Evidence map›Paper›PMID 28131823›Full record

ArticleCell systems2017

In Situ Peroxidase Labeling and Mass-Spectrometry Connects Alpha-Synuclein Directly to Endocytic Trafficking and mRNA Metabolism in Neurons.

Chee Yeun Chung, Vikram Khurana, Song Yi, Nidhi Sahni, Ken H Loh, Pavan K Auluck, Valeriya Baru, Namrata D Udeshi, Yelena Freyzon, Steven A Carr and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell systems, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

83 citing papers in PubMed, 125 citations in OpenAlex.

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23 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 7 institutions in 1 country.

Chee Yeun ChungWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA. Electronic address: cychung@yumanity.com.
Vikram KhuranaWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA; Ann Romney Center for Neurologic Disease, Department of Neurology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA; Harvard Stem Cell Institute, Cambridge, MA 02138, USA. Electronic address: vkhurana@bwh.harvard.edu.
Song YiCenter for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215; Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.
Nidhi SahniCenter for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215; Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.
Ken H LohDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.
Pavan K AuluckWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
Valeriya BaruWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
Namrata D UdeshiThe Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA.
Yelena FreyzonWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
Steven A CarrThe Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA.
David E HillCenter for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215; Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.
Marc VidalCenter for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215; Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.
Alice Y TingDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.
Susan LindquistWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Howard Hughes Medical Institute, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Whitehead Institute for Biomedical Research · USBroad Institute · USDana-Farber Cancer Institute · USHarvard University · USMassachusetts Institute of Technology · USBrigham and Women's Hospital · USHoward Hughes Medical Institute · US

Funding

The C. elegans Interactome ProjectR01HG001715 · NHGRI · MASSACHUSETTS GENERAL HOSPITAL · PI HILL, DAVID E., ROTH, FREDERICK P · 1998 to 2010
$16.5M
Mapping the first half of the REFERENCE human binary protein interactomeU01HG001715 · NHGRI · DANA-FARBER CANCER INST · PI HILL, DAVID E., ROTH, FREDERICK P · 2012 to 2014
$5.4M
Resource ProjectU41HG001715 · NHGRI · DANA-FARBER CANCER INST · PI HILL, DAVID E. · 2015 to 2017
$4.7M
Elucidating the Biological Differences Between Distinct Fibrillar and Non-Fibrillar Alpha-Synuclein Inclusions in Human Stem-Cell ModelsR01NS109209 · NINDS · BRIGHAM AND WOMEN'S HOSPITAL · PI KHURANA, VIKRAM · 2020 to 2024
$4.5M
Structure-Based Prediction of the InteractomeR01GM081871 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BERGER, BONNIE · 2008 to 2020
$4.3M
Embryonal Brain Tumor NetworksU01CA184898 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI FRAENKEL, ERNEST, MESIROV, JILL P. · 2014 to 2019
$3.6M
A Systems Biology Approach to Reveal Huntington's Disease MechanismsR01GM089903 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI FRAENKEL, ERNEST · 2010 to 2014
$2.4M
Molecular Dissection of Synucleinopathies Using Yeast, Rodent and Human iPS CellsK01AG038546 · NIA · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI CHUNG, CHEE YEUN · 2011 to 2014
$530k
Howard Hughes Medical InstituteNCI NIH HHS U01 CA184898NHGRI NIH HHS R01 HG001715NHGRI NIH HHS U01 HG001715NHGRI NIH HHS U41 HG001715NIA NIH HHS K01 AG038546NIGMS NIH HHS R01 GM081871NIGMS NIH HHS R01 GM089903NINDS NIH HHS R01 NS109209
6 · The paper itself

Abstract

Synucleinopathies, including Parkinson's disease (PD), are associated with the misfolding and mistrafficking of alpha-synuclein (α-syn). Here, using an ascorbate peroxidase (APEX)-based labeling method combined with mass spectrometry, we defined a network of proteins in the immediate vicinity of α-syn in living neurons to shed light on α-syn function. This approach identified 225 proteins, including synaptic proteins, proteins involved in endocytic vesicle trafficking, the retromer complex, phosphatases and mRNA binding proteins. Many were in complexes with α-syn, and some were encoded by genes known to be risk factors for PD and other neurodegenerative diseases. Endocytic trafficking and mRNA translation proteins within this spatial α-syn map overlapped with genetic modifiers of α-syn toxicity, developed in an accompanying study (Khurana et al., this issue of Cell Systems). Our data suggest that perturbation of these particular pathways is directly related to the spatial localization of α-syn within the cell. These approaches provide new avenues to systematically examine protein function and pathology in living cells.

Indexed as

alpha-SynucleinAnimalsAscorbate PeroxidasesCells, CulturedHEK293 CellsHumansHydrogen PeroxideMass SpectrometryNeuronsParkinson DiseaseProtein TransportRatsRNA, Messengeralpha-SynucleinAscorbate PeroxidasesHydrogen PeroxideRNA, Messenger

Identifiers

PMID28131823
PMCPMC5578869
OpenAlexW2582852527

What OpenQuestion holds

Textmetadata
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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.