Age-Related Changes in Human Crystallins Determined from Comparative Analysis of Post-translational Modifications in Young and Aged Lens: Does Deamidation Contribute to Crystallin Insolubility?-Reference-Cited by-同舟云学术

Age-Related Changes in Human Crystallins Determined from Comparative Analysis of Post-translational Modifications in Young and Aged Lens: Does Deamidation Contribute to Crystallin Insolubility?

Published:2006-09-08 Issue:10 Volume:5 Page:2554-2566
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

Wilmarth P. A.¹,Tanner S.¹,Dasari S.¹,Nagalla S. R.¹,Riviere M. A.¹,Bafna V.¹,Pevzner P. A.¹,David L. L.¹

Affiliation:

1. Department of Integrative Biosciences, School of Dentistry, Oregon Health and Science University, 611 South West Campus Drive, Portland, Oregon 97239, Bioinformatics Program, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0404, Department of Pediatrics, Oregon Health and Science University, 3181 South West Sam Jackson Park Road, Portland, Oregon 97239-3098, and Department of Computer Science and Engineering, University of California, San Diego, 9500 Gilman Drive, La...

Publisher

American Chemical Society (ACS)

Subject

General Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/pr050473a

Reference67 articles.

1. Sequence Analysis of βA3, βB3, and βA4 Crystallins Completes the Identification of the Major Proteins in Young Human Lens

2. High-Throughput Identification of Proteins and Unanticipated Sequence Modifications Using a Mass-Based Alignment Algorithm for MS/MS de Novo Sequencing Results

3. Identification of Protein Modifications Using MS/MS de Novo Sequencing and the OpenSea Alignment Algorithm

4. In vivo carbamylation and acetylation of water-soluble human lens αB-crystallin lysine 92

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