Mechanochemistry of the alternatively spliced spectrin-actin binding domain in membrane skeletal protein 4.1.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference59 articles.
1. Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability.
2. Phosphorylation reduces the affinity of protein 4.1 for spectrin
3. Properties of red cell membrane proteins: mechanism of spectrin and band 4.1 interaction
4. Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1.
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2. Protein 4.1R Exon 16 3′ Splice Site Activation Requires Coordination among TIA1, Pcbp1, and RBM39 during Terminal Erythropoiesis;Molecular and Cellular Biology;2017-05
3. A dynamic alternative splicing program regulates gene expression during terminal erythropoiesis;Nucleic Acids Research;2014-01-17
4. Isoforms of protein 4.1 are differentially distributed in heart muscle cells: Relation of 4.1R and 4.1G to components of the Ca2+ homeostasis system;Experimental Cell Research;2012-08
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