Associated Papers
Potential role of βB1 crystallin in cataract formation:a systematic review.
Li M et al.
Archives of Biochemistry and Biophysics, 2025
Heteromeric formation with βA3 protects the low thermal stability of βB1-L116P.
Xu J et al.
The British Journal of Ophthalmology, 2023
Congenital cataract-causing mutation βB1-L116P is prone to amyloid fibrils aggregation and protease degradation with low structural stability.
Liu J et al.
International Journal of Biological Macromolecules, 2022
A novel missense mutation of CRYBB1 causes congenital cataract in a Chinese family.
Ji Y et al.
European Journal of Ophthalmology, 2021
A Novel Mutation p.S93R in CRYBB1 Associated with Dominant Congenital Cataract and Microphthalmia.
Jin A et al.
Current Eye Research, 2020
Novel mutations in CRYBB1/CRYBB2 identified by targeted exome sequencing in Chinese families with congenital cataract.
Chen P et al.
International Journal of Ophthalmology, 2018
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