Evidence map›Paper›PMID 30662006›Full record

ArticleThe Journal of biological chemistry2019

Species-specific differences in nonlysosomal glucosylceramidase GBA2 function underlie locomotor dysfunction arising from loss-of-function mutations.

Marina A Woeste, Sina Stern, Diana N Raju, Elena Grahn, Dominik Dittmann, Katharina Gutbrod, Peter Dörmann, Jan N Hansen, Sophie Schonauer, Carina E Marx and 10 more

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
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  9. A novel mutation in theeNeurologicalSci · 2020
    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

20 authors at 6 institutions in 2 countries.

Marina A WoesteFrom the Institute of Innate Immunity, University Hospital, University of Bonn, 53127 Bonn, Germany.
Sina Sternthe German Center for Neurodegenerative Diseases (DZNE), 53127 Bonn, Germany.
Diana N RajuFrom the Institute of Innate Immunity, University Hospital, University of Bonn, 53127 Bonn, Germany.ORCID 0000-0002-0482-0941
Elena Grahnthe Center of Advanced European Studies and Research (Caesar), 53175 Bonn, Germany.
Dominik DittmannFrom the Institute of Innate Immunity, University Hospital, University of Bonn, 53127 Bonn, Germany.
Katharina Gutbrodthe Institute of Molecular Physiology and Biotechnology of Plants, University of Bonn, 53115 Bonn, Germany.
Peter Dörmannthe Institute of Molecular Physiology and Biotechnology of Plants, University of Bonn, 53115 Bonn, Germany.ORCID 0000-0002-5845-9370
Jan N HansenFrom the Institute of Innate Immunity, University Hospital, University of Bonn, 53127 Bonn, Germany.ORCID 0000-0002-0489-7535
Sophie Schonauerthe Center of Advanced European Studies and Research (Caesar), 53175 Bonn, Germany.
Carina E Marxthe Center of Advanced European Studies and Research (Caesar), 53175 Bonn, Germany.
Hussein Hamzehthe Center of Advanced European Studies and Research (Caesar), 53175 Bonn, Germany.
Heinz G Körschenthe Center of Advanced European Studies and Research (Caesar), 53175 Bonn, Germany.ORCID 0000-0003-3927-1433
Johannes M F G Aertsthe Leiden Institute of Chemistry, Leiden University, 2333 CD Leiden, The Netherlands.
Wolfgang Bönigkthe Center of Advanced European Studies and Research (Caesar), 53175 Bonn, Germany.
Heike Endepolsthe Institute of Radiochemistry and Experimental Molecular Imaging (IREMB) and Department of Nuclear Medicine, University Hospital of Cologne, 50937 Cologne, Germany.
Roger Sandhoffthe Department of Cellular and Molecular Pathology, German Cancer Research Center, Heidelberg, Germany.
Matthias Geyerthe Institute of Structural Biology, University Hospital, University of Bonn, 53127 Bonn, Germany.
Thomas K Bergerthe Center of Advanced European Studies and Research (Caesar), 53175 Bonn, Germany.
Frank Bradkethe German Center for Neurodegenerative Diseases (DZNE), 53127 Bonn, Germany.
Dagmar WachtenFrom the Institute of Innate Immunity, University Hospital, University of Bonn, 53127 Bonn, Germany, dwachten@uni-bonn.de.ORCID 0000-0003-4800-6332
University of Bonn · DECenter of Advanced European Studies and Research · DEGerman Center for Neurodegenerative Diseases · DEGerman Cancer Research Center · DELeiden University · NLUniversity of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nonlysosomal glucosylceramidase β2 (GBA2) catalyzes the hydrolysis of glucosylceramide to glucose and ceramide. Mutations in the human

Indexed as

Loss of Function MutationAnimalsbeta-GlucosidaseBiocatalysisCerebellar AtaxiaGlucosylceramidaseHumansLocomotionMiceMice, KnockoutSpastic Paraplegia, HereditarySpecies Specificitybeta-Glucosidasebeta-glucosidase 2, mouseGBA2 protein, humanGlucosylceramidaseactin cytoskeletonataxiacerebellar ataxiacytoskeletonGBA2glucosylceramideglycerosphingolipidneurite outgrowthneuroscienceβ-glucosidases

Identifiers

PMID30662006
PMCPMC6422076
OpenAlexW2908691738

What OpenQuestion holds

Textmetadata
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.