Protéines virales (métabolisme) < Protéines végétales (MeSH) < Protéines végétales (analyse)

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List of bibliographic references indexed by Protéines végétales (MeSH)

Number of relevant bibliographic references: 10.

Ident.	Authors (with country if any)	Title
000271 (2008)	Fang Li [République populaire de Chine] ; Yi Zhang ; Meimei Wang ; Ying Zhang ; Xiaoliang Wu ; Xingqi Guo	Molecular cloning and expression characteristics of alternative oxidase gene of cotton (Gossypium hirsutum).
000274 (2008)	Shukui Guo [Canada] ; Jason Boyd ; Ramaswami Sammynaiken ; Michèle C. Loewen	Identification and characterization of a unique cysteine residue proximal to the catalytic site of Arabidopsis thaliana carotenoid cleavage enzyme 1.
000431 (2000)	J F Eisses [États-Unis] ; J P Stasser ; M. Ralle ; J H Kaplan ; N J Blackburn	Domains I and III of the human copper chaperone for superoxide dismutase interact via a cysteine-bridged Dicopper(I) cluster.
000442 (1999)	T. Putilina [États-Unis] ; P. Wong ; S. Gentleman	The DHHC domain: a new highly conserved cysteine-rich motif.
000529 (1989)	S. Dahlin [Suède] ; B. Reinhammar ; J. Angström	Proton-metal distance determination in cobalt(II) stellacyanin by 1H nuclear magnetic resonance relaxation measurements including Curie-spin effects: a proposed structure of the metal-binding region.
000544 (1984)	H R Engeseth ; D R Mcmillin ; J D Otvos	Comparative Cd-113 nuclear magnetic resonance studies of Cd(II)-substituted blue copper proteins.
000545 (1982)	J. Peisach ; L. Powers ; W E Blumberg ; B. Chance	Stellacyanin. Studies of the metal-binding site using x-ray absorption spectroscopy.
000548 (1976)	J W Hare ; E I Solomon ; H B Gray	Infrared spectral studies of metal binding effects on the secondary structure of bean plastocyanin.
000549 (1969)	C. Nicolau ; A J Kalb ; J. Yariv	Electron spin resonance study of the transition metal-binding site of concanavalin A.
000550 (1968)	A J Kalb ; A. Levitzki	Metal-binding sites of concanavalin A and their role in the binding of alpha-methyl d-glucopyranoside.

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