The Sequence of Human βB1-Crystallin cDNA Allows Mass Spectrometric Detection of βB1 Protein Missing Portions of Its N-terminal Extension
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference36 articles.
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1. Eye lens β-crystallins are predicted by native ion mobility-mass spectrometry and computations to form compact higher-ordered heterooligomers;Structure;2023-09
2. Cataract-causing variant Q70P damages structural stability of βB1-crystallin and increases its tendency to form insoluble aggregates;International Journal of Biological Macromolecules;2023-07
3. Modifications of Long‐Lived Proteins that Affect Protein Solubility;Long‐lived Proteins in Human Aging and Disease;2021-02-05
4. Exploring the folding process of human βB2-crystallin using multiscale molecular dynamics and the Markov state model;Physical Chemistry Chemical Physics;2020
5. Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain;Protein & Cell;2016-06-18
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