Evidence map›Paper›PMID 30181269›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Mammalian STT3A/B oligosaccharyltransferases segregate N-glycosylation at the translocon from lipid-linked oligosaccharide hydrolysis.

Hua Lu, Charles S Fermaintt, Natalia A Cherepanova, Reid Gilmore, Nan Yan, Mark A Lehrman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 42 citations in OpenAlex.

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  17. Global view of human protein glycosylation pathways and functions.Nature reviews. Molecular cell biology · 2020
    Review
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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

6 authors at 3 institutions in 1 country.

Hua LuDepartment of Pharmacology, University of Texas (UT) Southwestern Medical Center, Dallas, TX 75390.
Charles S FermainttDepartment of Immunology, UT Southwestern Medical Center, Dallas, TX 75390.
Natalia A CherepanovaDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605.
Reid GilmoreDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605.
Nan YanDepartment of Immunology, UT Southwestern Medical Center, Dallas, TX 75390.ORCID 0000-0002-0637-3989
Mark A LehrmanDepartment of Pharmacology, University of Texas (UT) Southwestern Medical Center, Dallas, TX 75390; mark.lehrman@utsouthwestern.edu.
Southwestern Medical CenterSouthwestern Medical Center · USUniversity 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
The N-Glycosylation Pathway And Signaling By Free Mannose-6-PhosphateR01GM038545 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LEHRMAN, MARK · 1987 to 2017
$5.7M
A DNase-Independent Function of TREX1/DNase III in Systemic Lupus ErythematosusR01AR067135 · NIAMS · UT SOUTHWESTERN MEDICAL CENTER · PI YAN, NAN · 2014 to 2018
$1.8M
NIAMS NIH HHS R01 AR067135NIGMS NIH HHS R01 GM038545NIGMS NIH HHS R01 GM043768
6 · The paper itself

Abstract

Oligosaccharyltransferases (OSTs) N-glycosylate proteins by transferring oligosaccharides from lipid-linked oligosaccharides (LLOs) to asparaginyl residues of Asn-Xaa-Ser/Thr acceptor sequons. Mammals have OST isoforms with STT3A or STT3B catalytic subunits for cotranslational or posttranslational N-glycosylation, respectively. OSTs also hydrolyze LLOs, forming free oligosaccharides (fOSs). It has been unclear whether hydrolysis is due to one or both OSTs, segregated from N-glycosylation, and/or regulated. Transfer and hydrolysis were assayed in permeabilized HEK293 kidney and Huh7.5.1 liver cells lacking STT3A or STT3B. Transfer by both STT3A-OST and STT3B-OST with synthetic acceptors was robust. LLO hydrolysis by STT3B-OST was readily detected and surprisingly modulated: Without acceptors, STT3B-OST hydrolyzed Glc

Indexed as

AnimalsCell LineEndoplasmic ReticulumExodeoxyribonucleasesGene Knockout TechniquesGlycosylationHexosyltransferasesHumansHydrolysisIsoenzymesLipopolysaccharidesMembrane ProteinsMiceOligosaccharidesPhosphoproteinsProtein Processing, Post-TranslationalExodeoxyribonucleasesHexosyltransferasesIsoenzymeslipid-linked oligosaccharidesLipopolysaccharidesMembrane ProteinsOligosaccharidesPhosphoproteinsSTT3A protein, humanSTT3B protein, humanthree prime repair exonuclease 1dolicholglycosylationoligosaccharyltransferaseSTT3ASTT3B

Identifiers

PMID30181269
PMCPMC6156661
OpenAlexW2889905198

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.