Evidence map›Paper›PMID 21300897›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.

Michael Boyce, Isaac S Carrico, Anjali S Ganguli, Seok-Ho Yu, Matthew J Hangauer, Sarah C Hubbard, Jennifer J Kohler, Carolyn R Bertozzi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
175citing papers in PubMed, 1 pooled it
9.2field-weighted citation impact, top 1% 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

175 citing papers in PubMed, 1 synthesis or guideline pooled it, 347 citations in OpenAlex.

  1. Pooled it
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  13. Testing cellular provenance in the cancer extracellular matrix.Frontiers in cell and developmental biology · 2026
    Review
  14. Article
  15. Review
  16. O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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115 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Michael BoyceDepartments of Chemistry and Molecular and Cell Biology and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA.
Isaac S Carrico
Anjali S Ganguli
Seok-Ho Yu
Matthew J Hangauer
Sarah C Hubbard
Jennifer J Kohler
Carolyn R Bertozzi
University of California, Berkeley · USThe University of Texas Southwestern Medical Center · USUniversity of California, San Francisco · US

Funding

Studies of Protein GlycosylationR01GM066047 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERTOZZI, CAROLYN · 2002 to 2014
$3.8M
Glycomics with Staudinger activated fluorogenic dyesF32GM069157 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CARRICO, ISAAC S · 2003 to 2006
$124k
Howard Hughes Medical InstituteNCI NIH HHS PC080659NIGMS NIH HHS F32 GM069157NIGMS NIH HHS GM066047NIGMS NIH HHS GM069157NIGMS NIH HHS R01 GM066047
6 · The paper itself

Abstract

Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability. Despite its broad functional significance, the dynamic and posttranslational nature of O-GlcNAc signaling makes it challenging to study using traditional molecular and cell biological techniques alone. Here, we report that metabolic cross-talk between the N-acetylgalactosamine salvage and O-GlcNAcylation pathways can be exploited for the tagging and identification of O-GlcNAcylated proteins. We found that N-azidoacetylgalactosamine (GalNAz) is converted by endogenous mammalian biosynthetic enzymes to UDP-GalNAz and then epimerized to UDP-N-azidoacetylglucosamine (GlcNAz). O-GlcNAc transferase accepts UDP-GlcNAz as a nucleotide-sugar donor, appending an azidosugar onto its native substrates, which can then be detected by covalent labeling using azide-reactive chemical probes. In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins. Our work provides a blueprint for a wide variety of future chemical approaches to identify, visualize, and characterize dynamic O-GlcNAc signaling.

Indexed as

Affinity LabelsMetabolic Networks and PathwaysReceptor Cross-TalkAcetylgalactosamineAcetylglucosamineCell LineChromatography, AffinityGlycosylationHumansMethodsProtein Processing, Post-TranslationalAcetylgalactosamineAcetylglucosamineAffinity Labels

Identifiers

PMID21300897
PMCPMC3044403
OpenAlexW2059725389

What OpenQuestion holds

Textmetadata
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.