Prominent Role of the Ig-like V Domain intrans-Interactions of Nectins
Open Access
- 1 July 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (30) , 27006-27013
- https://doi.org/10.1074/jbc.m203228200
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Nectin4/PRR4, a New Afadin-associated Member of the Nectin Family That Trans-interacts with Nectin1/PRR1 through V Domain InteractionJournal of Biological Chemistry, 2001
- Organization of the rat Tage4 gene and herpesvirus entry activity of the encoded proteinGene, 2001
- The novel receptors that mediate the entry of herpes simplex viruses and animal alphaherpesviruses into cellsReviews in Medical Virology, 2000
- Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family that interacts with afadinGene, 2000
- Three Classes of Cell Surface Receptors for Alphaherpesvirus EntryVirology, 2000
- The murine homolog of human Nectin1δ serves as a species nonspecific mediator for entry of human and animal αherpesviruses in a pathway independent of a detectable binding to gDProceedings of the National Academy of Sciences, 2000
- Nectin-3, a New Member of Immunoglobulin-like Cell Adhesion Molecules That Shows Homophilic and Heterophilic Cell-Cell Adhesion ActivitiesJournal of Biological Chemistry, 2000
- Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding geneGene, 1995
- The human PRR2 gene, related to the human poliovirus receptor gene (PVR), is the true homolog of the murine MPH geneGene, 1995
- Cellular receptor for poliovirus: Molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamilyCell, 1989