Evidence map›Paper›PMID 31048377›Full record

ArticleThe Journal of biological chemistry2019

E46K-like α-synuclein mutants increase lipid interactions and disrupt membrane selectivity.

Matteo Rovere, Alex E Powers, Haiyang Jiang, Julia C Pitino, Luis Fonseca-Ornelas, Dushyant S Patel, Alessandro Achille, Ralf Langen, Jobin Varkey, Tim Bartels

Open access · hybridAbstract read
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 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Parkinson disease is a fatty acidopathy.Nature reviews. Neurology · 2025
    Review
  3. Article
  4. Glaucomatous retinal ganglion cells: death and protection.International journal of ophthalmology · 2025
    Review
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  17. Pathogenic Mechanisms of Cytosolic and Membrane-Enriched α-Synuclein Converge on Fatty Acid Homeostasis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 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

10 authors at 3 institutions in 2 countries.

Matteo RovereFrom the Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115.ORCID 0000-0002-3260-4955
Alex E PowersFrom the Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115.ORCID 0000-0002-0732-3780
Haiyang JiangFrom the Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115.
Julia C PitinoFrom the Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115.
Luis Fonseca-OrnelasFrom the Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115.
Dushyant S PatelFrom the Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115.
Alessandro Achillethe Department of Computer Science, University of California, Los Angeles, California 90095.
Ralf Langenthe Zilkha Neurogenetic Institute, University of Southern California, Los Angeles, California 90033, and.
Jobin Varkeythe Zilkha Neurogenetic Institute, University of Southern California, Los Angeles, California 90033, and.
Tim BartelsFrom the Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, t.bartels@ucl.ac.uk.
Brigham and Women's Hospital · USUniversity of Southern California · USUniversity of California, Los Angeles · US

Funding

Molecular mechanisms of huntingtin misfoldingR01NS084345 · NINDS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LANGEN, RALF · 2015 to 2019
$2.2M
Membrane remodeling by alpha-synuclein: implications for function and diseaseR01GM115736 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LANGEN, RALF · 2015 to 2018
$1.3M
Pathological Changes of Alpha-Synuclein Structure in the BrainR21NS104576 · NINDS · BRIGHAM AND WOMEN'S HOSPITAL · PI SELKOE, DENNIS J · 2018 to 2019
$492k
NIGMS NIH HHS R01 GM115736NINDS NIH HHS R01 NS084345NINDS NIH HHS R21 NS104576
6 · The paper itself

Abstract

Parkinson's disease (PD) is one of the most common neurodegenerative disorders, and both genetic and histopathological evidence have implicated the ubiquitous presynaptic protein α-synuclein (αSyn) in its pathogenesis. Recent work has investigated how disrupting αSyn's interaction with membranes triggers trafficking defects, cellular stress, and apoptosis. Special interest has been devoted to a series of mutants exacerbating the effects of the E46K mutation (associated with autosomal dominant PD) through homologous Glu-to-Lys substitutions in αSyn's N-terminal region (

Indexed as

Mutationalpha-SynucleinCell MembraneGlutamic AcidHumansLipidsLysineMutant Proteinsalpha-SynucleinGlutamic AcidLipidsLysineMutant Proteins11/3 helixCDintrinsically disordered proteinisothermal titration calorimetry (ITC)large unilamellar vesicleneurodegenerationParkinson diseaseprotein–lipid interactionsmall unilamellar vesicleα-synuclein

Identifiers

PMID31048377
PMCPMC6597829
OpenAlexW2943672274

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.