Evidence map›Paper›PMID 20595391›Full record

ArticleThe Journal of biological chemistry2010

Reevaluation of phosphorylation sites in the Parkinson disease-associated leucine-rich repeat kinase 2.

Xiaojie Li, Darren J Moore, Yulan Xiong, Ted M Dawson, Valina L Dawson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. LRRK2 and idiopathic Parkinson's disease.Trends in neurosciences · 2022
    Review
  9. Article
  10. Curcumin Reduced HFrontiers in aging neuroscience · 2021
    Article
  11. Article
  12. Kinase Domain Is a Dynamic Hub for Driving LRRK2 Allostery.Frontiers in molecular neuroscience · 2020
    Article
  13. Review
  14. LRRK2 activation in idiopathic Parkinson's disease.Science translational medicine · 2018
    Article
  15. The LRRK2 signalling system.Cell and tissue research · 2018
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Heterogeneity of leucine-rich repeat kinase 2 mutations: genetics, mechanisms and therapeutic implications.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2014
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Xiaojie LiNeuroRegeneration and Stem Cell Programs, Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Darren J Moore
Yulan Xiong
Ted M Dawson
Valina L Dawson
Stem Cell Institute · PAJohns Hopkins Medicine · USSociety for Neuroscience · US

Funding

Understanding Mechanisms of a-synuclein pathologyP50NS038377 · NINDS · JOHNS HOPKINS UNIVERSITY · PI KO, HANSEOK · 1998 to 2019
$38.8M
NINDS NIH HHS NS38377NINDS NIH HHS P50 NS038377
6 · The paper itself

Abstract

Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene have been identified as an important cause of late-onset, autosomal dominant familial Parkinson disease and contribute to sporadic Parkinson disease. LRRK2 is a large complex protein with multiple functional domains, including a Roc-GTPase, protein kinase, and multiple protein-protein interaction domains. Previous studies have suggested an important role for kinase activity in LRRK2-induced neuronal toxicity and inclusion body formation. Disease-associated mutations in LRRK2 also tend to increase kinase activity. Thus, enhanced kinase activity may therefore underlie LRRK2-linked disease. Similar to the closely related mixed-lineage kinases, LRRK2 can undergo autophosphorylation in vitro. Three putative autophosphorylation sites (Thr-2031, Ser-2032, and Thr-2035) have been identified within the activation segment of the LRRK2 kinase domain based on sequence homology to mixed-lineage kinases. Phosphorylation at one or more of these sites is critical for the kinase activity of LRRK2. Sensitive phospho-specific antibodies to each of these three sites have been developed and validated by ELISA, dot-blot, and Western blot analysis. Using these antibodies, we have found that all three putative sites are phosphorylated in LRRK2, and Ser-2032 and Thr-2035 are the two important sites that regulate LRRK2 kinase activity.

Indexed as

Amino Acid SequenceAnimalsAntibodies, Phospho-SpecificBlotting, WesternCell LineCells, CulturedEnzyme ActivationEnzyme-Linked Immunosorbent AssayHumansHydrogen PeroxideLeucine-Rich Repeat Serine-Threonine Protein Kinase-2MiceMolecular Sequence DataMutationParkinson DiseasePhosphorylationAntibodies, Phospho-SpecificHydrogen PeroxideLeucine-Rich Repeat Serine-Threonine Protein Kinase-2LRRK2 protein, humanLrrk2 protein, mouseProtein Serine-Threonine Kinases

Identifiers

PMID20595391
PMCPMC2937988
OpenAlexW1991219393

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.