about
Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimersUnbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson diseaseLeucine-rich repeat kinase 2 interacts with p21-activated kinase 6 to control neurite complexity in mammalian brainImmunohistochemical detection of transgene expression in the brain using small epitope tags.Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis.MicroRNA-205 regulates the expression of Parkinson's disease-related leucine-rich repeat kinase 2 protein.In silico, in vitro and cellular analysis with a kinome-wide inhibitor panel correlates cellular LRRK2 dephosphorylation to inhibitor activity on LRRK2.Chemical genetic approach identifies microtubule affinity-regulating kinase 1 as a leucine-rich repeat kinase 2 substrate.Pharmacological LRRK2 kinase inhibition induces LRRK2 protein destabilization and proteasomal degradationPAK6 Phosphorylates 14-3-3γ to Regulate Steady State Phosphorylation of LRRK2.Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation.LRRK2 Phosphorylation: Behind the Scenes.RAB7L1-Mediated Relocalization of LRRK2 to the Golgi Complex Causes Centrosomal Deficits via RAB8ARab32 interacts with SNX6 and affects retromer-dependent Golgi traffickingInhibition of LRRK2 or Casein Kinase 1 Results in LRRK2 Protein DestabilizationRAB8, RAB10 and RILPL1 contribute to both LRRK2 kinase-mediated centrosomal cohesion and ciliogenesis deficits
P50
Q24298093-46A329A7-3800-4F3A-87E1-91EF530D6A83Q24336432-497BC4BE-1F9C-4528-917F-84B88CD0AEB1Q28267434-C3439357-4CE9-4E09-A6B8-316540F5FF52Q33532297-FD002F0E-28E8-4166-BC04-76E6933A09C7Q33595218-209D806E-0BC1-48DF-8812-06DCB5CA8325Q36525872-A4BE3BD8-802E-4048-B858-659770301E17Q40188432-73038241-86C1-4235-85DB-CC27558DA991Q41099991-DD889352-86ED-4A47-AC46-3F058B8FFD07Q41163700-91E1C230-E43C-4E90-8205-FEA47B19ED00Q47222316-6FF2A800-1719-4653-92D8-A928A79C9672Q48192270-296B81AC-8097-46D2-AFDC-A80C7EEC5D76Q49549170-9BD9D642-5B86-4D28-864B-7B0632B892FCQ59329253-75D963DF-2BB6-4008-A9C9-0B96D749724CQ61818367-B9C4EE2B-B5F0-4E2B-9C20-668AE3C04669Q90787077-34571D23-730D-466D-B3BF-80B869C16A96Q92716998-F725AE8B-4E58-492C-A0D3-AB04768F1D67
P50
description
researcher, ORCID id # 0000-0002-6417-4670
@en
wetenschapper
@nl
name
Evy Lobbestael
@ast
Evy Lobbestael
@en
Evy Lobbestael
@es
Evy Lobbestael
@nl
type
label
Evy Lobbestael
@ast
Evy Lobbestael
@en
Evy Lobbestael
@es
Evy Lobbestael
@nl
altLabel
Lobbestael E
@en
prefLabel
Evy Lobbestael
@ast
Evy Lobbestael
@en
Evy Lobbestael
@es
Evy Lobbestael
@nl
P1053
H-7537-2018
P106
P31
P4012
P496
0000-0002-6417-4670