Unknown

Dataset Information

0

Compact Parkin only: insights into the structure of an autoinhibited ubiquitin ligase.


ABSTRACT: Mutations in Parkin represent ~50% of disease-causing defects in autosomal recessive-juvenile onset Parkinson's disease (AR-JP). Recently, there have been four structural reports of autoinhibited forms of this RING-IBR-RING (RBR) ubiquitin ligase (E3) by the Gehring, Komander, Johnston and Shaw groups. The important advances from these studies set the stage for the next steps in understanding the molecular basis for Parkinson's disease (PD).

SUBMITTER: Byrd RA 

PROVIDER: S-EPMC3730235 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Compact Parkin only: insights into the structure of an autoinhibited ubiquitin ligase.

Byrd R Andrew RA   Weissman Allan M AM  

The EMBO journal 20130712 15


Mutations in Parkin represent ~50% of disease-causing defects in autosomal recessive-juvenile onset Parkinson's disease (AR-JP). Recently, there have been four structural reports of autoinhibited forms of this RING-IBR-RING (RBR) ubiquitin ligase (E3) by the Gehring, Komander, Johnston and Shaw groups. The important advances from these studies set the stage for the next steps in understanding the molecular basis for Parkinson's disease (PD). ...[more]

Similar Datasets

| S-EPMC3730226 | biostudies-literature
| S-EPMC4859148 | biostudies-literature
| S-EPMC4003245 | biostudies-literature
| S-EPMC4609183 | biostudies-literature
| S-EPMC3886920 | biostudies-literature
| S-EPMC5646993 | biostudies-literature
| S-EPMC3709503 | biostudies-literature
| S-EPMC2614788 | biostudies-literature
| S-EPMC3341078 | biostudies-literature
| S-EPMC1356342 | biostudies-literature