Evidence map›Paper›PMID 31202133›Full record

ReviewCurrent opinion in virology2019

Glycosylation of viral surface proteins probed by mass spectrometry.

Audra A Hargett, Matthew B Renfrow

Abstract readReview
In one paragraph

Review in Current opinion in virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. State-of-the-Art Glycomics Technologies in Glycobiotechnology.Advances in biochemical engineering/biotechnology · 2021
    Article
  20. The Importance of Glycosylation in COVID-19 Infection.Advances in experimental medicine and biology · 2021
    Article
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.

Audra A HargettDepartment of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Matthew B RenfrowDepartment of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL 35294, USA. Electronic address: renfrow@uab.edu.

Funding

ZINC DIETARY ALTERATIONS OF CADMIUM INDUCED HEPATIC TOXICITY IN RATSS06GM008111 · NIGMS · FLORIDA AGRICULTURAL AND MECHANICAL UNIV · PI REAMS, ROMONIA RENEE · 1989 to 2008
$9.1M
Training Program in Cell, Molecular, and Developmental BiologyT32GM008111 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI YODER, BRADLEY K. · 1985 to 2022
$5.4M
Analytical tools for the analysis of clustered O-glycans in clinical samplesR01GM098539 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI RENFROW, MATTHEW B · 2011 to 2019
$2.7M
NIGMS NIH HHS R01 GM098539NIGMS NIH HHS S06 GM008111NIGMS NIH HHS T32 GM008111
6 · The paper itself

Abstract

Glycosylation is a common and biologically significant post-translational modification that is found on numerous virus surface proteins (VSPs). Many of these glycans affect virulence through modulating virus receptor binding, masking antigenic sites, or by stimulating the host immune response. Mass spectrometry (MS) has arisen as a pivotal technique for the characterization of VSP glycosylation. This review will cover how MS-based analyses, such as released glycan profiles, glycan site localization, site-occupancy, and site-specific heterogeneity, are being utilized to map VSP glycosylation. Furthermore, this review will provide information on how MS glycoprofiling data are being used in conjunction with molecular and structural experiments to provide a better understanding of the role of specific glycans in VSP function.

Indexed as

Protein Processing, Post-TranslationalVirus Physiological PhenomenaGlycosylationMass SpectrometryMembrane ProteinsPolysaccharidesProtein BindingViral Matrix ProteinsVirulenceVirusesMembrane ProteinsPolysaccharidesViral Matrix Proteins

Identifiers

PMID31202133
PMCPMC7102858

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.