Author: Song, Jae-Hyoung; Shim, Aeri; Kim, Yeon-Jeong; Ahn, Jae-Hee; Kwon, Bo-Eun; Pham, Thuy Trang; Lee, Jongkook; Chang, Sun-Young; Ko, Hyun-Jeong
Title: Antiviral and Anti-Inflammatory Activities of Pochonin D, a Heat Shock Protein 90 Inhibitor, against Rhinovirus Infection Document date: 2018_5_2
ID: 0bwf8f1i_3
Snippet: Hsp90, a 90 kDa heat shock protein, is a highly abundant, essential, and evolutionarily conserved molecular chaperone at the center of a large protein-folding network (Geller et al., 2013) . There are two cytoplasmic isoforms of Hsp90 in mammals. Hsp90α is an inducible isoform, whereas Hsp90β is expressed constitutively. Hsp90 function is regulated by a cohort of co-chaperones that modulate its ATPase cycle, enabling it to acquire and select cl.....
Document: Hsp90, a 90 kDa heat shock protein, is a highly abundant, essential, and evolutionarily conserved molecular chaperone at the center of a large protein-folding network (Geller et al., 2013) . There are two cytoplasmic isoforms of Hsp90 in mammals. Hsp90α is an inducible isoform, whereas Hsp90β is expressed constitutively. Hsp90 function is regulated by a cohort of co-chaperones that modulate its ATPase cycle, enabling it to acquire and select client proteins, and to provide a link with other chaperone systems including proteasome degradation systems for protein degradation (Geller et al., 2012) .
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