Role of the dimeric structure in Cu,Zn superoxide dismutase. pH-dependent, reversible denaturation of the monomeric enzyme from Escherichia coli.
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Dynamics-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 siteInvestigation of the active site of Escherichia coli Cu,Zn superoxide dismutase reveals the absence of the copper-coordinated water molecule. is the water molecule really necessary for the enzymatic mechanism?Regulatory and structural properties differentiating the chromosomal and the bacteriophage-associated Escherichia coli O157:H7 Cu, Zn superoxide dismutases.A primary role for disulfide formation in the productive folding of prokaryotic Cu,Zn-superoxide dismutase.A histidine-rich metal binding domain at the N terminus of Cu,Zn-superoxide dismutases from pathogenic bacteria: a novel strategy for metal chaperoning.The megavirus chilensis Cu,Zn-superoxide dismutase: the first viral structure of a typical cellular copper chaperone-independent hyperstable dimeric enzymeHeterologous expression and biochemical characterization of a highly active and stable chloroplastic CuZn-superoxide dismutase from Pisum sativumPurification and characterization of thermostable monomeric chloroplastic Cu/Zn superoxide dismutase from Chenopodium murale.Regulatory and structural differences in the Cu,Zn-superoxide dismutases of Salmonella enterica and their significance for virulence.Increased expression of periplasmic Cu,Zn superoxide dismutase enhances survival of Escherichia coli invasive strains within nonphagocytic cells.Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving.Modification of cysteine 111 in Cu/Zn superoxide dismutase results in altered spectroscopic and biophysical properties.A novel heme protein, the Cu,Zn-superoxide dismutase from Haemophilus ducreyi.Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis.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.Multi-metal-dependent nucleic acid enzymes.Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase.The regulation and role of the periplasmic copper, zinc superoxide dismutase of Escherichia coli.
P2860
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P2860
Role of the dimeric structure in Cu,Zn superoxide dismutase. pH-dependent, reversible denaturation of the monomeric enzyme from Escherichia coli.
description
1998 nî lūn-bûn
@nan
1998 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մարտին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Role of the dimeric structure ...... enzyme from Escherichia coli.
@ast
Role of the dimeric structure ...... enzyme from Escherichia coli.
@en
type
label
Role of the dimeric structure ...... enzyme from Escherichia coli.
@ast
Role of the dimeric structure ...... enzyme from Escherichia coli.
@en
prefLabel
Role of the dimeric structure ...... enzyme from Escherichia coli.
@ast
Role of the dimeric structure ...... enzyme from Escherichia coli.
@en
P2093
P2860
P356
P1476
Role of the dimeric structure ...... enzyme from Escherichia coli.
@en
P2093
Battistoni A
Desideri A
Folcarelli S
Giartosio A
P2860
P304
P356
10.1074/JBC.273.10.5655
P407
P577
1998-03-01T00:00:00Z