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Ubiquitin is phosphorylated by PINK1 to activate parkin

2014· article· en· 1,484 citations· W2052889619 on OpenAlex· 10.1038/nature13392

Why is this work in the frame?

A frame that forgets how it found something cannot be audited. These are the routes that admitted this work.

Canadian affiliationAn author listed a Canadian institution. This is the only route the usual frame has.
Canadian funderA Canadian agency funded it. The work may carry no Canadian affiliation at all.

Abstract

No abstract. This is not a gap in this database — OpenAlex has none either. 23.3% of the frame is in this state, and the screen finds HALF as much metaresearch here, so the absence is a measured bias rather than a missing field.

The record

Venue
Nature
Topic
Mitochondrial Function and Pathology
Field
Biochemistry, Genetics and Molecular Biology
Canadian institutions
Montreal Neurological Institute and HospitalMcGill University
Funders
Canadian Institutes of Health Research
Keywords
ParkinPINK1UbiquitinUbiquitin ligaseCell biologyMitochondrionBiologyPhosphorylationMitophagyKinaseBiochemistryChemistryMolecular biologyAutophagyParkinson's disease
Has abstract in OpenAlex
no