Targeting Sirtuins: Substrate Specificity and Inhibitor Design

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research

Standard

Targeting Sirtuins: Substrate Specificity and Inhibitor Design. / Rajabi, Nima; Galleano, Iacopo; Madsen, Andreas Stahl; Olsen, Christian Adam.

Progress in Molecular Biology and Translational Science: Sirtuins in Health and Disease. Elsevier, 2018. p. 25-69 (Progress in Molecular Biology and Translational Science, Vol. 154).

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research

Harvard

Rajabi, N, Galleano, I, Madsen, AS & Olsen, CA 2018, Targeting Sirtuins: Substrate Specificity and Inhibitor Design. in Progress in Molecular Biology and Translational Science: Sirtuins in Health and Disease. Elsevier, Progress in Molecular Biology and Translational Science, vol. 154, pp. 25-69.

APA

Rajabi, N., Galleano, I., Madsen, A. S., & Olsen, C. A. (2018). Targeting Sirtuins: Substrate Specificity and Inhibitor Design. In Progress in Molecular Biology and Translational Science: Sirtuins in Health and Disease (pp. 25-69). Elsevier. Progress in Molecular Biology and Translational Science Vol. 154

Vancouver

Rajabi N, Galleano I, Madsen AS, Olsen CA. Targeting Sirtuins: Substrate Specificity and Inhibitor Design. In Progress in Molecular Biology and Translational Science: Sirtuins in Health and Disease. Elsevier. 2018. p. 25-69. (Progress in Molecular Biology and Translational Science, Vol. 154).

Author

Rajabi, Nima ; Galleano, Iacopo ; Madsen, Andreas Stahl ; Olsen, Christian Adam. / Targeting Sirtuins: Substrate Specificity and Inhibitor Design. Progress in Molecular Biology and Translational Science: Sirtuins in Health and Disease. Elsevier, 2018. pp. 25-69 (Progress in Molecular Biology and Translational Science, Vol. 154).

Bibtex

@inbook{e21e5eda63c04e1e8b769c068fcb370c,
title = "Targeting Sirtuins: Substrate Specificity and Inhibitor Design",
abstract = "Lysine residues across the proteome are modified by posttranslational modifications (PTMs) that significantly enhance the structural and functional diversity of proteins. For lysine, the most abundant PTM is ɛ-N-acetyllysine (Kac), which plays numerous roles in regulation of important cellular functions, such as gene expression (epigenetic effects) and metabolism. A family of enzymes, namely histone deacetylases (HDACs), removes these PTMs. A subset of these enzymes, the sirtuins (SIRTs), represent class III HDAC and, unlike the rest of the family, these hydrolases are NAD+-dependent. Although initially described as deacetylases, alternative deacylase functions for sirtuins have been reported, which expands the potential cellular roles of this class of enzymes. Currently, sirtuins are investigated as therapeutic targets for the treatment of diseases that span from cancers to neurodegenerative disorders. In the present book chapter, we review and discuss the current literature on novel ɛ-N-acyllysine PTMs, targeted by sirtuins, as well as mechanism-based sirtuin inhibitors inspired by their substrates.",
author = "Nima Rajabi and Iacopo Galleano and Madsen, {Andreas Stahl} and Olsen, {Christian Adam}",
year = "2018",
month = feb,
day = "3",
language = "English",
series = "Progress in Molecular Biology and Translational Science",
publisher = "Elsevier",
pages = "25--69",
booktitle = "Progress in Molecular Biology and Translational Science",
address = "Netherlands",

}

RIS

TY - CHAP

T1 - Targeting Sirtuins: Substrate Specificity and Inhibitor Design

AU - Rajabi, Nima

AU - Galleano, Iacopo

AU - Madsen, Andreas Stahl

AU - Olsen, Christian Adam

PY - 2018/2/3

Y1 - 2018/2/3

N2 - Lysine residues across the proteome are modified by posttranslational modifications (PTMs) that significantly enhance the structural and functional diversity of proteins. For lysine, the most abundant PTM is ɛ-N-acetyllysine (Kac), which plays numerous roles in regulation of important cellular functions, such as gene expression (epigenetic effects) and metabolism. A family of enzymes, namely histone deacetylases (HDACs), removes these PTMs. A subset of these enzymes, the sirtuins (SIRTs), represent class III HDAC and, unlike the rest of the family, these hydrolases are NAD+-dependent. Although initially described as deacetylases, alternative deacylase functions for sirtuins have been reported, which expands the potential cellular roles of this class of enzymes. Currently, sirtuins are investigated as therapeutic targets for the treatment of diseases that span from cancers to neurodegenerative disorders. In the present book chapter, we review and discuss the current literature on novel ɛ-N-acyllysine PTMs, targeted by sirtuins, as well as mechanism-based sirtuin inhibitors inspired by their substrates.

AB - Lysine residues across the proteome are modified by posttranslational modifications (PTMs) that significantly enhance the structural and functional diversity of proteins. For lysine, the most abundant PTM is ɛ-N-acetyllysine (Kac), which plays numerous roles in regulation of important cellular functions, such as gene expression (epigenetic effects) and metabolism. A family of enzymes, namely histone deacetylases (HDACs), removes these PTMs. A subset of these enzymes, the sirtuins (SIRTs), represent class III HDAC and, unlike the rest of the family, these hydrolases are NAD+-dependent. Although initially described as deacetylases, alternative deacylase functions for sirtuins have been reported, which expands the potential cellular roles of this class of enzymes. Currently, sirtuins are investigated as therapeutic targets for the treatment of diseases that span from cancers to neurodegenerative disorders. In the present book chapter, we review and discuss the current literature on novel ɛ-N-acyllysine PTMs, targeted by sirtuins, as well as mechanism-based sirtuin inhibitors inspired by their substrates.

UR - http://dx.doi.org/10.1016/bs.pmbts.2017.11.003

M3 - Book chapter

T3 - Progress in Molecular Biology and Translational Science

SP - 25

EP - 69

BT - Progress in Molecular Biology and Translational Science

PB - Elsevier

ER -

ID: 199215102