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Article

Congenital microcornea-cataract syndrome-causing mutation X253R increases βB1-crystallin hydrophobicity to promote aggregate formation.

The Biochemical journal - 15 Jul 2016

Leng Xiao-Yao, Li Hai-Yun, Wang Jing, Qi Liang-Bo, Xi Yi-Bo, Yan Yong-Bin

Abstract excerpt

The high solubility and lifelong stability of crystallins are crucial to the maintenance of lens transparency and optical properties. Numerous crystallin mutations have been linked to congenital cataract, which is one of the leading causes of newborn blindness. Besides cataract, several crystallin mutations have also been linked to syndromes such as congenital microcornea-cataract syndrome (CMCC). However, the...

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Cataract
Circular Dichroism
Corneal Diseases
HeLa Cells
Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Aggregation, Pathological

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PMID: 27208166
DOI: 10.1042/BCJ20160247

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Congenital microcornea-cataract syndrome-causing mutation X253R increases βB1-crystallin hydrophobicity to promote aggregate formation.PMID 27208166Read ↗

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