Evidence map›Paper›PMID 36063654›Full record

ArticleBioorganic & medicinal chemistry2022

Catalytic covalent inhibition of cyclooxygenase-1 by a biomimetic acyltransferase.

Wei Bao, Baruch Turniansky, John Koh

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioorganic & medicinal chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-weighted citation impact, top 49% 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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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

3 authors at 1 institution in 1 country.

Wei BaoUniversity of Delaware, 102 Brown Laboratory, Newark, DE 19716, USA.
Baruch TurnianskyUniversity of Delaware, 102 Brown Laboratory, Newark, DE 19716, USA.
John KohUniversity of Delaware, 102 Brown Laboratory, Newark, DE 19716, USA. Electronic address: johnkoh@udel.edu.
University of Delaware · US

Funding

This renovation project will create over 1455 sq. ft. of state- of-the-art reseaP20GM104316 · NIGMS · UNIVERSITY OF DELAWARE · PI FOX, JOSEPH M · 2014 to 2024
$26.8M
Pilot Research Subproject ProgramP30GM110758 · NIGMS · UNIVERSITY OF DELAWARE · PI BEEBE, THOMAS PAUL · 2014 to 2018
$5.8M
NIGMS NIH HHS P20 GM104316NIGMS NIH HHS P30 GM110758
6 · The paper itself

Abstract

Covalent binding enzyme inhibitors have grown in acceptance in therapeutic discovery. Several recent examples of protein-targeting acyl-transfer catalysts covalently modify protein targets in cellular systems but generally do not affect protein function. In this study, a small molecule has been developed for the first time that can achieve catalytic covalent inhibition of the inflammatory response enzyme, cyclooxygenase-1, in cells using only endogenous acetyl-CoA as a co-substrate. By utilizing a catalytic inhibitor which can self-regenerate, a sustained inhibitory response is achieved in cells compared to the analogous non-catalytic covalent cyclooxygenase antagonist, acetylsalicylic acid (aspirin).

Indexed as

AcyltransferasesBiomimeticsAcetyl Coenzyme AAspirinCyclooxygenase 1Cyclooxygenase 2Enzyme InhibitorsAcetyl Coenzyme AAcyltransferasesAspirinCyclooxygenase 1Cyclooxygenase 2Enzyme InhibitorsAcyl-transfer catalysisCatalytic covalent inhibitorCovalent inhibitorCyclooxygenaseProtein acetylation

Identifiers

PMID36063654
PMCPMC11697132
OpenAlexW4293559816

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.