Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress. - Wikidata - awgldk - TriplyDB

Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress.

Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress.

http://www.wikidata.org/entity/Q35698011

about

Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondria SIRT2 as a Therapeutic Target for Age-Related Disorders SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1 Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice Effects of Oxidative Stress on Mesenchymal Stem Cell Biology Sirtuin functions and modulation: from chemistry to the clinic Mitochondrial Redox Signaling and Tumor Progression Critical Roles of Reactive Oxygen Species in Age-Related Impairment in Ischemia-Induced Neovascularization by Regulating Stem and Progenitor Cell Function The Role of Mitochondrial DNA in Mediating Alveolar Epithelial Cell Apoptosis and Pulmonary Fibrosis Forever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration Regulation of glycolysis and gluconeogenesis by acetylation of PKM and PEPCK Impact of oxidative stress on exercising skeletal muscle Protective effects and mechanisms of sirtuins in the nervous system Sirtuin 1 and sirtuin 3: physiological modulators of metabolism Redox regulation of mitochondrial biogenesis SIRT1 and SIRT2: emerging targets in neurodegeneration New insights into the role of mitochondrial dynamics and autophagy during oxidative stress and aging in the heart Sirtuins in hematological aging and malignancy Regulation of Akt signaling by sirtuins: its implication in cardiac hypertrophy and aging Sirtuins in Cancer: a Balancing Act between Genome Stability and Metabolism PGC-1α, mitochondrial dysfunction, and Huntington's disease Exploring the electrostatic repulsion model in the role of Sirt3 in directing MnSOD acetylation status and enzymatic activity Cell cycle regulators guide mitochondrial activity in radiation-induced adaptive response Sirtuins, metabolism, and DNA repair From sirtuin biology to human diseases: an update Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases Protein lysine acylation and cysteine succination by intermediates of energy metabolism Involvement of free radicals in breast cancer Role of mitochondria in nonalcoholic fatty liver disease The role of sirtuins in cardiac disease Mitochondrial protein acetylation as a cell-intrinsic, evolutionary driver of fat storage: chemical and metabolic logic of acetyl-lysine modifications Function of the SIRT3 mitochondrial deacetylase in cellular physiology, cancer, and neurodegenerative disease Redox control of senescence and age-related disease SIRT3 in Cardiac Physiology and Disease Quality control systems in cardiac aging The hallmarks of aging Mitochondrial protein acetylation is driven by acetyl-CoA from fatty acid oxidation Interplay between oxidant species and energy metabolism Oxidative stress and ROS metabolism via down-regulation of sirtuin 3 expression in Cmah-null mice affect hearing loss

P2860

Q21129226-B879E304-EAF6-4761-9427-7F0EE398B0C5 Q21129286-BF698639-FE42-48AA-A671-EDC4C315A8DC Q24294017-5EC7F812-7FDC-44A7-AC85-FE719E127808 Q24304507-C1B4C1F0-6A2A-4EA1-A4CA-77865E82FA7C Q24597912-D6859296-D850-475D-9334-63AEABA28A6C Q26740408-7494FA07-20A6-4339-9E79-DB2C2935EF1A Q26745884-80C954CC-A7C9-4629-B24C-C224D99865BD Q26749592-2CB5005B-094A-4E7F-9562-A74E23A2B24C Q26772290-B7D95546-5AEF-4ED8-B5E7-A9A4CE908771 Q26786969-C19528B6-2F1E-42E0-98D9-DD2E7DAD137A Q26825012-776E4343-700F-4C0D-BB62-DA3830E27410 Q26825322-6FE68C53-645D-448E-BFFE-AF28C02F51F5 Q26825387-D55A26C2-994F-4C9A-8CA5-9BDDB5381180 Q26825585-CC77F0AE-3428-4F6E-8DD6-93804983BD9A Q26828607-5CDA3DF9-9689-4E23-BCEB-8821D3689E8A Q26849213-BA72A6A0-9E7C-444E-8605-3C8D90CDE7A4 Q26864929-48780000-3654-44D3-9CDE-8091E89617DC Q26865574-A5ACFA86-2329-4A87-A144-000DD9A08982 Q26991467-EFE81183-C2F7-48CA-BB9A-09D555647047 Q26998765-5995F76D-6A0C-4D33-A906-24F0483AEE21 Q27001553-2F1540AE-6E86-412B-8822-F1D60465D352 Q27001671-A0284CC2-210E-4DD9-A8F6-D317F46C1D76 Q27014003-20B4A726-24C8-4301-9484-F816CBB7220D Q27014767-E938B615-C556-4061-A1A4-7CE63C072B3E Q27015759-AE1993C9-2DF2-48B8-A327-1C1F91BB61A3 Q27022606-D0A85F6C-FF87-4D1B-97B8-1678FB248748 Q27024524-572AC641-6D23-4AB2-ADD0-E3309F4168A1 Q27027406-42405049-79EF-424A-B668-DAE8337C73D8 Q27027944-085619D6-4147-4E62-B3F2-5BCA7D7B8959 Q27028142-39DADE21-2C2A-4A78-B7F8-DB67DAA425F1 Q27693274-4DBD24A8-4052-4693-9AB5-697405D8EE12 Q27694582-7BA8A39A-FF7E-498D-A9B8-5F2D2341EA16 Q28068499-C903E5C9-5F47-43FE-B96F-1A73FB9709D4 Q28074230-1B80B6CC-3FBA-42C3-BC86-0B3D7CBDF193 Q28076837-CF514A7C-6AFD-4539-9203-15D7D2C90919 Q28084341-FE70F31B-9F62-4DDE-8331-FABAC330BC82 Q28131641-AFF57CDB-C0E6-48DE-84C9-FBDA008818AC Q28307555-C235AF93-FA83-4139-9695-B711055B0FC3 Q28383905-DFC27FBF-DF24-43E8-9831-22AC300B1F84 Q28389690-4BE07C8F-5981-499E-A35D-9DF4F550DAC0

P2860

Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress.

http://www.wikidata.org/entity/Q35698011

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

2010年论文

@zh

2010年论文

@zh-cn

name

Sirt3-mediated deacetylation o ...... ctivity in response to stress.

@ast

Sirt3-mediated deacetylation o ...... ctivity in response to stress.

@en

type

label

Sirt3-mediated deacetylation o ...... ctivity in response to stress.

@ast

Sirt3-mediated deacetylation o ...... ctivity in response to stress.

@en

prefLabel

Sirt3-mediated deacetylation o ...... ctivity in response to stress.

@ast

Sirt3-mediated deacetylation o ...... ctivity in response to stress.

@en

P1433

Q35698011-BC5FA5D0-869E-4904-A527-9871CCF472B3

P1476

Q35698011-FAABFA11-62B8-4B09-A8F3-E5517B595EF6

P2093

Q35698011-46DEC0A4-EB65-433B-B6AB-97D18B9E3446

Q35698011-484415E4-841A-4333-AD17-8EE007F7B11A

Q35698011-742D6DB2-2556-465C-8AB1-26E21B5852A3

Q35698011-80086D60-2CE9-45D8-9720-44F9E2E6D524

Q35698011-9D8A6BA6-2BD3-4532-A51D-E99F3A7BDA91

Q35698011-A4190632-706A-4C7C-855F-E2B2EF88048E

Q35698011-B8BE8B7B-5C18-44A5-B181-2DC4C9651061

Q35698011-C1948470-4027-4C27-A995-D571F16C1B3D

Q35698011-CD5B98D2-634E-474D-BA78-D7BF7712F3F1

Q35698011-DE5E2F47-6953-4E16-9236-7AD834A924A8

P2860

Q35698011-17F20CBF-5219-47F1-A04A-0E18262397F7

Q35698011-1CCB4594-3C14-464E-AA73-168AB6566B8D

Q35698011-272E9379-4E40-4412-B059-C767D3B2A2B5

Q35698011-27CB9057-B143-4348-BEAE-67A1756F3DB2

Q35698011-2909BA4E-5070-4897-9424-DCB91AEAD75D

Q35698011-31254485-CA10-4364-837E-490DB1CBAA2F

Q35698011-3A0D0307-78EB-449F-BEE0-788B129A4C0E

Q35698011-53E9F9D6-35BB-4EF2-92BC-04C99BF3D2D8

Q35698011-A38BB654-14CC-4C3C-9491-C6F5CB29A7C4

Q35698011-AC13034C-341E-4D74-B234-3AEF4B8B0333

P304

Q35698011-F3398056-A1D9-4BC4-BBBF-7B54922810AF

P31

Q35698011-A54DA49B-08EB-4102-89C5-581AD499455A

P356

Q35698011-C937E0BB-0CE3-4432-8C43-0A12D6B7B7A1

P433

Q35698011-3F5478C7-FD28-4F99-992C-79630C267E9F

P478

Q35698011-632FFD3C-B2C3-4215-86C2-52FCAC82D4DC

P50

Q35698011-5BB56166-149A-49FC-9773-EEE6999CA79D

Q35698011-DE97EB1F-0834-467C-9DD3-3D421D5D7B88

Q35698011-F6412FAA-997B-485E-853A-0D031FD6FBA2

P577

Q35698011-61AE2F79-1294-48C6-A6E6-C52508C27737

P5875

Q35698011-5E064285-0BA2-4BE3-B727-B667C93207BC

P698

Q35698011-6B2BCCE6-78C3-4A45-8515-838DF29A5C61

P932

Q35698011-C9FC9D9E-0734-4D24-9C4D-C30349966A1D

P356

J.MOLCEL.2010.12.013

P1433

P1476

Sirt3-mediated deacetylation o ...... activity in response to stress

@en

P2093

Alicia K Olivier

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

David Gius

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

Haiyan Jiang

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

Hyun-Seok Kim

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

J Daniel Pennington

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

Ozkan Ozden

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

Randa Tao

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

Salisha Hill

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

Seong-Hoon Park

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

W Hayes McDonald

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

P2860

Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

SIRT1 deacetylates and positively regulates the nuclear receptor LXR

SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria

SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress

The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase

Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation

The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells

Recent progress in the biology and physiology of sirtuins

A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis

Treatment of non-alcoholic fatty liver disease.

P304

893-904

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

P31

scholarly article

P356

10.1016/J.MOLCEL.2010.12.013

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

P433

6

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

P478

40

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

P50

Charles Robert Flynn

Douglas R Spitz

Mitchell C Coleman

P577

2010-12-01T00:00:00Z

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

P5875

49697141

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

P698

21172655

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

P932

3266626

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