![Structural basis for small molecule targeting of Doublecortin Like Kinase 1 with DCLK1-IN-1 | Communications Biology Structural basis for small molecule targeting of Doublecortin Like Kinase 1 with DCLK1-IN-1 | Communications Biology](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs42003-021-02631-y/MediaObjects/42003_2021_2631_Fig1_HTML.png)
Structural basis for small molecule targeting of Doublecortin Like Kinase 1 with DCLK1-IN-1 | Communications Biology
![LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity. - Abstract - Europe PMC LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity. - Abstract - Europe PMC](https://europepmc.org/articles/PMC3989289/bin/nihms560742f3.jpg)
LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity. - Abstract - Europe PMC
![Regulators of proteostasis are translationally repressed in fibroblasts from sporadic and LRRK2-G2019S Parkinson's patients | bioRxiv Regulators of proteostasis are translationally repressed in fibroblasts from sporadic and LRRK2-G2019S Parkinson's patients | bioRxiv](https://www.biorxiv.org/content/biorxiv/early/2022/01/20/2022.01.17.476095/F1.large.jpg)
Regulators of proteostasis are translationally repressed in fibroblasts from sporadic and LRRK2-G2019S Parkinson's patients | bioRxiv
![A pan-cancer assessment of alterations of the kinase domain of ULK1, an upstream regulator of autophagy | Scientific Reports A pan-cancer assessment of alterations of the kinase domain of ULK1, an upstream regulator of autophagy | Scientific Reports](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fs41598-020-71527-4/MediaObjects/41598_2020_71527_Fig2_HTML.png)
A pan-cancer assessment of alterations of the kinase domain of ULK1, an upstream regulator of autophagy | Scientific Reports
![A proteomic analysis of LRRK2 binding partners reveals interactions with multiple signaling components of the WNT/PCP pathway | Molecular Neurodegeneration | Full Text A proteomic analysis of LRRK2 binding partners reveals interactions with multiple signaling components of the WNT/PCP pathway | Molecular Neurodegeneration | Full Text](https://media.springernature.com/lw685/springer-static/image/art%3A10.1186%2Fs13024-017-0193-9/MediaObjects/13024_2017_193_Fig3_HTML.gif)
A proteomic analysis of LRRK2 binding partners reveals interactions with multiple signaling components of the WNT/PCP pathway | Molecular Neurodegeneration | Full Text
![A proteomic analysis of LRRK2 binding partners reveals interactions with multiple signaling components of the WNT/PCP pathway | Molecular Neurodegeneration | Full Text A proteomic analysis of LRRK2 binding partners reveals interactions with multiple signaling components of the WNT/PCP pathway | Molecular Neurodegeneration | Full Text](https://media.springernature.com/lw685/springer-static/image/art%3A10.1186%2Fs13024-017-0193-9/MediaObjects/13024_2017_193_Fig5_HTML.gif)
A proteomic analysis of LRRK2 binding partners reveals interactions with multiple signaling components of the WNT/PCP pathway | Molecular Neurodegeneration | Full Text
![LRRK2 regulates endoplasmic reticulum-mitochondrial tethering through the PERK-mediated ubiquitination pathway. - Abstract - Europe PMC LRRK2 regulates endoplasmic reticulum-mitochondrial tethering through the PERK-mediated ubiquitination pathway. - Abstract - Europe PMC](https://europepmc.org/articles/PMC6960452/bin/EMBJ-39-e100875-g005.jpg)
LRRK2 regulates endoplasmic reticulum-mitochondrial tethering through the PERK-mediated ubiquitination pathway. - Abstract - Europe PMC
![Cocrystal structure of Roco4 kinase and compound 19 . (A) Overlay of... | Download Scientific Diagram Cocrystal structure of Roco4 kinase and compound 19 . (A) Overlay of... | Download Scientific Diagram](https://www.researchgate.net/profile/Arjan-Kortholt/publication/275277405/figure/fig3/AS:294643607588869@1447259918135/Cocrystal-structure-of-Roco4-kinase-and-compound-19-A-Overlay-of-the-AppCp-blue.png)
Cocrystal structure of Roco4 kinase and compound 19 . (A) Overlay of... | Download Scientific Diagram
![Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson's-disease-related mutant alpha-synuclein. - Abstract - Europe PMC Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson's-disease-related mutant alpha-synuclein. - Abstract - Europe PMC](https://europepmc.org/articles/PMC2807409/bin/nihms159829f2.jpg)
Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson's-disease-related mutant alpha-synuclein. - Abstract - Europe PMC
![LRRK2 G2019S mutation attenuates microglial motility by inhibiting focal adhesion kinase. - Abstract - Europe PMC LRRK2 G2019S mutation attenuates microglial motility by inhibiting focal adhesion kinase. - Abstract - Europe PMC](https://europepmc.org/articles/PMC4647842/bin/ncomms9255-f6.jpg)
LRRK2 G2019S mutation attenuates microglial motility by inhibiting focal adhesion kinase. - Abstract - Europe PMC
![A pan-cancer assessment of alterations of the kinase domain of ULK1, an upstream regulator of autophagy | Scientific Reports A pan-cancer assessment of alterations of the kinase domain of ULK1, an upstream regulator of autophagy | Scientific Reports](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41598-020-71527-4/MediaObjects/41598_2020_71527_Fig1_HTML.png)
A pan-cancer assessment of alterations of the kinase domain of ULK1, an upstream regulator of autophagy | Scientific Reports
![LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity. - Abstract - Europe PMC LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity. - Abstract - Europe PMC](https://europepmc.org/articles/PMC3989289/bin/nihms560742f2.jpg)
LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity. - Abstract - Europe PMC
![Biomolecules | Free Full-Text | Kinases on Double Duty: A Review of UniProtKB Annotated Bifunctionality within the Kinome | HTML Biomolecules | Free Full-Text | Kinases on Double Duty: A Review of UniProtKB Annotated Bifunctionality within the Kinome | HTML](https://www.mdpi.com/biomolecules/biomolecules-12-00685/article_deploy/html/images/biomolecules-12-00685-g001.png)