MKK6 binds and regulates expression of Parkinson's disease-related protein LRRK2 (Q24294736)

10

object named as

Hoon Ryu

0 references

Mark R Cookson

11

object named as

Mark R Cookson

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author name string

Cindy H Hsu

1

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Diane Chan

2

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Shamol Saha

4

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Maria D Guillily

5

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Andrew Ferree

6

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Kesav Raghavan

7

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Grace C Shen

8

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Lilach Segal

9

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Benjamin Wolozin

Journal of Neurochemistry

12

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language of work or name

English

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publication date

March 2010

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published in

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volume

112

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page(s)

1593-604

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issue

6

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cites work

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The Parkinson disease-associated protein kinase LRRK2 exhibits MAPKKK activity and phosphorylates MKK3/6 and MKK4/7, in vitro

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The R1441C mutation of LRRK2 disrupts GTP hydrolysis

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Identification of potential protein interactors of Lrrk2

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GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease

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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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The familial Parkinsonism gene LRRK2 regulates neurite process morphology

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Kinase activity of mutant LRRK2 mediates neuronal toxicity

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Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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27 September 2017

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LRK-1, a C. elegans PARK8-related kinase, regulates axonal-dendritic polarity of SV proteins

30 May 2018

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29 November 2018

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10.1111/J.1471-4159.2010.06568.X

29 November 2018

Identifiers

DOI

1 reference

2437168

2437168

1 reference

1 reference

1 reference