Evidence map›Paper›PMID 32994222›Full record

ArticleThe Journal of biological chemistry2020

Increasing kinase domain proximity promotes MST2 autophosphorylation during Hippo signaling.

Thao Tran, Jaba Mitra, Taekjip Ha, Jennifer M Kavran

Abstract 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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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.

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.

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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.

Thao TranDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA.
Jaba MitraDepartment of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA; Department of Biophysics and Biophysical Chemistry, School of Medicine, Johns Hopkins University, Baltimore, Maryland, USA.
Taekjip HaDepartment of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA; Department of Biophysics and Biophysical Chemistry, School of Medicine, Johns Hopkins University, Baltimore, Maryland, USA; T. C. Jenkins Department of Biophysics, Krieger School of Arts and Sciences, Johns Hopkins University, Baltimore, Maryland, USA; Department of Biomedical Engineering, Johns Hopkins University, Baltimore, Maryland, USA; Howard Hughes Medical Institute, Baltimore, Maryland, USA.
Jennifer M KavranDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, USA; Department of Biophysics and Biophysical Chemistry, School of Medicine, Johns Hopkins University, Baltimore, Maryland, USA; Department of Biomedical Engineering, Johns Hopkins University, Baltimore, Maryland, USA; Department of Oncology, School of Medicine, Johns Hopkins University, Baltimore, Maryland, USA. Electronic address: jkavran@jhu.edu.

Funding

TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Single Molecule Studies of Nucleic Acids RemodelingR35GM122569 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Taekjip Ha · 2017 to 2026
$3.5M
Mechanistic studies of core Hippo pathway kinases-Equipment SupplementR01GM134000 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI KAVRAN, JENNIFER MARIE · 2019 to 2023
$1.7M
NCI NIH HHS T32 CA009110NIGMS NIH HHS R01 GM134000NIGMS NIH HHS R35 GM122569
6 · The paper itself

Abstract

The Hippo pathway plays an important role in developmental biology, mediating organ size by controlling cell proliferation through the activity of a core kinase cassette. Multiple upstream events activate the pathway, but how each controls this core kinase cassette is not fully understood. Activation of the core kinase cassette begins with phosphorylation of the kinase MST1/2 (also known as STK3/4). Here, using a combination of

Indexed as

Protein MultimerizationEnzyme ActivationHEK293 CellsHippo KinasesHippo Signaling PathwayHumansPhosphorylationProtein DomainsProtein Serine-Threonine KinasesSerine-Threonine Kinase 3Signal TransductionHippo KinasesProtein Serine-Threonine KinasesSerine-Threonine Kinase 3STK3 protein, humanenzyme mechanismHippo pathwayMST1MST1 (mammalian sterile 20-like kinase 1)MST2MST2 (mammalian sterile 20-like kinase 2)Salvador (sav)serine/threonine protein kinasesignal transduction

Identifiers

PMID32994222
PMCPMC7681014

What OpenQuestion holds

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Registered trials

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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.