Evidence map›Paper›PMID 32535199›Full record

ReviewCellular signalling2020

Phosphorylation of the mRNA cap-binding protein eIF4E and cancer.

Xiaotong Yang, Wu Zhong, Ruifeng Cao

Open access · greenAbstract readReview
In one paragraph

Review in Cellular signalling, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

48 citing papers in PubMed, 84 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

3 authors at 3 institutions in 2 countries.

Xiaotong YangSchool of Medicine, Tsinghua University, Beijing 100084, China; National Engineering Research Center for the Emergency Drug, Beijing Institute of Pharmacology and Toxicology, Beijing 100850, China; Department of Biomedical Sciences, University of Minnesota Medical School, Duluth, MN 55812, USA.
Wu ZhongNational Engineering Research Center for the Emergency Drug, Beijing Institute of Pharmacology and Toxicology, Beijing 100850, China. Electronic address: zhongwu@bmi.ac.cn.
Ruifeng CaoDepartment of Biomedical Sciences, University of Minnesota Medical School, Duluth, MN 55812, USA; Department of Neuroscience, University of Minnesota Medical School, Minneapolis, MN 55455, USA. Electronic address: rcao@umn.edu.
Capital Medical University · CNNational Institutes for Food and Drug Control · CNUniversity of Minnesota, Duluth · US

Funding

Mammalian target of rapamycin signaling and the suprachiasmatic circadian clockR01NS118026 · NINDS · UNIVERSITY OF MINNESOTA · PI CAO, RUIFENG (RAY) · 2020 to 2024
$1.8M
NINDS NIH HHS R01 NS118026
6 · The paper itself

Abstract

Dysregulated protein synthesis is frequently involved in oncogenesis and cancer progression. Translation initiation is thought to be the rate-limiting step in protein synthesis, and the mRNA 5' cap-binding protein eukaryotic translation initiation factor 4E (eIF4E) is a pivotal factor that initiates translation. The activities of eIF4E are regulated at multiple levels, one of which is through its phosphorylation at Serine 209 by the mitogen-activated protein kinase-interacting kinases (MNKs, including MNK1 and MNK2). Benefiting from novel mouse genetic tools and pharmacological MNK inhibitors, our understanding of a role for eIF4E phosphorylation in tumor biology and cancer therapy has greatly evolved in recent years. Importantly, recent studies have found that the level of eIF4E phosphorylation is frequently upregulated in a wide variety of human cancer types, and phosphorylation of eIF4E drives a number of important processes in cancer biology, including cell transformation, proliferation, apoptosis, metastasis and angiogenesis. The MNK-eIF4E axis is being assessed as a therapeutic target either alone or in combination with other therapies in different cancer models. As novel MNK inhibitors are being developed, experimental studies bring new hope to cure human cancers that are not responsive to traditional therapies. Herein we review recent progress on our understanding of a mechanistic role for phosphorylation of eIF4E in cancer biology and therapy.

Indexed as

Eukaryotic Initiation Factor-4EHumansNeoplasmsEIF4E protein, humanEukaryotic Initiation Factor-4ECancereIF4EMNKPhosphorylationTranslational control

Identifiers

PMID32535199
PMCPMC8049097
OpenAlexW3035669930

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.