Evidence map›Paper›PMID 39601221›Full record

ArticleACS infectious diseases2024

Decarboxylation of the Catalytic Lysine Residue by the C5α-Methyl-Substituted Carbapenem NA-1-157 Leads to Potent Inhibition of the OXA-58 Carbapenemase.

Marta Toth, Nichole K Stewart, Ailiena O Maggiolo, Pojun Quan, Md Mahbub Kabir Khan, John D Buynak, Clyde A Smith, Sergei B Vakulenko

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS infectious diseases, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. 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

8 authors.

Marta TothDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Nichole K StewartDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Ailiena O MaggioloStanford Synchrotron Radiation Lightsource, Stanford University, Menlo Park, California 94025, United States.
Pojun QuanDepartment of Chemistry, Southern Methodist University, Dallas, Texas 75275, United States.
Md Mahbub Kabir KhanDepartment of Chemistry, Southern Methodist University, Dallas, Texas 75275, United States.
John D BuynakDepartment of Chemistry, Southern Methodist University, Dallas, Texas 75275, United States.ORCID 0000-0003-1007-791X
Clyde A SmithStanford Synchrotron Radiation Lightsource, Stanford University, Menlo Park, California 94025, United States.ORCID 0000-0002-1885-1511
Sergei B VakulenkoDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.ORCID 0000-0002-5327-8124

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
Carbapenemase-Stable Carbapenem Antibiotics for Treatment of Multidrug-Resistant Acinetobacter baumannii InfectionsR01AI155723 · NIAID · UNIVERSITY OF NOTRE DAME · PI BUYNAK, JOHN D, VAKULENKO, SERGEI · 2021 to 2025
$3.9M
Optimization of Atypical Antimycobacterial Carbapenem AntibioticsR01AI174599 · NIAID · SOUTHERN METHODIST UNIVERSITY · PI JOHN D BUYNAK, Konstantin V Korotkov · 2023 to 2026
$2.8M
Antibiotics Designed to Counter Resistant 21st Century PathogensR15AI142699 · NIAID · SOUTHERN METHODIST UNIVERSITY · PI BUYNAK, JOHN D · 2019 to 2019
$437k
NIAID NIH HHS R01 AI155723NIAID NIH HHS R01 AI174599NIAID NIH HHS R15 AI142699NIGMS NIH HHS P30 GM133894
6 · The paper itself

Abstract

Antibiotic resistance in bacteria is a major global health concern. The wide spread of carbapenemases, bacterial enzymes that degrade the last-resort carbapenem antibiotics, is responsible for multidrug resistance in bacterial pathogens and has further significantly exacerbated this problem.

Indexed as

Acinetobacter baumanniiAnti-Bacterial AgentsBacterial Proteinsbeta-Lactamase Inhibitorsbeta-LactamasesCarbapenemsLysineMicrobial Sensitivity TestsCatalytic DomainDecarboxylationKineticsAnti-Bacterial AgentsBacterial Proteinsbeta-Lactamase Inhibitorsbeta-LactamasescarbapenemaseCarbapenemsLysineAcinetobacterantibiotic resistanceinhibitorOXA-58 carbapenemaseX-ray structure

Identifiers

PMID39601221
PMCPMC11972452

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.