Evidence map›Paper›PMID 29769739›Full record

ArticleNature chemical biology2018

Membrane association of monotopic phosphoglycosyl transferase underpins function.

Leah C Ray, Debasis Das, Sonya Entova, Vinita Lukose, Andrew J Lynch, Barbara Imperiali, Karen N Allen

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed, 51 citations in OpenAlex.

  1. Glycoconjugate diversification inbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Proteome-wide bioinformatic annotation and functional validation of the monotopic phosphoglycosyl transferase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  16. Defining Early Steps inbioRxiv : the preprint server for biology · 2023
    Article
  17. Review
  18. A New Face of the Old Gene: Deletion of theInternational journal of molecular sciences · 2023
    Article
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Leah C RayProgram in Biomolecular Pharmacology, Boston University School of Medicine, Boston, MA, USA.ORCID http://orcid.org/0000-0002-4590-3110
Debasis DasDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID http://orcid.org/0000-0001-8967-3348
Sonya EntovaDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
Vinita LukoseDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID http://orcid.org/0000-0002-8086-1040
Andrew J LynchDepartment of Chemistry, Boston University, Boston, MA, USA.
Barbara ImperialiDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA. imper@mit.edu.
Karen N AllenProgram in Biomolecular Pharmacology, Boston University School of Medicine, Boston, MA, USA. drkallen@bu.edu.ORCID http://orcid.org/0000-0001-7296-0551
Massachusetts Institute of Technology · USBoston University · US

Funding

PRE-DOCTORAL TRAINING IN THE BIOLOGICAL SCIENCEST32GM007287 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BELL, STEPHEN P., KEATING, AMY E · 1985 to 2019
$40.8M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
SPECIFICITY IN CO- AND POST-TRANSLATIONAL MODIFICATIONR01GM039334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALLEN, KAREN N., IMPERIALI, BARBARA · 1993 to 2025
$8.0M
TRAINING IN BIOMOLECULAR PHARMACOLOGYT32GM008541 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI FARB, DAVID H · 1997 to 2022
$5.2M
NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM039334NIGMS NIH HHS T32 GM007287NIGMS NIH HHS T32 GM008541
6 · The paper itself

Abstract

Polyprenol phosphate phosphoglycosyl transferases (PGTs) catalyze the first membrane-committed step in assembly of essential glycoconjugates. Currently there is no structure-function information to describe how monotopic PGTs coordinate the reaction between membrane-embedded and soluble substrates. We describe the structure and mode of membrane association of PglC, a PGT from Campylobacter concisus. The structure reveals a unique architecture, provides mechanistic insight and identifies ligand-binding determinants for PglC and the monotopic PGT superfamily.

Indexed as

CampylobacterCatalysisCatalytic DomainCell MembraneCloning, MolecularCysteineGlycoconjugatesGlycosyltransferasesLigandsMutationPhosphatesPhosphorylationProtein DomainsProtein FoldingProtein Structure, SecondaryStructure-Activity RelationshipCysteineGlycoconjugatesGlycosyltransferasesLigandsPhosphates

Identifiers

PMID29769739
PMCPMC6202225
OpenAlexW2803725206

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.