Evidence map›Paper›PMID 34328508›Full record

ArticleThe Biochemical journal2021

From structure to ætiology: a new window on the biology of leucine-rich repeat kinase 2 and Parkinson's disease.

Susanne Herbst, Patrick A Lewis

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

Article in The Biochemical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 34% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

2 authors at 1 institution in 2 countries.

Susanne HerbstDepartment of Comparative Biomedical Science, Royal Veterinary College, Royal College Street, London, U.K.
Patrick A LewisDepartment of Comparative Biomedical Science, Royal Veterinary College, Royal College Street, London, U.K.ORCID 0000-0003-4537-0489
Royal Veterinary College · GB

Funding

Medical Research Council G0701075Medical Research Council G0901254Medical Research Council MR/N026004/1
6 · The paper itself

Abstract

Since the discovery of mutations in leucine-rich repeat kinase 2 (LRRK2) as an underlying genetic cause for the development of Parkinson's disease (PD) in 2004 (Neuron 44, 601-607; Neuron 44, 595-600), and subsequent efforts to develop LRRK2 kinase inhibitors as a therapy for Parkinson's (Expert Opin. Ther. Targets 21, 751-753), elucidating the atomic resolution structure of LRRK2 has been a major goal of research into this protein. At over 250 kDa, the large size and complicated domain organisation of LRRK2 has made this a highly challenging target for structural biologists, however, a number of recent studies using both in vitro and in situ approaches (Nature 588, 344-349; Cell 182, 1508-1518.e1516; Cell 184, 3519-3527.e3510) have provided important new insights into LRRK2 structure and the complexes formed by this protein.

Indexed as

MutationBiocatalysisCryoelectron MicroscopyCrystallography, X-RayGenetic Predisposition to DiseaseHumansLeucine-Rich Repeat Serine-Threonine Protein Kinase-2Models, MolecularParkinson DiseaseProtein DomainsProtein Kinase InhibitorsProtein MultimerizationSignal TransductionTime FactorsLeucine-Rich Repeat Serine-Threonine Protein Kinase-2Protein Kinase Inhibitorsleucine-rich repeat kinaseneurodegenerationParkinson's disease

Identifiers

PMID34328508
PMCPMC8331089
OpenAlexW3184877446

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.