Evidence map›Paper›PMID 36177749›Full record

ArticleIUBMB life2023

Phosphorylation, compartmentalization, and cardiac function.

Kerrie B Collins, John D Scott

Open access · greenAbstract read
In one paragraph

Article in IUBMB life, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Kerrie B CollinsDepartment of Pharmacology, University of Washington, School of Medicine, Seattle, Washington, USA.ORCID 0000-0001-9553-1928
John D ScottDepartment of Pharmacology, University of Washington, School of Medicine, Seattle, Washington, USA.ORCID 0000-0002-0367-8146
University of Washington · US

Funding

CARDIOVASCULAR RESEARCH TRAINING PROGRAMT32HL007828 · NHLBI · UNIVERSITY OF WASHINGTON · PI Francis Kim, Farid Moussavi-Harami · 1997 to 2026
$10.2M
Defective PKA Signaling in Cushing's SyndromeR01DK119192 · NIDDK · UNIVERSITY OF WASHINGTON · PI John D Scott · 2018 to 2026
$4.4M
AKAP Modulation of Renal SignalingR01DK119186 · NIDDK · UNIVERSITY OF WASHINGTON · PI SCOTT, JOHN D · 2019 to 2022
$1.5M
MOLECULAR ANALYSIS OF PKA-ANCHORING PROTEIN INTERACTIONR01GM048231 · NIGMS · OREGON HEALTH AND SCIENCE UNIVERSITY · PI SCOTT, JOHN D · 1992 to 2003
$858k
AKAP Integration of Phosphorylation and Ubiquitin SignalingF32HL160558 · NHLBI · UNIVERSITY OF WASHINGTON · PI COLLINS, KERRIE B · 2022 to 2022
$70k
NHLBI NIH HHS F32 HL160558NHLBI NIH HHS HL007828NHLBI NIH HHS HL160558NHLBI NIH HHS T32 HL007828NIDDK NIH HHS DK119186NIDDK NIH HHS DK119192NIDDK NIH HHS R01 DK119186NIDDK NIH HHS R01 DK119192NIGMS NIH HHS R01 GM048231NIH HHS R01DK119186NIH HHS R01DK119192
6 · The paper itself

Abstract

Protein phosphorylation is a fundamental element of cell signaling. First discovered as a biochemical switch in glycogen metabolism, we now know that this posttranslational modification permeates all aspects of cellular behavior. In humans, over 540 protein kinases attach phosphate to acceptor amino acids, whereas around 160 phosphoprotein phosphatases remove phosphate to terminate signaling. Aberrant phosphorylation underlies disease, and kinase inhibitor drugs are increasingly used clinically as targeted therapies. Specificity in protein phosphorylation is achieved in part because kinases and phosphatases are spatially organized inside cells. A prototypic example is compartmentalization of the cyclic adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase A through association with A-kinase anchoring proteins. This configuration creates autonomous signaling islands where the anchored kinase is constrained in proximity to activators, effectors, and selected substates. This article primarily focuses on A kinase anchoring protein (AKAP) signaling in the heart with an emphasis on anchoring proteins that spatiotemporally coordinate excitation-contraction coupling and hypertrophic responses.

Indexed as

A Kinase Anchor ProteinsCyclic AMP-Dependent Protein KinasesHumansPhosphorylationProtein KinasesSignal TransductionA Kinase Anchor ProteinsCyclic AMP-Dependent Protein KinasesProtein KinasesA kinase anchoring proteinscardiac biologycell signalingprotein kinase Aprotein phosphorylationspatial biology

Identifiers

PMID36177749
PMCPMC10049969
OpenAlexW4298087202

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.