Evidence map›Paper›PMID 24486885›Full record

ArticleNeuroscience letters2014

Transgenic mice expressing S129 phosphorylation mutations in α-synuclein.

Valerie Drews Escobar, Yien-Ming Kuo, Bonnie M Orrison, Benoit I Giasson, Robert L Nussbaum

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

Article in Neuroscience letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

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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

5 authors at 3 institutions in 1 country.

Valerie Drews EscobarDepartment of Medicine, University of California San Francisco, San Francisco, CA 94143, USA; Institute for Human Genetics, University of California San Francisco, San Francisco, CA 94143, USA.
Yien-Ming KuoDepartment of Medicine, University of California San Francisco, San Francisco, CA 94143, USA; Institute for Human Genetics, University of California San Francisco, San Francisco, CA 94143, USA.
Bonnie M OrrisonGenetic Disease Research Branch, NHGRI, National Institutes of Health, Bethesda, MD 20892, USA.
Benoit I GiassonDepartment of Pharmacology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
Robert L NussbaumDepartment of Medicine, University of California San Francisco, San Francisco, CA 94143, USA; Institute for Human Genetics, University of California San Francisco, San Francisco, CA 94143, USA. Electronic address: nussbaumr@humgen.ucsf.edu.
University of California, San Francisco · USNational Human Genome Research Institute · USUniversity of Pennsylvania · US

Funding

Project IV: "Alpha-Synuclein Strains & Diverse Synucleinopathies"P50NS053488 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI TROJANOWSKI, JOHN Q. · 2007 to 2017
$20.9M
Intramural NIH HHS Z99 LM999999NINDS NIH HHS NS053488NINDS NIH HHS P50 NS053488
6 · The paper itself

Abstract

Aggregated α-synuclein is a predominant constituent of Lewy bodies, the intracellular protein aggregates seen in Parkinson's disease. While most α-synuclein in the nervous system is unphosphorylated, the majority of α-synuclein in Lewy bodies is phosphorylated at serine 129 (S129). We developed transgenic mice expressing human SNCA with either a phosphomimic (S129D) or a non-phosphorylatable (S129A) mutation, on a mouse Snca knockout background. Transgenic lines with each mutation expressing the human α-synuclein protein at levels ranging from 0.3 to 1.9 fold of endogenous mouse protein were chosen to avoid toxic overexpression effects. We previously demonstrated an altered distribution of presynaptic vesicles in Snca knockout mice, as well as enhanced interaction between presynaptic cytoskeletal proteins and α-synuclein when phosphorylated at S129 or carrying an S129D mutation. We therefore examined α-synuclein's synaptic localization and the distribution of presynaptic vesicles in these mutants. In addition, we evaluated the transgenic lines for reduced colonic motility, an early marker of α-synuclein pathology, and α-synuclein aggregates. No abnormalities were detected in mice expressing either phosphorylation mutant protein as their only α-synuclein protein. These results suggest the S129A and S129D mutations have no obvious effect on α-synuclein function.

Indexed as

alpha-SynucleinAnimalsBrainCells, CulturedColonEnteric Nervous SystemFemaleGastrointestinal MotilityHumansLewy BodiesMaleMice, TransgenicMutationNeuronsPhosphorylationSynapsesalpha-SynucleinLewy bodiesParkinson's diseasePhosphorylationTransgenicα-synuclein

Identifiers

PMID24486885
PMCPMC4059511
OpenAlexW2051781586

What OpenQuestion holds

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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.