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Crystallographic structure of a small molecule SIRT1 activator-enzyme complex

Crystallographic structure of a small molecule SIRT1 activator-enzyme complex

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4506539

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

SIRT1, the founding member of the mammalian family of seven NAD
+
-dependent sirtuins, is composed of 747 amino acids forming a catalytic domain and extended N- and C-terminal regions. We report the design and characterization of an engineered human SIRT1 construct (mini-hSIRT1) containing the minimal structural elements required for lysine d...

Alternative Titles

Full title

Crystallographic structure of a small molecule SIRT1 activator-enzyme complex

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4506539

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4506539

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms8645

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