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UnknownIntramolecular feedback regulation of the LRRK2 Roc G domain by a LRRK2 kinase-dependent mechanism.
Not available
S-EPMC11658767 | biostudies-literature
UnknownParkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3.
Not available
S-EPMC3890784 | biostudies-literature
UnknownMultifunctional centromere binding factor 1 is essential for chromosome segregation in the human pathogenic yeast Candida glabrata.
Not available
S-EPMC87199 | biostudies-literature
ProteomicsMapping of nanobody binding sites on human LRRK2 by CX-MS
As part of an in-depth characterization of nanobodies directed against the human Leucine-rich repeat kinase 2 (LRRK2), epitopes of the nanobodies bound to LRRK2 were mapped by chemical crosslinking combined with mass spectrometry using the CID-cleavable crosslinker disuccinimidyl sulfoxide (DSSO).
ORGANISM(S): Homo sapiens (Human) 
2022-02-27 | PXD030063 | Pride
Cl-ms Lrrk2 Dsso Nanobodies Cx-ms Crosslinking Cid-cleavable 
ProteomicsUsher syndrome proteins ADGRV1 (USH2C) and CIB2 (USH1J) interact and share a common interactome containing TRiC/CCT-BBS chaperonins
The human Usher syndrome (USH) is the most common form of a sensory hereditary ciliopathy characterized by progressive vision and hearing loss. Mutations in the genes ADGRV1 and CIB2 have been associated with two distinct sub-types of USH, namely USH2C and USH1J. The proteins encoded by the two gene...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD042629 | Pride
Usher syndrome Tap Interactome 
UnknownMass spectrometric identification of novel posttranslational modification sites in Huntingtin.
Not available
S-EPMC3845347 | biostudies-literature
UnknownStructural insights into the GTP-driven monomerization and activation of a bacterial LRRK2 homolog using allosteric nanobodies.
Not available
S-EPMC11052575 | biostudies-literature
ProteomicsAnalysis of LRRK2 proximity proteome using BioID
To determine the proximity proteome of the Parkinson’s protein LRRK2, three different BioID approaches have been applied. Besides the original BirA-based BioID tag (BioID1), we have generated datasets using BioID2 and miniTurbo (mT), a truncated version of the TurboID tag.
ORGANISM(S): Homo sapiens (Human) 
2026-05-19 | PXD048832 | Pride
ProteomicsEffect of type I and type II kinase inhibitors on the LRRK2 proximity proteome
Type I and type II inhibitors have been demonstrated to stabilize LRRK2 either in an active or inactive kinase conformation. Furthermore, one type I inhibitors show a marked reduction in LRRK2 N-terminal phosphorylation on Serine 910 and 935. In this study, we generated comparative proximity proteom...
ORGANISM(S): Homo sapiens (Human) 
2026-05-19 | PXD048806 | Pride
ProteomicsAnalysis of Rab29 co-expression on the LRRK2 proximity proteome
Rab29 has been shown to bind the LRRK2 N-terminal Armadillo domain in µM affinity and act as upstream-effector localizing LRRK2 to endosomal membranes/ lysosomes. To determine the Rab29-dependent proximity proteome of the Parkinson’s protein LRRK2, three different BioIDapproaches have been applied. ...
ORGANISM(S): Homo sapiens (Human) 
2026-05-19 | PXD048808 | Pride
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