Shuxia Peng

TL;DR: Initial studies support the development of Hsp90β-selective inhibitors as a method to overcome the detriments associated with pan-inhibition, and rationally design an HSp90 inhibitor that displays high selectivity for the Hsp 90β isoform.

TL;DR: In this article, the authors describe a structure-based approach that was used to design the first Hsp90a-selective inhibitors, which exhibit > 50-fold selectivity versus other Hsp 90 isoforms.

TL;DR: The identification of the structure and function of a SAMD9/9L effector domain that functions by binding to double-stranded nucleic acids (dsNA) and determined the crystal structure of the domain in complex with DNA revealed a potential therapeutic target for SAMD7/7L-associated human diseases.

TL;DR: The results reveal a protein modality for enclosing the lipid bilayer and provide molecular insight into a viral machinery involved in generating and/or stabilizing open-ended membranes.

TL;DR: The structure of MDCC-labeled Hsp 90α MD and CTD reported here provides the first direct visual insight into allosteric binding inhibitors of Hsp90 MD or CTD and provides a basis for the design of novel drugs for the treatment of cancer and neurodegenerative diseases.