Structural transitions modulate the chaperone activities of Grp94.

Mirikar, Duhita; Bushman, Yevheniia; Truman, Andrew W

Mirikar, Duhita; Bushman, Yevheniia; Truman, Andrew W.

Afiliação

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 em En | MEDLINE | ID: mdl-38906726

ABSTRACT

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.

Palavras-chave

BiP; DEER; Grp94; Hsp90; endoplasmic reticulum (ER); protein folding

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Trends Biochem Sci Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Estados Unidos

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