Lewis X structures in the O antigen side-chain promote adhesion of Helicobacter pylori to the gastric epithelium. - Wikidata - awgldk - TriplyDB

Lewis X structures in the O antigen side-chain promote adhesion of Helicobacter pylori to the gastric epithelium.

Lewis X structures in the O antigen side-chain promote adhesion of Helicobacter pylori to the gastric epithelium.

http://www.wikidata.org/entity/Q38982556

about

Role for alpha-L-fucosidase in the control of Helicobacter pylori-infected gastric cancer cells Pathogenesis of Helicobacter pylori infection Colonize, evade, flourish: how glyco-conjugates promote virulence of Helicobacter pylori Phase variation in H type I and Lewis a epitopes of Helicobacter pylori lipopolysaccharide Helicobacter pylori does not require Lewis X or Lewis Y expression to colonize C3H/HeJ mice.Helicobacter pylori lipopolysaccharide modification, Lewis antigen expression, and gastric colonization are cholesterol-dependent.Molecular mimicry in Helicobacter pylori infections.Phenotypic variation of Helicobacter pylori isolates from geographically distinct regions detected by lectin typing Relationship of anti-Lewis x and anti-Lewis y antibodies in serum samples from gastric cancer and chronic gastritis patients to Helicobacter pylori-mediated autoimmunity Clinical relevance and diversity of two homologous genes encoding glycosyltransferases in Helicobacter pylori.Helicobacter pylori adhesins: review and perspectives.Living dangerously: how Helicobacter pylori survives in the human stomach.O-antigen structural variation: mechanisms and possible roles in animal/plant-microbe interactions.Crosstalk between Helicobacter pylori and gastric epithelial cells is impaired by docosahexaenoic acid.O-antigen protects gram-negative bacteria from histone killing.Genomic basis of endosymbiont-conferred protection against an insect parasitoid.Characterization of Helicobacter pylori lytic transglycosylases Slt and MltD.Persistent bacterial infections: the interface of the pathogen and the host immune system.Interaction of Helicobacter pylori with C-type lectin dendritic cell-specific ICAM grabbing nonintegrin Anti-Lewis X antibody promotes Helicobacter pylori adhesion to gastric epithelial cells Expression of Lewis(b) blood group antigen in Helicobacter pylori does not interfere with bacterial adhesion property Roles of gastric mucin-type O-glycans in the pathogenesis of Helicobacter pylori infection.Novel Helicobacter pylori therapeutic targets: the unusual suspects.The Role of Helicobacter pylori Outer Membrane Proteins in Adherence and Pathogenesis Helicobacter pylori adhesion to gastric epithelial cells is mediated by glycan receptors.Strategies used by helicobacter pylori to establish persistent infection Uptake of Helicobacter pylori outer membrane vesicles by gastric epithelial cells.Influence of Lewis antigen expression by Helicobacter pylori on bacterial internalization by gastric epithelial cells.Limited role of lipopolysaccharide Lewis antigens in adherence of Helicobacter pylori to the human gastric epithelium.Characterization of a waaF mutant of Helicobacter pylori strain 26695 provides evidence that an extended lipopolysaccharide structure has a limited role in the invasion of gastric cancer cells.Galectin-3 binds to Helicobacter pylori O-antigen: it is upregulated and rapidly secreted by gastric epithelial cells in response to H. pylori adhesion.The RecA protein of Helicobacter pylori requires a posttranslational modification for full activity.Helicobacter pylori modulates the T helper cell 1/T helper cell 2 balance through phase-variable interaction between lipopolysaccharide and DC-SIGN.Cloning and expression of Helicobacter pylori GDP-l-fucose synthesizing enzymes (GMD and GMER) in Saccharomyces cerevisiae.Viral vector-mediated delivery of competing glycosyltransferases modifies epitope expression cell specifically.Overexpression of mltA in Edwardsiella tarda reduces resistance to antibiotics and enhances lethality in zebra fish.Lewis epitopes on outer membrane vesicles of relevance to Helicobacter pylori pathogenesis.Glycoengineering of host mimicking type-2 LacNAc polymers and Lewis X antigens on bacterial cell surfaces.A single aromatic amino acid at the carboxyl terminus of Helicobacter pylori {alpha}1,3/4 fucosyltransferase determines substrate specificity.Comparison of lipopolysaccharides composition of two different strains of Helicobacter pylori.

P2860

Q24322779-71BE6266-2765-4F95-B2C6-30061DBCAEF4 Q24679810-9EC32035-2CD1-422A-AEEC-DA9E8A6EB54F Q26866466-4BDC03CE-6670-407C-B14D-0A050F0697BA Q28344784-1B418CC4-AFDF-48DC-8433-10E3BF2911CA Q30453240-EF20F771-0A71-4917-9875-135DD3CBB2F0 Q33518000-6B44F896-9DA5-4062-B9C7-1CCC9072A49A Q33805866-AC9617D2-C21A-4CFE-AFDF-F8A10F44FF5D Q33946030-BFA60F55-1500-4F5C-9EBE-C5E8100C2640 Q34008471-8E1EF54A-8CCB-4749-A041-DC9426314914 Q34046265-8D322572-FDCF-429E-BEA8-80FA6CC9E5D3 Q34141597-EBEDF016-C41E-4AE1-B1A8-B34428416FE4 Q34271593-018C8535-DF45-40F6-9E93-F6B948FEA07F Q34635579-E146159D-169D-4743-B4E2-4C882172E2A3 Q34663892-930272F7-36F0-4187-9331-585CDFFCB1A6 Q34948718-1374CEC9-011E-4AA3-A854-5E76946629EC Q35634482-5BFCEB8A-6D66-48D8-B3B6-5BBEFF04A80E Q35634808-858CF017-3146-4E0B-9500-61A68C1F6BC8 Q35889600-EA3FC851-AA60-4ED4-9E4D-98291B794028 Q35894070-4AFBE8EE-70E4-4640-B584-FAB8A8FAD3B7 Q35913506-E14F88C1-7536-4D55-880D-96708B03AB32 Q36506298-D73D0FDE-7B6B-4505-B1A5-CCEA79AD72CD Q37154039-4FECBCFF-587A-4E5A-9BED-7FF895444095 Q37593108-B7BF2EE6-D18C-46CA-BC3A-F7AD5982131C Q37651461-476372C3-93CD-468C-83BF-3531904B1638 Q37762469-E79FD226-41F5-4A3E-AD5D-3D80DD1FCBE6 Q38681982-EE4832C5-F990-445E-877F-1A64D7C582E0 Q39650801-713BBE71-16C9-42EC-87D8-F9DEB5B0F7EE Q39746037-FB858758-774A-4360-B19F-474153AE32A5 Q39746142-065E2955-DA7F-411C-93D0-48A9E24D80DD Q40074924-A46BCA2B-254E-43E1-9657-CD8DDBB122F6 Q40338123-79FDF01B-E8DD-4AA5-B07D-A5383FE8F21F Q40469116-76C671B6-2F56-4AF3-AF84-E19C9AC552C5 Q42971159-749CA5A0-7F72-4253-B334-2F28C05AEBBB Q43817987-94505DDA-A634-4D55-A0E7-4FBB9E1867C3 Q43916542-2E584B85-CC03-411E-B79E-5430E10B49E4 Q44296311-2020B9BC-1EE7-4C71-999C-2D36FD7A445D Q44740334-758A5D05-AB67-4B50-A8E1-BE9B44C0D821 Q45368813-8BE36592-14B9-483C-B1EC-AFB0B42D0BBB Q46693385-A8AF89A8-EED2-4360-B8FD-A50BEF44145F Q47161254-4341734B-BB3A-412B-B0F7-6770466CA645

P2860

Lewis X structures in the O antigen side-chain promote adhesion of Helicobacter pylori to the gastric epithelium.

http://www.wikidata.org/entity/Q38982556

description

2000 nî lūn-bûn

@nan

2000年の論文

@ja

2000年学术文章

@wuu

2000年学术文章

@zh-cn

2000年学术文章

@zh-hans

2000年学术文章

@zh-my

2000年学术文章

@zh-sg

2000年學術文章

@yue

2000年學術文章

@zh

2000年學術文章

@zh-hant

name

Lewis X structures in the O an ...... ori to the gastric epithelium.

@en

type

label

Lewis X structures in the O an ...... ori to the gastric epithelium.

@en

prefLabel

Lewis X structures in the O an ...... ori to the gastric epithelium.

@en

P1433

Q38982556-EE6B6132-A3A9-41EC-AA3C-D6FC430FFA22

P1476

Q38982556-EA0ADE92-E35F-41E4-B6CE-5F3848469C08

P2093

Q38982556-30DB9123-B651-428F-8178-6AD7C554BC0C

Q38982556-9D3538AB-F862-4D66-AA6F-21212848A56C

Q38982556-ABD23FAA-18CE-4064-9843-619A5ECFD98F

Q38982556-B2ECA348-5DD0-4B41-94D4-AF61158707FB

Q38982556-B9EA1A28-46F0-4F2F-8BF2-E3823505B94C

Q38982556-C77C7423-EEDD-4D3C-AD1C-CC4ACAF5F5EF

Q38982556-E4A6C15F-D01F-43FF-8CD4-45F8B7873923

P2860

Q38982556-07D4351B-C1B0-4E00-9760-9A11BA36686E

Q38982556-0A0A00ED-AAFB-4ED6-BCA1-FD1A8C3DCC9C

Q38982556-0B8784A5-5668-47C6-9303-80F751C18348

Q38982556-25A09DD0-2D08-4613-9DC7-6E9781D789EA

Q38982556-38A6D438-D2EA-4892-BB09-F50AC30A413E

Q38982556-3DF57BD4-AB12-44BD-A3D1-9A4B6C80D2E4

Q38982556-53F44303-ADEF-47DD-85B0-CD11296C87CD

Q38982556-6283E839-10F9-4886-975B-12FAFA388AFF

Q38982556-72701032-0BB5-4D7D-9409-DB80F2111185

Q38982556-73D2258D-5BF1-478B-A8E6-E1EFA1DF20A6

P304

Q38982556-E76D0CBF-5531-4961-9EB9-4FFCA26320BB

P31

Q38982556-DC806842-DF83-46EA-A8CC-0B4D07187C35

P356

Q38982556-A11AC101-85AA-4263-8687-FAA58F6B9C69

P407

Q38982556-7CE4C6AC-4294-471D-AAA1-C4C743D20BD8

P433

Q38982556-0F97167D-3D58-48AE-96A5-4680EBB223DD

P478

Q38982556-8080CE78-2086-44A5-8FD3-827CBED55E89

P577

Q38982556-C71F4652-5202-4A33-8204-B533F2B1EE2C

P5875

Q38982556-21B69B1A-ED83-4292-A5A5-9C4F1494392B

P698

Q38982556-949578DC-5882-42EF-937C-91736F288459

P921

Q38982556-730985BA-5F33-4A54-92AD-0F29EDF98612

P356

J.1365-2958.2000.01823.X

P1433

Molecular Microbiology

P1476

Lewis X structures in the O an ...... ori to the gastric epithelium.

@en

P2093

Edwards NJ

http://www.w3.org/2001/XMLSchema#string

Faller G

http://www.w3.org/2001/XMLSchema#string

High NJ

http://www.w3.org/2001/XMLSchema#string

Monteiro MA

http://www.w3.org/2001/XMLSchema#string

Moran AP

http://www.w3.org/2001/XMLSchema#string

Roberts IS

http://www.w3.org/2001/XMLSchema#string

Walsh EJ

http://www.w3.org/2001/XMLSchema#string

P2860

Genetic and functional characterization of the alpAB gene locus essential for the adhesion of Helicobacter pylori to human gastric tissue.

PADGEM-dependent adhesion of platelets to monocytes and neutrophils is mediated by a lineage-specific carbohydrate, LNF III (CD15).

Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging.

Lack of correlation between Lewis antigen expression by Helicobacter pylori and gastric epithelial cells in infected patients.

Epithelial attachment alters the outcome of Helicobacter pylori infection

An in vitro adherence assay reveals that Helicobacter pylori exhibits cell lineage-specific tropism in the human gastric epithelium.

Variation of gonococcal lipooligosaccharide structure is due to alterations in poly-G tracts in lgt genes encoding glycosyl transferases.

Phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae contributes to persistence in the respiratory tract and sensitivity to serum killing mediated by C-reactive protein.

Lipopolysaccharide of the Helicobacter pylori type strain NCTC 11637 (ATCC 43504): structure of the O antigen chain and core oligosaccharide regions.

Lipopolysaccharides of Helicobacter pylori strains P466 and MO19: structures of the O antigen and core oligosaccharide regions.

P304

1530-1539

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1046/J.1365-2958.2000.01823.X

http://www.w3.org/2001/XMLSchema#string

P407

P433

6

http://www.w3.org/2001/XMLSchema#string

P478

35

http://www.w3.org/2001/XMLSchema#string

P577

2000-03-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

12556573

http://www.w3.org/2001/XMLSchema#string

P698

10760152

http://www.w3.org/2001/XMLSchema#string

P921

Helicobacter pylori