Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface
about
Superoxide dismutase from the eukaryotic thermophile Alvinella pompejana: structures, stability, mechanism, and insights into amyotrophic lateral sclerosisStructural properties of periplasmic SodCI that correlate with virulence in Salmonella enterica serovar TyphimuriumA potential role for periplasmic superoxide dismutase in blocking the penetration of external superoxide into the cytosol of Gram-negative bacteriaA prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystalA histidine-rich metal binding domain at the N terminus of Cu,Zn-superoxide dismutases from pathogenic bacteria: a novel strategy for metal chaperoning.The 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.Altered Levels of Zinc and N-methyl-D-aspartic Acid Receptor Underlying Multiple Organ Dysfunctions After Severe Trauma.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.Haemophilus influenzae and oxidative stress.Complete Amino Acid Sequence of a Copper/Zinc-Superoxide Dismutase from Ginger Rhizome.Presence of copper- and zinc-containing superoxide dismutase in commensal Haemophilus haemolyticus isolates can be used as a marker to discriminate them from nontypeable H. influenzae isolates.A novel heme protein, the Cu,Zn-superoxide dismutase from Haemophilus ducreyi.
P2860
Q27653085-C38B5C66-C4AB-44E5-8997-2D0ACA7427D4Q28563582-2AF5C60B-5708-4416-BF55-7E9123A07966Q28611508-6240CA4C-3646-474C-94D2-5CE57FF446D8Q28907138-D302207C-9A0C-4DED-A9D4-C8EBAD3BEDDAQ33947845-031A6382-75D4-4B95-9127-71B456A71AC6Q34993111-92A1EE21-2861-4535-AF54-1B8D72BFE24EQ35049047-787A92DC-8DB6-49EB-B4F3-2FB1963BE7B6Q35563989-F17461A7-B127-47C4-9085-11E23397DC81Q36064230-85ABDCAF-AC11-42F9-9E17-7DFEDBF44957Q36271516-E311A0C1-CD75-4243-B2B4-7CEBEEE59668Q36297476-83EA0E9B-5586-4C5D-BFE8-42F6C281307BQ38037547-B2D115A6-A143-4ADB-AD6A-E62A60ABA0E3Q38968618-0857A247-E945-42E7-A880-3C49E77825EBQ41068665-986E01E6-6CA8-4BD5-ACF3-C19F0E23C01BQ43615458-FBF724DE-6C7B-4B99-A1F1-2E9C675AE32D
P2860
Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface
description
2000 nî lūn-bûn
@nan
2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Cu,Zn superoxide dismutase str ...... th a conserved dimer interface
@ast
Cu,Zn superoxide dismutase str ...... th a conserved dimer interface
@en
Cu,Zn superoxide dismutase str ...... th a conserved dimer interface
@nl
type
label
Cu,Zn superoxide dismutase str ...... th a conserved dimer interface
@ast
Cu,Zn superoxide dismutase str ...... th a conserved dimer interface
@en
Cu,Zn superoxide dismutase str ...... th a conserved dimer interface
@nl
prefLabel
Cu,Zn superoxide dismutase str ...... th a conserved dimer interface
@ast
Cu,Zn superoxide dismutase str ...... th a conserved dimer interface
@en
Cu,Zn superoxide dismutase str ...... th a conserved dimer interface
@nl
P2093
P356
P1476
Cu,Zn superoxide dismutase str ...... th a conserved dimer interface
@en
P2093
E D Getzoff
K T Forest
P R Langford
P304
P356
10.1006/JMBI.1999.3448
P407
P577
2000-02-11T00:00:00Z