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Article

Parkin interacts with LIM Kinase 1 and reduces its cofilin-phosphorylation activity via ubiquitination

21 Apr 2007

Abstract excerpt

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Share to Neurological disorders and treatments
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Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 17512523
DOI: 10.1016/j.yexcr.2007.04.016

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

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Parkin interacts with LIM Kinase 1 and reduces its cofilin-phosphorylation activity via ubiquitinationPMID 17512523Read ↗

Interplay between components of a novel LIM kinase–slingshot phosphatase complex regulates cofilinSemantic proximity Read ↗

Regulation of Parkin E3 ubiquitin ligase activitySemantic proximity Read ↗

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Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin‐like domainSemantic proximity Read ↗

Parkin is linked to the ubiquitin pathwaySemantic proximity Read ↗

Parkin–phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activitySemantic proximity Read ↗

SH3 Domains from a Subset of BAR Proteins Define a Ubl-Binding Domain and Implicate Parkin in Synaptic UbiquitinationSemantic proximity Read ↗

A mechanistic review of Parkin activation.Semantic proximity Read ↗

A substrate-interacting region of Parkin directs ubiquitination of the mitochondrial GTPase Miro1Semantic proximity Read ↗

PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial MotilitySemantic proximity Read ↗

A substrate-interacting region of Parkin directs ubiquitination of the mitochondrial GTPase Miro1Semantic proximity Read ↗

LIM kinases: cofilin and beyondSemantic proximity Read ↗

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