Evidence map›Paper›PMID 34335956›Full record

ArticleTheranostics2021

STK39 promotes breast cancer invasion and metastasis by increasing SNAI1 activity upon phosphorylation.

Zhaoping Qiu, Bo Dong, Weijie Guo, Rychahou Piotr, Greg Longmore, Xiuwei Yang, Zhiyong Yu, Jiong Deng, B Mark Evers, Yadi Wu

Open access · goldAbstract read
In one paragraph

Article in Theranostics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 17 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

10 authors at 1 institution in 1 country.

Zhaoping QiuDepartment of Pharmacology & Nutritional Sciences, University of Kentucky, College of Medicine, Lexington, KY 40506, United States.
Bo DongDepartment of Pharmacology & Nutritional Sciences, University of Kentucky, College of Medicine, Lexington, KY 40506, United States.
Weijie GuoMarkey Cancer Center, the University of Kentucky, College of Medicine, Lexington, KY 40506, United States.
Rychahou PiotrDepartment of Surgery, University of Kentucky, College of Medicine, Lexington, KY 40506, United States.
Greg LongmoreDepartment of Medicine (Oncology), Cell Biology and Physiology, Washington University, St. Louis.
Xiuwei YangDepartment of Pharmacology & Nutritional Sciences, University of Kentucky, College of Medicine, Lexington, KY 40506, United States.
Zhiyong YuDepartment of Oncology, Shandong Cancer Hospital Affiliated to Shandong University, Shandong Academy of Medical Sciences, Jinan, Shandong, China.
Jiong DengKey Laboratory of Cell Differentiation and Apoptosis of Chinese Minister of Education, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
B Mark EversDepartment of Surgery, University of Kentucky, College of Medicine, Lexington, KY 40506, United States.
Yadi WuDepartment of Pharmacology & Nutritional Sciences, University of Kentucky, College of Medicine, Lexington, KY 40506, United States.
Shanghai Jiao Tong University · CN

Funding

University of Kentucky Markey Cancer Center Support Grant ECIA SupplementP30CA177558 · NCI · UNIVERSITY OF KENTUCKY · PI Bernard Mark Evers · 2013 to 2026
$38.3M
University of Kentucky Center for Cancer MetabolismP20GM121327 · NIGMS · UNIVERSITY OF KENTUCKY · PI Jianhang Jia · 2017 to 2026
$25.0M
Tumor stromal effects of DDR2 in metastasis regulationR01CA223758 · NCI · WASHINGTON UNIVERSITY · PI LONGMORE, GREGORY D. · 2018 to 2022
$1.9M
Characterize the role of EBF1 in breast cancer progressionR01CA230758 · NCI · UNIVERSITY OF KENTUCKY · PI WU, YADI · 2018 to 2023
$1.7M
NCI NIH HHS P30 CA177558NCI NIH HHS R01 CA223758NCI NIH HHS R01 CA230758NIGMS NIH HHS P20 GM121327
6 · The paper itself

Abstract

SNAI1 is widely regarded as a master driver of epithelial-mesenchymal transition (EMT) and associated with breast cancer progression and metastasis. This pro-malignant role is strongly linked to posttranslational modification, especially phosphorylation, which controls its protein levels and subcellular localization. While multiple kinases are implicated in regulation of SNAI1 stability, the precise mechanism by which SNAI1 is stabilized in tumors remains to be fully elucidated.

Indexed as

AnimalsBreast NeoplasmsCell Line, TumorCell MovementEpithelial-Mesenchymal TransitionFemaleGene Expression Regulation, NeoplasticHumansMiceMice, SCIDNeoplasm InvasivenessPhosphorylationProtein Serine-Threonine KinasesSnail Family Transcription FactorsTranscription FactorsProtein Serine-Threonine KinasesSNAI1 protein, humanSnail Family Transcription FactorsSTK39 protein, humanTranscription FactorsEMTphosphorylationSNAI1stabilizationSTK39

Identifiers

PMID34335956
PMCPMC8315073
OpenAlexW3174396414

What OpenQuestion holds

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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 OpenQuestion graph.