Regulation of Integrin Affinity States through an NP XY Motif in the β Subunit Cytoplasmic Domain
Open Access
- 1 April 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (15) , 8553-8558
- https://doi.org/10.1074/jbc.270.15.8553
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Internalization of the α5β1 Integrin Does Not Depend on "NPXY" SignalsBiochemical and Biophysical Research Communications, 1994
- Regulation of alpha 6 beta 1 integrin laminin receptor function by the cytoplasmic domain of the alpha 6 subunit.The Journal of cell biology, 1993
- Interchangeable alpha chain cytoplasmic domains play a positive role in control of cell adhesion mediated by VLA-4, a beta 1 integrin.The Journal of Experimental Medicine, 1993
- Distinct functions of integrin alpha and beta subunit cytoplasmic domains in cell spreading and formation of focal adhesionsThe Journal of cell biology, 1993
- Functional role of the cytoplasmic domain of the integrin alpha 5 subunitThe Journal of cell biology, 1993
- Identification of amino acid sequences in the integrin beta 1 cytoplasmic domain implicated in cytoskeletal associationThe Journal of cell biology, 1992
- Integrins: Versatility, modulation, and signaling in cell adhesionCell, 1992
- The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformationCell, 1991
- Expression and function of chicken integrin beta 1 subunit and its cytoplasmic domain mutants in mouse NIH 3T3 cells.The Journal of cell biology, 1990
- Amino acid sequence of the human fibronectin receptor.The Journal of cell biology, 1987