Deamidation Alters the Structure and Decreases the Stability of Human Lens βΑ3-Crystallin-Reference-Cited by-同舟云学术

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Deamidation Alters the Structure and Decreases the Stability of Human Lens βΑ3-Crystallin

Published:2007-07-01 Issue:30 Volume:46 Page:8861-8871
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Takata Takumi¹,Oxford Julie T.¹,Brandon Theodore R.¹,Lampi Kirsten J.¹

Affiliation:

1. Department of Integrative Biosciences, School of Dentistry, Oregon Health & Science University, 611 SW Campus Drive, Portland, Oregon 97239-3098, and Department of Biology, Boise State University, 1910 University Drive, Boise, Idaho 83725

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi700487q

Reference59 articles.

Cited by 52 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

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2. The Functional Significance of High Cysteine Content in Eye Lens γ-Crystallins;Biomolecules;2024-05-17

3. Quantitative and structural changes of blood platelet cytoskeleton proteins in multiple sclerosis (MS);Journal of Autoimmunity;2024-05

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

5. Mapping the GALNT1 substrate landscape with versatile proteomics tools;2022-08-24

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