Evidence map›Paper›PMID 18957203›Full record

ArticleCell2008

Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation.

Elizabeth M Duncan, Tara L Muratore-Schroeder, Richard G Cook, Benjamin A Garcia, Jeffrey Shabanowitz, Donald F Hunt, C David Allis

Abstract read
In one paragraph

Article in Cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 185 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
185citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

185 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Specific tracking of N-terminal clipping on histone H3 inMarine life science & technology · 2026
    Article
  5. Article
  6. Review
  7. Linker histone regulates the myeloid versus lymphoid bifurcation of multipotent hematopoietic stem and progenitors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. On the Hunt for the Histone Code.Molecular & cellular proteomics : MCP · 2024
    Article
  18. Review
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Elizabeth M DuncanLaboratory of Chromatin Biology, The Rockefeller University, New York, NY 10065, USA.
Tara L Muratore-Schroeder
Richard G Cook
Benjamin A Garcia
Jeffrey Shabanowitz
Donald F Hunt
C David Allis

Funding

PROTEIN SEQUENCING BY TANDEM MASS SPECTROMETRYR01GM037537 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1987 to 2023
$17.8M
ENZYMOLOGY &BIOLOGICAL FUNC OF HISTONE ACETYLATIONR37GM053512 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI ALLIS, CHARLES DAVID · 1999 to 2008
$4.2M
ROLE OF MACROH2A IN CHROMATIN STRUCTURE AND FUNCTIONR01GM049351 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI PEHRSON, JOHN R. · 1993 to 2011
$4.1M
NUCLEAR DETERMINATION AND DIFFERENTIATION IN DEVELOPMENTR01GM053512 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI ALLIS, CHARLES DAVID · 1995 to 1998
–
NIGMS NIH HHS GM37537NIGMS NIH HHS GM53512NIGMS NIH HHS R01 GM037537NIGMS NIH HHS R01 GM049351NIGMS NIH HHS R37 GM053512
6 · The paper itself

Abstract

Chromatin undergoes developmentally-regulated structural and chemical changes as cells differentiate, which subsequently lead to differences in cellular function by altering patterns of gene expression. To gain insight into chromatin alterations that occur during mammalian differentiation, we turned to a mouse embryonic stem cell (ESC) model. Here we show that histone H3 is proteolytically cleaved at its N-terminus during ESC differentiation. We map the sites of H3 cleavage and identify Cathepsin L as a protease responsible for proteolytically processing the N-terminal H3 tail. In addition, our data suggest that H3 cleavage may be regulated by covalent modifications present on the histone tail itself. Our studies underscore the intriguing possibility that histone proteolysis, brought about by Cathepsin L and potentially other family members, plays a role in development and differentiation that was not previously recognized.

Indexed as

Cell DifferentiationAmino Acid SequenceAnimalsCathepsin LCathepsinsChromatinCysteine EndopeptidasesEmbryonic Stem CellsHistone CodeHistonesMiceMolecular Sequence DataRNA InterferenceCathepsin LCathepsinsChromatinCtsl protein, mouseCysteine EndopeptidasesHistones

Identifiers

PMID18957203
PMCPMC2579750

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.