rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1992-2-21
|
pubmed:abstractText |
The intercellular adhesion molecule-1 (ICAM-1, CD54) is one of three putative endothelial receptors that mediate in vitro cytoadherence of P. falciparum-infected erythrocytes. Since cytoadherence to postcapillary venular endothelium is thought to be a major factor in the virulence of P. falciparum malaria, we have examined the interaction between ICAM-1 and the P. falciparum-infected cell, and have compared it with the interaction to the physiological counter receptor, the leukocyte integrin LFA-1. Our results demonstrate that the malaria-binding site resides in the first two domains of the ICAM-1 molecule and overlaps, but is distinct from, the LFA-1 site.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0092-8674
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
68
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
71-81
|
pubmed:dateRevised |
2009-9-29
|
pubmed:meshHeading |
pubmed-meshheading:1370656-Amino Acid Sequence,
pubmed-meshheading:1370656-Animals,
pubmed-meshheading:1370656-Antibodies, Monoclonal,
pubmed-meshheading:1370656-Base Sequence,
pubmed-meshheading:1370656-Binding Sites,
pubmed-meshheading:1370656-Cell Adhesion,
pubmed-meshheading:1370656-Cell Adhesion Molecules,
pubmed-meshheading:1370656-Epitopes,
pubmed-meshheading:1370656-Erythrocytes,
pubmed-meshheading:1370656-Humans,
pubmed-meshheading:1370656-Intercellular Adhesion Molecule-1,
pubmed-meshheading:1370656-Lymphocyte Function-Associated Antigen-1,
pubmed-meshheading:1370656-Malaria, Falciparum,
pubmed-meshheading:1370656-Mice,
pubmed-meshheading:1370656-Models, Molecular,
pubmed-meshheading:1370656-Molecular Sequence Data,
pubmed-meshheading:1370656-Mutagenesis, Site-Directed,
pubmed-meshheading:1370656-Oligodeoxyribonucleotides,
pubmed-meshheading:1370656-Plasmodium falciparum,
pubmed-meshheading:1370656-Protein Conformation,
pubmed-meshheading:1370656-Receptors, Virus,
pubmed-meshheading:1370656-Sequence Homology, Nucleic Acid
|
pubmed:year |
1992
|
pubmed:articleTitle |
The binding site on ICAM-1 for Plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site.
|
pubmed:affiliation |
Molecular Parasitology Group, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, England.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|