Evidence map›Paper›PMID 32229585›Full record

ArticleThe Journal of biological chemistry2020

A

Anju Sreelatha, Christine Nolan, Brenden C Park, Krzysztof Pawłowski, Diana R Tomchick, Vincent S Tagliabracci

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. 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
3.4field-weighted citation impact, top 9% 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, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. ThemBio · 2022
    Article
  11. Article
  12. Review
  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

6 authors at 3 institutions in 2 countries.

Anju SreelathaDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390. Electronic address: anju.sreelatha@utsouthwestern.edu.
Christine NolanDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Brenden C ParkDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Krzysztof PawłowskiInstitute of Biology, Warsaw University of Life Sciences, Warsaw 02-787, Poland.
Diana R TomchickDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas 75390; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Vincent S TagliabracciDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390; Harold C. Simmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, Dallas, Texas 75390; Hamon Center for Regenerative Science and Medicine, University of Texas Southwestern Medical Center, Dallas, Texas 75390. Electronic address: vincent.tagliabracci@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · USSouthwestern Medical Center · USWarsaw University of Life Sciences · PL

Funding

RENAL CONTROL OF BODY COMPOSITION AND BLOOD PRESSURET32DK007257 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI BAUM, MICHEL GERARD, MOE, ORSON W · 1986 to 2021
$5.0M
Breathing life into dead enzymesDP2GM137419 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI TAGLIABRACCI, VINCENT SCOTT · 2019 to 2020
$2.6M
Antioxidant signaling by protein AMPylationR01GM135189 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI TAGLIABRACCI, VINCENT SCOTT · 2020 to 2023
$1.3M
Phosphorylation of FGF23 coordinates crosstalk between the skeleton and kidneyR00DK099254 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI TAGLIABRACCI, VINCENT SCOTT · 2015 to 2017
$746k
Single Crystal X-ray Diffractometer equipped with Hybrid Pixel Array Detector and In Situ Crystallization Plate Screening CapS10OD025018 · OD · UT SOUTHWESTERN MEDICAL CENTER · PI TOMCHICK, DIANA R. · 2018 to 2018
$453k
NIDDK NIH HHS R00 DK099254NIDDK NIH HHS T32 DK007257NIGMS NIH HHS DP2 GM137419NIGMS NIH HHS R01 GM135189NIH HHS S10 OD025018
6 · The paper itself

Abstract

The transfer of a phosphate from ATP to a protein substrate, a modification known as protein phosphorylation, is catalyzed by protein kinases. Protein kinases play a crucial role in virtually every cellular activity. Recent studies of atypical protein kinases have highlighted the structural similarity of the kinase superfamily despite notable differences in primary amino acid sequence. Here, using a bioinformatics screen, we searched for putative protein kinases in the intracellular bacterial pathogen

Indexed as

Host-Pathogen InteractionsEnzyme ActivationLegionella pneumophilaModels, MolecularPhytic AcidProtein ConformationProtein KinasesPhytic AcidProtein Kinasesallosteric regulationbacterial pathogenesisbacterial protein kinaseeffectorenzyme structureinositol hexikisphosphateinositol phosphateLegionella

Identifiers

PMID32229585
PMCPMC7196655
OpenAlexW3014003583

What OpenQuestion holds

Textmetadata
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.