An N-linked high-mannose type oligosaccharide, expressed at the major outer membrane protein of Chlamydia trachomatis, mediates attachment and infectivity of the microorganism to HeLa cells.
about
The Role of the Immune Response in Chlamydia trachomatis Infection of the Male Genital Tract: A Double-Edged SwordProtein disulfide isomerase, a component of the estrogen receptor complex, is associated with Chlamydia trachomatis serovar E attached to human endometrial epithelial cellsGlycosylation of Pseudomonas aeruginosa 1244 pilin: glycan substrate specificity.Human mannose-binding protein inhibits infection of HeLa cells by Chlamydia trachomatis.Phylogenetic analysis of the Chlamydia trachomatis major outer membrane protein and examination of potential pathogenic determinants.The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin.A genomic island in Pseudomonas aeruginosa carries the determinants of flagellin glycosylationChlamydial genomics and vaccine antigen discovery.Characterization of outer membrane proteins in Chlamydia trachomatis LGV serovar L2.Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50.Identification of polymorphic outer membrane proteins of Chlamydia psittaci 6BCProtein glycosylation in Helicobacter pylori: beyond the flagellins?Surface accessibility of the 70-kilodalton Chlamydia trachomatis heat shock protein following reduction of outer membrane protein disulfide bonds.Influence of pilin glycosylation on Pseudomonas aeruginosa 1244 pilus functionThe sweet tooth of bacteria: common themes in bacterial glycoconjugates.Cleavage of the N-linked oligosaccharide from the surfaces of Chlamydia species affects infectivity in the mouse model of lung infection.Never say never again: protein glycosylation in pathogenic bacteria.Biomineralization of Schlumbergerella floresiana, a significant carbonate-producing benthic foraminifer.In vitro passage selects for Chlamydia muridarum with enhanced infectivity in cultured cells but attenuated pathogenicity in mouse upper genital tract.Analysis of the Mycoplasma genitalium MgpB Adhesin to Predict Membrane Topology, Investigate Antibody Accessibility, Characterize Amino Acid Diversity, and Identify Functional and Immunogenic Epitopes.Analysis of Humoral Immune Responses to Surface and Virulence-Associated Chlamydia abortus Proteins in Ovine and Human Abortions by Use of a Newly Developed Line ImmunoassayIdentification of OmpA-Like Protein of Tannerella forsythia as an O-Linked Glycoprotein and Its Binding Capability to Lectins.O-linked glycosylation ensures the normal conformation of the autotransporter adhesin involved in diffuse adherence.Unveiling New Molecular Factors Useful for Detection of Pelvic Inflammatory Disease due to Chlamydia trachomatis Infection.Retinoic acid inhibits the infectivity and growth of Chlamydia pneumoniae in epithelial and endothelial cells through different receptors.Modification of Pseudomonas aeruginosa Pa5196 type IV Pilins at multiple sites with D-Araf by a novel GT-C family Arabinosyltransferase, TfpW.Retinoic acid prevents Chlamydia pneumoniae-induced foam cell development in a mouse model of atherosclerosisProtein-linked glycans in periodontal bacteria: prevalence and role at the immune interface.Bioanalytical tools for the discovery of eukaryotic glycoproteins applied to the analysis of bacterial glycoproteins.Chlamydia pneumoniae induces expression of pro-atherogenic factors through activation of the lectin-like oxidized LDL receptor-1Structural and genetic characterization of glycosylation of type a flagellin in Pseudomonas aeruginosa.Mannose-binding lectin 2 (Mbl2) gene polymorphisms are related to protein plasma levels, but not to heart disease and infection by Chlamydia.Cleavage of the N-linked oligosaccharide from the surfaces of Chlamydia species affects attachment and infectivity of the organisms in human epithelial and endothelial cellsGlycosylation of TRPM4 and TRPM5 channels: molecular determinants and functional aspects.Modulation of host signaling and cellular responses by ChlamydiaChlamydia pneumoniae binds to the lectin-like oxidized LDL receptor for infection of endothelial cells.Low mannose-binding lectin levels and MBL2 gene polymorphisms associate with Chlamydia pneumoniae antibodies.Chlamydia pneumoniae GroEL1 protein is cell surface associated and required for infection of HEp-2 cellsChlamydia pneumoniae uses the mannose 6-phosphate/insulin-like growth factor 2 receptor for infection of endothelial cells.Chlamydia-dependent biosynthesis of a heparan sulphate-like compound in eukaryotic cells.
P2860
Q26851537-C7907A90-3D8E-4E0A-9B05-D647620B07F3Q31078384-8E690E99-8E48-44EB-99F8-82CE43CA6F64Q31116468-7E2234D4-0B0F-4871-A34C-97261675DF03Q33752459-C710527C-A1ED-4EE1-9790-CEE6BF3E09DBQ33757462-AA859EC9-11BF-4C09-827D-762810B25CEDQ33786797-184AD647-1A0E-463E-9891-4CE12FD07FC7Q33930997-FE99438B-934C-42B9-9789-6F101E506D1AQ33935087-6A13A960-53FA-4F77-9B3D-FDDC4F6F24DDQ33996097-07E8097B-641A-4F72-9D12-52E1BE6FE739Q34001332-DD18AD6B-744A-402A-B8F1-860008A11088Q34006897-554AB88F-C32A-4912-8381-3DD1CE97BD2CQ34045005-5820FB11-8248-44A4-B8C3-45F6CD09C039Q34117174-F4C07F4A-99DD-4128-B2AC-FB865649F83FQ34194800-4D473AD9-BF46-4A04-96AE-35B0CC20A6DFQ34297837-EC7D9D79-3D05-45C2-8766-691D4B8DC043Q34601721-84B48EC7-557D-4D82-B383-C73B7BA4182DQ34746990-AB35A592-59CB-4A60-B64F-54991AEF1C8AQ35137016-836161C5-9C6E-4B3B-9C67-4816B6762F3DQ35439847-3215A99A-1FB2-4D51-AD6E-F6E668E7EAF9Q35779686-CB1B55F5-9509-4398-B4C5-12D72EC5638DQ36021944-EE408C1B-3DEC-4AEE-8965-E668EC0423B4Q36154915-C7259195-4343-4BFB-B5C3-B6DAC5CDA6ACQ36314641-C623D2D6-F6E7-4BA1-A609-17848F83F1E0Q36337305-E0E8F220-7E13-4370-944F-FADD200BEAB4Q36732330-B2AFD863-AB9A-415E-A210-92820170B7F9Q36958076-35092085-3D2D-4646-9E47-6069A8114284Q37009782-EDC54E5D-A060-40D1-8E8E-9E68E7C4D869Q37232860-444D8FFC-8854-429C-BC50-64C23B856027Q37390672-64DEEBC4-9D3D-4180-B3E2-F49A73493B44Q37412127-0FB3950B-AE16-4644-9B46-FE03C02C43B7Q37425198-8FFE5EE5-1958-4A6F-A5D1-CB9470A07658Q37535679-5E97846F-EF60-4317-9DD1-8589C4213229Q37582922-EA3BAD08-A6B0-43A2-B764-B804041A363CQ37598862-667AD8A1-84E6-4BBC-9E79-8964D0B9718BQ37845494-700C3695-5EF8-4473-BC47-7782862C0D2FQ37850239-93C8B296-8E42-4D7C-BC35-80E4F5B0EF45Q37853983-C1D2802D-4FDE-4A5E-9999-F0AFC258B506Q37857945-C79F6C9A-83A3-42BB-A296-7AE55B3F7154Q37864340-AD6AD9FD-B41D-4C92-8B17-CF2F335F821EQ37874931-270AECAA-A6BE-432C-B934-559B7179DD68
P2860
An N-linked high-mannose type oligosaccharide, expressed at the major outer membrane protein of Chlamydia trachomatis, mediates attachment and infectivity of the microorganism to HeLa cells.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
An N-linked high-mannose type ...... e microorganism to HeLa cells.
@en
An N-linked high-mannose type ...... e microorganism to HeLa cells.
@nl
type
label
An N-linked high-mannose type ...... e microorganism to HeLa cells.
@en
An N-linked high-mannose type ...... e microorganism to HeLa cells.
@nl
prefLabel
An N-linked high-mannose type ...... e microorganism to HeLa cells.
@en
An N-linked high-mannose type ...... e microorganism to HeLa cells.
@nl
P2093
P2860
P356
P1476
An N-linked high-mannose type ...... e microorganism to HeLa cells.
@en
P2093
P2860
P304
P356
10.1172/JCI119109
P407
P577
1996-12-01T00:00:00Z