Evidence map›Paper›PMID 35305898›Full record

ReviewTrends in biochemical sciences2022

Seeing the forest through the trees: characterizing the glycoproteome.

Meg Critcher, Abdullah A Hassan, Mia L Huang

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. 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
  3. Ocular surface glycocalyx in health and disease.Frontiers in cell and developmental biology · 2025
    Review
  4. Article
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  8. 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

3 authors at 1 institution in 1 country.

Meg CritcherSkaggs Graduate School of Chemical and Biological Sciences, Scripps Research, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA; Department of Molecular Medicine, Scripps Research, 120 Scripps Way, Jupiter, FL 33458, USA; Department of Molecular Medicine, Scripps Research, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA.
Abdullah A HassanDepartment of Molecular Medicine, Scripps Research, 120 Scripps Way, Jupiter, FL 33458, USA; Department of Molecular Medicine, Scripps Research, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA.
Mia L HuangSkaggs Graduate School of Chemical and Biological Sciences, Scripps Research, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA; Department of Molecular Medicine, Scripps Research, 120 Scripps Way, Jupiter, FL 33458, USA; Department of Molecular Medicine, Scripps Research, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA; Department of Chemistry, Scripps Research, 120 Scripps Way, Jupiter, FL 33458, USA. Electronic address: miahuang@scripps.edu.
Scripps Research Institute · US

Funding

Bridging the Glycome and Proteome with Chemical BiologyR35GM142462 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI Mia L Huang · 2021 to 2026
$2.9M
NIGMS NIH HHS R35 GM142462
6 · The paper itself

Abstract

Post-translational modifications (PTMs) immensely expand the diversity of the proteome. Glycosylation, among the most ubiquitous PTMs, is a dynamic and multifarious modification of proteins and lipids that generates an omnipresent foliage on the cell surface. The resulting protein glycoconjugates can serve important functions in biology. However, their vast complexity complicates the study of their structures, interactions, and functions. There is now a growing appreciation of the need to study glycans and proteins together as complete entities, as the sum of these two components can exhibit unique functions. In this review, we discuss the growing forestry toolbox to characterize the structure, interactions, and biological functions of protein glycoconjugates, as well as the potential payouts of understanding and controlling these enigmatic biomolecules.

Indexed as

ProteomeProteomicsGlycoconjugatesGlycosylationProtein Processing, Post-TranslationalGlycoconjugatesProteomeglycobiologyglycoconjugatesglycoproteomicsglycosylation

Identifiers

PMID35305898
PMCPMC12604481
OpenAlexW4220947270

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.