ReviewFuture medicinal chemistry2012
Current understanding of LRRK2 in Parkinson's disease: biochemical and structural features and inhibitor design.
Review in Future medicinal chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- Selective Stabilization of LRRK2 Kinase Conformations Reveals Distinct Modes of Action for Type I and II Inhibitors.Cell biochemistry and biophysics · 2026Article
- Boosting Brain Clean-Up: Can Targeting UPS Genes Offer Neuroprotection?Molecular neurobiology · 2025Review
- Comparative Molecular Dynamics Reveals How LRRK2 Inhibitors Distinguish G2019S from Wild-Type.Neurochemical research · 2025Article
- Genetic mutations in kinases: a comprehensive review on marketed inhibitors and unexplored targets in Parkinson's disease.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2025Review
- Advances in Molecular Docking Techniques for Targeting Protein Misfolding in Neurodegenerative Diseases.Current pharmaceutical biotechnology · 2025Review
- Pharmacology of LRRK2 with type I and II kinase inhibitors revealed by cryo-EM.Cell discovery · 2024Article
- Structural Insights and Development of LRRK2 Inhibitors for Parkinson's Disease in the Last Decade.Genes · 2022Review
- Exploring the focal role of LRRK2 kinase in Parkinson's disease.Environmental science and pollution research international · 2022Review
- Review
- NEAT1 on the Field of Parkinson's Disease: Offense, Defense, or a Player on the Bench?Journal of Parkinson's disease · 2021Review
- Allosteric inhibition of LRRK2, where are we now.Biochemical Society transactions · 2020Review
- Proteomic analysis reveals co-ordinated alterations in protein synthesis and degradation pathways in LRRK2 knockout mice.Human molecular genetics · 2018Article
- Current Therapeutic Molecules and Targets in Neurodegenerative Diseases Based on in silico Drug Design.Current neuropharmacology · 2018Review
- Structure, function, and leucine-rich repeat kinase 2: On the importance of reproducibility in understanding Parkinson's disease.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Altered Development of Synapse Structure and Function in Striatum Caused by Parkinson's Disease-Linked LRRK2-G2019S Mutation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- A triazole derivative elicits autophagic clearance of polyglutamine aggregation in neuronal cells.Drug design, development and therapy · 2016Article
- LRRK2 inhibitors and their potential in the treatment of Parkinson's disease: current perspectives.Clinical pharmacology : advances and applications · 2016Review
- Cellular processes associated with LRRK2 function and dysfunction.The FEBS journal · 2015Review
- Unique functional and structural properties of the LRRK2 protein ATP-binding pocket.The Journal of biological chemistry · 2014Article
- LRRK2, a puzzling protein: insights into Parkinson's disease pathogenesis.Experimental neurology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Since leucine-rich repeat kinase 2 (LRRK2) was linked to Parkinson's disease in 2004, kinase activity of LRRK2 has been believed to play a critical role in the pathogenesis of Parkinson's disease. As a result, identification of LRRK2 inhibitors has been a focus for drug discovery. However, most LRRK2 mutations do not simply increase kinase activity. In this review we summarize the potential mechanisms that regulate the kinase activity of LRRK2. We outline some currently available kinase inhibitors, including the identification of a DFG-out (type-II) inhibitor. Finally, we discuss the relationship of LRRK2 with tau and α-synuclein. The fact that all three proteins are autophapgy-related provides a future strategy for the identification of LRRK2 physiological substrate(s).
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.