14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization (Q24339094)

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David G Campbell

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Alban Ordureau

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Thomas Macartney

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Youren Tong

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Jie Shen

Creative Commons Attribution-NonCommercial 2.5 Generic

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language of work or name

English

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publication date

15 September 2010

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published in

Biochemical Journal

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volume

430

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issue

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page(s)

393-404

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start time

6 May 2020

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April 2022 Public Data File from Crossref

copyrighted

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cites work

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27 September 2017

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Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1.

27 September 2017

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27 September 2017

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14-3-3 protein is a component of Lewy bodies in Parkinson's disease-mutation analysis and association studies of 14-3-3 eta.

30 May 2018

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Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding

29 November 2018

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Comprehensive analysis of LRRK2 in publicly available Parkinson's disease cases and neurologically normal controls

29 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/20642453

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Phosphorylation-dependent interactions between enzymes of plant metabolism and 14-3-3 proteins

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/20642453

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1042/BJ20100483

1 reference

1 reference

1 reference

PubMed publication ID

20642453

1 reference