Evidence map›Paper›PMID 22483104›Full record

ArticleStructure (London, England : 1993)2012

Phosphorylation meets proteolysis.

Martin Renatus, Christopher J Farady

Open access · bronzeAbstract readComment
PubMed Publisher
In one paragraph

Article in Structure (London, England : 1993), 2012. 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
–field-weighted citation impact, top 90% 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, 4 citations in OpenAlex.

  1. Article
  2. Molecular and cellular regulation of human glucokinase.Archives of biochemistry and biophysics · 2019
    Review
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Martin RenatusNovartis Institutes for BioMedical Research, Forum 1, Novartis Campus, CH-4002 Basel, Switzerland. martin.renatus@novartis.com
Christopher J Farady
Novartis (Switzerland) · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation is a reversible post-translational modification that regulates many proteins and enzymes, including proteases, as shown by two recent publications. Huang and colleagues and Velázquez-Delgado and Hardy (this issue of Structure) describe how phosphorylation activates the protease activity of the deubiquitinating enzyme DUBA and how it inhibits caspase-6, respectively.

Identifiers

PMID22483104
OpenAlexW2058372471

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.