Nicotinamide-induced mitophagy: event mediated by high NAD+/NADH ratio and SIRT1 protein activation. - Wikidata - awgldk - TriplyDB

Nicotinamide-induced mitophagy: event mediated by high NAD+/NADH ratio and SIRT1 protein activation.

Nicotinamide-induced mitophagy: event mediated by high NAD+/NADH ratio and SIRT1 protein activation.

http://www.wikidata.org/entity/Q36003773

about

Sirt1 and the Mitochondria Mitochondrial targets for pharmacological intervention in human disease New Insights for Oxidative Stress and Diabetes Mellitus New method to assess mitophagy flux by flow cytometry Mild mitochondrial metabolic deficits by α-ketoglutarate dehydrogenase inhibition cause prominent changes in intracellular autophagic signaling: Potential role in the pathobiology of Alzheimer's disease Mitochondrial stress signaling promotes cellular adaptations Nicotinamide forestalls pathology and cognitive decline in Alzheimer mice: evidence for improved neuronal bioenergetics and autophagy procession.Nicotinamide ameliorates palmitate-induced ER stress in hepatocytes via cAMP/PKA/CREB pathway-dependent Sirt1 upregulation Polyol pathway exacerbated ischemia/reperfusion-induced injury in steatotic liver WISP1: Clinical insights for a proliferative and restorative member of the CCN family mTOR- and HIF-1α-mediated aerobic glycolysis as metabolic basis for trained immunity.Nicotinamide exerts antioxidative effects on senescent cells.Grape seed extract targets mitochondrial electron transport chain complex III and induces oxidative and metabolic stress leading to cytoprotective autophagy and apoptotic death in human head and neck cancer cells.The Redox Code.High-Dose Nicotinamide Suppresses ROS Generation and Augments Population Expansion during CD8(+) T Cell Activation Novel directions for diabetes mellitus drug discovery Mitochondrial complex I activity and NAD+/NADH balance regulate breast cancer progression.Autophagy in Ischemic Livers: A Critical Role of Sirtuin 1/Mitofusin 2 Axis in Autophagy Induction.Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADH Deacetylation by SIRT1 Reprograms Inflammation and Cancer SIRT1 is a Highly Networked Protein That Mediates the Adaptation to Chronic Physiological Stress.Potential Therapeutic Benefits of Maintaining Mitochondrial Health in Peripheral Neuropathies.MKK3 regulates mitochondrial biogenesis and mitophagy in sepsis-induced lung injury.Sirtuins' modulation of autophagy.Senescence suppressors: their practical importance in replicative lifespan extension in stem cells.Programming apoptosis and autophagy with novel approaches for diabetes mellitus.Integrative metabolomics as emerging tool to study autophagy regulation.Nicotinamide Adenine Dinucleotide Metabolism and Neurodegeneration.Harnessing the Power of SIRT1 and Non-coding RNAs in Vascular Disease.Nicotinamide protects hepatocytes against palmitate-induced lipotoxicity via SIRT1-dependent autophagy induction.Sirtuins as modifiers of Parkinson's disease pathology.Could Sirtuin Activities Modify ALS Onset and Progression?The pharmacological regulation of cellular mitophagy.Nicotinamide preferentially protects glycolysis in dermal fibroblasts under oxidative stress conditions.Nicotinamide is an inhibitor of SIRT1 in vitro, but can be a stimulator in cells.Modulation of Mitochondrial Membrane Potential and ROS Generation by Nicotinamide in a Manner Independent of SIRT1 and Mitophagy CYP-epoxygenase metabolites of docosahexaenoic acid protect HL-1 cardiac cells against LPS-induced cytotoxicity Through SIRT1 SIRT Is Required for EDP-Mediated Protective Responses toward Hypoxia-Reoxygenation Injury in Cardiac Cells.SIRT1 and stem cells: In the forefront with cardiovascular disease, neurodegeneration and cancer.New and revisited approaches to preserving the reperfused myocardium.

P2860

Q26772894-3430005C-A8F7-4D00-BCFD-7140B6AB8E77 Q26824514-D8EEE71C-4147-4AA6-8B2A-70259A5116C2 Q28080679-D6A98204-2959-4B64-A4D6-86111A91DDDB Q28383994-96A3AA85-26D8-474B-99FE-7B8A128A0584 Q28393932-D4BB3F5B-39CB-4135-8B76-FE4049FCF511 Q28395762-992FD377-3677-4ADE-AC2D-77E6EE4B69EF Q30537554-1259697D-0011-49F5-87D8-C159FBB3CE16 Q33731432-5EB52506-4F8C-41E6-9B5D-94A3AC2E1FED Q33746091-7A063EEB-93B1-4F1F-8C6F-116EE613FFBF Q34381111-43301C45-1A05-485C-A4E8-413E45531D41 Q34481477-02C13279-1068-4A8E-939D-1EE591EBAE3E Q35188501-823B1B06-8731-4842-B768-EC0A7D7C61F4 Q35812645-AC6FF8FC-0131-475B-BB30-0C83A4657E16 Q36086638-AF392563-6F66-4361-8A80-E718CEE0D4F6 Q36221473-44B6DEB3-3D99-4BAE-9856-FD23BCE1D9AB Q36487424-4DCE1D0F-8941-4ADB-BBC2-A6748B09B4BD Q36638143-C3610866-9F44-4A9E-8411-1734A7E6510F Q36657697-C61BFC5F-A605-49F1-96DF-D74EC18C392E Q36727468-B20AC566-8816-4CE6-8340-BC5F7A38D5EF Q37150502-1E00A6DA-B1BA-4FC6-A2C5-E8AB096AC3A7 Q37150520-633C0226-1E45-4906-8D2A-927F303D7FFE Q37168753-3DFB4488-FE50-4039-928F-1BAB45E29D57 Q37656058-DB17A71A-79DF-4645-AF25-4584B4253405 Q38108575-2D9641A2-A36E-4270-9F10-B93583597213 Q38232804-505592DF-C518-4AAA-99F9-C76301EAFE45 Q38367977-0B71A40E-E62A-46EA-8F0C-7E6F09EA3C36 Q38636818-28676441-8BFD-4351-882D-8ADB9D1246FC Q38678550-498FC164-B2B0-489C-8589-1479BF20BC96 Q38789540-6334CFB1-C398-4563-B0E7-9123408632D1 Q38803521-6C3B6328-CAFA-4A65-92DA-896F88DD7936 Q38893382-30703D22-F38D-447E-B628-F2385E37158A Q39036105-9BA86427-7E0B-44B5-8303-6483A659CEDB Q39095156-5E455D66-8450-4E85-A63F-2A734931649B Q39134303-A3DC20BC-025D-4AE7-8235-ECCDC55B815B Q39247299-3621F437-87C2-4B6F-93E5-E215EEBAB00C Q41288627-E2E890B7-D41F-43F2-A23A-9FB89DE864FE Q41443653-890757B2-6488-4237-BA22-FA236C41AF1F Q41877334-9C5D46AC-898E-4204-99A0-1777DF8A73BC Q43197576-D1D9BAF8-7962-4698-94E7-DD1C3CFC948D Q45064238-B041EDBA-F3A5-4D1E-9B3E-3582F663D526

P2860

Nicotinamide-induced mitophagy: event mediated by high NAD+/NADH ratio and SIRT1 protein activation.

http://www.wikidata.org/entity/Q36003773

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Nicotinamide-induced mitophagy ...... and SIRT1 protein activation.

@ast

Nicotinamide-induced mitophagy ...... and SIRT1 protein activation.

@en

type

label

Nicotinamide-induced mitophagy ...... and SIRT1 protein activation.

@ast

Nicotinamide-induced mitophagy ...... and SIRT1 protein activation.

@en

prefLabel

Nicotinamide-induced mitophagy ...... and SIRT1 protein activation.

@ast

Nicotinamide-induced mitophagy ...... and SIRT1 protein activation.

@en

P1433

Q36003773-5B40DB31-D262-430E-B64F-817C35C8559E

P1476

Q36003773-DCE78F6B-A2E9-47A5-B0D5-C90EB4375F19

P2093

Q36003773-24CBA8BC-DAA9-4AAE-B0F9-25C3555A3297

Q36003773-B208E03E-E958-4A9C-9BFE-AA9D0E55E205

Q36003773-C81B837E-A2EC-481E-BDE0-00DA776747D9

P2860

Q36003773-006E2674-ED76-4981-AFC6-2243BA96E1BC

Q36003773-03CA6DD2-B423-495D-9CE6-66BB892CD56E

Q36003773-04BAFADC-9418-41AE-A058-FC2B814AA26D

Q36003773-1A13B030-8B96-4C97-A645-A556CCAE0709

Q36003773-21FA2160-A755-4823-AE03-0294E7182E63

Q36003773-222D8DF7-8ADA-4C12-9542-688498A54AD0

Q36003773-2DDD9CD5-49CF-4084-95DB-53BCE4E2BD6A

Q36003773-43450A61-F0CC-4B93-8D13-F57D241E63AF

Q36003773-48F9C1F3-8B88-4C86-82B8-B70B48281F4B

Q36003773-4E1504C8-00CF-410D-A215-1080FC58B4C5

P304

Q36003773-765DD93E-B2EC-437A-9527-F2E300A00576

P31

Q36003773-A11DE532-A1F0-408A-84B7-0D163A34BCBA

P356

Q36003773-8EE0B14D-94A0-40E8-AD8B-3146473646CC

P407

Q36003773-940FA499-E5D1-4731-8EA1-FC21A9021933

P433

Q36003773-AC0E7A83-0B0D-451B-82BE-391682B0A9A0

P478

Q36003773-61864D64-5D20-4D0A-BBBC-ED9FAC56077A

P577

Q36003773-1E98E273-FE6E-4D9B-89AC-77A29B99EC1A

P698

Q36003773-F72E6BC8-7AE1-4E90-A77D-307332A81961

P932

Q36003773-AF3F8852-1720-403F-AD1A-6CA9C48EA344

P356

JBC.M112.363747

P1433

Journal of Biological Chemistry

P1476

Nicotinamide-induced mitophagy ...... and SIRT1 protein activation.

@en

P2093

Eun Seong Hwang

http://www.w3.org/2001/XMLSchema#string

Hyun Tae Kang

http://www.w3.org/2001/XMLSchema#string

So-young Jang

http://www.w3.org/2001/XMLSchema#string

P2860

hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase

Mitochondrial fission and fusion mediators, hFis1 and OPA1, modulate cellular senescence

Enzymes in the NAD+ salvage pathway regulate SIRT1 activity at target gene promoters

A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy

The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver

Biochemical effects of SIRT1 activators

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

Fission and selective fusion govern mitochondrial segregation and elimination by autophagy

Reconstructing eukaryotic NAD metabolism

Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan

P304

19304-19314

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M112.363747

http://www.w3.org/2001/XMLSchema#string

P407

P433

23

http://www.w3.org/2001/XMLSchema#string

P478

287

http://www.w3.org/2001/XMLSchema#string

P577

2012-04-09T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

22493485

http://www.w3.org/2001/XMLSchema#string

P932

3365962

http://www.w3.org/2001/XMLSchema#string