Evidence map›Paper›PMID 21397192›Full record

ArticleStructure (London, England : 1993)2011

Interferon-inducible protein 16: insight into the interaction with tumor suppressor p53.

Jack C C Liao, Robert Lam, Vaclav Brazda, Shili Duan, Mani Ravichandran, Justin Ma, Ting Xiao, Wolfram Tempel, Xiaobing Zuo, Yun-Xing Wang and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

62 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
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  10. Article
  11. Cells · 2023
    Article
  12. Article
  13. DNA and RNA Binding Proteins: From Motifs to Roles in Cancer.International journal of molecular sciences · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Review

2 more citing papers are in PubMed but not listed here.

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

12 authors at 7 institutions in 3 countries.

Jack C C LiaoCampbell Family Cancer Research Institute, Ontario Cancer Institute, University Health Network, Toronto, ON M5G 2C4, Canada.
Robert Lam
Vaclav Brazda
Shili Duan
Mani Ravichandran
Justin Ma
Ting Xiao
Wolfram Tempel
Xiaobing Zuo
Yun-Xing Wang
Nickolay Y Chirgadze
Cheryl H Arrowsmith
University Health Network · CAUniversity of Toronto · CAStructural Genomics Consortium · CACzech Academy of Sciences · CZFrederick National Laboratory for Cancer Research · USNational Institutes of Health · USOntario Institute for Cancer Research · CA

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI MONTELIONE, GAETANO T · 2010 to 2014
$36.9M
STRUCTURAL GENOMICS OF EUKARYOTIC MODEL ORGANISMSP50GM062413 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MONTELIONE, GAETANO T · 2000 to 2004
$33.5M
Search for the Structural Basis of Biomacromolecular Function and ActivityZIABC010379 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WANG, YUN XING M · 2009 to 2025
$30.4M
CIHRNIGMS NIH HHS GM67965NIGMS NIH HHS P50 GM062413NIGMS NIH HHS P50-GM62413-01NIGMS NIH HHS U54 GM094597Wellcome Trust
6 · The paper itself

Abstract

IFI16 is a member of the interferon-inducible HIN-200 family of nuclear proteins. It has been implicated in transcriptional regulation by modulating protein-protein interactions with p53 tumor suppressor protein and other transcription factors. However, the mechanisms of interaction remain unknown. Here, we report the crystal structures of both HIN-A and HIN-B domains of IFI16 determined at 2.0 and 2.35 Å resolution, respectively. Each HIN domain comprises a pair of tightly packed OB-fold subdomains that appear to act as a single unit. We show that both HIN domains of IFI16 are capable of enhancing p53-DNA complex formation and transcriptional activation via distinctive means. HIN-A domain binds to the basic C terminus of p53, whereas the HIN-B domain binds to the core DNA-binding region of p53. Both interactions are compatible with the DNA-bound state of p53 and together contribute to the effect of full-length IFI16 on p53-DNA complex formation and transcriptional activation.

Indexed as

Binding SitesCell Line, TumorCrystallizationCrystallography, X-RayDNADNA-Binding ProteinsEscherichia coliHumansInterferonsModels, MolecularNuclear ProteinsPhosphoproteinsProtein BindingProtein Interaction Domains and MotifsRecombinant ProteinsTranscriptional ActivationDNADNA-Binding ProteinsIFI16 protein, humanInterferonsNuclear ProteinsPhosphoproteinsRecombinant ProteinsTumor Suppressor Protein p53

Identifiers

PMID21397192
PMCPMC3760383
OpenAlexW2002934916

What OpenQuestion holds

Textmetadata
LicenceTDM
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.