%D8%A3%D9%84%D9%81%D8%A7-%D8%B3%D8%A7%D9%8A%D9%86%D9%88%D9%83%D9%84%D9%8A%D9%86Alfa-sinucle%C3%AFnaCategory:Alpha-synuclein%CE%91-SynucleinAlpha-synucleinAlfa-sinucle%C3%ADnaAlpha-synucl%C3%A9ineAlfa-sinucle%C3%ADna%D7%90%D7%9C%D7%A4%D7%90-%D7%A1%D7%99%D7%A0%D7%95%D7%A7%D7%9C%D7%90%D7%99%D7%9FAlfa-sinucleina%CE%91-%E3%82%B7%E3%83%8C%E3%82%AF%E3%83%AC%E3%82%A4%E3%83%B3Alpha-synucleinumAlfa-synucle%C3%AFneAlfa-sinucle%C3%ADnaAlfasynuklein%D0%90%D0%BB%D1%8C%D1%84%D0%B0-%D1%81%D0%B8%D0%BD%D1%83%D0%BA%D0%BB%D0%B5%D1%97%D0%BDQ288591
about
P688
DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formationWild-type but not Parkinson's disease-related ala-53 --> Thr mutant alpha -synuclein protects neuronal cells from apoptotic stimuliCa2+ binding to alpha-synuclein regulates ligand binding and oligomerizationTubulin seeds alpha-synuclein fibril formationMagnesium inhibits spontaneous and iron-induced aggregation of alpha-synucleinRelationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicityCoordination features and affinity of the Cu²+ site in the α-synuclein protein of Parkinson's diseaseAcceleration of alpha-synuclein aggregation by homologous peptidesRedox activity of α-synuclein-Cu is silenced by Zn₇-metallothionein-3Association of metallothionein-III with oligodendroglial cytoplasmic inclusions in multiple system atrophyA role for alpha-synuclein in the regulation of dopamine biosynthesisDequalinium-induced protofibril formation of alpha-synucleinInhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compoundsα-Synuclein modifies huntingtin aggregation in living cellsModulation of the trafficking of the human serotonin transporter by human alpha-synucleinThe chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicityThe H50Q mutation enhances α-synuclein aggregation, secretion, and toxicityα-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent mannerProteolytic cleavage of extracellular secreted {alpha}-synuclein via matrix metalloproteinasesalpha-Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeletonAlpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicityParkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer modelEvidence that alpha-synuclein functions as a negative regulator of Ca(++)-dependent alpha-granule release from human plateletsThe role of oxidative stress in Parkinson's diseaseParkinsonian neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and alpha-synuclein mutations promote Tau protein phosphorylation at Ser262 and destabilize microtubule cytoskeleton in vitroAlpha-synuclein and polyunsaturated fatty acids promote clathrin-mediated endocytosis and synaptic vesicle recyclingProteomics analysis identifies phosphorylation-dependent alpha-synuclein protein interactionsFK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53TMolecular determinants of α-synuclein mutants' oligomerization and membrane interactionsChaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by HipUpregulation of alpha-synuclein by lipopolysaccharide and interleukin-1 in human macrophagesPre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease modelsα-Synuclein as an intrinsically disordered monomer--fact or artefact?The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranesEvidence that alpha-synuclein does not inhibit phospholipase DMutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodiesFluorescence microscopy and 3D image reconstruction of cytokine initiated disruption of the Parkinson disease associated proteins alpha-synuclein, tau and ubiquitin in cultured glial cellsPolo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivoModulation of dopamine transporter function by alpha-synuclein is altered by impairment of cell adhesion and by induction of oxidative stressDirect visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain
P921
Q21146396-CBDF61C0-AF4E-4C5A-9288-B305AA1D375BQ22254116-062F0715-313C-44A6-B6AD-CEF7E57CF70FQ24291150-0264CFCB-322C-4F5A-A097-3FF5A04CE72BQ24291881-0B0013D2-38EE-4BBC-9D8F-174419BC6881Q24292317-89B0E705-0C91-4285-AE44-00A22F2DFEB7Q24293089-48510717-FE83-45F8-916C-ABB7741D8B3CQ24293110-59A52C80-83E3-4774-8401-8B715AEAD7B0Q24293132-E06B7802-E895-40AD-AEF7-FF1D2082D294Q24293189-4422735D-3D10-4AAE-AB58-F54BFEE26D43Q24293470-D10810D2-DFB5-4028-B825-618E892ED2DAQ24293727-CF2F13D7-AE99-4939-81BD-6D6549929366Q24298122-5FC6D0BA-A0E0-49B5-AA94-2B8D1733A8B9Q24298231-205C3824-7152-4992-91A7-6A51E5D2F17FQ24298430-EC919EBE-84C1-4A9D-AB5F-BEC48E445CC0Q24298523-E294FB0B-3910-4CD0-8DD5-0EC67CCF88E7Q24298721-16ABD824-32B9-42AE-904E-9C18F6F17FD3Q24299289-E7509FC9-BB5E-4417-B74C-9BB57D75964AQ24300131-686885EC-6682-46F7-A92D-E4D31EEA62B4Q24301116-719BACF2-A894-49E4-9825-F4A4DC4839B4Q24301691-5C8FF413-3223-494F-954D-220FE659CF93Q24301946-C973A13C-21CE-4753-B408-8EF1D19AA1A5Q24305472-26B29D09-12DA-40B7-943D-527A1BC6CA55Q24306916-1771938E-C375-4D0B-98D3-E105D70F3733Q24307946-432C76FF-B3DF-400C-9736-3FFE37E7E306Q24311461-B790BDBA-17AE-4D8D-882E-8A6ED551D101Q24311523-B12E9975-FADB-479C-A172-AE2668AE7C4DQ24311624-03FCA725-DD84-47D9-9683-F74917564B06Q24311758-5ADD6BD0-B888-4479-BE86-F34C9C5BC4E5Q24312185-D3BFD213-25A2-465F-B30F-FCE37A8D3087Q24312452-A0120EE8-AF6A-43B8-B655-B37D38F34F09Q24314013-D69175D3-1770-4426-978C-8707DA2AF529Q24315670-3B9AD49F-0EB5-4DB6-8315-09914F888F32Q24316089-72C2C37D-2259-411F-A857-AF28BEB03D97Q24316619-5F08741F-1A9E-4A9A-8994-8B899AB03E5BQ24316900-83224D4E-2DF0-4A50-8A8A-0C2AE5C73A4AQ24318474-A2222A93-011C-4DFE-AB92-E3021BA68A7BQ24318841-EA4265C4-5BA0-49C3-BA10-B318260A212AQ24320103-232BF177-F027-47A2-89D5-EB9E554FCFA2Q24320119-0874821A-C59F-4F02-99E1-AC163C41A9DCQ24321216-0787651E-37D9-4A32-BD3E-643F245BF855
P921
description
Protein
@de
mammalian protein found in Homo sapiens
@en
pattedyr-, menneskeprotein
@nn
protein
@id
protein
@sv
proteina
@it
proteinë
@sq
proteïne in Synuclein alpha
@nl
protèin
@ace
protéine
@fr
name
Alfa-sinucleina
@it
Alfa-sinucleína
@es
Alfa-sinucleína
@gl
Alfa-sinucleína
@pt
Alfa-sinucleïna
@ca
Alfa-synucleïne
@nl
Alfasynuklein
@sv
Alpha-synuclein
@en-ca
Alpha-synuclein
@en-gb
Alpha-synucleinum
@la
type
label
Alfa-sinucleina
@it
Alfa-sinucleína
@es
Alfa-sinucleína
@gl
Alfa-sinucleína
@pt
Alfa-sinucleïna
@ca
Alfa-synucleïne
@nl
Alfasynuklein
@sv
Alpha-synuclein
@en-ca
Alpha-synuclein
@en-gb
Alpha-synucleinum
@la
altLabel
Alfa-sinucleina
@es
Alfa-sinucleina
@pt
Alpha-Synuclein
@de
Alpha-Synuklein
@de
I+/--synuclein
@en
NACP
@en
Non-A beta component of AD amyloid
@en
Non-A4 component of amyloid precursor
@en
SNCA
@en
SNCA
@nn
prefLabel
Alfa-sinucleina
@it
Alfa-sinucleína
@es
Alfa-sinucleína
@gl
Alfa-sinucleína
@pt
Alfa-sinucleïna
@ca
Alfa-synucleïne
@nl
Alfasynuklein
@sv
Alpha-synuclein
@en-ca
Alpha-synuclein
@en-gb
Alpha-synucleinum
@la
P637
P638
P680
P681
P682
P705
P352
P6366
P637
P646
P2888
P31
P352
P373
Alpha-synuclein
P6366
2781449126
2910879917
P637
NP_001139526
NP_001139527
NP_001362214
NP_001362215
NP_001362216
NP_001362217
NP_001362219
XP_011530505
P638
P646
P680
P681
P682
P702
P703
P705
ENSP00000338345
ENSP00000343683
ENSP00000378437
ENSP00000378440
ENSP00000378442
ENSP00000396241
ENSP00000421485
ENSP00000422238
ENSP00000423445
ENSP00000426034
P7260
1.C.77.1.1