Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization (Q36780383)

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scientific article published on September 2010

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English	Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization	scientific article published on September 2010

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

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

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

2

object named as

Maria Deak

0 references

object named as

Nicolas Dzamko

1

0 references

Alan R. Prescott

object named as

Alan R Prescott

5

0 references

object named as

Dario R Alessi

6

0 references

Alastair D Reith

4

object named as

Alastair D Reith

1 reference

Europe PubMed Central

16 August 2017

PMC publication ID

author name string

Faycal Hentati

3

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

R Jeremy Nichols

7

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

language of work or name

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publication date

1 September 2010

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

number of pages

9

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based on heuristic

inferred from page(s)

Biochemical Journal

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Europe PubMed Central

PMC publication ID

16 August 2017

430

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

3

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

405-413

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

copyright license

Creative Commons Attribution 3.0 Unported

25 July 2019

1 reference

April 2022 Public Data File from Crossref

copyright status

0 references

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

1 reference

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Identification of the autophosphorylation sites of LRRK2.

1 reference

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

1 reference

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

1 reference

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LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model

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

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Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology

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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.

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Identifiers

10.1042/BJ20100784

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

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