Evidence map›Paper›PMID 31213525›Full record

ArticleThe Journal of biological chemistry2019

A temperature-dependent conformational shift in p38α MAPK substrate-binding region associated with changes in substrate phosphorylation profile.

Daniel Deredge, Patrick L Wintrode, Mohan E Tulapurkar, Ashish Nagarsekar, Yinghua Zhang, David J Weber, Paul Shapiro, Jeffrey D Hasday

Registry-linked trialAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT04545424 (Cooling to Help Injured Lungs), which is not on this map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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.

NCT04545424 phase2recruitingnot on this mapstarted 2021, after this paper: background citation

Cooling to Help Injured Lungs (CHILL) Phase IIB Randomized Control Trial of Therapeutic Hypothermia in Patients With ARDS

TypeinterventionalSponsorUniversity of Maryland, BaltimoreRan2021 to 2026Enrolled340ConditionsRespiratory Distress Syndrome, AdultArmsHypothermia, Neuromuscular Blocking Agents, Standard of care
3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Daniel DeredgeDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland 21201.ORCID 0000-0002-6897-6523
Patrick L WintrodeDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland 21201.
Mohan E TulapurkarDivision of Pulmonary and Critical Care Medicine, Department of Medicine, Department of Medicine, University of Maryland School of Medicine, Baltimore, Maryland 21201.
Ashish NagarsekarDivision of Pulmonary and Critical Care Medicine, Department of Medicine, Department of Medicine, University of Maryland School of Medicine, Baltimore, Maryland 21201.
Yinghua ZhangDepartment of Physiology, University of Maryland School of Medicine, Baltimore, Maryland 21201.
David J WeberDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201.ORCID 0000-0002-8824-1110
Paul ShapiroDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland 21201.
Jeffrey D HasdayDivision of Pulmonary and Critical Care Medicine, Department of Medicine, Department of Medicine, University of Maryland School of Medicine, Baltimore, Maryland 21201 jhasday@medicine.umaryland.edu.ORCID 0000-0001-5011-5621

Funding

p38MAP kinase-dependent mechanisms of fever-enhanced acute lung injuryR01HL069057 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI HASDAY, JEFFREY D, SHAPIRO, PAUL S · 2003 to 2016
$4.6M
BLRD VA I01 BX002143NHLBI NIH HHS R01 HL069057
6 · The paper itself

Abstract

Febrile-range hyperthermia worsens and hypothermia mitigates lung injury, and temperature dependence of lung injury is blunted by inhibitors of p38 mitogen-activated protein kinase (MAPK). Of the two predominant p38 isoforms, p38α is proinflammatory and p38β is cytoprotective. Here, we analyzed the temperature dependence of p38 MAPK activation, substrate interaction, and tertiary structure. Incubating HeLa cells at 39.5 °C stimulated modest p38 activation, but did not alter tumor necrosis factor-α (TNFα)-induced p38 activation. In

Indexed as

TemperatureCells, CulturedHumansMitogen-Activated Protein Kinase 14PhosphorylationProtein BindingProtein ConformationSubstrate SpecificitySurface Plasmon ResonanceMitogen-Activated Protein Kinase 14hydrogen-deuterium exchangehyperthermiaMAPKAPK-2p38 MAPKprotein structurepulmonary damagepyrogensignalingsubstrate-docking sitesubstrate specificitytemperature-dependence

Identifiers

PMID31213525
PMCPMC6709627

What Socratic holds

Textmetadata
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Registered trials

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 Socratic graph.