Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins
about
Genealogy of an ancient protein family: the Sirtuins, a family of disordered membersIdentification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1Protective effects and mechanisms of sirtuins in the nervous systemAlternative functions of the brain transsulfuration pathway represent an underappreciated aspect of brain redox biochemistry with significant potential for therapeutic engagementSirtuin-dependent epigenetic regulation in the maintenance of genome integritySIRT3 and cancer: tumor promoter or suppressor?Protein deacetylase SIRT1 in the cytoplasm promotes nerve growth factor-induced neurite outgrowth in PC12 cellsEndothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1.Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1alpha in skeletal muscleThe fat-1 transgene in mice increases antioxidant potential, reduces pro-inflammatory cytokine levels, and enhances PPAR-gamma and SIRT-1 expression on a calorie restricted diet.SIRT3 substrate specificity determined by peptide arrays and machine learning.Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling.SIRT1 contributes to telomere maintenance and augments global homologous recombination.Sirtuin catalysis and regulationPathways for ischemic cytoprotection: role of sirtuins in caloric restriction, resveratrol, and ischemic preconditioning.Caloric excess or restriction mediated modulation of metabolic enzyme acetylation-proposed effects on cardiac growth and function.KAP1 Deacetylation by SIRT1 Promotes Non-Homologous End-Joining RepairSirtuin-3 (SIRT3) Protein Attenuates Doxorubicin-induced Oxidative Stress and Improves Mitochondrial Respiration in H9c2 Cardiomyocytes.Akt blocks the tumor suppressor activity of LKB1 by promoting phosphorylation-dependent nuclear retention through 14-3-3 proteins.Protein deacetylation by sirtuins: delineating a post-translational regulatory program responsive to nutrient and redox stressorsNAD(+)/NADH and skeletal muscle mitochondrial adaptations to exercise.Direct Transcriptional Effects of Apolipoprotein EMitochondrial sirtuins and metabolic homeostasisSelective overexpression of human SIRT1 in adipose tissue enhances energy homeostasis and prevents the deterioration of insulin sensitivity with ageing in miceCalorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.The emerging characterization of lysine residue deacetylation on the modulation of mitochondrial function and cardiovascular biology.Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3.Interactomic analysis of REST/NRSF and implications of its functional links with the transcription suppressor TRIM28 during neuronal differentiation.Antiaging properties of a grape-derived antioxidant are regulated by mitochondrial balance of fusion and fission leading to mitophagy triggered by a signaling network of Sirt1-Sirt3-Foxo3-PINK1-PARKIN.Sirtuins and Their Roles in Brain Aging and Neurodegenerative DisordersThe mitochondrial hinge protein, UQCRH, is a novel prognostic factor for hepatocellular carcinoma.Mitochondrial SIRT3 and heart disease.The SirT3 divining rod points to oxidative stress.Mitochondrial sirtuins--a new therapeutic target for repair and protection in multiple sclerosis.Sirtuins: from metabolic regulation to brain aging.Sirtuins in stress response: guardians of the genome.Upstream molecular signaling pathways of p27(Kip1) expression in human breast cancer cells in vitro: differential effects of 4-hydroxytamoxifen and deficiency of either D-(+)-glucose or L-leucineThe mitochondrial protein CHCHD2 primes the differentiation potential of human induced pluripotent stem cells to neuroectodermal lineages.Epigenetic Regulation of the Blimp-1 Gene (Prdm1) in B Cells Involves Bach2 and Histone Deacetylase 3.Sirtuin 3 acts as a negative regulator of autophagy dictating hepatocyte susceptibility to lipotoxicity.
P2860
Q21284005-36B7B85F-0066-47D8-BC14-E01E70ABA51CQ24304507-18BE9CA0-22C0-42BB-96E0-8EB19B82BEDBQ26825585-292F4587-7448-4411-8C9B-C18DC96FC2CFQ26851534-CCAEFA18-4E47-48D1-A963-806A8E638730Q27026871-04ACA795-DA68-4D85-963F-9C1F25591609Q28390097-AD05BDBA-131F-44C5-953E-8F573CA3AA91Q28570744-7C8AA332-F624-4844-B75D-DA5FBA0CEEC6Q30830249-3947271F-AC86-4BAC-B948-8177E06D6A1DQ33627876-62F11C49-1689-4092-B040-873804869775Q33717017-9173C20C-282C-4A01-8F27-311E00917950Q33718384-1F1C2F23-C128-463E-8603-488D3660CD83Q34024056-1F7BF040-3BD0-47DF-84C3-55201D990211Q34439644-543BCE4A-1EA9-49AF-8977-562F1092EE48Q34453795-B42AA407-59C5-47FB-BA83-258AF10C41CEQ34763027-43D49755-EBB5-4B8A-B67E-202B741E6E81Q35028393-2215431C-DAF3-483D-B67F-50623BC52733Q35532757-E9A7C34C-7746-4168-8C8E-1FF8AC3B2933Q35536301-62488143-F53F-4ED4-9D9C-BC43DC49DDD0Q35964171-9DAD74A0-AD46-4B55-8F8E-93766319AF2BQ36099563-4F4184E9-650D-4910-91CE-84025F4D2AF6Q36176007-070088B3-550E-470B-9873-1796E0F8A737Q36480230-590039D0-1C93-45E3-893A-E0858BE864A1Q36751888-36F4FC25-52DB-4AE6-B4AA-505C9DDCC256Q36881816-E78EBDC5-22B0-458E-9AB5-B1E44154A9BBQ36991517-6DF46076-857A-4B49-8627-F0884B5D0B29Q37398734-703D204E-EEEE-47D3-B525-5A6E8D801544Q37484275-88DC3678-0566-4A4A-8C5A-B715DA63DF57Q37504788-0A35F363-D5B0-4922-AA52-A185B2A274F2Q37616776-603FBFBC-71B5-4CD4-ABFF-FACBF9D24D15Q37710177-3B648AE3-6817-48B5-9C4C-22DFA1E98848Q37747422-35DFB4BF-AF91-4B5A-BBE6-04CCDC1FA018Q37777912-94B233BC-2563-4605-A7CC-E9B2E7BDAEB5Q37887129-709670D9-63D6-421B-9D6D-C2AE20C4B0EBQ38019568-9663EC11-CDFA-4116-B7C3-6F051093B554Q38124259-33C5AFC8-0187-445B-875E-0EF1FDD2CD7BQ38133369-1204690C-04A7-4AAE-935E-624BB227D0BFQ38563401-B7AC0D7E-1084-45F8-A812-514EE01C34B5Q38733127-CDF4D0D8-04F4-4BF1-B7A4-73AE008F3D8BQ38801648-6FE9E870-D6F1-44BF-BBEB-149E23ABE2E7Q38822588-658BC756-8F2A-4362-9655-9AD99E67F766
P2860
Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins
description
2009 nî lūn-bûn
@nan
2009 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Identification and characteriz ...... metabolic effects of sirtuins
@ast
Identification and characteriz ...... metabolic effects of sirtuins
@en
Identification and characteriz ...... metabolic effects of sirtuins
@en-gb
Identification and characteriz ...... metabolic effects of sirtuins
@nl
type
label
Identification and characteriz ...... metabolic effects of sirtuins
@ast
Identification and characteriz ...... metabolic effects of sirtuins
@en
Identification and characteriz ...... metabolic effects of sirtuins
@en-gb
Identification and characteriz ...... metabolic effects of sirtuins
@nl
prefLabel
Identification and characteriz ...... metabolic effects of sirtuins
@ast
Identification and characteriz ...... metabolic effects of sirtuins
@en
Identification and characteriz ...... metabolic effects of sirtuins
@en-gb
Identification and characteriz ...... metabolic effects of sirtuins
@nl
P2093
P3181
P356
P1433
P1476
Identification and characteriz ...... metabolic effects of sirtuins
@en
P2093
Chi-Ming Che
Ivy K M Law
Karen S L Lam
Priscilla T Y Leung
P304
P3181
P356
10.1002/PMIC.200800738
P407
P577
2009-05-01T00:00:00Z