Evidence map›Paper›PMID 29703734›Full record

ArticleApplied and environmental microbiology2018

An ATP-Dependent Ligase with Substrate Flexibility Involved in Assembly of the Peptidyl Nucleoside Antibiotic Polyoxin.

Rong Gong, Jianzhao Qi, Pan Wu, You-Sheng Cai, Hongmin Ma, Yang Liu, He Duan, Meng Wang, Zixin Deng, Neil P J Price and 1 more

Abstract read
In one paragraph

Article in Applied and environmental microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

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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

11 authors.

Rong GongKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Jianzhao QiKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Pan WuKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
You-Sheng CaiKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Hongmin MaKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Yang LiuKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
He DuanKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Meng WangKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Zixin DengKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Neil P J PriceAgricultural Research Service, U.S. Department of Agriculture, National Center for Agricultural Utilization Research, Peoria, Illinois, USA.
Wenqing ChenKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, China wqchen@whu.edu.cn.ORCID 0000-0003-2557-8960

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyoxin (POL) is an unusual peptidyl nucleoside antibiotic, in which the peptidyl moiety and nucleoside skeleton are linked by an amide bond. However, their biosynthesis remains poorly understood. Here, we report the deciphering of PolG as an ATP-dependent ligase responsible for the assembly of POL. A

Indexed as

Adenosine TriphosphateAnti-Bacterial AgentsAntifungal AgentsBinding SitesBiosynthetic PathwaysLigasesModels, MolecularMultigene FamilyOxamic AcidPyrimidine NucleosidesStreptomycesStructural Homology, ProteinSubstrate SpecificitySynthetic BiologyAdenosine TriphosphateAnti-Bacterial AgentsAntifungal Agentscarbamoylpolyoxamic acidLigasesOxamic AcidpolyoxinPyrimidine Nucleosidesamide bondATP-dependent ligasepeptidyl nucleoside antibioticpolyoxinsynthetic biology

Identifiers

PMID29703734
PMCPMC6007123

What OpenQuestion holds

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Registered trials

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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.