Evidence map›Paper›PMID 39699947›Full record

ArticleeLife2024

Intramolecular feedback regulation of the LRRK2 Roc G domain by a LRRK2 kinase-dependent mechanism.

Bernd K Gilsbach, Franz Y Ho, Benjamin Riebenbauer, Xiaojuan Zhang, Giambattista Guaitoli, Arjan Kortholt, Christian Johannes Gloeckner

Abstract read
In one paragraph

Article in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. The structural basis for LRRK2's activation and autoinhibition.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. 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

7 authors.

Bernd K GilsbachGerman Center for Neurodegenerative diseases (DZNE), Tübingen, Germany.
Franz Y HoDepartment of Cell Biochemistry, University of Groningen, Groningen, Netherlands.
Benjamin RiebenbauerGerman Center for Neurodegenerative diseases (DZNE), Tübingen, Germany.
Xiaojuan ZhangDepartment of Cell Biochemistry, University of Groningen, Groningen, Netherlands.
Giambattista GuaitoliGerman Center for Neurodegenerative diseases (DZNE), Tübingen, Germany.
Arjan KortholtDepartment of Cell Biochemistry, University of Groningen, Groningen, Netherlands.ORCID https://orcid.org/0000-0001-8174-6397
Christian Johannes GloecknerGerman Center for Neurodegenerative diseases (DZNE), Tübingen, Germany.ORCID https://orcid.org/0000-0001-6494-6944

Funding

Michael J. Fox Foundation for Parkinson's Research 8068.04
6 · The paper itself

Abstract

The Parkinson's disease (PD)-linked protein Leucine-Rich Repeat Kinase 2 (LRRK2) consists of seven domains, including a kinase and a Roc G domain. Despite the availability of several high-resolution structures, the dynamic regulation of its unique intramolecular domain stack is nevertheless still not well understood. By in-depth biochemical analysis, assessing the Michaelis-Menten kinetics of the Roc G domain, we have confirmed that LRRK2 has, similar to other Roco protein family members, a K

Indexed as

Leucine-Rich Repeat Serine-Threonine Protein Kinase-2Feedback, PhysiologicalGuanosine TriphosphateHumansKineticsParkinson DiseasePhosphorylationProtein DomainsGuanosine TriphosphateLeucine-Rich Repeat Serine-Threonine Protein Kinase-2LRRK2 protein, humanbiochemistrychemical biologyGTPaseLRRK2Michaelis–Menten kineticsnegative feedback loopnoneparkinson's diseasePD

Identifiers

PMID39699947
PMCPMC11658767

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.