Deamidation of Human βB1 Alters the Elongated Structure of the Dimer-Reference-Cited by-同舟云学术

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Deamidation of Human βB1 Alters the Elongated Structure of the Dimer

Published:2001-03 Issue:3 Volume:72 Page:279-288
ISSN:0014-4835
Container-title:Experimental Eye Research
language:en
Short-container-title:Experimental Eye Research

Author:

Lampi Kirsten J.,Oxford Julie T.,Bachinger Hans Peter,Shearer Thomas R.,David Larry L.,Kapfer Deborah M.

Publisher

Elsevier BV

Subject

Cellular and Molecular Neuroscience,Sensory Systems,Ophthalmology

Reference24 articles.

1. Size of human lens β-crystallin aggregates are distinguished by N-terminal truncation of βB1;Ajaz;J. Biol. Chem.,1997

2. The C-terminal domain of cartilage matrix protein assembles into a triple-stranded alpha-helical coiled-coil structure;Beck;J. Mol. Biol.,1996

3. Structural aspects of bovine β-crystallins: physical characterization including dissociation-association behavior;Bindels;Exp. Eye Res.,1981

4. Bovine lens crystallins do contain helical structure: a circular dichroism study;Bloemendal;Biochim. Biophys. Acta,1999

5. the conformation of T4 bacteriophage dihydrofolate reductase from circular dichroism;Compton;J. Biol. Chem.,1987

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1. Cumulative asparagine to aspartate deamidation fails to perturb γD‐crystallin structure and stability;Protein Science;2024-07-18

2. Eye lens β-crystallins are predicted by native ion mobility-mass spectrometry and computations to form compact higher-ordered heterooligomers;Structure;2023-09

3. ATCUN-like Copper Site in βB2-Crystallin Plays a Protective Role in Cataract-Associated Aggregation;Inorganic Chemistry;2023-06-28

4. Deamidation of the human eye lens protein γS-crystallin accelerates oxidative aging;Structure;2022-05

5. Research Progress of Molecular Recognition and Interaction of Crystallins Linking Cataract;CHEM J CHINESE U;2021

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