Evidence map›Paper›PMID 21245151›Full record

ArticleThe Journal of biological chemistry2011

A multiprotein binding interface in an intrinsically disordered region of the tumor suppressor protein interferon regulatory factor-1.

Vikram Narayan, Petr Halada, Lenka Hernychová, Yuh Ping Chong, Jitka Žáková, Ted R Hupp, Borivoj Vojtesek, Kathryn L Ball

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

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  5. NFAT5, which protects against hypertonicity, is activated by that stress via structuring of its intrinsically disordered domain.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

8 authors at 4 institutions in 3 countries.

Vikram NarayanCRUK Interferon and Cell Signalling Group, Cell Signalling Unit, Edinburgh Cancer Research UK Centre, University of Edinburgh, Edinburgh EH4 2XR, United Kingdom.
Petr Halada
Lenka Hernychová
Yuh Ping Chong
Jitka Žáková
Ted R Hupp
Borivoj Vojtesek
Kathryn L Ball
University of Defence · CZEdinburgh Cancer Research · GBInstitute of Microbiology · BYMasaryk Memorial Cancer Institute · CZ

Funding

Cancer Research UK C377/A6355
6 · The paper itself

Abstract

The interferon-regulated transcription factor and tumor suppressor protein IRF-1 is predicted to be largely disordered outside of the DNA-binding domain. One of the advantages of intrinsically disordered protein domains is thought to be their ability to take part in multiple, specific but low affinity protein interactions; however, relatively few IRF-1-interacting proteins have been described. The recent identification of a functional binding interface for the E3-ubiquitin ligase CHIP within the major disordered domain of IRF-1 led us to ask whether this region might be employed more widely by regulators of IRF-1 function. Here we describe the use of peptide aptamer-based affinity chromatography coupled with mass spectrometry to define a multiprotein binding interface on IRF-1 (Mf2 domain; amino acids 106-140) and to identify Mf2-binding proteins from A375 cells. Based on their function as known transcriptional regulators, a selection of the Mf2 domain-binding proteins (NPM1, TRIM28, and YB-1) have been validated using in vitro and cell-based assays. Interestingly, although NPM1, TRIM28, and YB-1 all bind to the Mf2 domain, they have differing amino acid specificities, demonstrating the degree of combinatorial diversity and specificity available through linear interaction motifs.

Indexed as

Gene Expression RegulationAmino Acid MotifsAmino Acid SequenceCell Line, TumorChromatography, AffinityDNA-Binding ProteinsHumansInterferon Regulatory Factor-1Molecular Sequence DataNuclear ProteinsNucleophosminPeptidesProtein BindingProtein Interaction MappingRepressor ProteinsSequence Homology, Amino AcidDNA-Binding ProteinsInterferon Regulatory Factor-1NPM1 protein, humanNuclear ProteinsNucleophosminPeptidesRepressor ProteinsTRIM28 protein, humanTripartite Motif-Containing Protein 28Ubiquitin-Protein LigasesY-Box-Binding Protein 1YBX1 protein, human

Identifiers

PMID21245151
PMCPMC3077630
OpenAlexW2094983680

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.