Evidence map›Paper›PMID 32502861›Full record

ArticleEuropean journal of medicinal chemistry2020

Inhibitor design to target a unique feature in the folate pocket of Staphylococcus aureus dihydrofolate reductase.

N Prasad Muddala, John C White, Baskar Nammalwar, Ian Pratt, Leonard M Thomas, Richard A Bunce, K Darrell Berlin, Christina R Bourne

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in European journal of medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 45% 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

0 citing papers in PubMed, 8 citations in OpenAlex.

No citing paper in PubMed yet.

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 at 2 institutions in 1 country.

N Prasad MuddalaDepartment of Chemistry, Oklahoma State University, 107 Physical Sciences I, Stillwater, OK, 74078, USA.
John C WhiteDepartment of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK, 73019, USA.
Baskar NammalwarDepartment of Chemistry, Oklahoma State University, 107 Physical Sciences I, Stillwater, OK, 74078, USA.
Ian PrattDepartment of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK, 73019, USA.
Leonard M ThomasDepartment of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK, 73019, USA.
Richard A BunceDepartment of Chemistry, Oklahoma State University, 107 Physical Sciences I, Stillwater, OK, 74078, USA.
K Darrell BerlinDepartment of Chemistry, Oklahoma State University, 107 Physical Sciences I, Stillwater, OK, 74078, USA.
Christina R BourneDepartment of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK, 73019, USA. Electronic address: cbourne@ou.edu.
Oklahoma State University · USUniversity of Oklahoma · US

Funding

Structure-Function Studies of MsvR, a Methanogen-Specific Transcriptional RegulaP20GM103640 · NIGMS · UNIVERSITY OF OKLAHOMA · PI THOMAS, LEONARD M · 2012 to 2021
$20.4M
Broad-spectrum Antifolates for Treatment of Drug Resistant Bacillus anthracisR01AI090685 · NIAID · OKLAHOMA STATE UNIVERSITY STILLWATER · PI BUNCE, RICHARD A · 2010 to 2014
$3.9M
NIAID NIH HHS R01 AI090685NIGMS NIH HHS P20 GM103640
6 · The paper itself

Abstract

Staphylococcus aureus (Sa) is a serious concern due to increasing resistance to antibiotics. The bacterial dihydrofolate reductase enzyme is effectively inhibited by trimethoprim, a compound with antibacterial activity. Previously, we reported a trimethoprim derivative containing an acryloyl linker and a dihydophthalazine moiety demonstrating increased potency against S. aureus. We have expanded this series and assessed in vitro enzyme inhibition (K

Indexed as

Drug DesignBinding SitesEnzyme InhibitorsMicrobial Sensitivity TestsStaphylococcus aureusStructure-Activity RelationshipTetrahydrofolate DehydrogenaseTrimethoprimEnzyme InhibitorsTetrahydrofolate DehydrogenaseTrimethoprim2,4-DiaminopyrimidineAlkyl dihydrophthalazinesAntibacterialDihydrofolate reductaseEnzyme inhibitionFolate pathwayHeck couplingStaphylococcal aureus

Identifiers

PMID32502861
PMCPMC7932028
OpenAlexW3028541477

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.