about
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicityHomeodomain-interacting protein kinases, a novel family of co-repressors for homeodomain transcription factorsThe novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells.Generation and characterization of novel conformation-specific monoclonal antibodies for α-synuclein pathology.Antagonizing Neuronal Toll-like Receptor 2 Prevents Synucleinopathy by Activating Autophagy.Cell-to-cell transmission of non-prion protein aggregates.Controlling the mass action of alpha-synuclein in Parkinson's disease.The secreted oligomeric form of α-synuclein affects multiple steps of membrane trafficking.Lack of direct role of parkin in the steady-state level and aggregation of alpha-synuclein and the clearance of pre-formed aggregates.Intravesicular localization and exocytosis of alpha-synuclein and its aggregates.FcγRIIB mediates the inhibitory effect of aggregated α-synuclein on microglial phagocytosis.Cell-to-cell transmission of α-synuclein aggregates.Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions.Neurodegeneration: Aggregates feel the strain.A detergent-insoluble membrane compartment contains A beta in vivo.Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes.Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease.Novel covalent modifications of alpha-synuclein during the recovery from proteasomal dysfunctionA novel mechanism of interaction between alpha-synuclein and biological membranes
P50
Q24299289-40ADA2DA-FEDE-40ED-BA06-59D750735377Q28118264-514F458D-C2AA-4BD5-98D6-0B750F9D3EE1Q33991720-0FCA9621-F949-47A9-A55A-251610F985B5Q35621190-9B7C20AA-4DE8-455F-BD7D-5E5EDB0E477AQ36577891-334D3421-A9C4-4AF7-9282-3E6EBD85D4C5Q37200740-9CB5DC09-8468-4988-9588-72A626BB9192Q37240113-1F50D2E5-A76F-4EBB-8B18-1A0D0E91E9E4Q39208192-3A7F86DD-C80A-46BA-84E3-0B74FA401C82Q40346142-8042AEAC-DD91-462D-B90C-85C308BE0D92Q40405368-6DC68FA1-1051-426E-8B51-4BD16A46807AQ40570024-70B8863B-5AC9-407D-920D-1DA01F60424FQ42426303-6BEBF71A-C921-4DDB-BB20-5D531CEC5B9FQ43117414-B8C67452-AA28-4604-9ABC-F8C7A44DFFF9Q45981825-7AA9C7CE-AA47-420F-BA04-066629764C46Q47982783-1CDDED28-4717-401F-BFC7-F6DC3DA065ADQ48521558-A6FE8657-834B-4687-9D56-1FBFBF419623Q48830095-AF8C235A-BDE8-4461-B6FD-C65A8998EB3AQ79807995-61E9A0E1-57FB-454C-89EE-28CCC1D00A43Q83952593-CA41FF23-1D31-4756-B432-25EA206521C1
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Seung-Jae Lee
@ast
Seung-Jae Lee
@en
Seung-Jae Lee
@es
Seung-Jae Lee
@nl
Seung-Jae Lee
@sl
type
label
Seung-Jae Lee
@ast
Seung-Jae Lee
@en
Seung-Jae Lee
@es
Seung-Jae Lee
@nl
Seung-Jae Lee
@sl
prefLabel
Seung-Jae Lee
@ast
Seung-Jae Lee
@en
Seung-Jae Lee
@es
Seung-Jae Lee
@nl
Seung-Jae Lee
@sl
P108
P106
P1153
7601417921
P21
P31
P496
0000-0002-5155-5335
P569
2000-01-01T00:00:00Z