Evidence map›Paper›PMID 31964716›Full record

ArticleThe Journal of biological chemistry2020

A tripartite cooperative mechanism confers resistance of the protein kinase A catalytic subunit to dephosphorylation.

Tung O Chan, Roger S Armen, Santosh Yadav, Sushrut Shah, Jin Zhang, Brian C Tiegs, Nikhil Keny, Brian Blumhof, Deepak A Deshpande, Ulrich Rodeck and 1 more

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 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 52% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

11 authors at 1 institution in 1 country.

Tung O ChanCenter for Translational Medicine and Korman Respiratory Institute, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107; Sydney Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107. Electronic address: tung.chan@jefferson.edu.
Roger S ArmenDepartment of Pharmaceutical Sciences, College of Pharmacy, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Santosh YadavCenter for Translational Medicine and Korman Respiratory Institute, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Sushrut ShahCenter for Translational Medicine and Korman Respiratory Institute, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Jin ZhangCenter for Translational Medicine and Korman Respiratory Institute, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Brian C TiegsCenter for Translational Medicine and Korman Respiratory Institute, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Nikhil KenyCenter for Translational Medicine and Korman Respiratory Institute, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Brian BlumhofCenter for Translational Medicine and Korman Respiratory Institute, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Deepak A DeshpandeCenter for Translational Medicine and Korman Respiratory Institute, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Ulrich RodeckSydney Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107; Department of Dermatology and Cutaneous Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Raymond B PennCenter for Translational Medicine and Korman Respiratory Institute, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
Thomas Jefferson University · US

Funding

G Protein-Coupled Receptor Signaling in Airway Smooth MuR01HL058506 · NHLBI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI RAYMOND B. PENN · 2001 to 2026
$9.3M
NHLBI NIH HHS R01 HL058506
6 · The paper itself

Abstract

Phosphorylation of specific residues in the activation loops of AGC kinase group (protein kinase A, G, and C families) is required for activity of most of these kinases, including the catalytic subunit of PKA (PKAc). Although many phosphorylated AGC kinases are sensitive to phosphatase-mediated dephosphorylation, the PKAc activation loop uniquely resists dephosphorylation, rendering it "constitutively" phosphorylated in cells. Previous biophysical experiments and structural modeling have suggested that the N-terminal myristoylation signal and the C-terminal F

Indexed as

Amino Acid MotifsCatalytic DomainCell AdhesionCell LineCell MovementCyclic AMP-Dependent Protein KinasesCytosolHEK293 CellsHumansMutagenesis, Site-DirectedPhosphorylationProto-Oncogene Proteins c-aktRecombinant ProteinsSignal TransductionCyclic AMP-Dependent Protein KinasesProto-Oncogene Proteins c-aktRecombinant ProteinsAkt PKBcAMP-dependent protein kinasedephosphorylationphosphatasePKAprotein kinase Bserine/threonine protein kinasesignal transductionstructure–function

Identifiers

PMID31964716
PMCPMC7062156
OpenAlexW3002925336

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.