Evidence map›Paper›PMID 28256131›Full record

ReviewChemical reviews2017

YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.

Brandon J Burkhart, Christopher J Schwalen, Greg Mann, James H Naismith, Douglas A Mitchell

Abstract readReview
In one paragraph

Review in Chemical reviews, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
17.4field-weighted citation impact, top 1% 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

105 citing papers in PubMed, 217 citations in OpenAlex.

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45 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 4 countries.

Brandon J Burkhart
Christopher J Schwalen
Greg MannBiomedical Science Research Complex, University of St Andrews , BSRC North Haugh, St Andrews KY16 9ST, United Kingdom.
James H NaismithBiomedical Science Research Complex, University of St Andrews , BSRC North Haugh, St Andrews KY16 9ST, United Kingdom.ORCID http://orcid.org/0000-0001-6744-5061
University of Illinois Urbana-Champaign · USUniversity of St Andrews · GBCenter for Genomic Science · IT

Funding

Training Program in Chemistry-Interface with BiologyT32GM070421 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HERGENROTHER, PAUL · 2005 to 2019
$5.4M
Enzyme Chemistry and Biological Function of RiPP-like Modifications.R01GM097142 · NIGMS · VANDERBILT UNIVERSITY · PI MITCHELL, DOUGLAS ALAN · 2012 to 2024
$4.1M
A common denominator of pathogenesis; a rare opportunity for novel therapeutic deDP2OD008463 · OD · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI MITCHELL, DOUGLAS ALAN · 2011 to 2011
$2.4M
European Research Council 339367NIGMS NIH HHS R01 GM097142NIGMS NIH HHS T32 GM070421NIH HHS DP2 OD008463
6 · The paper itself

Abstract

With advances in sequencing technology, uncharacterized proteins and domains of unknown function (DUFs) are rapidly accumulating in sequence databases and offer an opportunity to discover new protein chemistry and reaction mechanisms. The focus of this review, the formerly enigmatic YcaO superfamily (DUF181), has been found to catalyze a unique phosphorylation of a ribosomal peptide backbone amide upon attack by different nucleophiles. Established nucleophiles are the side chains of Cys, Ser, and Thr which gives rise to azoline/azole biosynthesis in ribosomally synthesized and posttranslationally modified peptide (RiPP) natural products. However, much remains unknown about the potential for YcaO proteins to collaborate with other nucleophiles. Recent work suggests potential in forming thioamides, macroamidines, and possibly additional post-translational modifications. This review covers all knowledge through mid-2016 regarding the biosynthetic gene clusters (BGCs), natural products, functions, mechanisms, and applications of YcaO proteins and outlines likely future research directions for this protein superfamily.

Indexed as

Protein Processing, Post-TranslationalAnimalsAzolesHumansPeptidesStructure-Activity RelationshipAzolesPeptides

Identifiers

PMID28256131
PMCPMC5406272
OpenAlexW2593608868

What OpenQuestion holds

Textmetadata
LicenceTDM
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.