Pharmacological inhibition of LRRK2 cellular phosphorylation sites provides insight into LRRK2 biology. (Q38044449)

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13 February 2020

title

Pharmacological inhibition of LRRK2 cellular phosphorylation sites provides insight into LRRK2 biology (English)

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13 February 2020

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1

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13 February 2020

author name string

Spencer B Hermanson

2

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13 February 2020

Coby B Carlson

3

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13 February 2020

Steven M Riddle

4

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13 February 2020

Kurt W Vogel

5

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13 February 2020

Kun Bi

6

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13 February 2020

R Jeremy Nichols

7

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13 February 2020

publication date

1 October 2012

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Biochemical Society Transactions

13 February 2020

published in

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volume

40

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issue

5

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page(s)

1158-1162

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LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity

13 February 2020

cites work

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Leucine-rich repeat kinase 2 mutants I2020T and G2019S exhibit altered kinase inhibitor sensitivity.

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Zeroing in on LRRK2-linked pathogenic mechanisms in Parkinson's disease.

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Kinetic mechanistic studies of wild-type leucine-rich repeat kinase 2: characterization of the kinase and GTPase activities

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First neuropathological description of a patient with Parkinson's disease and LRRK2 p.N1437H mutation

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14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

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Kinase activity is required for the toxic effects of mutant LRRK2/dardarin

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LRRK2 Parkinson disease mutations enhance its microtubule association.

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Investigation of leucine-rich repeat kinase 2 : enzymological properties and novel assays.

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Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity

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Parkinson's disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity

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Identification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motif

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Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2.

21 January 2018

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The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites

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Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities

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Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease

21 January 2018

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Phosphorylation of LRRK2 serines 955 and 973 is disrupted by Parkinson’s disease mutations and LRRK2 pharmacological inhibition

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Identification of compounds that inhibit the kinase activity of leucine-rich repeat kinase 2.

21 January 2018

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Identification of chemicals to inhibit the kinase activity of leucine-rich repeat kinase 2 (LRRK2), a Parkinson’s disease-associated protein

21 January 2018

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Inhibitors of leucine-rich repeat kinase-2 protect against models of Parkinson's disease

21 January 2018

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Development of a high-throughput AlphaScreen assay measuring full-length LRRK2(G2019S) kinase activity using moesin protein substrate

21 January 2018

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Characterization of TAE684 as a potent LRRK2 kinase inhibitor

21 January 2018

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Chemoproteomics-based design of potent LRRK2-selective lead compounds that attenuate Parkinson's disease-related toxicity in human neurons

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Identification of the autophosphorylation sites of LRRK2.

21 January 2018

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Phosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's disease

21 January 2018

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Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization

21 January 2018

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Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.

21 January 2018

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Screening for novel LRRK2 inhibitors using a high-throughput TR-FRET cellular assay for LRRK2 Ser935 phosphorylation

21 January 2018

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21 January 2018

Identifiers

DOI

10.1042/BST20120137

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22988882%20AND%20SRC:MED&resulttype=core&format=json

13 February 2020

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