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Sebastien Moniot

Explore the profile of Sebastien Moniot including associated specialties, affiliations and a list of published articles. Areas
Snapshot
Articles 27
Citations 840
Followers 0
Related Specialties
Chemistry
Biochemistry
Cell Biology
Top 10 Co-Authors
Clemens Steegborn
Mikael Elias
Michael Weyand
Eric Chabriere
Aleksey G Kazantsev
Luisa Quinti
Ken Scott
Wolfram Saenger
Ellen Gerhardt
Zrinka Marijanovic
Published In
J Med Chem
J Mol Biol
Proc Natl Acad Sci U S A
Acta Crystallogr Sect F Struct Biol Cryst Commun
J Struct Biol
Affiliations
Soon will be listed here.
Recent Articles
11.
Thienopyrimidinone Based Sirtuin-2 (SIRT2)-Selective Inhibitors Bind in the Ligand Induced Selectivity Pocket
Sundriyal S, Moniot S, Mahmud Z, Yao S, Di Fruscia P, Reynolds C, et al.
J Med Chem . 2017 Jan; 60(5):1928-1945. PMID: 28135086
Sirtuins (SIRTs) are NAD-dependent deacylases, known to be involved in a variety of pathophysiological processes and thus remain promising therapeutic targets for further validation. Previously, we reported a novel thienopyrimidinone...
12.
SIRT2- and NRF2-Targeting Thiazole-Containing Compound with Therapeutic Activity in Huntington's Disease Models
Quinti L, Casale M, Moniot S, Pais T, Van Kanegan M, Kaltenbach L, et al.
Cell Chem Biol . 2016 Jul; 23(7):849-861. PMID: 27427231
There are currently no disease-modifying therapies for the neurodegenerative disorder Huntington's disease (HD). This study identified novel thiazole-containing inhibitors of the deacetylase sirtuin-2 (SIRT2) with neuroprotective activity in ex vivo...
13.
1,4-Dihydropyridines Active on the SIRT1/AMPK Pathway Ameliorate Skin Repair and Mitochondrial Function and Exhibit Inhibition of Proliferation in Cancer Cells
Valente S, Mellini P, Spallotta F, Carafa V, Nebbioso A, Polletta L, et al.
J Med Chem . 2015 Dec; 59(4):1471-91. PMID: 26689352
Modulators of sirtuins are considered promising therapeutic targets for the treatment of cancer, cardiovascular, metabolic, inflammatory, and neurodegenerative diseases. Here we prepared new 1,4-dihydropyridines (DHPs) bearing changes at the C2/C6,...
14.
The sirtuin-2 inhibitor AK7 is neuroprotective in models of Parkinson's disease but not amyotrophic lateral sclerosis and cerebral ischemia
Chen X, Wales P, Quinti L, Zuo F, Moniot S, Herisson F, et al.
PLoS One . 2015 Jan; 10(1):e0116919. PMID: 25608039
Sirtuin deacetylases regulate diverse cellular pathways and influence disease processes. Our previous studies identified the brain-enriched sirtuin-2 (SIRT2) deacetylase as a potential drug target to counteract neurodegeneration. In the present...
15.
The discovery of a highly selective 5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one SIRT2 inhibitor that is neuroprotective in an in vitro Parkinson's disease model
Di Fruscia P, Zacharioudakis E, Liu C, Moniot S, Laohasinnarong S, Khongkow M, et al.
ChemMedChem . 2014 Nov; 10(1):69-82. PMID: 25395356
Sirtuins, NAD(+) -dependent histone deacetylases (HDACs), have recently emerged as potential therapeutic targets for the treatment of a variety of diseases. The discovery of potent and isoform-selective inhibitors of this...
16.
Crystal structures of human soluble adenylyl cyclase reveal mechanisms of catalysis and of its activation through bicarbonate
Kleinboelting S, Diaz A, Moniot S, van den Heuvel J, Weyand M, Levin L, et al.
Proc Natl Acad Sci U S A . 2014 Feb; 111(10):3727-32. PMID: 24567411
cAMP is an evolutionary conserved, prototypic second messenger regulating numerous cellular functions. In mammals, cAMP is synthesized by one of 10 homologous adenylyl cyclases (ACs): nine transmembrane enzymes and one...
17.
Molecular architecture of the human protein deacetylase Sirt1 and its regulation by AROS and resveratrol
Lakshminarasimhan M, Curth U, Moniot S, Mosalaganti S, Raunser S, Steegborn C
Biosci Rep . 2013 Apr; 33(3). PMID: 23548308
Sirtuins are NAD+-dependent protein deacetylases regulating metabolism, stress responses and ageing processes. Among the seven mammalian Sirtuins, Sirt1 is the physiologically best-studied isoform. It regulates nuclear functions such as chromatin...
18.
Crystal structure analysis of human Sirt2 and its ADP-ribose complex
Moniot S, Schutkowski M, Steegborn C
J Struct Biol . 2013 Mar; 182(2):136-43. PMID: 23454361
Sirtuins are NAD(+)-dependent protein deacetylases that regulate metabolism and aging-related processes. Sirt2 is the only cytoplasmic isoform among the seven mamalian Sirtuins (Sirt1-7) and structural information concerning this isoform is...
19.
Crystallization and preliminary crystal structure analysis of the ligand-binding domain of PqsR (MvfR), the Pseudomonas quinolone signal (PQS) responsive quorum-sensing transcription factor of Pseudomonas aeruginosa
Xu N, Yu S, Moniot S, Weyand M, Blankenfeldt W
Acta Crystallogr Sect F Struct Biol Cryst Commun . 2012 Sep; 68(Pt 9):1034-9. PMID: 22949189
The opportunistic bacterial pathogen Pseudomonas aeruginosa employs three transcriptional regulators, LasR, RhlR and PqsR, to control the transcription of a large subset of its genes in a cell-density-dependent process known...
20.
Structures, substrates, and regulators of Mammalian sirtuins - opportunities and challenges for drug development
Moniot S, Weyand M, Steegborn C
Front Pharmacol . 2012 Feb; 3:16. PMID: 22363286
Sirtuins are NAD(+)-dependent protein deacetylases regulating metabolism, stress responses, and aging processes. Mammalia have seven Sirtuin isoforms, Sirt1-7, which differ in their substrate specificities and subcellular localizations. The physiological functions...