Helicobacter pylori attachment to gastric cells induces cytoskeletal rearrangements and tyrosine phosphorylation of host cell proteins.
about
Common themes in microbial pathogenicity revisitedHelicobacter pylori Eradication in Patients with Immune Thrombocytopenic Purpura: A Review and the Role of BiogeographyHelicobacter pylori infection, but not low-dose aspirin, results in a local reduction of the secretory leukocyte protease inhibitor in gastroduodenal mucosaAltered states: involvement of phosphorylated CagA in the induction of host cellular growth changes by Helicobacter pyloriGenetic and functional characterization of the alpAB gene locus essential for the adhesion of Helicobacter pylori to human gastric tissue.Gene expression profiling of Helicobacter pylori reveals a growth-phase-dependent switch in virulence gene expression.Translocation of the Helicobacter pylori CagA protein in gastric epithelial cells by a type IV secretion apparatus.Effect of Helicobacter pylori VacA on gene expression of gastric cancer cells.Role of AmiA in the morphological transition of Helicobacter pylori and in immune escapeRecombination-based in vivo expression technology identifies Helicobacter pylori genes important for host colonizationAttaching and effacing Escherichia coli downregulate DNA mismatch repair protein in vitro and are associated with colorectal adenocarcinomas in humansChronic Helicobacter pylori infection induces an apoptosis-resistant phenotype associated with decreased expression of p27(kip1)Molecular and cellular activities of Helicobacter pylori pathogenic factors.Initiation and Maintenance of Gastric Cancer: A Focus on CD44 Variant Isoforms and Cancer Stem Cells.Host determinants of Helicobacter pylori infection and its clinical outcome.Adherence and invasion of mouse-adapted H pylori in different epithelial cell lines.Prevalence of Helicobacter pylori vacA, cagA, iceA and oipA genotypes in Tunisian patientsHelicobacter pylori determinants of pathogenicity.Comparison of Helicobacter pylori virulence gene expression in vitro and in the Rhesus macaque.Helicobacter pylori CagA: analysis of sequence diversity in relation to phosphorylation motifs and implications for the role of CagA as a virulence factor.Concurrent proinflammatory and apoptotic activity of a Helicobacter pylori protein (HP986) points to its role in chronic persistence.Clinical relevance of the babA2 genotype of Helicobacter pylori in Japanese clinical isolatesEmergence of diverse Helicobacter species in the pathogenesis of gastric and enterohepatic diseases.Role of gamma interferon in Helicobacter pylori-induced gastric inflammatory responses in a mouse modelMultiple genes in the left half of the cag pathogenicity island of Helicobacter pylori are required for tyrosine kinase-dependent transcription of interleukin-8 in gastric epithelial cells.Helicobacter pylori possesses two CheY response regulators and a histidine kinase sensor, CheA, which are essential for chemotaxis and colonization of the gastric mucosaMycobacterium avium invades the intestinal mucosa primarily by interacting with enterocytesApoptotic signaling pathway activated by Helicobacter pylori infection and increase of apoptosis-inducing activity under serum-starved conditions.Involvement of a plasmid in virulence of Campylobacter jejuni 81-176.Effect of cold starvation, acid stress, and nutrients on metabolic activity of Helicobacter pylori.Diverse phenotypes resulting from polyphosphate kinase gene (ppk1) inactivation in different strains of Helicobacter pyloriResponses of endoscopy patients in Ladakh, India, to Helicobacter pylori whole-cell and Cag A antigensLiving dangerously: how Helicobacter pylori survives in the human stomach.Pathogenicity islands in bacterial pathogenesisHelicobacter pylori CagA protein can be tyrosine phosphorylated in gastric epithelial cells.Protein-protein interactions among Helicobacter pylori cag proteinsInduction of host signal transduction pathways by Helicobacter pylori.Tyrosine phosphorylation of the Helicobacter pylori CagA antigen after cag-driven host cell translocation.Helicobacter pylori: resurrection of the cancer link.Virulence of enteropathogenic Escherichia coli, a global pathogen
P2860
Q24643808-024A7DA0-84BB-4B40-91CE-5F2DF05AA99CQ26865062-EF8D6E21-EF76-4A35-8F9C-5F8EEC81232CQ28194601-7FC44DF6-A91D-452F-BCB4-6F9BAE20FDC1Q28776428-EF8F6B61-1C36-436B-BC01-192455AC2C80Q30175791-95692631-B366-478E-9F20-79345F5CCEB5Q30477751-31FB59E2-DD6E-4FBB-8626-260CC771747AQ30981200-C63668A7-EF04-48C8-AA2E-FE2D90C8E5A4Q33210194-F6FB241F-6EC4-497E-9AE3-66AD485F4C5AQ33258466-27C1C675-CC2C-4B5A-8B4C-34875720223EQ33369702-2E8CD8F3-42A2-43BF-B260-7F7AE913B10AQ33444726-377AA675-C924-4675-B74A-3277C86B362EQ33600141-09B4961B-ADE6-4B64-9C2A-85D17F6A7EE9Q33665535-4EA36CD2-AF8E-4F51-8D73-33939240CAB6Q33711746-95AB3472-D4C5-42BE-B142-E4F421ECFE39Q33723758-B27319D1-1E45-4DE8-9599-316AAA301EDAQ33787697-5B463CA3-55D4-4F21-B263-4AF6EC3E4D60Q33793033-72443882-D766-4E4F-8FAE-46A98C564254Q33840157-58D60D2A-5B51-425F-A966-61870792BA5CQ33946722-57185D6A-4E49-4AD2-8FCB-E1488DC5F297Q33955737-69D5577B-EBE4-46E1-93AE-124640082BDEQ33971472-8EE86630-017B-433A-B0BF-7722CB36E444Q33972835-4BDB3CB8-5E32-487B-BA12-4F7583ACACBDQ33975615-044A34AE-75DB-4C22-8C0D-69AFBEFEAB4BQ34000020-2A23CA5B-6CAB-4C61-B7EB-88DB1542B662Q34001367-B1F0FD94-757A-47E7-8013-CCDFC28AC145Q34003888-6AB58A45-47FD-4BFE-8FC9-9DCB9A1236C9Q34006320-E5A11A54-CF87-4AFF-A6BF-A264E3E51610Q34007325-3495D95D-DC54-454C-BE86-876962D508D8Q34007504-C101A69D-0F05-47E9-8083-B3A2588FA775Q34097007-3A0C76BE-6B72-47C6-9B7D-43CEA9D5544DQ34124303-A6399F28-FA7D-4204-BFCD-424D5A566026Q34173965-90C59080-F5BD-4544-ADC4-C429E1EF34D3Q34271593-6E959138-A0E9-441D-97B3-C58C73068032Q34290188-FCEA5CFC-97CE-42C6-AE9A-E9A50B725C20Q34507295-592B94AF-E307-43E2-A6DE-6B2B8DFBFC42Q34697771-85CE2001-4278-4253-A442-4F368CC2D50EQ34741347-3DC0E456-AF7E-4F89-A474-7B824B98CC7AQ35015052-9AE57C17-C096-4E96-8476-946F49D91D5AQ35050947-B72B413D-63FA-4F4E-9210-354DE0BFC3C8Q35176257-E602956A-348C-4BBE-941A-527A7E0DE7D3
P2860
Helicobacter pylori attachment to gastric cells induces cytoskeletal rearrangements and tyrosine phosphorylation of host cell proteins.
description
1996 nî lūn-bûn
@nan
1996 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
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
name
Helicobacter pylori attachment ...... ylation of host cell proteins.
@ast
Helicobacter pylori attachment ...... ylation of host cell proteins.
@en
Helicobacter pylori attachment ...... ylation of host cell proteins.
@nl
type
label
Helicobacter pylori attachment ...... ylation of host cell proteins.
@ast
Helicobacter pylori attachment ...... ylation of host cell proteins.
@en
Helicobacter pylori attachment ...... ylation of host cell proteins.
@nl
prefLabel
Helicobacter pylori attachment ...... ylation of host cell proteins.
@ast
Helicobacter pylori attachment ...... ylation of host cell proteins.
@en
Helicobacter pylori attachment ...... ylation of host cell proteins.
@nl
P2093
P2860
P921
P356
P1476
Helicobacter pylori attachment ...... ylation of host cell proteins.
@en
P2093
P2860
P304
P356
10.1073/PNAS.93.3.1259
P407
P577
1996-02-01T00:00:00Z