Evidence map›Paper›PMID 36346917›Full record

ArticleACS chemical biology2022

Probing Monotopic Phosphoglycosyl Transferases from Complex Cellular Milieu.

Alyssa J Anderson, Leah M Seebald, Christine A Arbour, Barbara Imperiali

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Review
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

4 authors at 1 institution in 1 country.

Alyssa J AndersonDepartment of Biology and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.ORCID 0000-0003-4871-4283
Leah M SeebaldDepartment of Biology and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.
Christine A ArbourDepartment of Biology and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.ORCID 0000-0001-6056-296X
Barbara ImperialiDepartment of Biology and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.ORCID 0000-0002-5749-7869
Massachusetts Institute of Technology · US

Funding

SPECIFICITY IN CO- AND POST-TRANSLATIONAL MODIFICATIONR01GM039334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALLEN, KAREN N., IMPERIALI, BARBARA · 1993 to 2025
$8.0M
Structure and function of the monotopic phosphoglycosyl transferase superfamily: Initiators of biosynthesis of complex bacterial glycoconjugatesR01GM131627 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALLEN, KAREN N. · 2019 to 2025
$3.1M
Design and synthesis of nucleoside-based small molecules to inhibit phosphoglycosyl transferasesF32GM136023 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ARBOUR, CHRISTINE · 2020 to 2023
$234k
NIGMS NIH HHS F32 GM136023NIGMS NIH HHS R01 GM039334NIGMS NIH HHS R01 GM131627
6 · The paper itself

Abstract

Monotopic phosphoglycosyl transferase enzymes (monoPGTs) initiate the assembly of prokaryotic glycoconjugates essential for bacterial survival and proliferation. MonoPGTs belong to an expansive superfamily with a diverse and richly annotated sequence space; however, the biochemical roles of most monoPGTs in glycoconjugate biosynthesis pathways remain elusive. To better understand these critical enzymes, we have implemented activity-based protein profiling (ABPP) probes as protein-centric, membrane protein compatible tools that lay the groundwork for understanding the activity and regulation of the monoPGT superfamily from a cellular proteome. With straightforward gel-based readouts, we demonstrate robust, covalent labeling at the active site of various representative monoPGTs from cell membrane fractions using 3-phenyl-2H-azirine probes.

Indexed as

GlycoconjugatesTransferasesAzirinesCatalytic DomainCell MembraneMembrane Proteins3-phenyl-2H-azirineAzirinesGlycoconjugatesMembrane ProteinsTransferases

Identifiers

PMID36346917
PMCPMC9703085
OpenAlexW4308531618

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.