Protein 4.2 Binds to the Carboxyl-terminal EF-hands of Erythroid α-Spectrin in a Calcium- and Calmodulin-dependent Manner
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference83 articles.
1. Visualization of the hexagonal lattice in the erythrocyte membrane skeleton.
2. Identification and Functional Characterization of Protein 4.1R and Actin-Binding Sites in Erythrocyte β Spectrin: Regulation of the Interactions by Phosphatidylinositol-4,5-bisphosphate
3. The C-Terminal Domain of alpha-Spectrin is Structurally Related to Calmodulin
4. Mutations in the murine erythroid α-spectrin gene alter spectrin mRNA and protein levels and spectrin incorporation into the red blood cell membrane skeleton
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3. Cell physiology and molecular mechanism of anion transport by erythrocyte band 3/AE1;American Journal of Physiology-Cell Physiology;2021-12-01
4. Calcium modulates the domain flexibility and function of an α-actinin similar to the ancestral α-actinin;Proceedings of the National Academy of Sciences;2020-08-26
5. Dystrophin and Spectrin, Two Highly Dissimilar Sisters of the Same Family;Subcellular Biochemistry;2017
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