Alteration of a developmentally regulated, heat-stable polypeptide in the lens of the Philly mouse. Implications for cataract formation.-Reference-Cited by-同舟云学术

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Alteration of a developmentally regulated, heat-stable polypeptide in the lens of the Philly mouse. Implications for cataract formation.

Published:1988-12 Issue:35 Volume:263 Page:19218-19221
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Nakamura M,Russell P,Carper D A,Inana G,Kinoshita J H

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference24 articles.

1. Aggregation behavior of the bovine β-crystallin Bp chain studied by limited proteolysis

2. Homology between the primary structures of the major bovine beta-crystallin chains

3. Cell Biology of the Eye;Bettelheim,1982

4. Molecular and Cellular Biology of the Eye Lens;Bloemendal,1981

5. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Cited by 10 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

1. Pooling Aqueous Humor Samples: Bias in 2D-LC-MS/MS Strategy?;Journal of Proteome Research;2009-12-29

2. Nucleic Acids;Biochemistry of the Eye;2003

3. Progressive modifications of mouse lens crystallins in cataracts induced by buthionine sulfoximine;Experimental Eye Research;1992-04

4. Deletion mutation in an eye lens beta-crystallin. An animal model for inherited cataracts.;Journal of Biological Chemistry;1991-04

5. Lens Proteins and Their Genes;Progress in Nucleic Acid Research and Molecular Biology;1991

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