Evidence map›Paper›PMID 10022840›Full record

ArticleThe EMBO journal1999

Assembly requirements of PU.1-Pip (IRF-4) activator complexes: inhibiting function in vivo using fused dimers.

A L Brass, A Q Zhu, H Singh

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

87 citing papers in PubMed, 199 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Expanding the DNA Motif Lexicon of the Transcriptional Regulatory Code.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. The dynamic functions of IRF4 in B cell malignancies.Clinical and experimental medicine · 2023
    Review
  16. Article
  17. Review
  18. Review
  19. Review
  20. Dendritic cells in cancer immunology.Cellular & molecular immunology · 2022
    Review

27 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

3 authors at 2 institutions in 1 country.

A L BrassHoward Hughes Medical Institute, The University of Chicago, 5841 S. Maryland Avenue, MC1028, Chicago IL 60637, USA.
A Q Zhu
H Singh
University of Chicago · USHoward Hughes Medical Institute · US

Funding

NICHD NIH HHS HD07009
6 · The paper itself

Abstract

Gene expression in higher eukaryotes appears to be regulated by specific combinations of transcription factors binding to regulatory sequences. The Ets factor PU.1 and the IRF protein Pip (IRF-4) represent a pair of interacting transcription factors implicated in regulating B cell-specific gene expression. Pip is recruited to its binding site on DNA by phosphorylated PU.1. PU.1-Pip interaction is shown to be template directed and involves two distinct protein-protein interaction surfaces: (i) the ets and IRF DNA-binding domains; and (ii) the phosphorylated PEST region of PU.1 and a lysine-requiring putative alpha-helix in Pip. Thus, a coordinated set of protein-protein and protein-DNA contacts are essential for PU.1-Pip ternary complex assembly. To analyze the function of these factors in vivo, we engineered chimeric repressors containing the ets and IRF DNA-binding domains connected by a flexible POU domain linker. When stably expressed, the wild-type fused dimer strongly repressed the expression of a rearranged immunoglobulin lambda gene, thereby establishing the functional importance of PU.1-Pip complexes in B cell gene expression. Comparative analysis of the wild-type dimer with a series of mutant dimers distinguished a gene regulated by PU.1 and Pip from one regulated by PU.1 alone. This strategy should prove generally useful in analyzing the function of interacting transcription factors in vivo, and for identifying novel genes regulated by such complexes.

Indexed as

Amino Acid SequenceAnimalsB-LymphocytesDimerizationDNA-Binding ProteinsEnhancer Elements, GeneticGene Expression RegulationImmunoglobulin lambda-ChainsInterferon Regulatory Factor-4Interferon Regulatory FactorsMiceMolecular Sequence DataMutationProtein EngineeringProto-Oncogene ProteinsProto-Oncogene Protein Spi-1DNA-Binding ProteinsImmunoglobulin lambda-ChainsInterferon Regulatory Factor-4Interferon Regulatory FactorsProto-Oncogene ProteinsProto-Oncogene Protein Spi-1Recombinant Fusion ProteinsRepressor ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID10022840
PMCPMC1171190
OpenAlexW2121496836

What OpenQuestion holds

Texttitle and abstract
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.