The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane
- 1 August 1998
- journal article
- Published by Elsevier BV in Trends in Biochemical Sciences
- Vol. 23 (8), 281-282
- https://doi.org/10.1016/s0968-0004(98)01237-7
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Regulation of CD44-Protein 4.1 Interaction by Ca2+and CalmodulinPublished by Elsevier BV ,1997
- Moesin Interacts with the Cytoplasmic Region of Intercellular Adhesion Molecule-3 and Is Redistributed to the Uropod of T Lymphocytes during Cell PolarizationThe Journal of cell biology, 1997
- Identification of the Protein 4.1 Binding Interface on Glycophorin C and p55, a Homologue of the Drosophila discs-large Tumor Suppressor ProteinPublished by Elsevier BV ,1995
- ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons.The Journal of cell biology, 1994
- Membrane-actin microfilament connections: an increasing diversity of players related to band 4.1Current Opinion in Cell Biology, 1994
- Red blood cell glycophorinsBlood, 1992
- Identification of the protein 4.1 binding site to phosphatidylserine vesiclesBiochemistry, 1988
- Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton.Proceedings of the National Academy of Sciences of the United States of America, 1986
- Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositideNature, 1985
- Glycophorin is linked by band 4.1 protein to the human erythrocyte membrane skeletonNature, 1984