Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperones. - Wikidata - awgldk - TriplyDB

Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperones.

Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperones.

http://www.wikidata.org/entity/Q40634794

about

PARIS (ZNF746) repression of PGC-1α contributes to neurodegeneration in Parkinson's disease Dopamine covalently modifies and functionally inactivates parkin Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection How does parkin ligate ubiquitin to Parkinson's disease?Parkin-mediated monoubiquitination of the PDZ protein PICK1 regulates the activity of acid-sensing ion channels Parkin Regulation and Neurodegenerative Disorders Pathologic and therapeutic implications for the cell biology of parkin Mitochondria and mitophagy: the yin and yang of cell death control Molecular chaperone-mediated rescue of mitophagy by a Parkin RING1 domain mutant Mitophagy and heart failure Parkin is protective against proteotoxic stress in a transgenic zebrafish model Parkin occurs in a stable, non-covalent, approximately 110-kDa complex in brain The effects of oxidative stress on parkin and other E3 ligases.Role of the ubiquitin proteasome system in Parkinson's disease.Identification and characterization of a novel endogenous murine parkin mutation.Emerging roles of mitochondria ROS in atherosclerotic lesions: causation or association?Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity.Are heat shock proteins therapeutic target for Parkinson's disease?Parkin loss of function contributes to RTP801 elevation and neurodegeneration in Parkinson's disease.Molecular chaperones in Parkinson's disease--present and future Mitochondrial dynamics and Parkinson's disease: focus on parkin.Mitochondrial Quality Control via the PGC1α-TFEB Signaling Pathway Is Compromised by Parkin Q311X Mutation But Independently Restored by Rapamycin Regulation of ubiquitin-proteasome system mediated degradation by cytosolic stress.Parkin cooperates with GDNF/RET signaling to prevent dopaminergic neuron degeneration The parkin protein as a therapeutic target in Parkinson's disease.Ubiquitin-proteasome system dysfunction in Parkinson's disease: current evidence and controversies.The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases.AF-6 is a positive modulator of the PINK1/parkin pathway and is deficient in Parkinson's disease.Emerging pathways in genetic Parkinson's disease: autosomal-recessive genes in Parkinson's disease--a common pathway?Parkin selectively alters the intrinsic threshold for mitochondrial cytochrome c release.Genetic insights into sporadic Parkinson's disease pathogenesis.Loss of NEDD4 contributes to RTP801 elevation and neuron toxicity: implications for Parkinson's disease.The role of parkin in familial and sporadic Parkinson's disease.Protective role of heat shock proteins in Parkinson's disease.Parkin, A Top Level Manager in the Cell's Sanitation Department.Proteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis.Parkin, PINK1 and mitochondrial integrity: emerging concepts of mitochondrial dysfunction in Parkinson's disease.Regulation of Parkin E3 ubiquitin ligase activity.E3 ubiquitin ligases in protein quality control mechanism.Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences.

P2860

Q24294809-8AB4DFA3-D2F8-45E9-BF29-B0B724B18F1A Q24338423-3BE864A3-7030-427F-BF26-ACE8DF843682 Q24339442-E9D9A078-31FD-413E-A9B9-414FF08FC1BA Q24537156-277BA74A-3C02-447F-B8D0-734BA7FEB7DD Q24679424-196E24FF-7533-41C9-BB49-D92C7C0F99B4 Q26770443-25056083-C2EC-48BE-8261-D675C4AD46F2 Q27010567-B257E784-0F0C-4860-8815-0FFD4680C91E Q27028020-893DA9EE-3289-4DCA-9C79-DCBAFD8CFE10 Q28116653-65F3E1E1-BC79-4EF7-996E-7C058147E0AC Q28388167-013A0D51-BD41-4568-8A68-6F20D81828D5 Q28474988-0EF121D8-01CD-4EAF-8A36-E3B387970F3C Q28505637-AC1A80A3-8328-41F2-85A6-C3280FFB5198 Q30273796-34CA3890-9F1C-446A-9DC4-A4895FD107A2 Q33307874-3814FDFF-180F-467F-BE3A-44E035A502A7 Q34012526-3D62E401-ACF3-4BEA-8568-3D1A6377CE98 Q34239967-266D0DE8-57A4-43AC-B168-89022F0823FC Q34528753-67A7672A-18AE-4E8D-9FBA-E6F2EC7ACC85 Q34597188-FE6E92BA-9E22-4696-AE4F-733C2C4ECEEA Q35679526-FDE477E2-F0F1-458F-9C87-3F3BEA8C7DB2 Q35688796-221C1828-8313-4648-9756-AB777D651023 Q35799161-401666BF-F5FD-4536-94D7-B9EC65D73FFC Q36064409-CAD71BDF-39B8-4CC6-A277-DFC42BDEDFB4 Q36095718-93456BF9-CF87-4E31-A538-E943F817E34B Q36179023-9559032A-B53E-4767-9CEE-849A4AC53E4A Q37004729-03387410-6FCC-45D7-823B-D33C3651DEFD Q37027500-333CD602-951A-43E4-8B14-A2B0BF0BC5D8 Q37064056-7976D891-91AE-470D-BFCD-65BDF0E6EB04 Q37243137-24FD0954-F832-48C7-8CCB-14879EB34F5F Q37330543-9946FE54-056B-4ECF-85C4-C6AD11BF523C Q37397403-FC2BF72F-656A-46D1-8CB2-131AF178EA76 Q37583402-6AA2BBB0-6E37-4324-A27E-81D44910A1CA Q37644778-C717B781-9FB6-40B8-869C-F7D9BEBFEC67 Q37699215-6EEAF3DE-B710-4A2E-B35F-724357CF5685 Q37826616-4F7328C1-A145-4822-B0D5-CF959CF57812 Q37883939-555616FF-37D3-438E-B9D4-7AD131814152 Q37918059-A8A7EE22-E1DF-4A7D-9B1A-53584E4E28EF Q37953288-10785BF8-E541-430D-A37C-D50735D81394 Q38004927-E7B3178B-5522-43EC-985D-321383C468A1 Q38011658-1F05DA07-8693-4E05-8B1E-3644A6CC1D6D Q38021865-FE26F9BC-A152-477B-BB11-2479DAE0F551

P2860

Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperones.

http://www.wikidata.org/entity/Q40634794

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

2003年论文

@zh

2003年论文

@zh-cn

name

Inactivation of parkin by oxid ...... role of molecular chaperones.

@en

type

label

Inactivation of parkin by oxid ...... role of molecular chaperones.

@en

altLabel

Inactivation of Parkin by Oxidative Stress and C-terminal Truncations

@en

prefLabel

Inactivation of parkin by oxid ...... role of molecular chaperones.

@en

P1433

Q40634794-960B6605-BB0C-4080-A993-4CC4DBB200CE

P1476

Q40634794-E0B44B88-7674-4F0D-A9A1-550A0FDB0BB7

P2093

Q40634794-02287CB9-64C3-4E08-AE16-73EAA4E034FE

Q40634794-46CAF646-AD89-4A79-97E7-C7EDECD9427C

Q40634794-478CB547-2A3F-4D0E-9447-6F256E91F869

P2860

Q40634794-006965D8-1ABB-4320-95E8-CE5A58413003

Q40634794-01D3619F-91D9-4817-985D-E5BC758261A7

Q40634794-0697BD11-C0EC-4E71-A293-7EF9D0AF4518

Q40634794-0B1312E4-FE72-4C12-8DEA-142AE38DF94B

Q40634794-0D4934A2-9BB8-4048-AC89-AE48D850E1A4

Q40634794-10694AF5-5510-4992-A51E-7736F18DE7F0

Q40634794-194B6D82-E767-425A-AA42-48A964B3B80A

Q40634794-1AD26956-49D7-4818-B77F-6DC0888E1715

Q40634794-1C4F42FE-301F-4C7B-A6DE-2CDD35DE4557

Q40634794-1F224882-F624-4E74-863B-0CC6184D6D25

P304

Q40634794-EB34A3D3-D2A6-4914-81BC-7B5B658D77EF

P31

Q40634794-3B22F669-1FF0-42FC-A577-9BF15D656918

P356

Q40634794-3BFA5C0C-3CD3-4FA8-99F9-7AAF03970FE6

P407

Q40634794-42A8F831-1DC4-4547-BDB8-C58D504E8641

P433

Q40634794-57DC47EF-60A6-470D-8360-76C7051A4618

P478

Q40634794-C82F2CBD-6914-4122-842B-2719577AC46A

P50

Q40634794-5501DB09-3A29-4E7C-A277-01AEE1201899

Q40634794-57C4C6DD-51DE-4882-AD5A-73443AE206A3

P577

Q40634794-C4EFB095-3380-4897-8605-2D3796F22D56

P698

Q40634794-61573D79-3A2A-448E-87EC-5960226E378D

P921

Q40634794-9EDD576E-DD84-4F85-9A0A-E7E345703D03

P356

P1433

Journal of Biological Chemistry

P1476

Inactivation of parkin by oxid ...... role of molecular chaperones.

@en

P2093

Iris H Henn

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

Penelope C Kay-Jackson

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

Ulrich Heller

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

P2860

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity

Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1

An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin

Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease

Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity

CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity

Molecular chaperones in the cytosol: from nascent chain to folded protein

P304

47199-47208

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

P31

scholarly article

P356

10.1074/JBC.M306769200

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

P407

P433

47

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

P478

278

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

P50

Konstanze F Winklhofer

P577

2003-09-12T00:00:00Z

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

P698

12972428

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

P921

molecular chaperones