Evidence map›Paper›PMID 31390192›Full record

ArticleJournal of the American Chemical Society2019

An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase.

Olga A Esakova, Alexey Silakov, Tyler L Grove, Douglas M Warui, Neela H Yennawar, Squire J Booker

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 43% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Design and characterization of a tunable open TEJournal of magnetic resonance (San Diego, Calif. : 1997) · 2025
    Article
  2. Article
  3. Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

6 authors at 1 institution in 1 country.

Pennsylvania State University · US

Funding

Radical Mechanisms of Iron-Sulfur ProteinsR35GM122595 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI SQUIRE J. BOOKER · 2017 to 2026
$3.4M
NIGMS NIH HHS R35 GM122595
6 · The paper itself

Abstract

Quinolinic acid is a common intermediate in the biosynthesis of nicotinamide adenine dinucleotide and its derivatives in all organisms that synthesize the molecule de novo. In most prokaryotes, it is formed from the condensation of dihydroxyacetone phosphate (DHAP) and iminoaspartate (IA) by the action of quinolinate synthase (NadA). NadA contains a [4Fe-4S] cluster cofactor with a unique noncysteinyl-ligated iron ion (Fe

Indexed as

Aspartic AcidBiocatalysisCrystallography, X-RayDihydroxyacetone PhosphateModels, MolecularMolecular StructureMultienzyme ComplexesPyrococcus horikoshiiAspartic AcidDihydroxyacetone Phosphateiminoaspartic acidMultienzyme Complexesquinolinic acid synthetase

Identifiers

PMID31390192
PMCPMC7029380
OpenAlexW2965702097

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.