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Structure
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Structure
Article . 2020 . Peer-reviewed
License: Elsevier Non-Commercial
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Structure
Article . 2020
Data sources: Europe PubMed Central
https://dx.doi.org/10.1016/j.s...
Article
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X Caps the Phosphate for Phospho-Rab GTPase Recognition in Ciliogenesis and Parkinson’s Disease

descriptionPublicationkeyboard_double_arrow_right Article 01 Apr 2020 English Publisher:Elsevier BVJournal:Structure, volume 28, pages 385-387 (issn: 0969-2126, Copyright policy )
Authors: Michael W, Struck; Gregory J, Pazour; David G, Lambright;

doi: 10.1016/j.str.2020.03.005

pmid: 32268075

X Caps the Phosphate for Phospho-Rab GTPase Recognition in Ciliogenesis and Parkinson’s Disease

Abstract

Some Rab GTPases, after activation by GDP to GTP exchange, are phosphorylated by the LRRK2 kinase implicated in Parkinson's disease. In the current issue of Structure, Waschbüsch et al. (2020) investigate the structural basis for recognition of active phospho-Rab GTPases by the RH2 domain of the effector protein RILPL2.

Related Organizations
Keywords

rab GTP-Binding Proteins, Humans, Parkinson Disease, Phosphorylation, Leucine-Rich Repeat Serine-Threonine Protein Kinase-2, Phosphates

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
0
Average
Average
Average
hybrid