Evidence map›Paper›PMID 26991100›Full record

ArticleCell chemical biology2016

Posttranslational Peptide-Modification Enzymes in Action: Key Roles for Leaders and Glutamate.

Manuel Montalbán-López, Oscar P Kuipers

Open access · bronzeAbstract readComment
PubMed Publisher
In one paragraph

Article in Cell chemical biology, 2016. 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
0.9field-weighted citation impact, top 22% 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, 6 citations in OpenAlex.

  1. Review
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Manuel Montalbán-LópezDepartment of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Nijenborgh 7, 9747 AG Groningen, the Netherlands.
Oscar P KuipersDepartment of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Nijenborgh 7, 9747 AG Groningen, the Netherlands. Electronic address: o.p.kuipers@rug.nl.
University of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this issue of Cell Chemical Biology, Ortega et al. (2016) determine the structure of another lantibiotic dehydratase with a tRNA(Glu)-dependent mechanism of modification. Moreover, they identify a common recognition motif involved in leader peptide binding in a number of different peptide-modification enzymes. These findings open up new mining possibilities and allow novel approaches in peptide engineering.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsBacterial ProteinsBacteriocinsBinding SitesEnzymesGenes, BacterialGlutamic AcidModels, MolecularMolecular Sequence DataPeptidesProtein BindingProtein EngineeringProtein Processing, Post-TranslationalProtein Sorting SignalsAnti-Bacterial AgentsBacterial ProteinsBacteriocinsEnzymesGlutamic AcidPeptidesProtein Sorting Signals

Identifiers

PMID26991100
OpenAlexW2299413472

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.