Evidence map›Paper›PMID 30609797›Full record

ReviewInternational journal of molecular sciences2019

Roco Proteins: GTPases with a Baroque Structure and Mechanism.

Lina Wauters, Wim Versées, Arjan Kortholt

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Chemical Genetic Targeting of the LRRK2 GTPase Domain.bioRxiv : the preprint server for biology · 2026
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  9. Structure of LRRK1 and mechanisms of autoinhibition and activation.Nature structural & molecular biology · 2023
    Article
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  11. Exploring the focal role of LRRK2 kinase in Parkinson's disease.Environmental science and pollution research international · 2022
    Review
  12. Nanobodies as allosteric modulators of Parkinson's disease-associated LRRK2.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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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.

Lina WautersVIB-VUB Center for Structural Biology, Pleinlaan 2, B-1050 Brussels, Belgium. Lina.Wauters@vub.be.
Wim VerséesVIB-VUB Center for Structural Biology, Pleinlaan 2, B-1050 Brussels, Belgium. Wim.Versees@vub.be.
Arjan KortholtDepartment of Cell Biochemistry, University of Groningen, NL-9747 AG Groningen, The Netherlands. A.Kortholt@rug.nl.ORCID 0000-0001-8174-6397

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations in leucine-rich repeat kinase 2 (LRRK2) are a common cause of genetically inherited Parkinson's Disease (PD). LRRK2 is a large, multi-domain protein belonging to the Roco protein family, a family of GTPases characterized by a central RocCOR (Ras of complex proteins/C-terminal of Roc) domain tandem. Despite the progress in characterizing the GTPase function of Roco proteins, there is still an ongoing debate concerning the working mechanism of Roco proteins in general, and LRRK2 in particular. This review consists of two parts. First, an overview is given of the wide evolutionary range of Roco proteins, leading to a variety of physiological functions. The second part focusses on the GTPase function of the RocCOR domain tandem central to the action of all Roco proteins, and progress in the understanding of its structure and biochemistry is discussed and reviewed. Finally, based on the recent work of our and other labs, a new working hypothesis for the mechanism of Roco proteins is proposed.

Indexed as

AnimalsDictyosteliumEvolution, MolecularGTP-Binding ProteinsGTP PhosphohydrolasesLeucine-Rich Repeat Serine-Threonine Protein Kinase-2Parkinson DiseaseProtein DomainsProtein Structure, TertiaryGTP-Binding ProteinsGTP PhosphohydrolasesLeucine-Rich Repeat Serine-Threonine Protein Kinase-2GTPase mechanismleucine-rich repeat kinase 2Parkinson’s diseaseRoco proteinsunconventional G-protein

Identifiers

PMID30609797
PMCPMC6337361

What OpenQuestion holds

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Registered trials

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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.