Evidence map›Paper›PMID 25081059›Full record

ArticleCell research2014

"PEST control": regulation of molecular barcodes by tyrosine phosphatases.

Karen M Doody, Nunzio Bottini

Open access · bronzeAbstract readComment
In one paragraph

Article in Cell research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Karen M DoodyDivision of Cellular Biology, La Jolla Institute for Allergy and Immunology, La Jolla, CA 92037, USA.
Nunzio BottiniDivision of Cellular Biology, La Jolla Institute for Allergy and Immunology, La Jolla, CA 92037, USA.
La Jolla Institute for Immunology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The emerging concept of "molecular barcodes" refers to the dynamic combination of post-translational modifications, often of different nature (e.g., phosphorylation and ubiquitination) that gives rise to multiple forms of a protein which can relay distinct signals throughout a cell. In a recent Cell Research paper by Wang et al., the authors report that a PEST domain-containing tyrosine phosphatase, PTPN18, is able to regulate both phosphorylation and ubiquitination of the HER2 oncogene, barcoding HER2 for increased proteasomal degradation rather than for intracellular trafficking.

Indexed as

Catalytic DomainUbiquitinationErb-b2 Receptor Tyrosine KinasesFemaleHumansProtein Tyrosine Phosphatases, Non-ReceptorErb-b2 Receptor Tyrosine KinasesProtein Tyrosine Phosphatases, Non-Receptor

Identifiers

PMID25081059
PMCPMC4152731
OpenAlexW2316062847

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.