Evidence map›Paper›PMID 30427558›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2019

Selective Inhibitors of a Human Prolyl Hydroxylase (OGFOD1) Involved in Ribosomal Decoding.

Cyrille C Thinnes, Christopher T Lohans, Martine I Abboud, Tzu-Lan Yeh, Anthony Tumber, Radosław P Nowak, Martin Attwood, Matthew E Cockman, Udo Oppermann, Christoph Loenarz and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.2field-weighted citation impact, top 48% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. 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

11 authors at 2 institutions in 3 countries.

Cyrille C ThinnesDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, UK.ORCID http://orcid.org/0000-0002-8619-9537
Christopher T LohansDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, UK.ORCID http://orcid.org/0000-0003-1094-0349
Martine I AbboudDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, UK.ORCID http://orcid.org/0000-0003-2141-5988
Tzu-Lan YehDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, UK.ORCID http://orcid.org/0000-0002-6265-6262
Anthony TumberDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, UK.ORCID http://orcid.org/0000-0003-1958-8353
Radosław P NowakStructural Genomics Consortium, University of Oxford, Headington, OX3 7DQ, UK.
Martin AttwoodCentre for Cellular and Molecular Physiology, University of Oxford, Oxford, OX3 7BN, UK.
Matthew E CockmanCentre for Cellular and Molecular Physiology, University of Oxford, Oxford, OX3 7BN, UK.ORCID http://orcid.org/0000-0002-3310-4821
Udo OppermannStructural Genomics Consortium, University of Oxford, Headington, OX3 7DQ, UK.ORCID http://orcid.org/0000-0001-9984-5342
Christoph LoenarzDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, UK.ORCID http://orcid.org/0000-0002-8843-2531
Christopher J SchofieldDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, UK.ORCID http://orcid.org/0000-0002-0290-6565
University of Oxford · GBUniversity of Freiburg · DE

Funding

Biotechnology and Biological Sciences Research Council BB/D011523/1Biotechnology and Biological Sciences Research Council BB/L009846/1Cancer Research UK 18245Cancer Research UK 23900Cancer Research UK 28285Cancer Research UK C5255/A16466Versus Arthritis 20522Wellcome Trust 106244/Z/14/Z
6 · The paper itself

Abstract

Human prolyl hydroxylases are involved in the modification of transcription factors, procollagen, and ribosomal proteins, and are current medicinal chemistry targets. To date, there are few reports on inhibitors selective for the different types of prolyl hydroxylases. We report a structurally informed template-based strategy for the development of inhibitors selective for the human ribosomal prolyl hydroxylase OGFOD1. These inhibitors did not target the other human oxygenases tested, including the structurally similar hypoxia-inducible transcription factor prolyl hydroxylase, PHD2.

Indexed as

Prolyl-Hydroxylase InhibitorsProlyl HydroxylasesCarrier ProteinsDrug DesignHumansNuclear ProteinsRibosomesStructure-Activity RelationshipSubstrate SpecificityCarrier ProteinsNuclear ProteinsOGFOD1 protein, humanProlyl-Hydroxylase InhibitorsProlyl Hydroxylases2-oxoglutarate oxygenasebarbiturateepigeneticshistone demethylasesinhibitorsmedicinal chemistryOGFOD1

Identifiers

PMID30427558
PMCPMC6471485
OpenAlexW2901595602

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.