Evidence map›Paper›PMID 28238724›Full record

ArticleCell chemical biology2017

Proximity Biotinylation as a Method for Mapping Proteins Associated with mtDNA in Living Cells.

Shuo Han, Namrata D Udeshi, Thomas J Deerinck, Tanya Svinkina, Mark H Ellisman, Steven A Carr, Alice Y Ting

Open access · bronzeAbstract read
In one paragraph

Article in Cell chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
8.1field-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

86 citing papers in PubMed, 128 citations in OpenAlex.

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  6. Cooperative Architecture of Mitochondrial Proteome Homeostasis.medRxiv : the preprint server for health sciences · 2026
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26 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Shuo HanDepartments of Genetics, Biology, and Chemistry, Stanford University, Stanford, CA 94305, USA.
Namrata D UdeshiBroad Institute of MIT and Harvard, Cambridge, MA 02142, USA.
Thomas J DeerinckNational Center for Microscopy and Imaging Research, University of California at San Diego, La Jolla, CA 92093, USA.
Tanya SvinkinaBroad Institute of MIT and Harvard, Cambridge, MA 02142, USA.
Mark H EllismanNational Center for Microscopy and Imaging Research, University of California at San Diego, La Jolla, CA 92093, USA.
Steven A CarrBroad Institute of MIT and Harvard, Cambridge, MA 02142, USA.
Alice Y TingDepartments of Genetics, Biology, and Chemistry, Stanford University, Stanford, CA 94305, USA. Electronic address: ayting@stanford.edu.
Broad Institute · USStanford University · USUniversity of California, San Diego · US

Funding

IVEM and Image Analysis ResourceP41GM103412 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ELLISMAN, MARK H · 2012 to 2019
$17.9M
New Probe and Methods for Correlated LM & EMR01GM086197 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ADAMS, STEPHEN ROY, BOASSA, DANIELA · 2008 to 2020
$8.3M
Spatially-resolved proteomic mapping of living cellsR01CA186568 · NCI · STANFORD UNIVERSITY · PI TING, ALICE Y · 2013 to 2018
$3.3M
NCI NIH HHS R01 CA186568NIGMS NIH HHS P41 GM103412NIGMS NIH HHS R01 GM086197
6 · The paper itself

Abstract

A recurring challenge in cell biology is to define the molecular components of macromolecular complexes of interest. The predominant method, immunoprecipitation, recovers only strong interaction partners that survive cell lysis and repeated detergent washes. We explored peroxidase-catalyzed proximity biotinylation, APEX, as an alternative, focusing on the mitochondrial nucleoid, the dynamic macromolecular complex that houses the mitochondrial genome. Via 1-min live-cell biotinylation followed by quantitative, ratiometric mass spectrometry, we enriched 37 nucleoid proteins, seven of which had never previously been associated with the nucleoid. The specificity of our dataset was very high, and we validated three hits by follow-up studies. For one novel nucleoid-associated protein, FASTKD1, we discovered a role in downregulation of mitochondrial complex I via specific repression of ND3 mRNA. Our study demonstrates that APEX is a powerful tool for mapping macromolecular complexes in living cells, and can identify proteins and pathways that have been missed by traditional approaches.

Indexed as

BiocatalysisBiotinylationDNA, MitochondrialElectron Transport Complex IHEK293 CellsHumansImmunoprecipitationMicroscopy, ElectronMicroscopy, FluorescenceMitochondriaMitochondrial ProteinsPeroxidaseRNA-Binding ProteinsRNA InterferenceRNA, Small InterferingDNA, MitochondrialElectron Transport Complex IFASTKD1 protein, humanMitochondrial ProteinsMT-ND3 protein, humanPeroxidaseRNA-Binding ProteinsRNA, Small InterferingAPEXAPEX2FASTKD1mappingmass spectrometrymitochondrianucleoidoxphosperoxidaseproteomics

Identifiers

PMID28238724
PMCPMC5886301
OpenAlexW2589155917

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.