Evidence map›Paper›PMID 31283204›Full record

ArticleBiochemistry2019

Structural Determinants for Substrate Selectivity in Guanine Deaminase Enzymes of the Amidohydrolase Superfamily.

Roger Shek, Tylene Hilaire, Jasper Sim, Jarrod B French

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. The Discovery ofACS catalysis · 2026
    Article
  3. Article
  4. Article
  5. Characterization of Guanine Deaminase fromFoods (Basel, Switzerland) · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Binding asymmetry and conformational studies of the AtGSDA dimer.Computational and structural biotechnology journal · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

4 authors at 1 institution in 1 country.

Roger ShekDepartment of Biochemistry and Cell Biology , Stony Brook University , Stony Brook , New York 11794 , United States.
Tylene HilaireDepartment of Biochemistry and Cell Biology , Stony Brook University , Stony Brook , New York 11794 , United States.
Jasper SimDepartment of Biochemistry and Cell Biology , Stony Brook University , Stony Brook , New York 11794 , United States.
Jarrod B FrenchDepartment of Biochemistry and Cell Biology , Stony Brook University , Stony Brook , New York 11794 , United States.ORCID 0000-0002-6762-1309
Stony Brook University · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Mechanisms that govern assembly and function of higher order protein structures of purine metabolic enzymesR35GM124898 · NIGMS · UNIVERSITY OF MINNESOTA · PI FRENCH, JARROD B · 2017 to 2021
$2.2M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R35 GM124898
6 · The paper itself

Abstract

Guanine deaminase is a metabolic enzyme, found in all forms of life, which catalyzes the conversion of guanine to xanthine. Despite the availability of several crystal structures, the molecular determinants of substrate orientation and mechanism remain to be elucidated for the amidohydrolase family of guanine deaminase enzymes. Here, we report the crystal structures of

Indexed as

AmidohydrolasesCatalytic DomainEscherichia coli ProteinsGuanine DeaminaseProtein BindingProtein Structure, SecondarySaccharomyces cerevisiae ProteinsSubstrate SpecificityAmidohydrolasesEscherichia coli ProteinsGuanine DeaminaseSaccharomyces cerevisiae Proteins

Identifiers

PMID31283204
PMCPMC6677139
OpenAlexW2959716108

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.