Evidence map›Paper›PMID 31296534›Full record

ArticleThe Journal of cell biology2019

Quantitative glycoproteomics reveals new classes of STT3A- and STT3B-dependent N-glycosylation sites.

Natalia A Cherepanova, Sergey V Venev, John D Leszyk, Scott A Shaffer, Reid Gilmore

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

52 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
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  6. N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025
    Review
  7. Review
  8. ER-resident CCDC134 safeguards TLR4 maturation by maintaining gp96 stability.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. CCDC134 controls TLR biogenesis through the ER chaperone Gp96.The Journal of experimental medicine · 2025
    Article
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  13. 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

5 authors at 1 institution in 1 country.

Natalia A CherepanovaDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA.
Sergey V VenevProgram in Bioinformatics and Integrative Biology, University of Massachusetts Medical School, Worcester, MA.
John D LeszykDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA.
Scott A ShafferDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA.
Reid GilmoreDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA reid.gilmore@umassmed.edu.ORCID 0000-0002-1656-4041
University of Massachusetts Chan Medical School · US

Funding

ASSEMBLY AND TRANSFER OF N-LINKED OLIGOSACCHARIDESR01GM043768 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GILMORE, JAMES REID · 1990 to 2018
$6.9M
NIGMS NIH HHS R01 GM043768
6 · The paper itself

Abstract

Human cells express two oligosaccharyltransferase complexes (STT3A and STT3B) with partially overlapping functions. The STT3A complex interacts directly with the protein translocation channel to mediate cotranslational glycosylation, while the STT3B complex can catalyze posttranslocational glycosylation. We used a quantitative glycoproteomics procedure to compare glycosylation of roughly 1,000 acceptor sites in wild type and mutant cells. Analysis of site occupancy data disclosed several new classes of STT3A-dependent acceptor sites including those with suboptimal flanking sequences and sites located within cysteine-rich protein domains. Acceptor sites located in short loops of multi-spanning membrane proteins represent a new class of STT3B-dependent site. Remarkably, the lumenal ER chaperone GRP94 was hyperglycosylated in STT3A-deficient cells, bearing glycans on five silent sites in addition to the normal glycosylation site. GRP94 was also hyperglycosylated in wild-type cells treated with ER stress inducers including thapsigargin, dithiothreitol, and NGI-1.

Indexed as

ProteomicsGlycoproteinsGlycosylationHEK293 CellsHeLa CellsHexosyltransferasesHSP70 Heat-Shock ProteinsHumansMembrane Proteinsglucose-regulated proteinsGlycoproteinsHexosyltransferasesHSP70 Heat-Shock ProteinsMembrane ProteinsSTT3A protein, humanSTT3B protein, human

Identifiers

PMID31296534
PMCPMC6683751
OpenAlexW2958279881

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.