Cryo-EM analysis of homodimeric full-length LRRK2 and LRRK1 protein complexes

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Cryo-EM analysis of homodimeric full-length LRRK2 and LRRK1 protein complexes is …
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scholarly articleQ13442814

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P6179Dimensions Publication ID1091161937
P356DOI10.1038/S41598-017-09126-Z
P932PMC publication ID5561129
P698PubMed publication ID28819229

P50authorHenning StahlbergQ14944139
Marie-Christine Chartier-HarlinQ58238824
Renée VancraenenbroeckQ114797025
Veerle BaekelandtQ30112409
Jean-Marc TaymansQ30112411
P2093author name stringMohamed Chami
Paul Baumgartner
Rosmarie Sütterlin
Robert McLeod
Kushal Sejwal
Hervé Rémigy
William Sibran
P2860cites workLeucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domainQ24293453
Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADPQ24293723
Expression, purification and preliminary biochemical and structural characterization of the leucine rich repeat namesake domain of leucine rich repeat kinase 2.Q54344107
Mechanisms in dominant parkinsonism: The toxic triangle of LRRK2, alpha-synuclein, and tau.Q36325784
Urinary LRRK2 phosphorylation predicts parkinsonian phenotypes in G2019S LRRK2 carriers.Q36706040
Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerizationQ37479332
Leucine-rich repeat kinase 2 (LRRK2) as a potential therapeutic target in Parkinson's diseaseQ38009436
The GTPase function of LRRK2Q38044433
Human leucine-rich repeat kinase 1 and 2: intersecting or unrelated functions?Q38044437
Targeting leucine-rich repeat kinase 2 in Parkinson's diseaseQ38160939
Prediction of the repeat domain structures and impact of parkinsonism-associated variations on structure and function of all functional domains of leucine-rich repeat kinase 2 (LRRK2).Q38182492
LRRK2 Pathways Leading to NeurodegenerationQ38501861
LRRK2 Kinase Inhibition as a Therapeutic Strategy for Parkinson's Disease, Where Do We Stand?Q38620229
Conformational heterogeneity of the Roc domains in C. tepidum Roc-COR and implications for human LRRK2 Parkinson mutationsQ40604356
How good can cryo-EM become?Q41603118
Optimization of protein buffer cocktails using ThermofluorQ43170490
Leucine-rich repeat kinase 1: a paralog of LRRK2 and a candidate gene for Parkinson's diseaseQ48308813
Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimersQ24298093
Differential protein-protein interactions of LRRK1 and LRRK2 indicate roles in distinct cellular signaling pathwaysQ24299578
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutantQ24306788
A direct interaction between leucine-rich repeat kinase 2 and specific β-tubulin isoforms regulates tubulin acetylationQ24310126
Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragmentQ24310262
The familial Parkinsonism gene LRRK2 regulates neurite process morphologyQ24317613
The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylationQ24318533
Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neuronsQ24628425
Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPaseQ27649733
Structure of the Roc–COR domain tandem of C. tepidum, a prokaryotic homologue of the human LRRK2 Parkinson kinaseQ27651307
Roco kinase structures give insights into the mechanism of Parkinson disease-related leucine-rich-repeat kinase 2 mutationsQ27681111
UCSF Chimera--a visualization system for exploratory research and analysisQ27860666
EMAN2: an extensible image processing suite for electron microscopyQ27861052
Genetics in Parkinson disease: Mendelian versus non-Mendelian inheritanceQ28077356
Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contactsQ28116245
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathologyQ28131833
Leucine-rich repeat kinase 2 interacts with p21-activated kinase 6 to control neurite complexity in mammalian brainQ28267434
Cryo-electron microscopy of vitrified specimensQ28288841
ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical spaceQ28817986
RELION: Implementation of a Bayesian approach to cryo-EM structure determinationQ29547673
Parkinson's diseaseQ29616302
High resolution single particle refinement in EMAN2.1.Q30385130
The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2.Q33292556
LRRK2 kinase activity is dependent on LRRK2 GTP binding capacity but independent of LRRK2 GTP bindingQ33999270
Roc, a Ras/GTPase domain in complex proteinsQ34280792
The genetics of Parkinson diseaseQ34604083
Has negative staining still a place in biomacromolecular electron microscopy?Q35656165
Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.Q35780973
P275copyright licenseCreative Commons Attribution 4.0 InternationalQ20007257
P6216copyright statuscopyrightedQ50423863
P433issue1
P407language of work or nameEnglishQ1860
P921main subjectcryogenic electron microscopyQ5190506
P304page(s)8667
P577publication date2017-08-17
P1433published inScientific ReportsQ2261792
P1476titleCryo-EM analysis of homodimeric full-length LRRK2 and LRRK1 protein complexes
P478volume7

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cites work (P2860)
Q61797022Crystal structure of the WD40 domain dimer of LRRK2
Q96953324LRRK2 Phosphorylation, More Than an Epiphenomenon
Q59099056Physiological and pathological functions of LRRK2: implications from substrate proteins
Q60921580Roco Proteins: GTPases with a Baroque Structure and Mechanism
Q89983587The LRRK2 N-terminal domain influences vesicle trafficking: impact of the E193K variant

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