Evidence map›Paper›PMID 30192413›Full record

ReviewMedicinal research reviews2019

Chemical space of Escherichia coli dihydrofolate reductase inhibitors: New approaches for discovering novel drugs for old bugs.

Bharath Srinivasan, Sam Tonddast-Navaei, Ambrish Roy, Hongyi Zhou, Jeffrey Skolnick

Open access · greenAbstract readReview
In one paragraph

Review in Medicinal research reviews, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  10. Frontiers in pharmacology · 2022
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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

5 authors at 1 institution in 1 country.

Bharath SrinivasanCenter for the Study of Systems Biology, School of Biology, Georgia Institute of Technology, Atlanta, Georgia.ORCID 0000-0003-0561-213X
Sam Tonddast-NavaeiCenter for the Study of Systems Biology, School of Biology, Georgia Institute of Technology, Atlanta, Georgia.
Ambrish RoyCenter for the Study of Systems Biology, School of Biology, Georgia Institute of Technology, Atlanta, Georgia.
Hongyi ZhouCenter for the Study of Systems Biology, School of Biology, Georgia Institute of Technology, Atlanta, Georgia.
Jeffrey SkolnickCenter for the Study of Systems Biology, School of Biology, Georgia Institute of Technology, Atlanta, Georgia.ORCID 0000-0002-1877-4958
Georgia Institute of Technology · US

Funding

Purchase of a GPU cluster for deep learning applications in protein-protein interaction and supercomplex prediction and biochemical literature annotation.R35GM118039 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI JEFFREY SKOLNICK · 2016 to 2026
$5.8M
NIGMS NIH HHS R35 GM118039
6 · The paper itself

Abstract

Escherichia coli Dihydrofolate reductase is an important enzyme that is essential for the survival of the Gram-negative microorganism. Inhibitors designed against this enzyme have demonstrated application as antibiotics. However, either because of poor bioavailability of the small-molecules resulting from their inability to cross the double membrane in Gram-negative bacteria or because the microorganism develops resistance to the antibiotics by mutating the DHFR target, discovery of new antibiotics against the enzyme is mandatory to overcome drug-resistance. This review summarizes the field of DHFR inhibition with special focus on recent efforts to effectively interface computational and experimental efforts to discover novel classes of inhibitors that target allosteric and active-sites in drug-resistant variants of EcDHFR.

Indexed as

AlgorithmsAllosteric SiteAnimalsAnti-Bacterial AgentsBacterial InfectionsCatalytic DomainDrug DesignDrug DiscoveryEnzyme InhibitorsEscherichia coliFolic Acid AntagonistsHumansLigandsPermeabilityStructure-Activity RelationshipTetrahydrofolate DehydrogenaseAnti-Bacterial AgentsEnzyme InhibitorsFolic Acid AntagonistsLigandsTetrahydrofolate Dehydrogenasedihydrofolate reductasedrug resistanceEscherichia coliquantitative structure-activity relationshipvirtual ligand screening

Identifiers

PMID30192413
PMCPMC6370515
OpenAlexW2890932215

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.