Evidence map›Paper›PMID 26745526›Full record

ArticleStructure (London, England : 1993)2016

PhnK: Another Piece of the Carbon-Phosphorus Lyase Puzzle.

David L Zechel

Abstract readComment
PubMed Publisher
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

David L ZechelDepartment of Chemistry, Queen's University, 90 Bader Lane, Kingston, ON K7L 3N6, Canada. Electronic address: dlzechel@chem.queensu.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite the fact that carbon-phosphorus lyase activity was first documented more than 50 years ago, we are yet to completely understand the details of how this enzyme system functions or what it looks like. In this issue of Structure, Yang et al. (2016) now provide a step forward with a view of how PhnK fits into the bigger picture of carbon-phosphorus lyase.

Indexed as

Models, MolecularEscherichia coli

Identifiers

What OpenQuestion holds

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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.