20][0 - 38]

Ident.	Authors (with country if any)	Title
001008 (2001)	N. Foloppe [Suède] ; J. Sagemark ; K. Nordstrand ; K D Berndt ; L. Nilsson	Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: comparison with functionally related proteins.
001011 (2001)	J W Cave [États-Unis] ; H S Cho ; A M Batchelder ; H. Yokota ; R. Kim ; D E Wemmer	Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii.
001029 (2001)	J S Fetrow [États-Unis] ; N. Siew ; J A Di Gennaro ; M. Martinez-Yamout ; H J Dyson ; J. Skolnick	Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight?
001081 (2000)	D Y Lee [Corée du Sud] ; B Y Ahn ; K S Kim	A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities.
001099 (1999)	K. Nordstrand [Suède] ; F. Slund ; A. Holmgren ; G. Otting ; K D Berndt	NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism.
001115 (1999)	M J Berardi [États-Unis] ; J H Bushweller	Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction.
001129 (1998)	C. Sun [États-Unis] ; M J Berardi ; J H Bushweller	The NMR solution structure of human glutaredoxin in the fully reduced form.
001177 (1997)	C. Sun [États-Unis] ; A. Holmgren ; J H Bushweller	Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form.
001178 (1997)	J J Kelley [États-Unis] ; T M Caputo ; S F Eaton ; T M Laue ; J H Bushweller	Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements.
001192 (1996)	D M Lemaster [États-Unis]	Structural determinants of the catalytic reactivity of the buried cysteine of Escherichia coli thioredoxin.
001201 (1996)	R. Koradi [Suisse] ; M. Billeter ; K. Wüthrich	MOLMOL: a program for display and analysis of macromolecular structures.
001204 (1996)	F. Aslund [Suède] ; K. Nordstrand ; K D Berndt ; M. Nikkola ; T. Bergman ; H. Ponstingl ; H. Jörnvall ; G. Otting ; A. Holmgren	Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis.
001218 (1995)	D L Rabenstein [États-Unis] ; K K Millis	Nuclear magnetic resonance study of the thioltransferase-catalyzed glutathione/glutathione disulfide interchange reaction.
001220 (1995)	T. Kortemme [Allemagne] ; T E Creighton	Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family.
001273 (1993)	J H Bushweller [Suisse] ; A. Holmgren ; K. Wüthrich	Biosynthetic 15N and 13C isotope labelling of glutathione in the mixed disulfide with Escherichia coli glutaredoxin documented by sequence-specific NMR assignments.
001280 (1992)	J H Bushweller [Suède] ; F. Aslund ; K. Wüthrich ; A. Holmgren	Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14----S) and its mixed disulfide with glutathione.
001295 (1991)	P. Sodano [Suisse] ; T H Xia ; J H Bushweller ; O. Björnberg ; A. Holmgren ; M. Billeter ; K. Wüthrich	Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin.
001299 (1991)	P. Sodano [Suisse] ; K V Chary ; O. Björnberg ; A. Holmgren ; B. Kren ; J A Fuchs ; K. Wüthrich	Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin. Sequence-specific assignments and secondary structure determination of the oxidized form.

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