Evidence map›Paper›PMID 31906402›Full record

ArticleBiomolecules2020

Kinetic, Thermodynamic, and Crystallographic Studies of 2-Triazolylthioacetamides as Verona Integron-Encoded Metallo-β-Lactamase 2 (VIM-2) Inhibitor.

Yang Xiang, Yue-Juan Zhang, Ying Ge, Yajun Zhou, Cheng Chen, Weixiao Yuan Wahlgren, Xiangshi Tan, Xi Chen, Ke-Wu Yang

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. 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
0.5field-weighted citation impact, top 46% 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, 7 citations in OpenAlex.

  1. Article
  2. 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

9 authors at 3 institutions in 2 countries.

Yang XiangKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, Chemical Biology Innovation Laboratory, College of Chemistry and Materials Science, Northwest University, Xi'an 710127, China.
Yue-Juan ZhangKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, Chemical Biology Innovation Laboratory, College of Chemistry and Materials Science, Northwest University, Xi'an 710127, China.
Ying GeKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, Chemical Biology Innovation Laboratory, College of Chemistry and Materials Science, Northwest University, Xi'an 710127, China.
Yajun ZhouDepartment of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200433, China.
Cheng ChenKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, Chemical Biology Innovation Laboratory, College of Chemistry and Materials Science, Northwest University, Xi'an 710127, China.
Weixiao Yuan WahlgrenDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 462, S-40530 Gothenburg, Sweden.ORCID 0000-0003-0413-165X
Xiangshi TanDepartment of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200433, China.
Xi ChenKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, Chemical Biology Innovation Laboratory, College of Chemistry and Materials Science, Northwest University, Xi'an 710127, China.
Ke-Wu YangKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, Chemical Biology Innovation Laboratory, College of Chemistry and Materials Science, Northwest University, Xi'an 710127, China.ORCID 0000-0003-2560-9659
Ministry of Education of the People's Republic of China · CNFudan University · CNUniversity of Gothenburg · SE

Funding

National Natural Science Foundation of China 21572179Shaanxi Province Project for International Science and Technology Cooperation 2019KW-068
6 · The paper itself

Abstract

Inhibition of β-lactamases presents a promising strategy to restore the β-lactams antibacterial activity to resistant bacteria. In this work, we found that aromatic carboxyl substituted 2-triazolylthioacetamides

Indexed as

Anti-Bacterial AgentsBacteriaBacterial Proteinsbeta-LactamasesBinding SitesCatalytic DomainCrystallography, X-RayEscherichia coliIntegronsKineticsMicrobial Sensitivity TestsModels, MolecularMolecular StructureProtein BindingStructure-Activity RelationshipThermodynamicsAnti-Bacterial AgentsBacterial Proteinsbeta-lactamase bla(vim-2)beta-LactamasesThioacetamideTriazoles2-triazolylthioacetamidesantibiotic resistancecrystallographic studymetallo-β-lactamase VIM-2 inhibitorthermodynamics

Identifiers

PMID31906402
PMCPMC7022493
OpenAlexW2998090004

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.