Structural and Functional Analysis of Disease-Linked p97 ATPase Mutant Complexes
IBMPFD/ALS is a genetic disorder caused by a single amino acid mutation on the p97 ATPase, promoting ATPase activity and cofactor dysregulation. The disease mechanism underlying p97 ATPase malfunction remains unclear. To understand how the mutation alters the ATPase regulation, we assembled a full-l...
Main Authors: | Purbasha Nandi, Shan Li, Rod Carlo A. Columbres, Feng Wang, Dewight R. Williams, Yu-Ping Poh, Tsui-Fen Chou, Po-Lin Chiu |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2021-07-01
|
Series: | International Journal of Molecular Sciences |
Subjects: | |
Online Access: | https://www.mdpi.com/1422-0067/22/15/8079 |
Similar Items
-
Molecular Mechanisms Driving and Regulating the AAA+ ATPase VCP/p97, an Important Therapeutic Target for Treating Cancer, Neurological and Infectious Diseases
by: Sepideh Valimehr, et al.
Published: (2023-04-01) -
A Dynamic molecular basis for malfunction in disease mutants of p97/VCP
by: Anne K Schuetz, et al.
Published: (2016-11-01) -
Skeletal muscle cell protein dysregulation highlights the pathogenesis mechanism of myopathy-associated p97/VCP R155H mutations
by: Anna Luzzi, et al.
Published: (2023-08-01) -
Impacts of p97 on Proteome Changes in Human Cells during Coronaviral Replication
by: Kai-Wen Cheng, et al.
Published: (2021-10-01) -
A novel function of AAA-ATPase p97/VCP in the regulation of cell motility
by: Khong, Nicole Zi Jia, et al.
Published: (2021)