Evidence map›Paper›PMID 10958670›Full record

ArticleMolecular and cellular biology2000

HCF-1 amino- and carboxy-terminal subunit association through two separate sets of interaction modules: involvement of fibronectin type 3 repeats.

A C Wilson, M Boutros, K M Johnson, W Herr

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

30 citing papers in PubMed, 48 citations in OpenAlex.

  1. Identification of a Polypeptide Inhibitor ofJournal of the American Chemical Society · 2024
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  8. Review
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  11. HCF-1 self-association via an interdigitated Fn3 structure facilitates transcriptional regulatory complex formation.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  12. Article
  13. Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  14. Article
  15. Transcriptional coactivator HCF-1 couples the histone chaperone Asf1b to HSV-1 DNA replication components.Proceedings of the National Academy of Sciences of the United States of America · 2010
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  16. Article
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  20. Site-specific proteolysis of the transcriptional coactivator HCF-1 can regulate its interaction with protein cofactors.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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

4 authors at 2 institutions in 1 country.

A C WilsonCold Spring Harbor Laboratory, New York 11724, USA.
M Boutros
K M Johnson
W Herr
Cold Spring Harbor Laboratory · USNew York University · US

Funding

CELLULAR FUNCTIONS OF HCFR01GM054598 · NIGMS · COLD SPRING HARBOR LABORATORY · PI MYERS, MICHAEL P · 1996 to 2005
$1.2M
NIGMS NIH HHS GM54598NIGMS NIH HHS R01 GM054598
6 · The paper itself

Abstract

When herpes simplex virus infects permissive cells, the viral regulatory protein VP16 forms a specific complex with HCF-1, a preexisting nuclear protein involved in cell proliferation. The majority of HCF-1 in the cell is a complex of associated amino (HCF-1(N))- and carboxy (HCF-1(C))-terminal subunits that result from an unusual proteolytic processing of a large precursor polypeptide. Here, we have characterized the structure and function of sequences required for HCF-1(N) and HCF-1(C) subunit association. HCF-1 contains two matched pairs of self-association sequences called SAS1 and SAS2. One of these matched association sequences, SAS1, consists of a short 43-amino-acid region of the HCF-1(N) subunit, which associates with a carboxy-terminal region of the HCF-1(C) subunit that is composed of a tandem pair of fibronectin type 3 repeats, a structural motif known to promote protein-protein interactions. Unexpectedly, the related protein HCF-2, which is not proteolyzed, also contains a functional SAS1 association element, suggesting that this element does not function solely to maintain HCF-1(N) and HCF-1(C) subunit association. HCF-1(N) subunits do not possess a nuclear localization signal. We show that, owing to a carboxy-terminal HCF-1 nuclear localization signal, HCF-1(C) subunits can recruit HCF-1(N) subunits to the nucleus.

Indexed as

Repetitive Sequences, Amino AcidAmino Acid SequenceBinding SitesCell LineCell Line, TransformedChromosome MappingConserved SequenceFibronectinsFungal ProteinsHerpes Simplex Virus Protein Vmw65HumansMolecular Sequence DataProteinsRecombinant Fusion ProteinsSequence Homology, Amino AcidTranscription FactorsFibronectinsFungal ProteinsHCFC2 protein, humanHerpes Simplex Virus Protein Vmw65ProteinsRecombinant Fusion ProteinsTranscription Factors

Identifiers

PMID10958670
PMCPMC86190
OpenAlexW2136206805

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.