Evidence map›Paper›PMID 31019074›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

The crystal structure of dGTPase reveals the molecular basis of dGTP selectivity.

Christopher O Barnes, Ying Wu, Jinhu Song, Guowu Lin, Elizabeth L Baxter, Aaron S Brewster, V Nagarajan, Andrew Holmes, S Michael Soltis, Nicholas K Sauter and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structural basis of transcription: RNA polymerase II substrate binding and metal coordination using a free-electron laser.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Mechanism by which T7 bacteriophage protein Gp1.2 inhibitsProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Versatile microporous polymer-based supports for serial macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2021
    Article
  12. Low-doseIUCrJ · 2020
    Article
  13. 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

13 authors at 4 institutions in 1 country.

Christopher O BarnesDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260.
Ying WuDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260.
Jinhu SongStructural Molecular Biology, Stanford Synchroton Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025.
Guowu LinDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260.
Elizabeth L BaxterStructural Molecular Biology, Stanford Synchroton Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025.
Aaron S BrewsterMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
V NagarajanJAN Scientific Inc., Seattle, WA 98105.
Andrew HolmesSwanson School of Engineering, University of Pittsburgh, Pittsburgh, PA 15260.
S Michael SoltisStructural Molecular Biology, Stanford Synchroton Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025.
Nicholas K SauterMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Jinwoo AhnDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260.
Aina E CohenStructural Molecular Biology, Stanford Synchroton Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025; acohen@slac.stanford.edu guc9@pitt.edu.
Guillermo CaleroDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260; acohen@slac.stanford.edu guc9@pitt.edu.
University of Pittsburgh · USSLAC National Accelerator Laboratory · USLawrence Berkeley National Laboratory · USStanford University · US

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CALERO, GUILLERMO ALBERTO · 2007 to 2018
$48.1M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
DIALS: New Computational Methods to Enable Challenging Crystallographic ExperimentsR01GM117126 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI SAUTER, NICHOLAS K · 2016 to 2023
$6.1M
Structural Studies of RNA Polymerase II Transcription Initiation and ElongationR01GM112686 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CALERO, GUILLERMO ALBERTO · 2015 to 2024
$2.8M
Structure and function relationships regulating SAMHD1's dual enzymatic activitiesR01GM116642 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI AHN, JINWOO · 2015 to 2018
$1.4M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P50 GM082251NIGMS NIH HHS R01 GM112686NIGMS NIH HHS R01 GM116642NIGMS NIH HHS R01 GM117126
6 · The paper itself

Abstract

Deoxynucleotide triphosphohydrolases (dNTPases) play a critical role in cellular survival and DNA replication through the proper maintenance of cellular dNTP pools. While the vast majority of these enzymes display broad activity toward canonical dNTPs, such as the dNTPase SAMHD1 that blocks reverse transcription of retroviruses in macrophages by maintaining dNTP pools at low levels,

Indexed as

Allosteric SiteBinding SitesCatalytic DomainCrystallography, X-RayDeoxyguanine NucleotidesEscherichia coliEscherichia coli ProteinsGTP PhosphohydrolasesModels, MolecularSAM Domain and HD Domain-Containing Protein 1Substrate SpecificityDeoxyguanine Nucleotidesdeoxyguanosine triphosphateEscherichia coli ProteinsGTP PhosphohydrolasesSAM Domain and HD Domain-Containing Protein 1dNTP triphosphohydrolasemetalloenzymesserial femtosecond crystallographyX-ray free-electron laser

Identifiers

PMID31019074
PMCPMC6511015
OpenAlexW2941382872

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.