Human SIRT3 tripeptidic inhibitors containing Nε-thioacetyl-lysine

Chen, Bing; Wang, Juan; Huang, Yajun; Zheng, Wei

doi:10.1016/j.bmcl.2015.07.008

Cited by 21 publications

(12 citation statements)

References 34 publications

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“…Figure 6 shows the 3D and 2D ligand receptor interactions demonstrated by molecular docking. Interestingly, the crucial interaction regions reported in the literature for known inhibitors (small molecules or peptides) were observed for 2-ME at both the canonical inhibitor and allosteric sites (42)(43)(44)(45)(46) Figure 6B-E.…”

Section: Molecular Dockingmentioning

confidence: 73%

2-Methoxyestradiol Affects Mitochondrial Biogenesis Pathway and Succinate Dehydrogenase Complex Flavoprotein Subunit A in Osteosarcoma Cancer Cells

Górska‐Ponikowska

Kuban–Jankowska

Eisler

et al. 2018

CGP

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Section: Molecular Dockingmentioning

confidence: 73%

2-Methoxyestradiol Affects Mitochondrial Biogenesis Pathway and Succinate Dehydrogenase Complex Flavoprotein Subunit A in Osteosarcoma Cancer Cells

Górska‐Ponikowska

Kuban–Jankowska

Eisler

et al. 2018

CGP

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“…Zheng et al also designed a variety of potent SIRT3 tripeptidic inhibitors containing N Ɛ -thioacetyl-lysine. However, their selectivity was generally not strong 192 . SIRT3-selective inhibitors can be obtained from other SIRT inhibitors by classical medicinal chemistry methods 108 .…”

Section: Targeting Sirt3 For Potential Therapiesmentioning

confidence: 99%

Mitochondrial Sirtuin 3: New emerging biological function and therapeutic target

Zhang¹,

Xiang²,

Liu³

et al. 2020

Theranostics

289

238

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Sirtuin 3 (SIRT3) is one of the most prominent deacetylases that can regulate acetylation levels in mitochondria, which are essential for eukaryotic life and inextricably linked to the metabolism of multiple organs. Hitherto, SIRT3 has been substantiated to be involved in almost all aspects of mitochondrial metabolism and homeostasis, protecting mitochondria from a variety of damage. Accumulating evidence has recently documented that SIRT3 is associated with many types of human diseases, including age-related diseases, cancer, heart disease and metabolic diseases, indicating that SIRT3 can be a potential therapeutic target. Here we focus on summarizing the intricate mechanisms of SIRT3 in human diseases, and recent notable advances in the field of small-molecule activators or inhibitors targeting SIRT3 as well as their potential therapeutic applications for future drug discovery.

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“…As a non‐hydrolyzable analog of AcK, N ε ‐thioacetyl‐ l ‐lysine (TAcK) has been used as an inhibitor for a number of deacetylases in the form of peptide or non‐peptide substrates . Recently, Söll's group utilized the flexizyme‐mediated tRNA aminoacylation and cell‐free translation systems to incorporate TAcK into histone H3, which was shown to be resistant to SIRT1 deacetylase .…”

mentioning

confidence: 99%

Genetically encoding thioacetyl‐lysine as a non‐deacetylatable analog of lysine acetylation in Escherichia coli

et al. 2017

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Reversible lysine acetylation is one of the most widely distributed post‐translational modifications; it is involved in a variety of biological processes and can be found in all three domains of life. Acetyltransferases and deacetylases work coordinately to control levels of protein acetylation. In this work, we applied the genetic code expansion strategy to site‐specifically incorporate Nε‐thioacetyl‐l‐lysine (TAcK) as an analog of Nε‐acetyl‐l‐lysine (AcK) into green fluorescent protein and malate dehydrogenase in Escherichia coli. We showed that TAcK could serve as an ideal functional mimic for AcK. It could also resist the bacterial sirtuin‐type deacetylase CobB. Thus, genetic incorporation of TAcK as a non‐deacetylatable analog of AcK into proteins will facilitate in vivo studies of protein acetylation.

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Human SIRT3 tripeptidic inhibitors containing Nε-thioacetyl-lysine

Cited by 21 publications

References 34 publications

2-Methoxyestradiol Affects Mitochondrial Biogenesis Pathway and Succinate Dehydrogenase Complex Flavoprotein Subunit A in Osteosarcoma Cancer Cells

2-Methoxyestradiol Affects Mitochondrial Biogenesis Pathway and Succinate Dehydrogenase Complex Flavoprotein Subunit A in Osteosarcoma Cancer Cells

Mitochondrial Sirtuin 3: New emerging biological function and therapeutic target

Genetically encoding thioacetyl‐lysine as a non‐deacetylatable analog of lysine acetylation in Escherichia coli

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