Carcinoembryonic antigen family receptor recognition by gonococcal Opa proteins requires distinct combinations of hypervariable Opa protein domains.
about
Structure of the Neisserial outer membrane protein Opa₆₀: loop flexibility essential to receptor recognition and bacterial engulfment.Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1Neisserial Opa Protein-CEACAM Interactions: Competition for Receptors as a Means of Bacterial Invasion and Pathogenesis.Functional characterization of antibodies against Neisseria gonorrhoeae opacity protein loopsThe effect of immune selection on the structure of the meningococcal opa protein repertoire.CEACAM1 recognition by bacterial pathogens is species-specificPathogenesis of Afa/Dr diffusely adhering Escherichia coli.Expression of Opacity Proteins Interferes with the Transmigration of Neisseria gonorrhoeae across Polarized Epithelial CellsCEACAM engagement by human pathogens enhances cell adhesion and counteracts bacteria-induced detachment of epithelial cells.Innate recognition by neutrophil granulocytes differs between Neisseria gonorrhoeae strains causing local or disseminating infections.Relative contributions of recombination and mutation to the diversification of the opa gene repertoire of Neisseria gonorrhoeae.The biology of Neisseria adhesins.Opa proteins and CEACAMs: pathways of immune engagement for pathogenic Neisseria.Opacity-associated adhesin repertoire in hyperinvasive Neisseria meningitidis.Interactions of meningococcal virulence factors with endothelial cells at the human blood-cerebrospinal fluid barrier and their role in pathogenicity.Molecular mechanisms involved in the interaction of Neisseria meningitidis with cells of the human blood-cerebrospinal fluid barrier.Two variable regions in carcinoembryonic antigen-related cell adhesion molecule1 N-terminal domains located in or next to monoclonal antibody and adhesion epitopes show evidence of recombination in rat but not in human.Mutational analysis of human CEACAM1: the potential of receptor polymorphism in increasing host susceptibility to bacterial infection.
P2860
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P2860
Carcinoembryonic antigen family receptor recognition by gonococcal Opa proteins requires distinct combinations of hypervariable Opa protein domains.
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Carcinoembryonic antigen famil ...... rvariable Opa protein domains.
@ast
Carcinoembryonic antigen famil ...... rvariable Opa protein domains.
@en
Carcinoembryonic antigen famil ...... rvariable Opa protein domains.
@nl
type
label
Carcinoembryonic antigen famil ...... rvariable Opa protein domains.
@ast
Carcinoembryonic antigen famil ...... rvariable Opa protein domains.
@en
Carcinoembryonic antigen famil ...... rvariable Opa protein domains.
@nl
prefLabel
Carcinoembryonic antigen famil ...... rvariable Opa protein domains.
@ast
Carcinoembryonic antigen famil ...... rvariable Opa protein domains.
@en
Carcinoembryonic antigen famil ...... rvariable Opa protein domains.
@nl
P2093
P2860
P1476
Carcinoembryonic antigen famil ...... rvariable Opa protein domains.
@en
P2093
Christopher C R Grant
Daniel M Hogan
Martine P Bos
Robert J Belland
P2860
P304
P356
10.1128/IAI.70.4.1715-1723.2002
P407
P577
2002-04-01T00:00:00Z