Sprague-Piercy, Marc A <br/><br/>
Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.  [electronic resource] 

 -  Biochimica et biophysica acta. General subjects  03 2020 
 - 129502 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. 
<br/><br/><label>ISSN: </label>1872-8006 
<br/><br/><label>Standard No.: </label>10.1016/j.bbagen.2019.129502  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Cataract--genetics<br/>Humans<br/>Hydrophobic and Hydrophilic Interactions<br/>Lens, Crystalline--metabolism<br/>Molecular Chaperones--metabolism<br/>Molecular Dynamics Simulation<br/>Mutation<br/>Protein Binding<br/>Protein Conformation<br/>Protein Folding<br/>Structure-Activity Relationship<br/>alpha-Crystallin B Chain--genetics<br/>gamma-Crystallins--chemistry