(Q45143202)

10 December 2017

title

Structural and functional in silico analysis of LRRK2 missense substitutions (English)

1 reference

10 December 2017

1 reference

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24488318%20AND%20SRC:MED&resulttype=core&format=json

3 June 2020

Jordi Pérez-Tur

series ordinal

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24488318%20AND%20SRC:MED&resulttype=core&format=json

3 June 2020

author name string

Marta Tormos-Pérez

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24488318%20AND%20SRC:MED&resulttype=core&format=json

3 June 2020

language of work or name

1 reference

2 February 2014

1 reference

Molecular Biology Reports

10 December 2017

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24488318%20AND%20SRC:MED&resulttype=core&format=json

3 June 2020

volume

41

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24488318%20AND%20SRC:MED&resulttype=core&format=json

3 June 2020

issue

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24488318%20AND%20SRC:MED&resulttype=core&format=json

3 June 2020

page(s)

2529-2542

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24488318%20AND%20SRC:MED&resulttype=core&format=json

https://scigraph.springernature.com/pub.10.1007/s11033-014-3111-z

3 June 2020

exact match

0 references

cites work

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LRRK2 and neurodegeneration

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LRRK2 in Parkinson's disease: protein domains and functional insights

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Ancient origin of the Parkinson disease gene LRRK2.

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Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism

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The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation

21 January 2018

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Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment

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Structure of the Roc–COR domain tandem of C. tepidum, a prokaryotic homologue of the human LRRK2 Parkinson kinase

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Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase

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

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

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Molecular analyses of the LRRK2 gene in European and North African autosomal dominant Parkinson's disease

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Analysis of LRRK2 accessory repeat domains: prediction of repeat length, number and sites of Parkinson's disease mutations

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Expression, purification and preliminary biochemical and structural characterization of the leucine rich repeat namesake domain of leucine rich repeat kinase 2.

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The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity

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

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PubMed

https://pubmed.ncbi.nlm.nih.gov/24488318

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Amino acid substitutions in the human genome: evolutionary implications of single nucleotide polymorphisms.

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/24488318

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1007/S11033-014-3111-Z

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24488318%20AND%20SRC:MED&resulttype=core&format=json

Dimensions Publication ID

3 June 2020

1021691849

0 references

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24488318%20AND%20SRC:MED&resulttype=core&format=json