Localizing the chaperone activity of erythroid spectrin
Author:
Affiliation:
1. Crystallography and Molecular Biology DivisionSaha Institute of Nuclear Physics Kolkata India
2. Homi Bhabha National Institute Mumbai India
Publisher
Wiley
Subject
Cell Biology,Structural Biology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/cm.21556
Reference84 articles.
1. Conformational Stabilities of the Structural Repeats of Erythroid Spectrin and Their Functional Implications
2. Protein Repeats: Structures, Functions, and Evolution
3. Hemoglobin interacting proteins and implications of spectrin hemoglobin interaction
4. 2D DIGE based proteomics study of erythrocyte cytosol in sickle cell disease: Altered proteostasis and oxidative stress
5. Initiation of Spectrin Dimerization Involves Complementary Electrostatic Interactions between Paired Triple-helical Bundles
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1. Spectrin: an alternate target for cytoskeletal drugs;Journal of Biomolecular Structure and Dynamics;2022-08-22
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3. Erythroid spectrin binding modulates peroxidase and catalase activity of heme proteins;IUBMB Life;2022-03-04
4. Comparative Analysis of Tryptophan Dynamics in Spectrin and Its Constituent Domains: Insights from Fluorescence;The Journal of Physical Chemistry B;2021-11-30
5. Saccharomyces cerevisiae Fpr1 functions as a chaperone to inhibit protein aggregation;International Journal of Biological Macromolecules;2021-11
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