Evidence map›Paper›PMID 10920196›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Autocatalytic proteolysis of the transcription factor-coactivator C1 (HCF): a potential role for proteolytic regulation of coactivator function.

J L Vogel, T M Kristie

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. 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
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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
  12. Herpes simplex virus infections are arrested in Oct-1-deficient cells.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  13. Article
  14. Article
  15. Interaction of HCF-1 with a cellular nuclear export factor.The Journal of biological chemistry · 2002
    Article
  16. Article
  17. 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

2 authors at 1 institution in 1 country.

J L VogelLaboratory of Viral Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
T M Kristie
National Institutes of Health · US

Funding

HCF-1, A Mammalian Factor Controlling HSV Gene ExpressionZIAAI000711 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI KRISTIE, THOMAS M · 2009 to 2017
$5.4M
NOVEL MAMMALIAN TRANSCRIPTION FACTOR INVOLVED IN HSV GENE EXPRESSIONZ01AI000711 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI KRISTIE, THOMAS M · 1994 to 2008
$1.3M
6 · The paper itself

Abstract

Site-specific proteolysis is an important biological mechanism for the regulation of cellular processes such as gene expression, cell signaling, development, and apoptosis. In transcriptional regulation, specific proteolysis regulates the localization and activity of many regulatory factors. The C1 factor (HCF), a cellular transcription factor and coactivator, undergoes site-specific proteolytic processing at a series of unusual amino acid reiterations to generate a family of amino- and carboxyl-terminal polypeptides that remain tightly associated. Expression and purification of bacterially expressed domains of the C1 factor identifies an autocatalytic activity that is responsible for the specific cleavage of the reiterations. In addition, coexpression of the autocatalytic domain with a heterologous protein containing a target cleavage site demonstrates that the C1 protease may also function in trans.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceCatalysisDNA-Binding ProteinsEscherichia coliFluorescent Antibody TechniqueHost Cell Factor C1Models, BiologicalMolecular Sequence DataMolecular WeightOctamer Transcription Factor-1Peptide FragmentsProtein Structure, TertiaryRecombinant Fusion ProteinsRepetitive Sequences, Amino AcidSequence AlignmentDNA-Binding ProteinsHost Cell Factor C1Octamer Transcription Factor-1Peptide FragmentsRecombinant Fusion ProteinsTranscription Factors

Identifiers

PMID10920196
PMCPMC16880
OpenAlexW1990148125

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.