Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.
Sign Up to like & getrecommendations! Published in 2018 at "Methods in molecular biology"
DOI: 10.1007/978-1-4939-7477-1_28
Abstract: Molecular chaperones are a diverse group of highly conserved proteins that transiently interact with partially folded polypeptide chains during normal cellular processes such as protein translation, translocation, and disassembly of protein complexes. Prior to folding… read more here.
Keywords: protein; hsp90; chaperones regulating; evidence hsp90 ... See more keywords
Hsp90 Co-chaperones Form Plastic Genetic Networks Adapted to Client Maturation.
Sign Up to like & getrecommendations! Published in 2020 at "Cell reports"
DOI: 10.1016/j.celrep.2020.108063
Abstract: Heat shock protein 90 (Hsp90) is a molecular chaperone regulating the activity of diverse client proteins together with a plethora of different co-chaperones. Whether these functionally cooperate has remained enigmatic. We analyze all double mutants… read more here.
Keywords: form plastic; hsp90 chaperones; client; chaperones form ... See more keywords