Extensive deamidation of RNase A inhibits its oligomerization through 3D domain swapping
Author:
Funder
Spanish Ministry of Economy and Competitiveness
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry
Reference72 articles.
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3. Thermal aggregation of ribonuclease A. A contribution to the understanding of the role of 3D domain swapping in protein aggregation;Gotte;J. Biol. Chem.,2003
4. The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1-A resolution;Liu;Proc. Natl. Acad. Sci. U. S. A.,1998
5. A domain-swapped RNase A dimer with implications for amyloid formation;Liu;Nat. Struct. Biol.,2001
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1. Slow Evolution toward “Super-Aggregation” of the Oligomers Formed through the Swapping of RNase A N-Termini: A Wish for Amyloidosis?;International Journal of Molecular Sciences;2022-09-23
2. RNase A Domain-Swapped Dimers Produced Through Different Methods: Structure–Catalytic Properties and Antitumor Activity;Life;2021-02-21
3. Biological Activities of Secretory RNases: Focus on Their Oligomerization to Design Antitumor Drugs;Frontiers in Immunology;2019-11-26
4. Raman-markers of X-ray radiation damage of proteins;International Journal of Biological Macromolecules;2018-05
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