Evidence map›Paper›PMID 31811090›Full record

ArticleThe Journal of biological chemistry2020

The regulatory protein 14-3-3β binds to the IQ motifs of myosin-IC independent of phosphorylation.

Huan-Hong Ji, E Michael Ostap

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 46% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. Putting the brakes on a myosin motor.The Journal of biological chemistry · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Huan-Hong JiPennsylvania Muscle Institute, Department of Physiology, and Center for Engineering Mechanobiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104.
E Michael OstapPennsylvania Muscle Institute, Department of Physiology, and Center for Engineering Mechanobiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104 ostap@pennmedicine.upenn.edu.
University of Pennsylvania · US

Funding

Molecular function of Myosin-lR37GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2016 to 2025
$5.3M
Molecular function of myosin-IR01GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 1998 to 2014
$4.4M
NIGMS NIH HHS R01 GM057247NIGMS NIH HHS R37 GM057247
6 · The paper itself

Abstract

Myosin-IC (Myo1c) has been proposed to function in delivery of glucose transporter type 4 (GLUT4)-containing vesicles to the plasma membrane in response to insulin stimulation. Current evidence suggests that, upon insulin stimulation, Myo1c is phosphorylated at Ser

Indexed as

14-3-3 ProteinsAmino Acid MotifsCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinDimerizationEgtazic AcidHumansMass SpectrometryMyosin Type IPhosphorylationProtein BindingRecombinant ProteinsUltracentrifugation14-3-3 ProteinsCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinEgtazic AcidMyo1c protein, mouseMyosin Type IRecombinant Proteins14-3-3 protein14-3-3βcalmodulin (CaM)cell motilitycell signalingcytoskeletonmolecular motormyo1cmyosinmyosin-IC

Identifiers

PMID31811090
PMCPMC7086031
OpenAlexW2993087884

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.