Evidence map›Paper›PMID 28362432›Full record

ArticleCell death and differentiation2017

Regulation of transcriptional activators by DNA-binding domain ubiquitination.

Vivien Landré, Bhindu Revi, Maria Gil Mir, Chandra Verma, Ted R Hupp, Nick Gilbert, Kathryn L Ball

Open access · bronzeAbstract read
In one paragraph

Article in Cell death and differentiation, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

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  8. High-Resolution Imaging of Human Cancer Proteins Using Microprocessor Materials.Chembiochem : a European journal of chemical biology · 2022
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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

7 authors at 3 institutions in 3 countries.

Vivien LandréCell Signalling Unit, ECRC, IGMM, University of Edinburgh, Edinburgh EH4 2XR, UK.
Bhindu ReviCell Signalling Unit, ECRC, IGMM, University of Edinburgh, Edinburgh EH4 2XR, UK.
Maria Gil MirCell Signalling Unit, ECRC, IGMM, University of Edinburgh, Edinburgh EH4 2XR, UK.
Chandra VermaBioinformatics Institute (A*STAR), 30 Biopolis Street, 07-01 Matrix Singapore 138671, Singapore.
Ted R HuppCell Signalling Unit, ECRC, IGMM, University of Edinburgh, Edinburgh EH4 2XR, UK.
Nick GilbertMRC Human Genetics Unit MRC, IGMM, University of Edinburgh, Edinburgh EH4 2XR, UK.
Kathryn L BallCell Signalling Unit, ECRC, IGMM, University of Edinburgh, Edinburgh EH4 2XR, UK.
University of Edinburgh · GBAgency for Science, Technology and Research · SGInstitute of Genetics and Cancer · GB

Funding

Medical Research Council MR/J00913X/1
6 · The paper itself

Abstract

Ubiquitin is a key component of the regulatory network that maintains gene expression in eukaryotes, yet the molecular mechanism(s) by which non-degradative ubiquitination modulates transcriptional activator (TA) function is unknown. Here endogenous p53, a stress-activated transcription factor required to maintain health, is stably monoubiquitinated, following pathway activation by IR or Nutlin-3 and localized to the nucleus where it becomes tightly associated with chromatin. Comparative structure-function analysis and in silico modelling demonstrate a direct role for DNA-binding domain (DBD) monoubiquitination in TA activation. When attached to the DBD of either p53, or a second TA IRF-1, ubiquitin is orientated towards, and makes contact with, the DNA. The contact is made between a predominantly cationic surface on ubiquitin and the anionic DNA. Our data demonstrate an unexpected role for ubiquitin in the mechanism of TA-activity enhancement and provides insight into a new level of transcriptional regulation.

Indexed as

Cell Line, TumorChromatinCrystallography, X-RayDNAHumansImidazolesInterferon Regulatory Factor-1LymphocytesMelanocytesModels, MolecularPiperazinesProtein BindingProtein DomainsProto-Oncogene Proteins c-mdm2ThermodynamicsTrans-ActivatorsChromatinDNAImidazolesInterferon Regulatory Factor-1MDM2 protein, humannutlin 3PiperazinesProto-Oncogene Proteins c-mdm2RCHY1 protein, humanTrans-ActivatorsTumor Suppressor Protein p53UbiquitinUbiquitin-Protein Ligases

Identifiers

PMID28362432
PMCPMC5423116
OpenAlexW2598830799

What OpenQuestion holds

Textmetadata
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.