Evidence map›Paper›PMID 17932026›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2008

Rapid detection, discovery, and identification of post-translationally myristoylated proteins during apoptosis using a bio-orthogonal azidomyristate analog.

Dale D O Martin, Gonzalo L Vilas, Jennifer A Prescher, Gurram Rajaiah, John R Falck, Carolyn R Bertozzi, Luc G Berthiaume

Abstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

53 citing papers in PubMed, 109 citations in OpenAlex.

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  12. Bioorthogonal chemistry.Nature reviews. Methods primers · 2021
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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

7 authors at 3 institutions in 2 countries.

Dale D O MartinUniversity of Alberta, Department of Cell Biology, Edmonton, AB T6G 2H7, Canada.
Gonzalo L Vilas
Jennifer A Prescher
Gurram Rajaiah
John R Falck
Carolyn R Bertozzi
Luc G Berthiaume
University of Alberta · CAHoward Hughes Medical Institute · USThe University of Texas Southwestern Medical Center · US

Funding

Novel Eicosanoids: Synthesis and FunctionR01GM031278 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI FALCK, JOHN R. · 1985 to 2012
$4.7M
Howard Hughes Medical InstituteNIGMS NIH HHS GM31278NIGMS NIH HHS R01 GM031278
6 · The paper itself

Abstract

Myristoylation is the attachment of the 14-carbon fatty acid myristate to the N-terminal glycine residue of proteins. Typically a co-translational modification, myristoylation of proapoptotic cysteinyl-aspartyl proteases (caspase)-cleaved Bid and PAK2 was also shown to occur post-translationally and is essential for their proper localization and proapoptotic function. Progress in the identification and characterization of myristoylated proteins has been impeded by the long exposure times required to monitor incorporation of radioactive myristate into proteins (typically 1-3 months). Consequently, we developed a nonradioactive detection methodology in which a bio-orthogonal azidomyristate analog is specifically incorporated co- or post-translationally into proteins at N-terminal glycines, chemoselectively ligated to tagged triarylphosphines and detected by Western blotting with short exposure times (seconds to minutes). This represents over a million-fold signal amplification in comparison to using radioactive labeling methods. Using rational prediction analysis to recognize putative internal myristoylation sites in caspase-cleaved proteins combined with our nonradioactive chemical detection method, we identify 5 new post-translationally myristoylatable proteins (PKC epsilon, CD-IC2, Bap31, MST3, and the catalytic subunit of glutamate cysteine ligase). We also demonstrate that 15 proteins undergo post-translational myristoylation in apoptotic Jurkat T cells. This suggests that post-translational myristoylation of caspase-cleaved proteins represents a novel mechanism widely used to regulate cell death.

Indexed as

ApoptosisProtein Processing, Post-TranslationalAnimalsAzidesBlotting, WesternCell LineChemistry Techniques, AnalyticalChlorocebus aethiopsCOS CellsGlycineHumansJurkat CellsMyristic AcidsProteinsTime FactorsAzidesGlycineMyristic AcidsProteins

Identifiers

PMID17932026
PMCPMC2865240
OpenAlexW2024894588

What OpenQuestion holds

Textmetadata
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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.