Evidence map›Paper›PMID 29808562›Full record

ArticleChemical biology & drug design2018

Druggability of the guanosine/adenosine/cytidine nucleoside hydrolase from Trichomonas vaginalis.

Rayyan Alam, Allen T Barbarovich, Wagma Caravan, Mirna Ismail, Angela Barskaya, David W Parkin, Brian J Stockman

Open access · greenAbstract read
In one paragraph

Article in Chemical biology & drug design, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure, Oligomerization and Activity Modulation in N-Ribohydrolases.International journal of molecular sciences · 2022
    Review
  4. Article
  5. NewRSC advances · 2019
    Article
  6. Article
  7. Review
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 1 institution in 1 country.

Rayyan AlamDepartment of Chemistry, Adelphi University, Garden City, New York.
Allen T BarbarovichDepartment of Chemistry, Adelphi University, Garden City, New York.
Wagma CaravanDepartment of Chemistry, Adelphi University, Garden City, New York.
Mirna IsmailDepartment of Chemistry, Adelphi University, Garden City, New York.
Angela BarskayaDepartment of Chemistry, Adelphi University, Garden City, New York.
David W ParkinDepartment of Chemistry, Adelphi University, Garden City, New York.
Brian J StockmanDepartment of Chemistry, Adelphi University, Garden City, New York.ORCID 0000-0002-8520-9588
Adelphi University · US

Funding

Nucleoside ribohydrolases as targets for Trichomonas vaginalis therapeutic agents. This project will evaluate two essential nucleoside ribohydrolase enzymes as targets for novel antitrichomonal drugs.R15AI128585 · NIAID · ADELPHI UNIVERSITY · PI STOCKMAN, BRIAN J · 2017 to 2017
$311k
NIAID NIH HHS R15 AI128585
6 · The paper itself

Abstract

Trichomonas vaginalis infects approximately 300 million people worldwide annually. Infected individuals have a higher susceptibility to more serious conditions such as cervical and prostate cancer. The parasite has developed increasing resistance to current drug therapies, with an estimated 5% of clinical cases resulting from resistant strains, creating the need for new therapeutic strategies with novel mechanisms of action. Nucleoside salvage pathway enzymes represent novel drug targets as these pathways are essential for the parasite's survival. The guanosine/adenosine/cytidine nucleoside hydrolase (GACNH) may be particularly important as its expression is upregulated under glucose-limiting conditions mimicking those that occur during infection establishment. GACNH was screened against the NIH Clinical Collection to explore its druggability. Seven compounds were identified with IC

Indexed as

AdenosineEnzyme InhibitorsInhibitory Concentration 50N-Glycosyl HydrolasesProtozoan ProteinsQuercetinRibavirinStructure-Activity RelationshipTrichomonas vaginalisAdenosineEnzyme InhibitorsN-Glycosyl HydrolasesProtozoan ProteinsQuercetinRibavirintaxifolinNIH clinical compound collectionNMRnucleoside hydrolaseribavirinTrichomonas vaginalis

Identifiers

PMID29808562
PMCPMC6163091
OpenAlexW2806792987

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.