(Q38044449)

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

13 February 2020

title

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

1 reference

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13 February 2020

1 reference

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

1 reference

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13 February 2020

Kurt W Vogel

5

1 reference

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13 February 2020

Kun Bi

6

1 reference

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13 February 2020

R Jeremy Nichols

7

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13 February 2020

publication date

1 October 2012

1 reference

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

Biochemical Society Transactions

13 February 2020

published in

1 reference

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13 February 2020

volume

40

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13 February 2020

issue

5

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13 February 2020

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

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

LRRK2 Parkinson disease mutations enhance its microtubule association.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

Characterization of TAE684 as a potent LRRK2 kinase inhibitor

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

Identification of the autophosphorylation sites of LRRK2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBST20120137

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

1 reference