Evidence map›Paper›PMID 37900285›Full record

ReviewFrontiers in cell and developmental biology2023

Insights from the protein interaction Universe of the multifunctional "Goldilocks" kinase DYRK1A.

Varsha Ananthapadmanabhan, Kathryn H Shows, Amanda J Dickinson, Larisa Litovchick

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in cell and developmental biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

11 citing papers in PubMed, 18 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

4 authors at 3 institutions in 1 country.

Varsha AnanthapadmanabhanDepartment of Internal Medicine, Division of Hematology, Oncology and Palliative Care, Virginia Commonwealth University, Richmond, VA, United States.
Kathryn H ShowsDepartment of Biology, Virginia State University, Petersburg, VA, United States.
Amanda J DickinsonDepartment of Biology, Virginia Commonwealth University, Richmond, VA, United States.
Larisa LitovchickDepartment of Internal Medicine, Division of Hematology, Oncology and Palliative Care, Virginia Commonwealth University, Richmond, VA, United States.
Virginia Commonwealth University · USVirginia Cancer Institute · USVirginia State University · US

Funding

SUCCEED Cancer Research Education Program (CREP)P20CA264067 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI MOSAVEL, MAGHBOEBA · 2021 to 2024
$845k
SUCCEED Pilot Project 2P20CA264068 · NCI · VIRGINIA STATE UNIVERSITY · PI FAISON, MILTON O, ROBERTS, DANIEL M. · 2021 to 2024
$843k
DYRK1A interaction network in development and diseaseR21HD105144 · NICHD · VIRGINIA COMMONWEALTH UNIVERSITY · PI DICKINSON, AMANDA JANE, LITOVCHICK, LARISA · 2022 to 2022
$414k
NCI NIH HHS P20 CA264067NCI NIH HHS P20 CA264068NICHD NIH HHS R21 HD105144
6 · The paper itself

Abstract

Human Dual specificity tyrosine (Y)-Regulated Kinase 1A (DYRK1A) is encoded by a dosage-dependent gene located in the Down syndrome critical region of human chromosome 21. The known substrates of DYRK1A include proteins involved in transcription, cell cycle control, DNA repair and other processes. However, the function and regulation of this kinase is not fully understood, and the current knowledge does not fully explain the dosage-dependent function of this kinase. Several recent proteomic studies identified DYRK1A interacting proteins in several human cell lines. Interestingly, several of known protein substrates of DYRK1A were undetectable in these studies, likely due to a transient nature of the kinase-substrate interaction. It is possible that the stronger-binding DYRK1A interacting proteins, many of which are poorly characterized, are involved in regulatory functions by recruiting DYRK1A to the specific subcellular compartments or distinct signaling pathways. Better understanding of these DYRK1A-interacting proteins could help to decode the cellular processes regulated by this important protein kinase during embryonic development and in the adult organism. Here, we review the current knowledge of the biochemical and functional characterization of the DYRK1A protein-protein interaction network and discuss its involvement in human disease.

Indexed as

DCAF7developmentFAM117BFAM53CGLCCI1proteomic analysisRNF169TROAP

Identifiers

PMID37900285
PMCPMC10600473
OpenAlexW4387573023

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.