Evidence map›Paper›PMID 26811536›Full record

ReviewThe Biochemical journal2016

The function of orthologues of the human Parkinson's disease gene LRRK2 across species: implications for disease modelling in preclinical research.

Rebekah G Langston, Iakov N Rudenko, Mark R Cookson

Open access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Functions of the RIP kinase family members in the skin.Cellular and molecular life sciences : CMLS · 2023
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. The Cell Biology of LRRK2 in Parkinson's Disease.Molecular and cellular biology · 2021
    Review
  12. Modeling Parkinson's Disease: Not Only Rodents?Frontiers in aging neuroscience · 2021
    Article
  13. RIPK protein kinase family: Atypical lives of typical kinases.Seminars in cell & developmental biology · 2021
    Review
  14. Article
  15. Progress inFrontiers in neuroscience · 2020
    Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
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

3 authors at 1 institution in 1 country.

Rebekah G LangstonCell Biology and Gene Expression Section, Laboratory of Neurogenetics, NIA, NIH, Bethesda, MD 20892, U.S.A.
Iakov N RudenkoCell Biology and Gene Expression Section, Laboratory of Neurogenetics, NIA, NIH, Bethesda, MD 20892, U.S.A.
Mark R CooksonCell Biology and Gene Expression Section, Laboratory of Neurogenetics, NIA, NIH, Bethesda, MD 20892, U.S.A. cookson@mail.nih.gov.
National Institutes of Health · US

Funding

Leucine rich repeat kinase 2 and dominantly inherited Parkinson diseaseZIAAG000948 · NIA · NATIONAL INSTITUTE ON AGING · PI COOKSON, MARK · 2009 to 2025
$18.3M
GTPase function of Leucine rich repeat kinase 2ZIAAG000937 · NIA · NATIONAL INSTITUTE ON AGING · PI COOKSON, MARK · 2010 to 2025
$9.2M
Intramural NIH HHS ZIA AG000937
6 · The paper itself

Abstract

In the period since LRRK2 (leucine-rich repeat kinase 2) was identified as a causal gene for late-onset autosomal dominant parkinsonism, a great deal of work has been aimed at understanding whether the LRRK2 protein might be a druggable target for Parkinson's disease (PD). As part of this effort, animal models have been developed to explore both the normal and the pathophysiological roles of LRRK2. However, LRRK2 is part of a wider family of proteins whose functions in different organisms remain poorly understood. In this review, we compare the information available on biochemical properties of LRRK2 homologues and orthologues from different species from invertebrates (e.g. Caenorhabditis elegans and Drosophila melanogaster) to mammals. We particularly discuss the mammalian LRRK2 homologue, LRRK1, and those species where there is only a single LRRK homologue, discussing examples where each of the LRRK family of proteins has distinct properties as well as those cases where there appear to be functional redundancy. We conclude that uncovering the function of LRRK2 orthologues will help to elucidate the key properties of human LRRK2 as well as to improve understanding of the suitability of different animal models for investigation of LRRK2-related PD.

Indexed as

Disease Models, AnimalAnimalsBiomedical ResearchCaenorhabditis elegansDrosophila melanogasterHumansParkinson DiseaseProtein Serine-Threonine KinasesProtein Serine-Threonine Kinasesanimal modelsdopaminergic neuronsGTPasekinaseLRRK2 homologueneurodegenerationpreclinical research

Identifiers

PMID26811536
PMCPMC5165698
OpenAlexW2253501177

What OpenQuestion holds

Textmetadata
LicenceTDM
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.