Evidence map›Paper›PMID 31706681›Full record

ArticleBioorganic chemistry2020

Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles.

Tristan J Smart, Refaat B Hamed, Timothy D W Claridge, Christopher J Schofield

Open access · hybridAbstract read
In one paragraph

Article in Bioorganic chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

6 citing papers in PubMed, 18 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

4 authors at 2 institutions in 1 country.

Tristan J SmartChemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.
Refaat B HamedChemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom; School of Chemistry and Biosciences, Faculty of Life Sciences, University of Bradford, Richmond Rd, Bradford BD7 1DP, United Kingdom.
Timothy D W ClaridgeChemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.
Christopher J SchofieldChemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom. Electronic address: christopher.schofield@chem.ox.ac.uk.
University of Oxford · GBUniversity of Bradford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L009846/1Wellcome Trust
6 · The paper itself

Abstract

Studies on the substrate selectivity of recombinant ferrous-iron- and 2-oxoglutarate-dependent proline hydroxylases (PHs) reveal that they can catalyse the production of dihydroxylated 5-, 6-, and 7-membered ring products, and can accept bicyclic substrates. Ring-substituted substrate analogues (such hydroxylated and fluorinated prolines) are accepted in some cases. The results highlight the considerable, as yet largely untapped, potential for amino acid hydroxylases and other 2OG oxygenases in biocatalysis.

Indexed as

BiocatalysisBridged Bicyclo CompoundsMolecular StructureProlyl HydroxylasesSubstrate SpecificityBridged Bicyclo CompoundsProlyl Hydroxylases2-Oxoglutarate oxygenasesAmino acid oxidationBiocatalysisl-prolineProline hydroxylase

Identifiers

PMID31706681
PMCPMC6958525
OpenAlexW2981867710

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.