Evidence map›Paper›PMID 35763562›Full record

ArticleACS infectious diseases2022

Live-Cell Profiling of Penicillin-Binding Protein Inhibitors in

Joshua D Shirley, Kelsie M Nauta, Erin E Carlson

Open access · greenAbstract read
In one paragraph

Article in ACS infectious diseases, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. ACS infectious diseases · 2024
    Article
  5. Article
  6. Penicillin-binding protein redundancy inApplied and environmental microbiology · 2024
    Article
  7. Review
  8. Review
  9. 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

3 authors at 1 institution in 1 country.

Joshua D ShirleyDepartment of Medicinal Chemistry, University of Minnesota, 208 Harvard Street SE, Minneapolis, Minnesota 55454, United States.
Kelsie M NautaDepartment of Chemistry, University of Minnesota, 207 Pleasant Street SE, Minneapolis, Minnesota 55455, United States.
Erin E CarlsonDepartment of Medicinal Chemistry, University of Minnesota, 208 Harvard Street SE, Minneapolis, Minnesota 55454, United States.ORCID 0000-0001-8287-8893
University of Minnesota · US

Funding

University of Minnesota Clinical and Translational Science Institute (UMN CTSI)UL1TR002494 · NCATS · UNIVERSITY OF MINNESOTA · PI BLAZAR, BRUCE R, WEISDORF, DANIEL J · 2018 to 2022
$34.9M
NRSA Training CoreTL1TR002493 · NCATS · UNIVERSITY OF MINNESOTA · PI FULKERSON, JAYNE ALLYN · 2018 to 2022
$3.1M
Chemical Methods to Characterize Penicillin-Binding Protein Function and InteractionsR01GM140486 · NIGMS · UNIVERSITY OF MINNESOTA · PI CARLSON, ERIN ELIZABETH · 2020 to 2023
$1.2M
Spaciotemporal Regulation of Specific Penicillin Binding Protein (PBP) Function Determined by New Activity-Based ApproachesR01GM128439 · NIGMS · UNIVERSITY OF MINNESOTA · PI CARLSON, ERIN ELIZABETH, WINKLER, MALCOLM E. · 2018 to 2019
$936k
NCATS NIH HHS TL1 TR002493NCATS NIH HHS UL1 TR002494NIGMS NIH HHS R01 GM128439NIGMS NIH HHS R01 GM140486
6 · The paper itself

Abstract

Penicillin-binding proteins (PBPs) make up an essential class of bacterial enzymes that carry out the final steps of peptidoglycan synthesis and regulate the recycling of this polymeric structure. PBPs are an excellent drug target and have been the most clinically relevant antibacterial target since the 1940s with the introduction of β-lactams. Despite this, a large gap in knowledge remains regarding the individual function and regulation of each PBP homologue in most bacteria. This can be attributed to a lack of chemical tools and methods that enable the study of individual PBPs in an activity-dependent manner and in their native environment. The development of such methods in Gram-negative bacteria has been particularly challenging due to the presence of an outer membrane and numerous resistance mechanisms. To address this, we have developed an optimized live-cell assay for screening inhibitors of the PBPs in

Indexed as

beta-LactamsEscherichia coliAnti-Bacterial AgentsGram-Negative BacteriaPenicillin-Binding ProteinsAnti-Bacterial Agentsbeta-LactamsPenicillin-Binding ProteinsEscherichia coliGram-negative bacteriaIC50outer-membranepenicillin-binding proteinspermeabilization

Identifiers

PMID35763562
PMCPMC10040144
OpenAlexW4283711656

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.