Evidence map›Paper›PMID 26567273›Full record

ArticleThe Biochemical journal2015

Use of a mutant OGA for detecting O-GlcNAc modified proteins.

Robert J Chalkley

Abstract readComment
PubMed Publisher
In one paragraph

Article in The Biochemical journal, 2015. 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

5 · Who and what money

Authors and funding

1 author.

Robert J ChalkleyDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94143, U.S.A. chalkley@cgl.ucsf.edu.

Funding

Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
NIGMS NIH HHS 8P41GM103481
6 · The paper itself

Abstract

In the previous issue of Biochemical Journal Mariappa et al. [(2015) Biochem J. 470,: 255-262] demonstrate a new method for visualizing O-linked N-acetylglucosamine (O-GlcNAc) modified proteins by making use of a catalytically dead version of the enzyme that normally removes this modification. They show their approach has broader specificity than current antibody-based techniques and higher specificity than lectin and chemical biology-based labelling approaches. This commentary discusses methods for O-GlcNAc detection and the significance of this work for characterizing this common, but currently poorly understood regulatory modification.

Indexed as

AnimalsBacterial Proteinsbeta-N-AcetylhexosaminidasesDrosophilaHumansBacterial Proteinsbeta-N-Acetylhexosaminidasesglycosylationmass spectrometryOGAO-linked N-acetylglucosamine (O-GlcNAc)

Identifiers

PMID26567273

What OpenQuestion holds

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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.