Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
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Structures of native and Fe-substituted SOD2 fromSaccharomyces cerevisiaeLipid modification of the Cu,Zn superoxide dismutase from Mycobacterium tuberculosisDynamics-function correlation in Cu, Zn superoxide dismutase: a spectroscopic and molecular dynamics simulation studyUnique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active siteStructural properties of periplasmic SodCI that correlate with virulence in Salmonella enterica serovar TyphimuriumExperimental and simulative dissociation of dimeric Cu,Zn superoxide dismutase doubly mutated at the intersubunit surfaceProtomers of protein hetero-oligomers tend to resemble each other more than expectedA histidine-rich metal binding domain at the N terminus of Cu,Zn-superoxide dismutases from pathogenic bacteria: a novel strategy for metal chaperoning.Nickel superoxide dismutase: structural and functional roles of Cys2 and Cys6.Detection, distribution and characterization of novel superoxide dismutases from Yersinia enterocolitica Biovar 1AThe structural biochemistry of the superoxide dismutases.Superoxide dismutases and superoxide reductases.Either periplasmic tethering or protease resistance is sufficient to allow a SodC to protect Salmonella enterica serovar Typhimurium from phagocytic superoxide.Periplasmic superoxide dismutase SodCI of Salmonella binds peptidoglycan to remain tethered within the periplasm.Structural, Functional, and Immunogenic Insights on Cu,Zn Superoxide Dismutase Pathogenic Virulence Factors from Neisseria meningitidis and Brucella abortus.A novel heme protein, the Cu,Zn-superoxide dismutase from Haemophilus ducreyi.Periplasmic competition for zinc uptake between the metallochaperone ZnuA and Cu,Zn superoxide dismutase.Distinctive functional features in prokaryotic and eukaryotic Cu,Zn superoxide dismutases.Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability.Single mutation at the intersubunit interface confers extra efficiency to Cu,Zn superoxide dismutase
P2860
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P2860
Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
@ast
Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
@en
Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
@nl
type
label
Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
@ast
Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
@en
Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
@nl
prefLabel
Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
@ast
Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
@en
Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
@nl
P2093
P50
P356
P1476
Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
@en
P2093
P304
P356
10.1006/JMBI.1998.2267
P407
P50
P577
1999-01-01T00:00:00Z