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The Journal of Biological Chemistry|December 14, 2011
Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activityXinping Xu, Evans Boateng Sarbeng, Christina Vorvis, et al.
Journal of Molecular Biology|July 19, 2011
The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct rolesDivya Prasanna Kumar, Christina Vorvis, Evans Boateng Sarbeng, et al.
The Journal of Biological Chemistry|December 7, 2019
An unexpected second binding site for polypeptide substrates is essential for Hsp70 chaperone activityHongtao Li, Huanyu Zhu, Evans Boateng Sarbeng, et al.
The Journal of Biological Chemistry|January 31, 2015
A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock proteinEvans Boateng Sarbeng, Qingdai Liu, Xueli Tian, et al.
Nature Structural & Molecular Biology|May 28, 2013
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATPRuifeng Qi, Evans Boateng Sarbeng, Qun Liu, et al.
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