Evidence map›Paper›PMID 31754071›Full record

ArticleMolecular cancer therapeutics2020

Development of a Novel Multi-Isoform ALDH Inhibitor Effective as an Antimelanoma Agent.

Saketh S Dinavahi, Raghavendra Gowda, Krishne Gowda, Christopher G Bazewicz, Venkat R Chirasani, Madhu Babu Battu, Arthur Berg, Nikolay V Dokholyan, Shantu Amin, Gavin P Robertson

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cancer therapeutics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  5. The Significance of Aldehyde Dehydrogenase 1 in Cancers.International journal of molecular sciences · 2024
    Review
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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

10 authors at 2 institutions in 2 countries.

Saketh S DinavahiDepartment of Pharmacology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania.
Raghavendra GowdaDepartment of Pharmacology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania.ORCID 0000-0002-6042-0520
Krishne GowdaDepartment of Pharmacology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania.ORCID 0000-0002-6042-0520
Christopher G BazewiczThe Melanoma and Skin Cancer Center, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania.ORCID 0000-0003-4299-400X
Venkat R ChirasaniDepartment of Pharmacology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania.
Madhu Babu BattuLaboratory of Molecular Cell Biology, Centre for DNA Fingerprinting and Diagnostics, Uppal, Hyderabad, India.
Arthur BergDepartment of Public Health Sciences, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania.
Nikolay V DokholyanDepartment of Pharmacology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania.ORCID 0000-0002-8225-4025
Shantu AminDepartment of Pharmacology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania.
Gavin P RobertsonDepartment of Pharmacology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania. gpr11@psu.edu.
Pennsylvania State University · USCentre for DNA Fingerprinting and Diagnostics · IN

Funding

Nanoscale programming of cellular and physiological phenotypes: EquipmentR35GM134864 · NIGMS · UNIVERSITY OF VIRGINIA · PI Nikolay Dokholyan · 2020 to 2026
$5.2M
Integrating cheminformatics and molecular simulations for virtual drug screeningR01GM114015 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOKHOLYAN, NIKOLAY · 2016 to 2019
$1.1M
NIGMS NIH HHS R01 GM114015NIGMS NIH HHS R35 GM134864
6 · The paper itself

Abstract

The aldehyde dehydrogenases (ALDH) are a major family of detoxifying enzymes that contribute to cancer progression and therapy resistance. ALDH overexpression is associated with a poor prognosis in many cancer types. The use of multi-ALDH isoform or isoform-specific ALDH inhibitors as anticancer agents is currently hindered by the lack of viable candidates. Most multi-ALDH isoform inhibitors lack bioavailability and are nonspecific or toxic, whereas most isoform-specific inhibitors are not effective as monotherapy due to the overlapping functions of ALDH family members. The present study details the development of a novel, potent, multi-isoform ALDH inhibitor, called KS100. The rationale for drug development was that inhibition of multiple ALDH isoforms might be more efficacious for cancer compared with isoform-specific inhibition. Enzymatic IC

Indexed as

Aldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAnimalsCell Line, TumorHumansMelanomaMiceTransfectionAldehyde DehydrogenaseAldehyde Dehydrogenase 1 Family

Identifiers

PMID31754071
PMCPMC10763724
OpenAlexW2989884456

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.