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A ribose-functionalized NAD+ with unexpected high activity and selectivity for protein poly-ADP-ribo...

A ribose-functionalized NAD+ with unexpected high activity and selectivity for protein poly-ADP-ribo...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_99a2c69f536344e0816740d2ed77a8f6

A ribose-functionalized NAD+ with unexpected high activity and selectivity for protein poly-ADP-ribosylation

About this item

Full title

A ribose-functionalized NAD+ with unexpected high activity and selectivity for protein poly-ADP-ribosylation

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2019-09, Vol.10 (1), p.4196-13, Article 4196

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Nicotinamide adenine dinucleotide (NAD
+
)-dependent ADP-ribosylation plays important roles in physiology and pathophysiology. It has been challenging to study this key type of enzymatic post-translational modification in particular for protein poly-ADP-ribosylation (PARylation). Here we explore chemical and chemoenzymatic synthesis of NAD

Alternative Titles

Full title

A ribose-functionalized NAD+ with unexpected high activity and selectivity for protein poly-ADP-ribosylation

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_99a2c69f536344e0816740d2ed77a8f6

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_99a2c69f536344e0816740d2ed77a8f6

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-019-12215-4

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