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Article

Capturing Differences in the Regulation of LRRK2 Dynamics and Conformational States by Small Molecule Kinase Inhibitors.

ACS chemical biology - 21 Apr 2023

Weng Jui-Hung, Ma Wen, Wu Jian, Sharma Pallavi Kaila, Silletti Steve, McCammon J Andrew, Taylor Susan

Abstract excerpt

Mutations in the human leucine rich repeat protein kinase-2 (LRRK2) create risk factors for Parkinson's disease, and pathological functions of LRRK2 are often correlated with aberrant kinase activity. Past research has focused on developing selective LRRK2 kinase inhibitors. In this study, we combined enhanced sampling simulations with HDX-MS to characterize the inhibitor-induced dynamic changes and the...

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Share to Leucine-Rich Repeat Serine-Threonine Protein Kinase-2
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 37043829
DOI: 10.1021/acschembio.2c00868
PMCID: PMC10127209

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HDX

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

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Capturing Differences in the Regulation of LRRK2 Dynamics and Conformational States by Small Molecule Kinase Inhibitors.PMID 37043829Read ↗

Capturing differences in the regulation of LRRK2 dynamics and conformational states by small molecule kinase inhibitorsSemantic proximity Read ↗

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