Your browser doesn't support javascript.
loading
Structural transitions modulate the chaperone activities of Grp94.
Mirikar, Duhita; Bushman, Yevheniia; Truman, Andrew W.
Affiliation
  • Mirikar D; Department of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, NC 28223, USA.
  • Bushman Y; Department of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, NC 28223, USA.
  • Truman AW; Department of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, NC 28223, USA. Electronic address: a.truman@charlotte.edu.
Trends Biochem Sci ; 2024 Jun 20.
Article in En | MEDLINE | ID: mdl-38906726
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.
Key words
Fulltext
Add to My VHL
Print
XML
PubMed Links
Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Trends Biochem Sci Year: 2024 Document type: Article Affiliation country: United States
Fulltext
Add to My VHL
Print
XML
PubMed Links
Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Trends Biochem Sci Year: 2024 Document type: Article Affiliation country: United States