Evidence map›Paper›PMID 27960262›Full record

ReviewChemical reviews2016

Chemical Glycoproteomics.

Krishnan K Palaniappan, Carolyn R Bertozzi

Abstract readReview
In one paragraph

Review in Chemical reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
13.1field-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

98 citing papers in PubMed, 283 citations in OpenAlex.

  1. Bifunctional Monosaccharides Preferentially Localize to Nuclear Subcompartments.Chembiochem : a European journal of chemical biology · 2026
    Article
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  5. Review
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  12. Photoionization of pyrenemethylamine-labeled oligosaccharides: a new MALDI-TOF precursor ion-type for efficient fragmentation.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Immunometabolic Maladaptations to the Tumor Microenvironment.Cold Spring Harbor perspectives in medicine · 2024
    Review
  19. Exploring serumHeliyon · 2024
    Article
  20. Article

38 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

2 authors.

Krishnan K PalaniappanVerily Life Sciences , 269 East Grand Ave., South San Francisco, California 94080, United States.
Carolyn R Bertozzi

Funding

Studies of Protein GlycosylationR01GM066047 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERTOZZI, CAROLYN · 2002 to 2014
$3.8M
Investigating the Surface GlycoproteomeR01CA200423 · NCI · STANFORD UNIVERSITY · PI Carolyn Bertozzi · 2015 to 2026
$3.8M
Howard Hughes Medical InstituteNCI NIH HHS R01 CA200423NIGMS NIH HHS R01 GM066047
6 · The paper itself

Abstract

Chemical tools have accelerated progress in glycoscience, reducing experimental barriers to studying protein glycosylation, the most widespread and complex form of posttranslational modification. For example, chemical glycoproteomics technologies have enabled the identification of specific glycosylation sites and glycan structures that modulate protein function in a number of biological processes. This field is now entering a stage of logarithmic growth, during which chemical innovations combined with mass spectrometry advances could make it possible to fully characterize the human glycoproteome. In this review, we describe the important role that chemical glycoproteomics methods are playing in such efforts. We summarize developments in four key areas: enrichment of glycoproteins and glycopeptides from complex mixtures, emphasizing methods that exploit unique chemical properties of glycans or introduce unnatural functional groups through metabolic labeling and chemoenzymatic tagging; identification of sites of protein glycosylation; targeted glycoproteomics; and functional glycoproteomics, with a focus on probing interactions between glycoproteins and glycan-binding proteins. Our goal with this survey is to provide a foundation on which continued technological advancements can be made to promote further explorations of protein glycosylation.

Indexed as

ProteomicsCarbohydratesGlycoproteinsGlycosylationHumansJurkat CellsMass SpectrometryOxidation-ReductionCarbohydratesGlycoproteins

Identifiers

PMID27960262
PMCPMC5327817
OpenAlexW4210808563

What OpenQuestion holds

Textmetadata
LicenceTDM
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.