Evidence map›Paper›PMID 30593505›Full record

ArticleThe Journal of biological chemistry2019

An internal ribosome entry site in the coding region of tyrosyl-DNA phosphodiesterase 2 drives alternative translation start.

Annie C Chou, Aaron Aslanian, Huaiyu Sun, Tony Hunter

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. 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
0.5field-weighted citation impact, top 37% 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, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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 1 institution in 1 country.

Annie C ChouFrom the Graduate Program in Biomedical Sciences, University of California, San Diego, La Jolla, California 92093 and.
Aaron Aslanianthe Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037.
Huaiyu Sunthe Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037.ORCID 0000-0002-7181-8112
Tony Hunterthe Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037 hunter@salk.edu.
Salk Institute for Biological Studies · US

Funding

Viral Vector Core (VVC)P30CA014195 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI Ye Zheng · 1985 to 2026
$82.8M
SOMATIC CELL CYCLE REGULATION BY PHOSPHORYLATIONR01CA080100 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI HUNTER, TONY R. · 1999 to 2018
$13.1M
SIGNAL TRANSDUCTION BY TYROSINE PHOSPHORYLATIONR01CA082683 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI HUNTER, TONY R. · 1999 to 2019
$12.2M
Contemporary Approaches to Cancer Cell Signaling and CommunicationT32CA009523 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DONOGHUE, DANIEL J, YANG, JING · 1985 to 2025
$12.1M
Salk Institute for Biological Studies NINDS Center Core GrantP30NS072031 · NINDS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI O'LEARY, DENNIS D · 2011 to 2015
$4.2M
Regulation of Receptor Tyrosine KinasesR01GM065490 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI DONOGHUE, DANIEL J · 2002 to 2005
$1.0M
NCI NIH HHS P30 CA014195NCI NIH HHS R01 CA080100NCI NIH HHS R01 CA082683NCI NIH HHS T32 CA009523NIGMS NIH HHS R01 GM065490NINDS NIH HHS P30 NS072031
6 · The paper itself

Abstract

Tyrosyl-DNA phosphodiesterase 2 (TDP2) is a multifunctional protein that has been implicated in a myriad of cellular pathways. Although most well-known for its phosphodiesterase activity removing stalled topoisomerase 2 from DNA, TDP2 has also been shown to interact with both survival and apoptotic mitogen-activated protein kinase (MAPK) signaling cascades. Moreover, it facilitates enterovirus replication and has been genetically linked to neurological disorders ranging from Parkinson's disease to dyslexia. To accurately evaluate TDP2 as a therapeutic target, we need to understand how TDP2 performs such a wide diversity of functions. Here, we use cancer cell lines modified with CRISPR/Cas9 or stably-expressed

Indexed as

Alternative SplicingGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticAmino Acid SequenceDNA-Binding ProteinsHumansInternal Ribosome Entry SitesNeoplasmsNuclear ProteinsPeptide Chain Initiation, TranslationalPhosphoric Diester HydrolasesProtein IsoformsRibosomesSequence HomologyTranscription FactorsTumor Cells, CulturedDNA-Binding ProteinsInternal Ribosome Entry SitesNuclear ProteinsPhosphoric Diester HydrolasesProtein IsoformsTDP2 protein, humanTranscription FactorsUbiquitinalternative translation initiation startDNA repaireukaryotic translation initiationinternal ribosomal entry site (IRES)phosphodiesterasetranslationtranslation controltranslation initiationtranslation regulationtyrosyl-DNA phosphodiesterase 2 (TDP2)

Identifiers

PMID30593505
PMCPMC6393593
OpenAlexW2906691277

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.