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

Targeting phosphatases as the next generation of disease modifying therapeutics for Parkinson's disease.

Neurochemistry international - 1 Nov 2012

Braithwaite Steven P, Voronkov Michael, Stock Jeffry B, Mouradian M Maral

Abstract excerpt

Phosphorylation is a key post-translational modification for cellular signaling, and abnormalities in this process are observed in several neurodegenerative disorders. Among these disorders, Parkinson's disease (PD) is particularly intriguing as there are both genetic causes of disease that involve phosphorylation, and pathological hallmarks of disease composed of a hyperphosphorylated protein. Two of the major...

Read the complete abstract on PubMed

Topics

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

Share to PINK1 gene
Share to Leucine-Rich Repeat Serine-Threonine Protein Kinase-2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Parkinson Disease

Share to Phosphoric Monoester Hydrolases

Share to Phosphorylation

Share to Protein Serine-Threonine Kinases

Source

Identifiers

PMID: 22342821
DOI: 10.1016/j.neuint.2012.01.031

Genes

PINK1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Targeting phosphatases as the next generation of disease modifying therapeutics for Parkinson's disease.PMID 22342821Read ↗

Phosphatases of Î±-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of ParkinsonismSemantic proximity Read ↗

Protein Kinases and Parkinson’s DiseaseSemantic proximity Read ↗

Kinases as Targets for Parkinson's Disease: From Genetics to TherapySemantic proximity Read ↗

Pathological Protein Targets in Parkinson's Disease: Progress Towards the Development of Disease-Modifying Therapies.Semantic proximity Read ↗

Kinase signaling pathways as potential targets in the treatment of Parkinson's disease.Semantic proximity Read ↗

Ubiquitin phosphorylation in Parkinson’s disease: Implications for pathogenesis and treatmentSemantic proximity Read ↗

LRRK2 Phosphorylation: Behind the Scenes.Semantic proximity Read ↗

PINK1 and Parkin – mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson's disease.Semantic proximity Read ↗

Leucine-rich repeat kinase 2 (LRRK2): an update on the potential therapeutic target for Parkinson’s diseaseSemantic proximity Read ↗

Leucine-rich repeat kinase 2 (LRRK2) as a potential therapeutic target in Parkinson's disease.Semantic proximity Read ↗

Pharmacological PINK1 activation ameliorates Pathology in Parkinson’s Disease modelsSemantic proximity Read ↗

LRRK2 and Proteostasis in Parkinson's Disease.Semantic proximity Read ↗

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