Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant.

Journal of neurochemistry - 1 Jan 2011

Daniëls Veronique, Vancraenenbroeck Renée, Law Bernard M H, Greggio Elisa, Lobbestael Evy, Gao Fangye, De Maeyer Marc, Cookson Mark R, Harvey Kirsten, Baekelandt Veerle, Taymans Jean-Marc

Abstract excerpt

Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene are the most prevalent known cause of autosomal dominant Parkinson's disease. The LRRK2 gene encodes a Roco protein featuring a Ras of complex proteins (ROC) GTPase and a kinase domain linked by the C-terminal of ROC (COR) domain. Here, w...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalytic Domain
Share to Cysteine
Share to GTP Phosphohydrolases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HEK293 Cells

Share to Leucine-Rich Repeat Serine-Threonine Protein Kinase-2

Share to Protein Multimerization

Share to Protein Serine-Threonine Kinases

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 21073465
DOI: 10.1111/j.1471-4159.2010.07105.x
PMCID: PMC3005098

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21073465-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant.PMID 21073465Read ↗

The Roc-COR tandem domain of leucine-rich repeat kinase 2 forms dimers and exhibits conventional Ras-like GTPase properties.Semantic proximity Read ↗

L'RRK de Triomphe: a solution for LRRK2 GTPase activity?Semantic proximity Read ↗

Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPaseSemantic proximity Read ↗

R1398 is the GTP-𝛾-phosphate sensor that drives the ROC G-domain switching mechanism unique to Parkinson's disease-associated LRRK2Semantic proximity Read ↗

The unconventional G-protein cycle of LRRK2 and Roco proteins.Semantic proximity Read ↗

Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment.Semantic proximity Read ↗

Allosteric modulation of the GTPase activity of a bacterial LRRK2 homolog by conformation-specific Nanobodies.Semantic proximity Read ↗

Heterogeneity of leucine-rich repeat kinase 2 mutations: genetics, mechanisms and therapeutic implications.Semantic proximity Read ↗

Structural biology of the LRRK2 GTPase and kinase domains: implications for regulationSemantic proximity Read ↗

Understanding the GTPase Activity of LRRK2: Regulation, Function, and Neurotoxicity.Semantic proximity Read ↗

Intramolecular feedback regulation of the LRRK2 Roc G domain by a LRRK2 kinase dependent mechanismSemantic proximity Read ↗

Contribution of GTPase activity to LRRK2-associated Parkinson disease.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.