Evidence map›Paper›PMID 36929701›Full record

ReviewBiochemical Society transactions2023

Insights into the cellular consequences of LRRK2-mediated Rab protein phosphorylation.

Rachel Fasiczka, Yahaira Naaldijk, Besma Brahmia, Sabine Hilfiker

Open access · hybridAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Biochemical Society transactions, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Elucidating the molecular interplay between LRRK2 and Rab GTPases.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Leucine-rich repeat kinase 2 at a glance.Journal of cell science · 2023
    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

4 authors at 1 institution in 1 country.

Rachel FasiczkaDepartment of Anesthesiology, Rutgers New Jersey Medical School, Newark, NJ 07103, U.S.A.
Yahaira NaaldijkDepartment of Anesthesiology, Rutgers New Jersey Medical School, Newark, NJ 07103, U.S.A.
Besma BrahmiaDepartment of Anesthesiology, Rutgers New Jersey Medical School, Newark, NJ 07103, U.S.A.
Sabine HilfikerDepartment of Anesthesiology, Rutgers New Jersey Medical School, Newark, NJ 07103, U.S.A.ORCID 0000-0002-5167-7682
Rutgers, The State University of New Jersey · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Point mutations in leucine-rich repeat kinase 2 (LRRK2) which cause Parkinson's disease increase its kinase activity, and a subset of Rab GTPases have been identified as endogenous LRRK2 kinase substrates. Their phosphorylation correlates with a loss-of-function for the membrane trafficking steps they are normally involved in, but it also allows them to bind to a novel set of effector proteins with dominant cellular consequences. In this brief review, we will summarize novel findings related to the LRRK2-mediated phosphorylation of Rab GTPases and its various cellular consequences in vitro and in the intact brain, and we will highlight major outstanding questions in the field.

Indexed as

Leucine-Rich Repeat Serine-Threonine Protein Kinase-2Parkinson Diseaserab GTP-Binding ProteinsHumansPhosphorylationLeucine-Rich Repeat Serine-Threonine Protein Kinase-2LRRK2 protein, humanrab GTP-Binding ProteinsciliogenesisLRRK2lysosomeParkinson's diseasephosphorylation/dephosphorylationRab protein

Identifiers

PMID36929701
PMCPMC10212515
OpenAlexW4327682522

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.