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Structural transitions modulate the chaperone activities of Grp94.
- Source :
-
Trends in biochemical sciences [Trends Biochem Sci] 2024 Sep; Vol. 49 (9), pp. 752-753. Date of Electronic Publication: 2024 Jun 20. - Publication Year :
- 2024
-
Abstract
- A recent study by Amankwah et al. reports how co-chaperone proteins and ATP hydrolysis fine-tune the function of endoplasmic reticulum (ER)-resident Hsp90 paralog Grp94.<br />Competing Interests: Declaration of Interests The authors declare no competing interests.<br /> (Published by Elsevier Ltd.)
Details
- Language :
- English
- ISSN :
- 0968-0004
- Volume :
- 49
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Trends in biochemical sciences
- Publication Type :
- Academic Journal
- Accession number :
- 38906726
- Full Text :
- https://doi.org/10.1016/j.tibs.2024.06.007