Evidence map›Paper›PMID 31324042›Full record

ArticleMolecules (Basel, Switzerland)2019

The 3

Federica Pisaneschi, Yu-Hsi Lin, Paul G Leonard, Nikunj Satani, Victoria C Yan, Naima Hammoudi, Sudhir Raghavan, Todd M Link, Dimitra K Georgiou, Barbara Czako and 1 more

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2019. 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
–field-weighted citation impact
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.

  1. Review
  2. Article
  3. BeyondMolecular therapy oncolytics · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Article
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

11 authors.

Federica PisaneschiDepartment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA. fpisaneschi@mdanderson.org.ORCID 0000-0002-1989-4417
Yu-Hsi LinDepartment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.
Paul G LeonardInstitute of Applied Cancer Science, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.
Nikunj SataniDepartment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.ORCID 0000-0003-3908-3731
Victoria C YanDepartment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.
Naima HammoudiDepartment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.
Sudhir RaghavanDepartment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.ORCID 0000-0001-5449-362X
Todd M LinkCore for Biomolecular Structure and Function, Department of Genomic Medicine, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.
Dimitra K GeorgiouDepartment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.ORCID 0000-0001-8786-2495
Barbara CzakoInstitute of Applied Cancer Science, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.
Florian L MullerDepartment of Cancer Systems Imaging, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA. fmuller@mdanderson.org.ORCID 0000-0001-7568-2948

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Fabien Delerue · 1985 to 2026
$290.8M
American Cancer Society RSG-15-145-01-CDDNational Comprehensive Cancer Network YIA170032NCI NIH HHS P30 CA016672NIH HHS CDP Spore P50CA127001-07University of Texas Rising STARs award
6 · The paper itself

Abstract

We recently reported that SF2312 ((1,5-dihydroxy-2-oxopyrrolidin-3-yl)phosphonic acid), a phosphonate antibiotic with a previously unknown mode of action, is a potent inhibitor of the glycolytic enzyme, Enolase. SF2312 can only be synthesized as a racemic-diastereomeric mixture. However, co-crystal structures with Enolase 2 (ENO2) have consistently shown that only the (3

Indexed as

Binding SitesEnzyme ActivationEnzyme InhibitorsModels, MolecularMolecular ConformationMolecular StructureOrganophosphonatesPhosphopyruvate HydrataseProtein BindingPyrrolidinonesSpectrum AnalysisStereoisomerismStructure-Activity Relationship(1,5-dihydroxy-2-oxopyrrolidin-3-yl)phosphonic acidEnzyme InhibitorsOrganophosphonatesPhosphopyruvate HydratasePyrrolidinoneschiralE. colienolaseenzyme inhibitorenzyme structureglycolysishydroxamatenatural productphosphonateX-ray crystallography

Identifiers

PMID31324042
PMCPMC6651268

What OpenQuestion holds

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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.