Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions
Author:
Funder
National Institute of General Medical Sciences
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Biochemistry
Link
https://link.springer.com/content/pdf/10.1007/s12192-020-01167-0.pdf
Reference125 articles.
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3. Assimon VA, Southworth DR, Gestwicki JE (2015) Specific binding of tetratricopeptide repeat proteins to heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90) is regulated by affinity and phosphorylation. Biochemistry 54:7120–7131
4. Benson DR, Lovell S, Mehzabeen N, Galeva N, Cooper A, Gao P, Battaile KP, Zhu H (2019) Crystal structures of the naturally fused CS and cytochrome b5 reductase (b5R) domains of Ncb5or reveal an expanded CS fold, extensive CS-b5R interactions and productive binding of the NAD(P)(+) nicotinamide ring. Acta Crystallogr D Struct Biol 75:628–638
5. Biebl MM, Riedl M, Buchner J (2020) Hsp90 Co-chaperones form plastic genetic networks adapted to client maturation. Cell Rep 32:108063
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