Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site
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SOD Enzymes and Microbial Pathogens: Surviving the Oxidative Storm of InfectionCopper homeostasis in Mycobacterium tuberculosisCsoR Is Essential for Maintaining Copper Homeostasis in Mycobacterium tuberculosisStructural Characterization of Zinc-deficient Human Superoxide Dismutase and Implications for ALSSuperoxide dismutase from the eukaryotic thermophile Alvinella pompejana: structures, stability, mechanism, and insights into amyotrophic lateral sclerosisCandida albicans SOD5 represents the prototype of an unprecedented class of Cu-only superoxide dismutases required for pathogen defenseSolution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domainCsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulatorSystematic comparison of crystal and NMR protein structures deposited in the protein data bank.Elemental economy: microbial strategies for optimizing growth in the face of nutrient limitation.A primary role for disulfide formation in the productive folding of prokaryotic Cu,Zn-superoxide dismutase.An oxidative environment promotes growth of Mycobacterium abscessus.Copper transport and trafficking at the host-bacterial pathogen interface.Trans-species communication in the Mycobacterium tuberculosis-infected macrophagePosttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.Mycobacterium tuberculosis Rv3402c enhances mycobacterial survival within macrophages and modulates the host pro-inflammatory cytokines production via NF-kappa B/ERK/p38 signalingMycobacterium tuberculosis and the intimate discourse of a chronic infection.Candida albicans adapts to host copper during infection by swapping metal cofactors for superoxide dismutaseStructural, Functional, and Immunogenic Insights on Cu,Zn Superoxide Dismutase Pathogenic Virulence Factors from Neisseria meningitidis and Brucella abortus.A copper-responsive global repressor regulates expression of diverse membrane-associated transporters and bacterial drug resistance in mycobacteria.Activation of superoxide dismutases: putting the metal to the pedal.Transcriptional characterization of the antioxidant response of Mycobacterium tuberculosis in vivo and during adaptation to hypoxia in vitro.Molecular insights into the metal selectivity of the copper(I)-sensing repressor CsoR from Bacillus subtilis.N-Terminal clustering of the O-glycosylation sites in the Mycobacterium tuberculosis lipoprotein SodC.Gelsolin-Cu/ZnSOD interaction alters intracellular reactive oxygen species levels to promote cancer cell invasion.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.Virulence factors of the Mycobacterium tuberculosis complexThe Phylogeny and Active Site Design of Eukaryotic Copper-only Superoxide Dismutases.Characterization of SodC, a periplasmic superoxide dismutase from Burkholderia cenocepacia.The superoxide dismutases of Bacillus anthracis do not cooperatively protect against endogenous superoxide stress.Redox environment is an intracellular factor to operate distinct pathways for aggregation of Cu,Zn-superoxide dismutase in amyotrophic lateral sclerosis.Structure-oriented bioinformatic approach exploring histidine-rich clusters in proteins.Eukaryotic Cu-only superoxide dismutases (SODs): A new class of SOD enzymes and SOD-like protein domains.Hydroperoxyl enters the bacteriumChemical Warfare at the Microorganismal Level: A Closer Look at the Superoxide Dismutase Enzymes of Pathogens.Understanding the role of interactions between host and Mycobacterium tuberculosis under hypoxic condition: an in silico approach
P2860
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P2860
Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site
description
2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2004
@ast
im August 2004 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2004/08/06)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/08/06)
@nl
наукова стаття, опублікована в серпні 2004
@uk
name
Unique features of the sodC-en ...... acking zinc in the active site
@ast
Unique features of the sodC-en ...... acking zinc in the active site
@en
Unique features of the sodC-en ...... acking zinc in the active site
@nl
type
label
Unique features of the sodC-en ...... acking zinc in the active site
@ast
Unique features of the sodC-en ...... acking zinc in the active site
@en
Unique features of the sodC-en ...... acking zinc in the active site
@nl
prefLabel
Unique features of the sodC-en ...... acking zinc in the active site
@ast
Unique features of the sodC-en ...... acking zinc in the active site
@en
Unique features of the sodC-en ...... acking zinc in the active site
@nl
P2093
P2860
P3181
P356
P1476
Unique features of the sodC-en ...... acking zinc in the active site
@en
P2093
Giuseppe Rotilio
Jens Z. Pedersen
Kristina Djinovic-Carugo
Melania D'Orazio
Oliviero Carugo
Peter O'Neill
P2860
P304
33447–33455
P3181
P356
10.1074/JBC.M404699200
P407
P577
2004-08-06T00:00:00Z