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Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.

机译：突变γ-晶状体蛋白的引起白内障的缺陷通过聚集途径进行，该途径绕过α-晶状体蛋白伴侣的识别。

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Kate L Moreau; Jonathan A King;
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1. Aggregation of deamidated human betaB2-crystallin and incomplete rescue by alpha-crystallin chaperone. [J] . Michiel M, Duprat E, Skouri Panet F, Experimental Eye Research . 2010,第6期

机译：脱酰胺化的人βB2-晶状蛋白的聚集和α-晶状蛋白伴侣的不完全拯救。
2. Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone. [J] . Acosta Sampson L, King J Journal of Molecular Biology . 2010,第1期

机译：人γD-，γC-和γS-晶状蛋白的部分折叠的聚集中间体被人αB-晶状蛋白伴侣识别并结合。
3. Functional Rescue of Cataract-Causing alpha A-G98R-Crystallin by Targeted Compensatory Suppressor Mutations in Human alpha A-Crystallin [J] . Phadte Ashutosh S., Mahalingam Sundararajan, Santhoshkumar Puttur, Biochemistry . 2019,第40期

机译：白内障α-G98r晶体通过靶向补偿抑制剂突变在人α-晶体中的功能拯救
4. Study of molecular mechanisms of UV-induced aggregation of crystallins and possibility of maintaining eye lens transparency [C] . L.V. Soustov, E.V. Chelnokov, N.M. Bityurin, Conference on ICONO: Nonlinear Laser Spectroscopy, High Precision Measurements, and Laser Biomedicine and Chemistry . 2006

机译：纤维素诱导晶体聚集的分子机制及维持眼睛透镜透明度的可能性研究
5. Molecular Biochemical Study of the Cataract-Associated Mutants in Human gammaD-Crystallin. [D] . Yeung, Cindy. 2013

机译：人gammaD-Crystallin中与白内障相关的突变体的分子生化研究。
6. Cataract-Causing Defect of a Mutant γ-Crystallin Proceeds through an Aggregation Pathway Which Bypasses Recognition by the α-Crystallin Chaperone [O] . Kate L. Moreau, Jonathan A. King 2009

机译：突变体γ-晶体的白内障缺陷通过聚集途径进行，该聚集途径绕过了α-晶体伴侣的识别。
7. Cataract-Causing Defect of a Mutant γ-Crystallin Proceeds through an Aggregation Pathway Which Bypasses Recognition by the α-Crystallin Chaperone [O] . Moreau, Kate L., King, Jonathan A. 2012

机译：突变体γ-晶体的白内障缺陷通过聚集途径进行，该聚集途径绕过了α-晶体伴侣的识别。

Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.

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