Evidence map›Paper›PMID 26308446›Full record

ArticlePloS one2015

Identification of Human N-Myristoylated Proteins from Human Complementary DNA Resources by Cell-Free and Cellular Metabolic Labeling Analyses.

Emi Takamitsu, Motoaki Otsuka, Tatsuki Haebara, Manami Yano, Kanako Matsuzaki, Hirotsugu Kobuchi, Koko Moriya, Toshihiko Utsumi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
0.6field-weighted citation impact, top 31% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

  1. Pooled it
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  9. Posttranslational modifications in proteins: resources, tools and prediction methods.Database : the journal of biological databases and curation · 2021
    Article
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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

8 authors at 2 institutions in 1 country.

Emi TakamitsuApplied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, Yamaguchi, 753-8515, Japan.
Motoaki OtsukaApplied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, Yamaguchi, 753-8515, Japan.
Tatsuki HaebaraApplied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, Yamaguchi, 753-8515, Japan.
Manami YanoApplied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, Yamaguchi, 753-8515, Japan.
Kanako MatsuzakiApplied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, Yamaguchi, 753-8515, Japan.
Hirotsugu KobuchiDepartment of Cell Chemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama, 700-8558, Japan.
Koko MoriyaApplied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, Yamaguchi, 753-8515, Japan.
Toshihiko UtsumiApplied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, Yamaguchi, 753-8515, Japan; Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi, 753-8515, Japan.
Yamaguchi University · JPOkayama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To identify physiologically important human N-myristoylated proteins, 90 cDNA clones predicted to encode human N-myristoylated proteins were selected from a human cDNA resource (4,369 Kazusa ORFeome project human cDNA clones) by two bioinformatic N-myristoylation prediction systems, NMT-The MYR Predictor and Myristoylator. After database searches to exclude known human N-myristoylated proteins, 37 cDNA clones were selected as potential human N-myristoylated proteins. The susceptibility of these cDNA clones to protein N-myristoylation was first evaluated using fusion proteins in which the N-terminal ten amino acid residues were fused to an epitope-tagged model protein. Then, protein N-myristoylation of the gene products of full-length cDNAs was evaluated by metabolic labeling experiments both in an insect cell-free protein synthesis system and in transfected human cells. As a result, the products of 13 cDNA clones (FBXL7, PPM1B, SAMM50, PLEKHN, AIFM3, C22orf42, STK32A, FAM131C, DRICH1, MCC1, HID1, P2RX5, STK32B) were found to be human N-myristoylated proteins. Analysis of the role of protein N-myristoylation on the intracellular localization of SAMM50, a mitochondrial outer membrane protein, revealed that protein N-myristoylation was required for proper targeting of SAMM50 to mitochondria. Thus, the strategy used in this study is useful for the identification of physiologically important human N-myristoylated proteins from human cDNA resources.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsCell-Free SystemChlorocebus aethiopsCOS CellsDNA, ComplementaryHEK293 CellsHumansMembrane ProteinsMicroscopy, FluorescenceMitochondriaMolecular Sequence DataMyristic AcidProtein BiosynthesisSequence Homology, Amino AcidDNA, ComplementaryMembrane ProteinsMyristic Acid

Identifiers

PMID26308446
PMCPMC4550359
OpenAlexW1930371700

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.