Periplasmic copper-zinc superoxide dismutase protects Haemophilus ducreyi from exogenous superoxide.
about
Identification of a novel sialic acid transporter in Haemophilus ducreyiHaemophilus ducreyi Outer membrane determinants, including DsrA, define two clonal populationsRole of Mycobacterium tuberculosis copper-zinc superoxide dismutaseIdentification and subcellular localization of a novel Cu,Zn superoxide dismutase of Mycobacterium tuberculosisHaemophilus ducreyi secretes a filamentous hemagglutinin-like protein.Involvement of the Haemophilus ducreyi gmhA gene product in lipooligosaccharide expression and virulence.Characterization of a WaaF (RfaF) homolog expressed by Haemophilus ducreyi.Characterization of a Haemophilus ducreyi mutant deficient in expression of cytolethal distending toxin.Identification of the znuA-encoded periplasmic zinc transport protein of Haemophilus ducreyi.Neutropenia restores virulence to an attenuated Cu,Zn superoxide dismutase-deficient Haemophilus ducreyi strain in the swine model of chancroid.Examination of early interactions between Haemophilus ducreyi and host cells by using cocultured HaCaT keratinocytes and foreskin fibroblasts.Haemophilus ducreyi associates with phagocytes, collagen, and fibrin and remains extracellular throughout infection of human volunteers.Cloning, overexpression, purification, and immunobiology of an 85-kilodalton outer membrane protein from Haemophilus ducreyiIn vitro and in vivo interactions of Haemophilus ducreyi with host phagocytes.A superoxide dismutase C mutant of Haemophilus ducreyi is virulent in human volunteers.Immunopathogenesis of Haemophilus ducreyi infection (chancroid)Haemophilus ducreyi targets Src family protein tyrosine kinases to inhibit phagocytic signaling.Mutations in the lspA1 and lspA2 genes of Haemophilus ducreyi affect the virulence of this pathogen in an animal model system.Detection and quantification of superoxide formed within the periplasm of Escherichia coliDksA and (p)ppGpp have unique and overlapping contributions to Haemophilus ducreyi pathogenesis in humans.Virulent Salmonella typhimurium has two periplasmic Cu, Zn-superoxide dismutases.Carbon storage regulator A contributes to the virulence of Haemophilus ducreyi in humans by multiple mechanisms.Roles for mannitol and mannitol dehydrogenase in active oxygen-mediated plant defense.The LspB protein is involved in the secretion of the LspA1 and LspA2 proteins by Haemophilus ducreyi.Haemophilus influenzae and oxidative stress.[Cu,Zn]-Superoxide dismutase mutants of the swine pathogen Actinobacillus pleuropneumoniae are unattenuated in infections of the natural host.Genes and enzymes of azetidine-2-carboxylate metabolism: detoxification and assimilation of an antibiotic.Inhibition of phagocytosis by Haemophilus ducreyi requires expression of the LspA1 and LspA2 proteins.A novel heme protein, the Cu,Zn-superoxide dismutase from Haemophilus ducreyi.Tomatidine and lycotetraose, hydrolysis products of alpha-tomatine by Fusarium oxysporum tomatinase, suppress induced defense responses in tomato cells.Identification and characterization of a heme periplasmic-binding protein in Haemophilus ducreyi.
P2860
Q24534699-4595DCA7-9894-4DEE-9795-5BD8E0E0C23AQ28241256-ECC138D4-73BC-4EBA-A88E-5D656EEEFE5EQ28486437-2106002C-FA11-4E64-9F79-5305446EB712Q28486918-1C515FCA-EB6E-4F19-B247-D338711B6064Q33741949-6BED23F8-F13C-4CF2-99C6-E0DA13BAB4C6Q33762114-F070AC42-BBCF-4BE9-AEC9-9D579F3E7686Q34000407-7140D4D0-19EA-4816-80F7-7692AE96CED9Q34001373-1BC3DE41-68C9-4A14-BC31-911E8BF64B04Q34001999-56D22460-1F13-4DC5-8B9B-18308E527B1DQ34002159-524FB84E-02BB-4113-A8F5-A6CAAA312767Q34002164-34BDEFBF-5E32-4955-9EB5-5E478F98889AQ34006973-F7FBF66B-DF08-49A7-BA82-5732A011D8D2Q34008280-EB8AF9F2-176D-4FB6-921F-C8FA15EDA634Q34116950-1AB44E16-12D4-451F-9B2F-4D2A21DDF4EDQ34120582-51BDB2E0-CD4B-4A40-B9DF-07DB179933E4Q34120627-14F9D1C5-0A94-4738-BA28-AA4CA7CF00DAQ34194693-B33E474E-DB0B-4335-89A8-157A8BD0BF36Q34931861-D7922943-43AE-40DE-B775-B3CF334E8746Q35075335-E2136956-81E9-4B94-ABCF-A4E94F6FE7ABQ35833852-A8FD8B6E-D9F8-4D1B-B9D7-0DB6E8A03750Q36398159-4537AF21-BA0D-4608-9C97-7014F5322F90Q36558726-8DEC95C9-B721-41C6-98A2-AD4C99967998Q36761027-5C37FD3F-1116-451F-AE29-37EFE12F3C57Q37115707-C161C002-0B31-4F28-8F5A-6F4FAB4D1BD2Q38037547-9EC97785-C105-42FF-9F4A-F5B961F9A365Q39520807-ED63466C-8435-4740-AA84-CA87905BF704Q39764985-B21933F7-C508-4C33-ABE1-7F90521D827EQ39913157-56ED3726-1FA7-415B-9605-1E03E5F04802Q43615458-F6BDCAC9-12AA-4E83-B61D-826187AB44E4Q44997387-989C4070-6F80-4089-B73E-56E67CE3A28DQ54367647-83F6415E-5C4D-4DA7-81AD-BF7A37200553
P2860
Periplasmic copper-zinc superoxide dismutase protects Haemophilus ducreyi from exogenous superoxide.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունվարին 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
Periplasmic copper-zinc supero ...... eyi from exogenous superoxide.
@ast
Periplasmic copper-zinc supero ...... eyi from exogenous superoxide.
@en
type
label
Periplasmic copper-zinc supero ...... eyi from exogenous superoxide.
@ast
Periplasmic copper-zinc supero ...... eyi from exogenous superoxide.
@en
prefLabel
Periplasmic copper-zinc supero ...... eyi from exogenous superoxide.
@ast
Periplasmic copper-zinc supero ...... eyi from exogenous superoxide.
@en
P2093
P2860
P1476
Periplasmic copper-zinc supero ...... eyi from exogenous superoxide.
@en
P2093
P2860
P304
P356
10.1046/J.1365-2958.1998.00687.X
P407
P577
1998-01-01T00:00:00Z