Evidence map›Paper›PMID 18640077›Full record

ArticleNanomedicine : nanotechnology, biology, and medicine2008

Mechanism of alpha-synuclein oligomerization and membrane interaction: theoretical approach to unstructured proteins studies.

Igor F Tsigelny, Yuriy Sharikov, Mark A Miller, Eliezer Masliah

Abstract read
In one paragraph

Article in Nanomedicine : nanotechnology, biology, and medicine, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

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  14. The Contribution ofNeural plasticity · 2017
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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

4 authors.

Igor F TsigelnyDepartment of Chemistry and Biochemistry, University of California San Diego, La Jolla, California 92093-0444, USA. itsigeln@ucsd.edu
Yuriy Sharikov
Mark A Miller
Eliezer Masliah

Funding

Tissue Culture CoreP01AG022074 · NIA · J. DAVID GLADSTONE INSTITUTES · PI MASLIAH, ELIEZER · 2003 to 2012
$27.0M
B-Synuclein as a Treatment for Lewy Body DiseaseR01AG018440 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI RISSMAN, ROBERT · 2001 to 2021
$5.2M
a-synuclein clearance strategies for the treatment of Lewy body disease.R37AG018440 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI MASLIAH, ELIEZER · 2006 to 2014
$2.7M
NIA NIH HHS AG02074,NIA NIH HHS AG18440NIA NIH HHS P01 AG022074NIA NIH HHS R01 AG018440NIA NIH HHS R37 AG018440
6 · The paper itself

Abstract

Misfolding and oligomerization of unstructured proteins is involved in the pathogenesis of Parkinson's disease (PD), Alzheimer's disease, Huntington's disease, and other neurodegenerative disorders. Elucidation of possible conformations of these proteins and their interactions with the membrane is necessary to understand the molecular mechanisms of neurodegeneration. We developed a strategy that makes it possible to elucidate the molecular mechanisms of alpha-synuclein aggregation-a key molecular event in the pathogenesis of PD. This strategy can be also useful for the study of other unstructured proteins involved in neurodegeneration. The results of these theoretical studies have been confirmed with biochemical and electrophysiological studies. Our studies provide insights into the molecular mechanism for PD initiation and progression, and provide a useful paradigm for identifying possible therapeutic interventions through computational modeling.

Indexed as

Computer Simulationalpha-SynucleinCell MembraneDimerizationModels, MolecularParkinson DiseaseProtein BindingProtein ConformationProtein Structure, Secondaryalpha-Synuclein

Identifiers

PMID18640077
PMCPMC2627560

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.