Evidence map›Paper›PMID 35011288›Full record

ArticleMolecules (Basel, Switzerland)2021

Zinc-Chelating Compounds as Inhibitors of Human and Bacterial Zinc Metalloproteases.

Fatema Rahman, Imin Wushur, Nabin Malla, Ove Alexander Høgmoen Åstrand, Pål Rongved, Jan-Olof Winberg, Ingebrigt Sylte

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. 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
0.3field-weighted citation impact, top 40% 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.

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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

7 authors at 2 institutions in 1 country.

Fatema RahmanMolecular Pharmacology and Toxicology, Department of Medical Biology, Faculty of Health Sciences, UiT-The Arctic University of Norway, NO-9037 Tromsø, Norway.
Imin WushurMolecular Pharmacology and Toxicology, Department of Medical Biology, Faculty of Health Sciences, UiT-The Arctic University of Norway, NO-9037 Tromsø, Norway.
Nabin MallaMolecular Pharmacology and Toxicology, Department of Medical Biology, Faculty of Health Sciences, UiT-The Arctic University of Norway, NO-9037 Tromsø, Norway.
Ove Alexander Høgmoen ÅstrandDepartment of Pharmaceutical Chemistry, School of Pharmacy, University of Oslo, NO-0316 Oslo, Norway.
Pål RongvedDepartment of Pharmaceutical Chemistry, School of Pharmacy, University of Oslo, NO-0316 Oslo, Norway.
Jan-Olof WinbergMolecular Pharmacology and Toxicology, Department of Medical Biology, Faculty of Health Sciences, UiT-The Arctic University of Norway, NO-9037 Tromsø, Norway.
Ingebrigt SylteMolecular Pharmacology and Toxicology, Department of Medical Biology, Faculty of Health Sciences, UiT-The Arctic University of Norway, NO-9037 Tromsø, Norway.ORCID 0000-0002-3290-3736
UiT The Arctic University of Norway · NOUniversity of Oslo · NO

Funding

Northern Norway Regional Health Authority HNF1514-20Tromsø research foundation xx
6 · The paper itself

Abstract

Inhibition of bacterial virulence is believed to be a new treatment option for bacterial infections. In the present study, we tested dipicolylamine (DPA), tripicolylamine (TPA), tris pyridine ethylene diamine (TPED), pyridine and thiophene derivatives as putative inhibitors of the bacterial virulence factors thermolysin (TLN), pseudolysin (PLN) and aureolysin (ALN) and the human zinc metalloproteases, matrix metalloprotease-9 (MMP-9) and matrix metalloprotease-14 (MMP-14). These compounds have nitrogen or sulfur as putative donor atoms for zinc chelation. In general, the compounds showed stronger inhibition of MMP-14 and PLN than of the other enzymes, with

Indexed as

Amino AcidsBacteriaCatalytic DomainChelating AgentsDose-Response Relationship, DrugEnzyme ActivationHumansMetalloproteasesModels, MolecularMolecular ConformationMolecular StructureProtease InhibitorsStructure-Activity RelationshipZinc CompoundsAmino AcidsChelating AgentsMetalloproteasesProtease InhibitorsZinc Compoundsbacterial virulence factorsdockingenzyme inhibitionmatrix metalloproteasesmolecular interactionszinc chelators

Identifiers

PMID35011288
PMCPMC8746695
OpenAlexW4200171662

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.