Evidence map›Paper›PMID 29454998›Full record

ArticleThe Journal of nutritional biochemistry2018

A cell death assay for assessing the mitochondrial targeting of proteins.

Daniel Camara Teixeira, Elizabeth L Cordonier, Subhashinee S K Wijeratne, Patricia Huebbe, Augusta Jamin, Sarah Jarecke, Matthew Wiebe, Janos Zempleni

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of nutritional biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Daniel Camara TeixeiraDepartment of Nutrition and Health Sciences, University of Nebraska-Lincoln, 316C Leverton Hall, Lincoln, NE 68583-0806, USA.
Elizabeth L CordonierDepartment of Nutrition and Health Sciences, University of Nebraska-Lincoln, 316C Leverton Hall, Lincoln, NE 68583-0806, USA.
Subhashinee S K WijeratneDepartment of Nutrition and Health Sciences, University of Nebraska-Lincoln, 316C Leverton Hall, Lincoln, NE 68583-0806, USA.
Patricia HuebbeDepartment of Nutrition and Health Sciences, University of Nebraska-Lincoln, 316C Leverton Hall, Lincoln, NE 68583-0806, USA.
Augusta JaminSchool of Veterinary Medicine and Biomedical Sciences, Nebraska Center for Virology, University of Nebraska-Lincoln, Ken Morrison Life Sciences Research Center, Rm 139, 4240 Fair Street, Lincoln, NE 68583-0900, USA.
Sarah JareckeDepartment of Nutrition and Health Sciences, University of Nebraska-Lincoln, 316C Leverton Hall, Lincoln, NE 68583-0806, USA.
Matthew WiebeSchool of Veterinary Medicine and Biomedical Sciences, Nebraska Center for Virology, University of Nebraska-Lincoln, Ken Morrison Life Sciences Research Center, Rm 139, 4240 Fair Street, Lincoln, NE 68583-0900, USA.
Janos ZempleniDepartment of Nutrition and Health Sciences, University of Nebraska-Lincoln, 316C Leverton Hall, Lincoln, NE 68583-0806, USA. Electronic address: jzempleni2@unl.edu.

Funding

The role of stress in the fetal origin of obesity and metabolic dysfunctionP20GM104320 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI ZEMPLENI, JANOS · 2014 to 2024
$24.9M
Vitamin-dependent modifications of histonesR01DK063945 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI ZEMPLENI, JANOS · 2004 to 2011
$2.3M
Essential role of biotin in cell proliferationR01DK060447 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI ZEMPLENI, JANOS · 2001 to 2004
$605k
NIDDK NIH HHS R01 DK060447NIDDK NIH HHS R01 DK063945NIGMS NIH HHS P20 GM104320
6 · The paper itself

Abstract

The mitochondrial proteome comprises 1000 to 1500 proteins, in addition to proteins for which the mitochondrial localization is uncertain. About 800 diseases have been linked with mutations in mitochondrial proteins. We devised a cell survival assay for assessing the mitochondrial localization in a high-throughput format. This protocol allows us to assess the mitochondrial localization of proteins and their mutants, and to identify drugs and nutrients that modulate the mitochondrial targeting of proteins. The assay works equally well for proteins directed to the outer mitochondrial membrane, inner mitochondrial membrane mitochondrial and mitochondrial matrix, as demonstrated by assessing the mitochondrial targeting of the following proteins: carnitine palmitoyl transferase 1 (consensus sequence and R123C mutant), acetyl-CoA carboxylase 2, uncoupling protein 1 and holocarboxylase synthetase. Our screen may be useful for linking the mitochondrial proteome with rare diseases and for devising drug- and nutrition-based strategies for altering the mitochondrial targeting of proteins.

Indexed as

Cell DeathCytological TechniquesProteomeCell SurvivalHEK293 CellsHumansMicroscopy, ConfocalMitochondriaMitochondrial ProteinsMutationProteomicsXenobioticsMitochondrial ProteinsProteomeXenobiotics3-chlorogenic acidAcetyl-CoA carboxylaseHigh-throughput screenMitochondriaProteome

Identifiers

PMID29454998
PMCPMC5971163

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.