Evidence map›Paper›PMID 34163896›Full record

ArticleChemical science2020

Synthesis of 2-oxoglutarate derivatives and their evaluation as cosubstrates and inhibitors of human aspartate/asparagine-β-hydroxylase.

Lennart Brewitz, Yu Nakashima, Christopher J Schofield

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed, 20 citations in OpenAlex.

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  13. Human Oxygenase Variants Employing a Single Protein FeAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  14. Human Oxygenase Variants Employing a Single Protein FeAngewandte Chemie (International ed. in English) · 2021
    Article
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

3 authors at 1 institution in 1 country.

Lennart BrewitzChemistry Research Laboratory, University of Oxford 12 Mansfield Road OX1 3TA Oxford UK christopher.schofield@chem.ox.ac.uk.ORCID https://orcid.org/0000-0002-9465-777X
Yu NakashimaChemistry Research Laboratory, University of Oxford 12 Mansfield Road OX1 3TA Oxford UK christopher.schofield@chem.ox.ac.uk.
Christopher J SchofieldChemistry Research Laboratory, University of Oxford 12 Mansfield Road OX1 3TA Oxford UK christopher.schofield@chem.ox.ac.uk.ORCID https://orcid.org/0000-0002-0290-6565
University of Oxford · GB

Funding

Cancer Research UK 18245Cancer Research UK 28285Wellcome Trust
6 · The paper itself

Abstract

2-Oxoglutarate (2OG) is involved in biological processes including oxidations catalyzed by 2OG oxygenases for which it is a cosubstrate. Eukaryotic 2OG oxygenases have roles in collagen biosynthesis, lipid metabolism, DNA/RNA modification, transcriptional regulation, and the hypoxic response. Aspartate/asparagine-β-hydroxylase (AspH) is a human 2OG oxygenase catalyzing post-translational hydroxylation of Asp/Asn-residues in epidermal growth factor-like domains (EGFDs) in the endoplasmic reticulum. AspH is of chemical interest, because its Fe(ii) cofactor is complexed by two rather than the typical three residues. AspH is upregulated in hypoxia and is a prognostic marker on the surface of cancer cells. We describe studies on how derivatives of its natural 2OG cosubstrate modulate AspH activity. An efficient synthesis of C3- and/or C4-substituted 2OG derivatives, proceeding

Identifiers

PMID34163896
PMCPMC8179049
OpenAlexW3112796674

What OpenQuestion holds

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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.