α-Synuclein and protein degradation systems: a reciprocal relationship. - Test2 - elhamkhani - TriplyDB

α-Synuclein and protein degradation systems: a reciprocal relationship.

α-Synuclein and protein degradation systems: a reciprocal relationship.

http://www.wikidata.org/entity/Q38039881

about

Chaperone-Mediated Autophagy and Mitochondrial Homeostasis in Parkinson's Disease The complex relationships between microglia, alpha-synuclein, and LRRK2 in Parkinson's disease Propagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.Elevated α-synuclein caused by SNCA gene triplication impairs neuronal differentiation and maturation in Parkinson's patient-derived induced pluripotent stem cells Seeking a mechanism for the toxicity of oligomeric α-synuclein VPS35 in Dopamine Neurons Is Required for Endosome-to-Golgi Retrieval of Lamp2a, a Receptor of Chaperone-Mediated Autophagy That Is Critical for α-Synuclein Degradation and Prevention of Pathogenesis of Parkinson's Disease VPS35, the Retromer Complex and Parkinson's Disease.Accumulation of α-synuclein in dementia with Lewy bodies is associated with decline in the α-synuclein-degrading enzymes kallikrein-6 and calpain-1.Structural features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy.Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies.New roles of glycosaminoglycans in α-synuclein aggregation in a cellular model of Parkinson disease.Icariin reduces α-synuclein over-expression by promoting α-synuclein degradation.Cysteine cathepsins are essential in lysosomal degradation of α-synuclein.Abnormal Salivary Total and Oligomeric Alpha-Synuclein in Parkinson's Disease.Up-regulation of SNCA gene expression: implications to synucleinopathies Repurposing the NRF2 Activator Dimethyl Fumarate as Therapy Against Synucleinopathy in Parkinson's Disease Lysosomal impairment in Parkinson's disease.Toll-like receptor 2 is increased in neurons in Parkinson's disease brain and may contribute to alpha-synuclein pathology.TMEM175 deficiency impairs lysosomal and mitochondrial function and increases α-synuclein aggregation.Targeting the chameleon: a focused look at α-synuclein and its roles in neurodegeneration.Parkinson's disease and alpha synuclein: is Parkinson's disease a prion-like disorder?Defective autophagy in Parkinson's disease: lessons from genetics.Chaperoning proteins for destruction: diverse roles of Hsp70 chaperones and their co-chaperones in targeting misfolded proteins to the proteasome The role of autophagy in epileptogenesis and in epilepsy-induced neuronal alterations.Protein Transmission, Seeding and Degradation: Key Steps for α-Synuclein Prion-Like Propagation Ubiquitin-dependent proteolysis in yeast cells expressing neurotoxic proteins.Posttranslational Modifications and Clearing of α-Synuclein Aggregates in Yeast Sirtuins and proteolytic systems: implications for pathogenesis of synucleinopathies.Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies.Chaperone-mediated autophagy and neurodegeneration: connections, mechanisms, and therapeutic implications.The possible involvement of mitochondrial dysfunctions in Lewy body dementia: a systematic review.DT-diaphorase Protects Against Autophagy Induced by Aminochrome-Dependent Alpha-Synuclein Oligomers.Endothelin-converting enzymes degrade α-synuclein and are reduced in dementia with Lewy bodies.Therapeutic potential of autophagy-enhancing agents in Parkinson's disease.Modulation of Neuroinflammation in the Central Nervous System: Role of Chemokines and Sphingolipids.Triptolide Promotes the Clearance of α-Synuclein by Enhancing Autophagy in Neuronal Cells.Mitochondrial impairment and oxidative stress compromise autophagosomal degradation of α-synuclein in oligodendroglial cells.Inhibition of UCH-L1 in oligodendroglial cells results in microtubule stabilization and prevents α-synuclein aggregate formation by activating the autophagic pathway: implications for multiple system atrophy.A combinatorial approach to identify calpain cleavage sites in the Machado-Joseph disease protein ataxin-3.The Neuroprotective Effect of Erythropoietin on Rotenone-Induced Neurotoxicity in SH-SY5Y Cells Through the Induction of Autophagy.

P2860

Q26740364-5444BE36-BADE-46A4-9E38-048558FA7554 Q26853537-AB580078-69EE-42A3-A23F-368CB79F6BEA Q27322513-3B8E7C84-DD9F-4C0F-A152-65036BC16E4F Q27329722-0F0E7FE7-AB02-478B-BA25-FFC49B4EC0B7 Q28080551-83210D21-F10C-486A-9D87-C5CE441BEF77 Q28116122-A2D24C24-160E-428F-8A66-98A1C36DF9E9 Q33708940-EA2B05FA-2729-489B-9EB7-51DCC93F4BC1 Q34739881-8321BFBC-0958-4242-A7B6-BE974C70C630 Q34964902-4A8AE30D-33A4-4E8A-BF53-AEE8089511E7 Q35152946-47252B90-1F86-4FBA-BFCD-C39DA17D43F8 Q35548527-A124694E-E00F-4D59-A2FF-FDE6F0D2C7AD Q35849000-92CFABE6-5C9B-4E23-A6BA-7C0D2849F5B6 Q35910069-2B5E2F51-B97B-4F0D-B432-9B9178657AB2 Q35969183-48AFBFCB-0255-4DF7-BD36-ECFCC823BC7F Q37004246-857A812F-0B8B-4B25-ABBB-126E893414EE Q37091371-A75F1145-0BBB-4161-877C-D47CE3AE2B3D Q37461364-1DC978AE-56ED-4E40-9AB7-6942CF3A30A4 Q37596779-04B15DED-C735-4889-9B91-DBCAC31DCA62 Q37682407-821AC638-A4D0-40AC-9FE4-29407BE21F89 Q38039857-7D4AB26E-D864-4E62-AF8B-C243A82DE46B Q38079791-B1DD1501-2CB8-4106-9A89-95063996FA72 Q38225786-F581DF8E-9A6D-4F2E-BFFA-B1B0B33CDB0C Q38230957-6B90C67E-05F2-4E26-A325-2BA7DD461AFE Q38248845-0086E6E1-4743-4BAA-A092-42F167C3D10F Q38303579-65C67CBD-ECF0-42D3-8A4B-8E2BDD96ECA8 Q38393072-5C325D23-73FF-4A94-A6CE-5B74A7FA4996 Q38444052-38806921-BB7C-4078-8679-809F76C44783 Q38462113-E401DAC4-F2DF-42F8-B6AA-7A7F6C821EBA Q38550428-3BB8AC66-9DB3-45AF-B90C-0E4B3808FFAA Q38553329-9803370C-55BE-4D5F-A2FF-4AA83D81B780 Q38582520-E8799EA3-14BA-41B0-B70F-CF89B1E25E85 Q38704492-907626ED-07B8-495B-9DBB-5A7B3E02BF2C Q38717493-A7A762B9-4184-44A7-BD16-5CCB095A6C0E Q38765856-E808BC41-9916-420A-9337-D29F94707C86 Q38774697-A143AC66-4424-408C-B4D0-861C56B65E61 Q38787738-8491710C-921C-455C-ACD7-1913B2419362 Q38849169-0666FDA9-7FBD-439D-96F4-168787AF7FD6 Q38872092-3F28217F-88AC-4477-87A6-EE29F366302B Q38882170-0B937401-2D11-4E22-A0EC-4CD2ACAA0EA2 Q38986871-37354D99-AEB0-4052-B49A-41865492ADB5

P2860

α-Synuclein and protein degradation systems: a reciprocal relationship.

http://www.wikidata.org/entity/Q38039881

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

α-Synuclein and protein degradation systems: a reciprocal relationship.

@en

type

label

α-Synuclein and protein degradation systems: a reciprocal relationship.

@en

prefLabel

α-Synuclein and protein degradation systems: a reciprocal relationship.

@en

P1433

Q38039881-AD15A003-4EA9-4B5F-A25C-2DBB1021E717

P1476

Q38039881-0A8CACC5-6E4C-4610-9C9B-5EE191E1F525

P2093

Q38039881-5539B286-667A-45DF-8D1B-BDB1B6E798D5

Q38039881-D8952932-064F-44DA-B230-7D22B83E633B

Q38039881-E6412A1B-7958-4A2A-86E6-F945FA032A1E

P2860

Q38039881-005C070C-D426-4B70-9798-062E74BBA792

Q38039881-034DBC50-99F7-473A-9E3C-A3F579C262E1

Q38039881-08310C08-8D43-48A4-BACF-454D824691DB

Q38039881-0A891C34-8DF3-4750-B2DF-330CCCDCD81C

Q38039881-0EA9EE17-7C1F-479E-B1B3-0AC0416FE662

Q38039881-100BB158-4BF7-4FAF-8BA3-495BE48BA9CA

Q38039881-1366DCC7-F1BD-453C-AE27-F7F592BC92C4

Q38039881-14764457-8A49-4EBE-98E7-12475CFAE325

Q38039881-19FC18FB-02DA-4000-9836-2082DC07EA96

Q38039881-1CB3FEAC-94C1-4205-8635-CC2274EBC40C

P2888

Q38039881-D92A1F4C-8354-4205-98C9-E7BFFF5A99BB

P304

Q38039881-D090034B-42A7-4C46-8686-E2F1751A3EB4

P31

Q38039881-BF60AB31-C33C-4EBE-8B1C-AB66C829AF02

P356

Q38039881-AE9D65D6-A710-4BBE-AA18-CC8D174801E4

P433

Q38039881-45094F86-82BA-4F42-B596-BDE51617A62C

P478

Q38039881-A4C6DCB0-C893-4C17-9C4F-2DB5CBF0CBF6

P577

Q38039881-C01E5202-CAB7-41B7-8157-45E455692054

P5875

Q38039881-C8605860-72E0-4AD9-BF55-DAD55428B6B9

P6179

Q38039881-2A678B4C-D9C9-4DBA-BF49-1CBF37064D75

P698

Q38039881-AA53D497-62E2-4B7F-870D-BB3225243B3B

P921

Q38039881-D2821C3A-6264-44B0-8519-1656B463F552

P356

S12035-012-8341-2

P1433

Molecular Neurobiology

P1476

α-Synuclein and protein degradation systems: a reciprocal relationship.

@en

P2093

Leonidas Stefanis

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

Maria Xilouri

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

Oystein Rod Brekk

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

P2860

Nix is a selective autophagy receptor for mitochondrial clearance

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

The spectrum of human kallikrein 6 (zyme/protease M/neurosin) expression in human tissues as assessed by immunohistochemistry

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

Proteolytic cleavage of extracellular secreted {alpha}-synuclein via matrix metalloproteinases

The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress

Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice

DJ-1 cleavage by matrix metalloproteinase 3 mediates oxidative stress-induced dopaminergic cell death

Gaucher disease glucocerebrosidase and α-synuclein form a bidirectional pathogenic loop in synucleinopathies

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

P2888

s12035-012-8341-2

P304

537-551

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

P31

scholarly article

P356

10.1007/S12035-012-8341-2

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

P433

2

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

P478

47

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

P577

2012-09-02T00:00:00Z

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

P5875

230783274

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

P6179

1003237161

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

P698

22941029

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

P921