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Histone H3.3 and its proteolytically processed form drive a cellular senescence programme

Histone H3.3 and its proteolytically processed form drive a cellular senescence programme

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4235654

Histone H3.3 and its proteolytically processed form drive a cellular senescence programme

About this item

Full title

Histone H3.3 and its proteolytically processed form drive a cellular senescence programme

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2014-11, Vol.5 (1), p.5210-5210, Article 5210

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The process of cellular senescence generates a repressive chromatin environment, however, the role of histone variants and histone proteolytic cleavage in senescence remains unclear. Here, using models of oncogene-induced and replicative senescence, we report novel histone H3 tail cleavage events mediated by the protease Cathepsin L. We find that c...

Alternative Titles

Full title

Histone H3.3 and its proteolytically processed form drive a cellular senescence programme

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4235654

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4235654

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms6210

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