Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients-Reference-Cited by-同舟云学术

Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients

Published:2016-01 Issue: Volume:82 Page:328-338
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Yousefi Reza,Javadi Sajjad,Amirghofran Sara,Oryan Ahmad,Moosavi-Movahedi Ali Akbar

Funder

Iran National Science Foundation

Research Councils of Shiraz University

UNESCO Chair on Interdisiplinary Research in Diabetes, University of Tehran

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference50 articles.

1. Ageing and vision: structure, stability and function of lens crystallins

2. The eye lens chaperone -crystallin forms defined globular assemblies

3. Advanced glycation endproducts—role in pathology of diabetic complications

4. Age-dependent protein modifications and declining proteasome activity in the human lens

5. Glucose Uptake by Isolated Normal and Diabetic Rat Lenses

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