Log in to save to my catalogue

Reading and erasing of the phosphonium analogue of trimethyllysine by epigenetic proteins

Reading and erasing of the phosphonium analogue of trimethyllysine by epigenetic proteins

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_099bbfd2e1894d158c026e859ca05b14

Reading and erasing of the phosphonium analogue of trimethyllysine by epigenetic proteins

About this item

Full title

Reading and erasing of the phosphonium analogue of trimethyllysine by epigenetic proteins

Publisher

London: Nature Publishing Group UK

Journal title

Communications chemistry, 2022-12, Vol.5 (1), p.1-11, Article 27

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

N
ε
-Methylation of lysine residues in histones plays an essential role in the regulation of eukaryotic transcription. The ‘highest’ methylation mark,
N
ε
-trimethyllysine, is specifically recognised by
N
ε
-trimethyllysine binding ‘reader’ domains, and undergoes demethylation, as catalysed by 2-oxoglutarate dependent JmjC o...

Alternative Titles

Full title

Reading and erasing of the phosphonium analogue of trimethyllysine by epigenetic proteins

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_099bbfd2e1894d158c026e859ca05b14

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_099bbfd2e1894d158c026e859ca05b14

Other Identifiers

ISSN

2399-3669

E-ISSN

2399-3669

DOI

10.1038/s42004-022-00640-4

How to access this item