The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins.
about
Role of the dimeric structure in Cu,Zn superoxide dismutase. pH-dependent, reversible denaturation of the monomeric enzyme from Escherichia coli.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.Detection, distribution and characterization of novel superoxide dismutases from Yersinia enterocolitica Biovar 1ARegulatory 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.Amsacta moorei entomopoxvirus expresses an active superoxide dismutase.Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving.A novel heme protein, the Cu,Zn-superoxide dismutase from Haemophilus ducreyi.Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability.
P2860
Q30176259-BEEC2F79-13BB-4C79-907D-5336B6265E99Q33373159-FCCA4368-8EC1-4E27-AE80-3E0C51940756Q33931193-AD550793-7FEC-4F6C-B7B7-ED5D3D60385EQ33947845-96973FBF-2DCE-49E7-ABF9-5408BC4CD354Q34737774-EB814F37-B188-4598-A54A-C037DCB74C7BQ36646314-2A37CD3F-FE0F-48B4-B428-0BF3899A02C6Q39513575-C3B530F9-80E5-41B7-A23C-DA2A4A15B14BQ39991443-DBBD08EC-CB51-4CAE-BB3F-E9248AE7B9E0Q42008235-191E3CE3-F1B4-4E47-A5BB-7A1A162C16B1Q43615458-9CB24FAD-44CE-463D-91F7-219C634C1CFEQ45107835-042C70F0-B4AE-4947-8BF8-5CADEF46022D
P2860
The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
The Cu,Zn superoxide dismutase ...... n in all the bacteriocupreins.
@en
The Cu,Zn superoxide dismutase ...... n in all the bacteriocupreins.
@nl
type
label
The Cu,Zn superoxide dismutase ...... n in all the bacteriocupreins.
@en
The Cu,Zn superoxide dismutase ...... n in all the bacteriocupreins.
@nl
prefLabel
The Cu,Zn superoxide dismutase ...... n in all the bacteriocupreins.
@en
The Cu,Zn superoxide dismutase ...... n in all the bacteriocupreins.
@nl
P2093
P2860
P356
P1433
P1476
The Cu,Zn superoxide dismutase ...... n in all the bacteriocupreins.
@en
P2093
Battistoni A
Folcarelli S
Gabbianelli R
P2860
P304
P356
10.1042/BJ3200713
P407
P478
320 ( Pt 3)
P577
1996-12-01T00:00:00Z