Regulation of sirtuin function by posttranslational modifications
about
Intracellular Mono-ADP-Ribosylation in Signaling and DiseaseProteomics in epigenetics: new perspectives for cancer researchThe role of sirtuins in cellular homeostasisAn acetylome peptide microarray reveals specificities and deacetylation substrates for all human sirtuin isoforms.Cross regulation of sirtuin 1, AMPK, and PPARγ in conjugated linoleic acid treated adipocytes.Resveratrol differentially regulates NAMPT and SIRT1 in Hepatocarcinoma cells and primary human hepatocytes.ING5 is phosphorylated by CDK2 and controls cell proliferation independently of p53Insight into the Mechanism of Intramolecular Inhibition of the Catalytic Activity of Sirtuin 2 (SIRT2).Sirtuin-dependent clock control: new advances in metabolism, aging and cancerPerspectives on translational and therapeutic aspects of SIRT1 in inflammaging and senescence.Skeletal muscle SIRT1 and the genetics of metabolic health: therapeutic activation by pharmaceuticals and exerciseMitochondrial dysfunction in metabolic syndrome and asthma.SIRT1: Regulator of p53 DeacetylationA proteomic perspective of Sirtuin 6 (SIRT6) phosphorylation and interactions and their dependence on its catalytic activity.SIRT1/PARP1 crosstalk: connecting DNA damage and metabolism.Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs.The interaction between acetylation and serine-574 phosphorylation regulates the apoptotic function of FOXO3.Expanding functions of intracellular resident mono-ADP-ribosylation in cell physiology.The diversity of histone versus nonhistone sirtuin substrates.Sirtuins and the circadian clock: bridging chromatin and metabolism.Molecular Links between Caloric Restriction and Sir2/SIRT1 Activation.Sirtuins and the Metabolic Hurdles in Cancer.ENPP1 processes protein ADP-ribosylation in vitro.A SIRT4-like auto ADP-ribosyltransferase is essential for the environmental growth of Mycobacterium smegmatis.Molecular architecture of the human protein deacetylase Sirt1 and its regulation by AROS and resveratrol.Sirt7 promotes adipogenesis in the mouse by inhibiting autocatalytic activation of Sirt1.Regulation of Sirtuin-Mediated Protein Deacetylation by Cardioprotective Phytochemicals.SIRT1-mediated ERβ suppression in the endothelium contributes to vascular aging.Obesity and aging diminish sirtuin 1 (SIRT1)-mediated deacetylation of SIRT3, leading to hyperacetylation and decreased activity and stability of SIRT3.Development of Activity-Based Chemical Probes for Human Sirtuins.Infection Reveals a Modification of SIRT2 Critical for Chromatin Association.The crystal structure of the Leishmania infantum Silent Information Regulator 2 related protein 1: Implications to protein function and drug design.Sirtuins in the Cardiovascular System: Potential Targets in Pediatric Cardiology.Histone deacetylase SIRT6 regulates chemosensitivity in liver cancer cells via modulation of FOXO3 activity
P2860
Q26783018-BFA8EF22-F3A7-4FBA-9110-4116AADA51C5Q27014943-D318450B-34AF-47A1-A485-7F697BA3859CQ28075581-7411279F-DD44-4B21-BDB0-46B5A0D82911Q30317729-319F8095-0CAF-4472-8C62-54BA72D74E16Q34479148-57820011-1B1E-4A3F-AA00-267E2D91FB9BQ35112888-9365B127-A03C-44B9-9256-CF0AB201A78BQ35599241-8C4F8511-17BC-4BBD-8353-DC8CF1CF91C2Q35788698-61D8AD48-F59A-483D-906C-AFA26B7D1952Q36176866-B6A16E0F-026F-4CCF-8373-0668DD773BB2Q36350770-22401DB1-6E06-4F7A-914B-C77BAD371D7FQ36925258-AAAA27F5-A3DB-4F2C-AD5D-8F526AD20535Q36942788-A76649CB-F837-4F9B-8355-2F854229937AQ37150526-F0E1B733-4D22-430D-AD5D-5BE0F8F2625DQ37428821-C7EF27FF-C288-4F44-8401-18FFA76A0FD5Q37502859-58544BF5-129B-48E0-93DD-D39EC63BBB65Q37649607-9A7B74DF-2928-4425-A083-D3307A6DED96Q37721158-EC4A0DA8-9461-4CF7-BC2D-E1233CBB5161Q38103617-BDDF7260-D724-443E-AC4B-029E062C4B6EQ38135829-3A35180B-34C3-454D-96B8-295825F5DD06Q38247938-028503EC-58E2-41F8-8DB6-37005CB5A66DQ38263220-2F2F0D2A-045F-4076-B170-CDF103133998Q38540810-C91FA0BA-02E8-4915-8F38-5A27FF321F48Q39608823-17938D69-A6EC-42C4-AB2C-00B50F495907Q40191162-DC7F76BD-19EA-4C67-8AF8-6C694D71EC58Q40721691-82931F4E-9C92-4544-B400-8669FBCCE1CBQ42263658-7644F259-F87B-4951-BCE8-CE116FC529ABQ45827486-9060A81D-CF51-4D43-A25A-EEA9ABD8328EQ46509480-BDABE68D-DDCD-48CC-B982-FF8B9EB4129FQ47952971-6EDE3492-98ED-4A7B-9E1B-2D5D3885E6BAQ49553888-F5E3711A-1214-47D5-ABCD-0B8B07BB54B5Q52309824-7961C7A8-0C9E-40B9-9FEF-197420C723A5Q52354384-87585CF3-A112-47EE-BF51-40B0D99028B0Q55341014-FBF4274F-11A2-4B66-ACF5-AD3CBA0FB84CQ58779328-2C755978-760F-49DC-82C6-A797C4D69687
P2860
Regulation of sirtuin function by posttranslational modifications
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Regulation of sirtuin function by posttranslational modifications
@en
Regulation of sirtuin function by posttranslational modifications.
@nl
type
label
Regulation of sirtuin function by posttranslational modifications
@en
Regulation of sirtuin function by posttranslational modifications.
@nl
prefLabel
Regulation of sirtuin function by posttranslational modifications
@en
Regulation of sirtuin function by posttranslational modifications.
@nl
P2860
P356
P1476
Regulation of sirtuin function by posttranslational modifications
@en
P2093
Franziska Flick
P2860
P356
10.3389/FPHAR.2012.00029
P577
2012-02-28T00:00:00Z