Baughman, Hannah E R <br/><br/>
HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.  [electronic resource] 

 -  The Journal of biological chemistry  02 2018 
 - 2687-2700 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1083-351X 
<br/><br/><label>Standard No.: </label>10.1074/jbc.M117.803411  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Motifs<br/>Amino Acid Substitution<br/>Amyloid--chemistry<br/>Anticoagulants--pharmacology<br/>Cryoelectron Microscopy<br/>Dimerization<br/>Down-Regulation--drug effects<br/>HSC70 Heat-Shock Proteins--chemistry<br/>HSP27 Heat-Shock Proteins--chemistry<br/>Heat-Shock Proteins<br/>Heparin--pharmacology<br/>Humans<br/>Kinetics<br/>Models, Molecular<br/>Molecular Chaperones<br/>Mutation<br/>Protein Aggregation, Pathological--metabolism<br/>Protein Interaction Domains and Motifs<br/>Protein Isoforms--chemistry<br/>Recombinant Fusion Proteins--chemistry<br/>Solubility<br/>tau Proteins--chemistry