Evidence map›Paper›PMID 26236937›Full record

ArticleNature chemical biology2015

Analysis of 51 cyclodipeptide synthases reveals the basis for substrate specificity.

Isabelle B Jacques, Mireille Moutiez, Jerzy Witwinowski, Emmanuelle Darbon, Cécile Martel, Jérôme Seguin, Emmanuel Favry, Robert Thai, Alain Lecoq, Steven Dubois and 3 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.4field-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

36 citing papers in PubMed, 77 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

13 authors at 2 institutions in 1 country.

Isabelle B JacquesCommissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie et de Technologies de Saclay (iBiTec-S), Service d'Ingénierie Moléculaire des Protéines, Gif-sur-Yvette, France.
Mireille MoutiezCommissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie et de Technologies de Saclay (iBiTec-S), Service d'Ingénierie Moléculaire des Protéines, Gif-sur-Yvette, France.
Jerzy WitwinowskiUniversité Paris-Sud, Centre National de la Recherche Scientifique (CNRS), Unité Mixte de Recherche (UMR) 8621, Institut de Génétique et Microbiologie, Orsay, France.
Emmanuelle DarbonUniversité Paris-Sud, Centre National de la Recherche Scientifique (CNRS), Unité Mixte de Recherche (UMR) 8621, Institut de Génétique et Microbiologie, Orsay, France.
Cécile MartelUniversité Paris-Sud, Centre National de la Recherche Scientifique (CNRS), Unité Mixte de Recherche (UMR) 8621, Institut de Génétique et Microbiologie, Orsay, France.
Jérôme SeguinCommissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie et de Technologies de Saclay (iBiTec-S), Service d'Ingénierie Moléculaire des Protéines, Gif-sur-Yvette, France.
Emmanuel FavryCommissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie et de Technologies de Saclay (iBiTec-S), Service d'Ingénierie Moléculaire des Protéines, Gif-sur-Yvette, France.
Robert ThaiCommissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie et de Technologies de Saclay (iBiTec-S), Service d'Ingénierie Moléculaire des Protéines, Gif-sur-Yvette, France.
Alain LecoqCommissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie et de Technologies de Saclay (iBiTec-S), Service d'Ingénierie Moléculaire des Protéines, Gif-sur-Yvette, France.
Steven DuboisCommissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie et de Technologies de Saclay (iBiTec-S), Service d'Ingénierie Moléculaire des Protéines, Gif-sur-Yvette, France.
Jean-Luc PernodetUniversité Paris-Sud, Centre National de la Recherche Scientifique (CNRS), Unité Mixte de Recherche (UMR) 8621, Institut de Génétique et Microbiologie, Orsay, France.ORCID 0000000261297093
Muriel GondryCommissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie et de Technologies de Saclay (iBiTec-S), Service d'Ingénierie Moléculaire des Protéines, Gif-sur-Yvette, France.
Pascal BelinCommissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie et de Technologies de Saclay (iBiTec-S), Service d'Ingénierie Moléculaire des Protéines, Gif-sur-Yvette, France.
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclodipeptide synthases (CDPSs) constitute a family of peptide bond-forming enzymes that use aminoacyl-tRNAs for the synthesis of cyclodipeptides. Here, we describe the activity of 41 new CDPSs. We also show that CDPSs can be classified into two main phylogenetically distinct subfamilies characterized by specific functional subsequence signatures, named NYH and XYP. All 11 previously characterized CDPSs belong to the NYH subfamily, suggesting that further special features may be yet to be discovered in the other subfamily. CDPSs synthesize a large diversity of cyclodipeptides made up of 17 proteinogenic amino acids. The identification of several CDPSs having the same specificity led us to determine specificity sequence motifs that, in combination with the phylogenetic distribution of CDPSs, provide a first step toward being able to predict the cyclodipeptides synthesized by newly discovered CDPSs. The determination of the activity of ten more CDPSs with predicted functions constitutes a first experimental validation of this predictive approach.

Indexed as

Amino Acid MotifsBacterial ProteinsComputational BiologyCyclizationDatabases, GeneticDipeptidesEscherichia coliFungal ProteinsGene ExpressionMolecular Sequence DataPeptide Biosynthesis, Nucleic Acid-IndependentPeptides, CyclicPeptide SynthasesPhylogenyProtein Structure, TertiaryRecombinant ProteinsBacterial ProteinsDipeptidesFungal ProteinsPeptides, CyclicPeptide SynthasesRecombinant ProteinsRNA, Transfer, Amino Acyl

Identifiers

PMID26236937
OpenAlexW1151780217

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.