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International Journal of Biological Macromolecules|December 10, 2017
Increasing susceptibility to oxidative stress by cataract-causing crystallin mutationsWei-Jie Zhao, Yong-Bin YanBiochemistry|May 1, 2019
Dissimilarity in the Contributions of the N-Terminal Domain Hydrophobic Core to the Structural Stability of Lens β/γ-CrystallinsKai Zhang, Wei-Jie Zhao, Ke Yao, et al.Journal of Molecular Biology|July 14, 2015
Congenital Cataract-Causing Mutation G129C in γC-Crystallin Promotes the Accumulation of Two Distinct Unfolding Intermediates That Form Highly Toxic AggregatesYi-Bo Xi, Xiang-Jun Chen, Wei-Jie Zhao, et al.Biochimica Et Biophysica Acta|November 20, 2012
Increasing βB1-crystallin sensitivity to proteolysis caused by the congenital cataract-microcornea syndrome mutation S129RSha Wang, Wei-Jie Zhao, Huihui Liu, et al.Biochemical and Biophysical Research Communications|September 17, 2018
Introduction of an extra tryptophan fluorophore by cataract-associating mutations destabilizes βB2-crystallin and promotes aggregationJia Xu, Wei-Jie Zhao, Xiang-Jun Chen, et al.Plos One|December 14, 2012
The congenital cataract-linked A2V mutation impairs tetramer formation and promotes aggregation of βB2-crystallinJia Xu, Sha Wang, Wei-Jie Zhao, et al.Biochimica Et Biophysica Acta|October 15, 2013
The importance of the last strand at the C-terminus in βB2-crystallin stability and assemblyKai Zhang, Wei-Jie Zhao, Xiao-Yao Leng, et al.International Journal of Biological Macromolecules|May 23, 2017
Effects of cataract-causing mutations W59C and W151C on βB2-crystallin structure, stability and foldingWei-Jie Zhao, Jia Xu, Xiang-Jun Chen, et al.Wiley Interdisciplinary Reviews. RNA|August 14, 2020
Diverse functions of deadenylases in DNA damage response and genomic integrityYong-Bin YanPageof 14