about
AROS has a context-dependent effect on SIRT1Synthesis and evaluation of substituted chroman-4-one and chromone derivatives as sirtuin 2-selective inhibitorsSirtuin functions and modulation: from chemistry to the clinicPeptides and Pseudopeptides as SIRT6 Deacetylation Inhibitors.The Identification of a SIRT6 Activator from Brown Algae Fucus distichusScreen of pseudopeptidic inhibitors of human sirtuins 1-3: two lead compounds with antiproliferative effects in cancer cells.Virtual Screening of Small Drug-Like Compounds Stimulating the Enzymatic Activity of Kallikrein-Related Peptidase 3 (KLK3).N-Acylethanolamines Bind to SIRT6Withaferin A induces heme oxygenase (HO-1) expression in endothelial cells via activation of the Keap1/Nrf2 pathway.Inhibition of BET bromodomains alleviates inflammation in human RPE cells.BET Inhibition Upregulates SIRT1 and Alleviates Inflammatory Responses.Development of molecules stimulating the activity of KLK3 - an update.Chroman-4-one- and chromone-based sirtuin 2 inhibitors with antiproliferative properties in cancer cells.Quinazolinecarboline alkaloid evodiamine as scaffold for targeting topoisomerase I and sirtuins.Discovery of salermide-related sirtuin inhibitors: binding mode studies and antiproliferative effects in cancer cells including cancer stem cells.Sirtuin 6 (SIRT6) Activity Assays.Virtual screening approach of sirtuin inhibitors results in two new scaffolds.Potent mechanism-based sirtuin-2-selective inhibition by an in situ-generated occupant of the substrate-binding site, "selectivity pocket" and NAD+-binding site.Interactions of inhibitor molecules with the human CYP2E1 enzyme active site.N(epsilon)-Modified lysine containing inhibitors for SIRT1 and SIRT2.Drug release from starch-acetate microparticles and films with and without incorporated alpha-amylase.Studying the catechol binding cavity in comparative models of human dopamine D2 receptor.Insights into ligand-elicited activation of human constitutive androstane receptor based on novel agonists and three-dimensional quantitative structure-activity relationship.Characterization of the binding properties of SIRT2 inhibitors with a N-(3-phenylpropenoyl)-glycine tryptamide backbone.Oxadiazole-carbonylaminothioureas as SIRT1 and SIRT2 inhibitors.Development of a 3D model for the human cannabinoid CB1 receptor.1,3,4-Oxadiazol-2-ones as fatty-acid amide hydrolase and monoacylglycerol lipase inhibitors: Synthesis, in vitro evaluation and insight into potency and selectivity determinants by molecular modelling.Quantitative insight into the design of compounds recognized by the L-type amino acid transporter 1 (LAT1).Withaferin A inhibits NF-kappaB activation by targeting cysteine 179 in IKKβ.Natural polyphenols as sirtuin 6 modulators.Identification of novel CYP2A6 inhibitors by virtual screening.Common and Distinct Interactions of Chemical Inhibitors with Cytochrome P450 CYP1A2, CYP2A6 and CYP2B6 Enzymes.Time-Dependent Inhibition of CYP2C19 by Isoquinoline Alkaloids: In Vitro and In Silico Analysis.Comparative and pharmacophore model for deacetylase SIRT1N,N'-Bisbenzylidenebenzene-1,4-diamines and N,N'-Bisbenzylidenenaphthalene-1,4-diamines as Sirtuin Type 2 (SIRT2) InhibitorsPredicting the drug concentration in starch acetate matrix tablets from ATR-FTIR spectra using multi-way methodsStructure-based design of pseudopeptidic inhibitors for SIRT1 and SIRT2Identification of novel SIRT3 inhibitor scaffolds by virtual screeningStudying SIRT6 regulation using H3K56 based substrate and small moleculesQuantitative insights for the design of substrate-based SIRT1 inhibitors
P50
Q24293274-E783A046-327C-4CCD-99F6-0C72015606B8Q24613541-5D73F030-DB9B-45B6-A8AD-C49A30A3B635Q26745884-405C4F1A-74A9-4839-BD1E-6980043B0B08Q33630602-87CDBEBD-F3C2-47A2-8F26-B61A51914523Q33833447-16CEE954-8FA7-46D4-9D6B-3DFA4E962F64Q34911055-9ED61281-2E5D-4A7E-A6E0-E85B932332DCQ36087908-ED33A3DA-5DDE-406F-90EF-B551C13475B7Q36744621-E4C95EF7-9AE7-4528-B72C-B5C6DE2201DBQ38292978-F34AEE5B-EF63-4D15-A998-0CDCF159A71CQ38776178-D227C35C-4934-4DDE-8AE6-97E1F79883CEQ38849159-B15175DC-0E41-4E29-8590-06FA8EC9F50AQ38887906-05A52C0E-C9C5-4F28-93ED-D7A1553B1FD0Q38941545-3A677BA7-C78D-4875-9D86-758C419E1F6EQ39084606-C46CE702-B00B-478B-8AB0-7CC462E962B5Q39236660-76543A6E-F9AA-44DF-A64A-C2315C84C132Q40973827-8EA5D72E-019E-4757-8279-EC91981943E2Q40982816-AE476241-CB95-4CB7-8CAC-27633773C59CQ42174323-1942F390-4565-43E1-938A-32C2757FBD4DQ42672976-282D6D28-3EC7-45BD-8472-2C6C115B63E4Q42970349-E6825187-01BF-4C9C-968B-1502A36D09A0Q44816222-20898E32-31FF-4397-85AE-248155DB3EC1Q45332546-7BC6E497-3628-42B9-A153-B7B8B48B5DF3Q46265569-E66580DE-9ADC-4FE9-8EEC-F5462A3E9274Q46431197-F00192CB-C898-4587-BB64-E4C01585E8A0Q46471893-F2DAA732-1B3A-4AF8-AF0C-2BE8B8A79BC1Q47429894-84FE9168-3FC7-44CB-A0A7-75AAE57E6895Q48096588-D9B488C4-49ED-44FD-80D9-6A52F0762B2CQ48554104-889C5009-35D1-45AE-9905-F82B3BD90FB7Q49050188-C20EC53E-671F-49BA-99D7-6B46D884294BQ51743284-5137F7AD-D72C-4A9F-BFA7-B911072B122BQ52299621-3916173C-ED56-4A61-955A-465279A076FEQ52308246-F3637E9A-FECF-41D1-9439-C05F33EF9717Q53340089-EEA754E7-8C53-4B71-8706-E3513018326CQ79356133-B3CD8C0D-1A84-4D2F-A56C-006890C25B5BQ79443941-C3D13C19-9C0B-429A-B5D7-7FB43C4F2CE4Q80556310-F8DF3E66-C08B-4AB9-9BBA-E9FB91D2D00CQ84896997-98C4E734-C96F-4239-8D1D-61B20AADB395Q86550421-EA77E528-F27B-40AB-A45A-02DE6B77F63DQ87367447-F1FD5237-157C-49FA-BDE8-0C9CF463366BQ87712702-6981837D-B26E-412B-B637-619CCC6CCB83
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Maija K Lahtela-Kakkonen
@ast
Maija K Lahtela-Kakkonen
@en
Maija K Lahtela-Kakkonen
@es
Maija K Lahtela-Kakkonen
@nl
Maija K Lahtela-Kakkonen
@sl
type
label
Maija K Lahtela-Kakkonen
@ast
Maija K Lahtela-Kakkonen
@en
Maija K Lahtela-Kakkonen
@es
Maija K Lahtela-Kakkonen
@nl
Maija K Lahtela-Kakkonen
@sl
prefLabel
Maija K Lahtela-Kakkonen
@ast
Maija K Lahtela-Kakkonen
@en
Maija K Lahtela-Kakkonen
@es
Maija K Lahtela-Kakkonen
@nl
Maija K Lahtela-Kakkonen
@sl
P106
P31
P496
0000-0001-7163-7728