about
Interplay of LRRK2 with chaperone-mediated autophagyDopamine-modified alpha-synuclein blocks chaperone-mediated autophagyPredictive Big Data Analytics: A Study of Parkinson's Disease Using Large, Complex, Heterogeneous, Incongruent, Multi-Source and Incomplete Observations.The nuclear envelope: an intriguing focal point for neurogenetic diseaseGenetic background modulates the phenotype of a mouse model of DYT1 dystoniaLamina-associated polypeptide 1: protein interactions and tissue-selective functionsThymidine kinase 2 (H126N) knockin mice show the essential role of balanced deoxynucleotide pools for mitochondrial DNA maintenance.alpha-Synuclein produces a long-lasting increase in neurotransmitter releaseRegulation of alpha-synuclein by bFGF in cultured ventral midbrain dopaminergic neuronsLoss of the dystonia-associated protein torsinA selectively disrupts the neuronal nuclear envelopeAlpha-synuclein involvement in hippocampal synaptic plasticity: role of NO, cGMP, cGK and CaMKIIA molecular mechanism underlying the neural-specific defect in torsinA mutant miceTorsinA hypofunction causes abnormal twisting movements and sensorimotor circuit neurodegenerationA novel function for the Caenorhabditis elegans torsin OOC-5 in nucleoporin localization and nuclear importA novel conditional knock-in approach defines molecular and circuit effects of the DYT1 dystonia mutation.The WD40 domain is required for LRRK2 neurotoxicity.Leucine-rich repeat kinase 2 for beginners: six key questions.Magic shotgun for Parkinson's disease?The ons and offs of inducible transgenic technology: a review.Cerebellothalamocortical pathway abnormalities in torsinA DYT1 knock-in mice.The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate.α-Synuclein-independent histopathological and motor deficits in mice lacking the endolysosomal Parkinsonism protein Atp13a2.Inherited isolated dystonia: clinical genetics and gene function.Mislocalization to the nuclear envelope: an effect of the dystonia-causing torsinA mutation.LRRK2 Parkinson disease mutations enhance its microtubule association.Forebrain deletion of the dystonia protein torsinA causes dystonic-like movements and loss of striatal cholinergic neurons.Access of torsinA to the inner nuclear membrane is activity dependent and regulated in the endoplasmic reticulum.Mouse models of neurodevelopmental disease of the basal ganglia and associated circuits.The roles of kinases in familial Parkinson's disease.Lamina-associated polypeptide-1 interacts with the muscular dystrophy protein emerin and is essential for skeletal muscle maintenanceNeuronal Nuclear Membrane Budding Occurs during a Developmental Window Modulated by Torsin Paralogs.Primary dystonia: molecules and mechanisms.The nuclear envelope as a signaling node in development and disease.Eighth International Chorea-Acanthocytosis Symposium: Summary of Workshop Discussion and Action Points.The biology and pathology of the familial Parkinson's disease protein LRRK2.Emerging common molecular pathways for primary dystonia.Clinical and scientific perspectives on movement disorders: Stanley Fahn's contributions.TorsinA controls TAN line assembly and the retrograde flow of dorsal perinuclear actin cables during rearward nuclear movement.Endolysosomal dysfunction in Parkinson's disease: Recent developments and future challenges.Nuclear envelope breakdown induced by herpes simplex virus type 1 involves the activity of viral fusion proteins.
P50
Q24322747-E6DEFC72-5106-4336-A233-3B17ECB63006Q24683089-6BF0024B-41A5-4A7E-A5DB-C37C43FF3ED3Q26779516-4682B98D-A1CC-4276-AA00-C30E49DEF2E7Q27006719-21F37819-0B3A-4D5B-89A2-8CB819E3F6B9Q27308647-6E45E11D-6929-4AD3-A0B0-41DE9EFA6A03Q27694535-471A27A6-AAB9-4077-8FD4-2159FB2C9813Q28504546-54C368A2-B2F5-465F-894C-62783ED41B73Q28510893-8884A1A7-DDDB-46BD-9215-83E7C9636CF4Q28569843-A9709267-33A3-4474-B0E3-3E7800154A31Q28589351-C0CB549F-0CA6-4723-B995-4B9729FC5369Q28591581-B75CB29F-08CC-4F69-BBF5-0A21CF329D26Q28594816-065D83ED-197E-4DD4-8BA8-4445671B9D3DQ30581663-A9EFB445-063C-4EF9-845E-331559E28853Q30651037-359A94CE-2DA9-43E5-A05E-69C4CBDFD109Q30670034-4F8E27C0-56DA-4BB3-99B8-24A25C2EFC74Q33521241-AEEEB40E-4DBE-489D-9685-06D6EEE8F3A2Q34259058-5481E0C4-3358-4693-AFCC-107DA58ADFC2Q34417369-7CC74EC5-4911-4702-A93C-1CA7FADC315BQ34462016-2F6BF2F6-560C-4C04-8FE8-875EA9489DEEQ34836384-39A183D0-B697-4918-AB70-C5C8008EEE4DQ35014887-C6F9F856-A804-4707-BCF0-4D6510A9F060Q35307748-B4495358-B258-4746-822B-1029D70E9DD1Q35340179-4B9ACA2E-8A1B-4D75-B775-8B9CF6E7BB7FQ35554495-12F981EB-BBD5-4658-AEF1-269D6D752710Q35688632-EE6FD107-BAFA-442B-BBDA-5ED118E16683Q35759092-817F53E5-01C1-46C5-93A6-E90C371458E5Q35968774-0DEE03AD-1C64-4C78-9F49-7019AC80248DQ36266325-CD571725-4450-4972-9B11-D449E2061910Q36989256-FDF079A3-8B4F-41E0-99D1-C003C90E9D07Q37233110-04025746-8E14-46C3-9D25-78C7ADB6CD92Q37333874-34FB804D-F25F-49EC-866D-FD0A749E973EQ37614200-19A2181F-EDDA-4451-AFD3-3F3EC17966ECQ37634713-7ABD757A-5974-4735-8FAC-FC53AE8ED196Q37648067-C212B9D5-D4A6-4285-8305-B3DB7B3E3896Q37699237-DB87319D-E5C3-44C5-9481-AF564911F568Q38124786-AB82C9DC-B7AB-4C19-82B1-C9917D3DF8A8Q38610367-B4D6C256-5E79-4DC5-938B-D51206B10FA3Q38714582-DADD3FAD-37C0-4CB8-9897-1CC56565A4B5Q38822081-1C8DE976-3C36-4EF2-B90B-9A164A1274E6Q38976723-5AAC408D-485F-4A80-9AFF-B37E11099E1B
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
William T Dauer
@ast
William T Dauer
@en
William T Dauer
@es
William T Dauer
@nl
type
label
William T Dauer
@ast
William T Dauer
@en
William T Dauer
@es
William T Dauer
@nl
altLabel
William Dauer
@en
prefLabel
William T Dauer
@ast
William T Dauer
@en
William T Dauer
@es
William T Dauer
@nl
P108
P106
P1153
6602164026
P31
P496
0000-0003-1775-7504