Evidence map›Paper›PMID 28323023›Full record

ReviewNeurobiology of disease2018

Internalization, axonal transport and release of fibrillar forms of alpha-synuclein.

Gregor Bieri, Aaron D Gitler, Michel Brahic

Open access · hybridAbstract readReview
In one paragraph

Review in Neurobiology of disease, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

69 citing papers in PubMed, 119 citations in OpenAlex.

  1. Review
  2. Structural Features of a Tiny Viral Protein, ORF7b of SARS-CoV-2.International journal of molecular sciences · 2026
    Article
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9 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Gregor BieriDepartment of Genetics, Stanford University School of Medicine, Stanford, CA 94305-5120, USA; Neurosciences Graduate Program, Stanford University School of Medicine, Stanford, CA 94305-5120, USA. Electronic address: gbieri@stanford.edu.
Aaron D GitlerDepartment of Genetics, Stanford University School of Medicine, Stanford, CA 94305-5120, USA.
Michel BrahicDepartment of Genetics, Stanford University School of Medicine, Stanford, CA 94305-5120, USA. Electronic address: mbrahic@stanford.edu.
Stanford University · US

Funding

Innovating Yeast and Human Genetics Approaches to Define Mechanisms of Neurodegenerative DiseaseR35NS097263 · NINDS · STANFORD UNIVERSITY · PI GITLER, AARON D. · 2017 to 2024
$8.6M
NINDS NIH HHS R35 NS097263
6 · The paper itself

Abstract

Intra-neuronal protein aggregates made of fibrillar alpha-synuclein (α-syn) are the hallmark of Parkinson's disease (PD). With time, these aggregates spread through the brain following axonal projections. Understanding the mechanism of this spread is central to the study of the progressive nature of PD. Here we review data relevant to the uptake, transport and release of α-syn fibrils. We summarize several cell surface receptors that regulate the uptake of α-syn fibrils by neurons. The aggregates are then transported along axons, both in the anterograde and retrograde direction. The kinetics of transport suggests that they are part of the slow component b of axonal transport. Recent findings indicate that aggregated α-syn is secreted by neurons by non-canonical pathways that may implicate various molecular chaperones including USP19 and the DnaJ/Hsc70 complex. Additionally, α-syn fibrils may also be released and transmitted from neuron-to-neuron via exosomes and tunneling nanotubes. Understanding these different mechanisms and molecular players underlying α-syn spread is crucial for the development of therapies that could halt the progression of α-syn-related degenerative diseases.

Indexed as

alpha-SynucleinAnimalsAxonal TransportHumansNeurodegenerative DiseasesNeuronsalpha-SynucleinAlpha-synucleinAxonal transportExosomeFibrilsParkinson's diseasePrionSpreadTunneling nanotubeUnconventional secretion

Identifiers

PMID28323023
PMCPMC5600643
OpenAlexW2596953817

What OpenQuestion holds

Textmetadata
LicenceTDM
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.