Evidence map›Paper›PMID 15297877›Full record

ArticleThe EMBO journal2004

Crystal structure of the nuclear effector of Notch signaling, CSL, bound to DNA.

Rhett A Kovall, Wayne A Hendrickson

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

78 citing papers in PubMed, 159 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Biophysics of Notch Signaling.Annual review of biophysics · 2021
    Review
  10. Review
  11. Article
  12. A Novel Flow Cytometric Assay to Identify Inhibitors of RBPJ-DNA Interactions.SLAS discovery : advancing life sciences R & D · 2020
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. An RBPJ-Cells · 2019
    Article
  19. Article
  20. Transcription factor Ptf1a in development, diseases and reprogramming.Cellular and molecular life sciences : CMLS · 2019
    Review

18 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

2 authors at 1 institution in 1 country.

Rhett A KovallDepartment of Biochemistry and Molecular Biophysics, Howard Hughes Medical Institute, Columbia University, New York, NY 10032, USA.
Wayne A Hendrickson
Howard Hughes Medical Institute · US

Funding

ANOMALOUS-SCATTERING STUDIES OF MACROMOLECULAR STRUCTURER37GM034102 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HENDRICKSON, WAYNE A. · 1994 to 2003
$1.4M
ANOMALOUS-SCATTERING STUDIES OF PROTEIN STRUCTURER01GM034102 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HENDRICKSON, WAYNE A. · 1985 to 2008
$1.3M
NIGMS NIH HHS GM34102NIGMS NIH HHS R01 GM034102NIGMS NIH HHS R37 GM034102
6 · The paper itself

Abstract

Notch signaling is a conserved pathway of communication between neighboring cells that results in cell fate specification, and CSL is the universal transcriptional effector of Notch signaling. The Notch intracellular domain translocates to the nucleus after proteolytic release upon Notch extracellular engagement, and there it displaces corepressors from DNA-bound CSL and recruits activators of Notch target genes. Here we report the 2.85 A crystal structure of CSL with a target DNA. CSL comprises three structurally integrated domains: its amino (NTD)- and carboxy (CTD)-terminal domains are strikingly similar to those of Rel transcription factors, but a surprising beta-trefoil domain (BTD) is inserted between them. CSL-bound DNA is recognized specifically by conserved residues from NTD and BTD. A hydrophobic pocket on BTD is identified as the likely site of Notch interaction with CSL, which has functional implications for the mechanism of Notch signaling.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBinding SitesCaenorhabditis elegans ProteinsCrystallography, X-RayDNA-Binding ProteinsDNA, RecombinantDrosophila ProteinsHumansImmunoglobulin J Recombination Signal Sequence-Binding ProteinIn Vitro TechniquesMacromolecular SubstancesMembrane ProteinsModels, MolecularMolecular Sequence DataCaenorhabditis elegans ProteinsDNA-Binding ProteinsDNA, RecombinantDrosophila ProteinsImmunoglobulin J Recombination Signal Sequence-Binding ProteinLAG-1 protein, C elegansMacromolecular SubstancesMembrane ProteinsNuclear ProteinsRBPJ protein, humanReceptors, NotchRecombinant ProteinsRepressor ProteinsSu(H) protein, Drosophila

Identifiers

PMID15297877
PMCPMC516623
OpenAlexW2140173252

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.