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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

The In Situ Structure of Parkinson’s Disease-Linked LRRK2
Reika Watanabe, Robert Buschauer, Jan Böhning, et al.
Cell (2020) Vol. 182, Iss. 6, pp. 1508-1518.e16
Open Access | Times Cited: 191

Showing 1-25 of 191 citing articles:

The promise and the challenges of cryo‐electron tomography
Martin Turk, Wolfgang Baumeister
FEBS Letters (2020) Vol. 594, Iss. 20, pp. 3243-3261
Open Access | Times Cited: 263
Structure of LRRK2 in Parkinson’s disease and model for microtubule interaction
Colin K. Deniston, John Salogiannis, Sebastian Mathea, et al.
Nature (2020) Vol. 588, Iss. 7837, pp. 344-349
Open Access | Times Cited: 201
Preparing samples from whole cells using focused-ion-beam milling for cryo-electron tomography
Felix Wagner, Reika Watanabe, Ruud Schampers, et al.
Nature Protocols (2020) Vol. 15, Iss. 6, pp. 2041-2070
Open Access | Times Cited: 160
Structural analysis of the full-length human LRRK2
Alexander Myasnikov, Hanwen Zhu, Patricia Hixson, et al.
Cell (2021) Vol. 184, Iss. 13, pp. 3519-3527.e10
Open Access | Times Cited: 157
Increased LRRK2 kinase activity alters neuronal autophagy by disrupting the axonal transport of autophagosomes
C. Alexander Boecker, Juliet Goldsmith, Dan Dou, et al.
Current Biology (2021) Vol. 31, Iss. 10, pp. 2140-2154.e6
Open Access | Times Cited: 137
Discovery of XL01126: A Potent, Fast, Cooperative, Selective, Orally Bioavailable, and Blood–Brain Barrier Penetrant PROTAC Degrader of Leucine-Rich Repeat Kinase 2
Xingui Liu, Alexia F. Kalogeropulou, Sofia Domingos, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 37, pp. 16930-16952
Open Access | Times Cited: 110
Better, Faster, Cheaper: Recent Advances in Cryo–Electron Microscopy
Eugene Chua, Joshua H. Mendez, Micah Rapp, et al.
Annual Review of Biochemistry (2022) Vol. 91, Iss. 1, pp. 1-32
Open Access | Times Cited: 105
Neuromelanin in Parkinson’s Disease: Tyrosine Hydroxylase and Tyrosinase
Toshiharu Nagatsu, Akira Nakashima, Hirohisa Watanabe, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 8, pp. 4176-4176
Open Access | Times Cited: 92
Impact of 100 LRRK2 variants linked to Parkinson's disease on kinase activity and microtubule binding
Alexia F. Kalogeropulou, Elena Purlyte, Francesca Tonelli, et al.
Biochemical Journal (2022) Vol. 479, Iss. 17, pp. 1759-1783
Open Access | Times Cited: 87
The material properties of a bacterial-derived biomolecular condensate tune biological function in natural and synthetic systems
Keren Lasker, Steven Boeynaems, Vinson Lam, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 85
In-Cell Structural Biology by NMR: The Benefits of the Atomic Scale
François‐Xavier Theillet
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9497-9570
Open Access | Times Cited: 81
Bringing Structure to Cell Biology with Cryo-Electron Tomography
Lindsey N. Young, Elizabeth Villa
Annual Review of Biophysics (2023) Vol. 52, Iss. 1, pp. 573-595
Open Access | Times Cited: 77
Perspective on the current state of the LRRK2 field
Jean‐Marc Taymans, Matt Fell, Tim Greenamyre, et al.
npj Parkinson s Disease (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 70
Serial Lift-Out: sampling the molecular anatomy of whole organisms
Oda Helene Schiøtz, Christoph J. O. Kaiser, Sven Klumpe, et al.
Nature Methods (2023) Vol. 21, Iss. 9, pp. 1684-1692
Open Access | Times Cited: 54
Integrating cellular electron microscopy with multimodal data to explore biology across space and time
Caitlyn L McCafferty, Sven Klumpe, Rommie E. Amaro, et al.
Cell (2024) Vol. 187, Iss. 3, pp. 563-584
Open Access | Times Cited: 41
Leucine-Rich Repeat Kinases
Dario R. Alessi, Suzanne R. Pfeffer
Annual Review of Biochemistry (2024) Vol. 93, Iss. 1, pp. 261-287
Closed Access | Times Cited: 17
Advances in elucidating the function of leucine-rich repeat protein kinase-2 in normal cells and Parkinson's disease
Matthew Taylor, Dario R. Alessi
Current Opinion in Cell Biology (2020) Vol. 63, pp. 102-113
Open Access | Times Cited: 116
The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
Veronika Obšilová, Tomáš Obšil
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 22, pp. 8824-8824
Open Access | Times Cited: 71
High-resolution in situ structure determination by cryo-electron tomography and subtomogram averaging using emClarity
Tao Ni, Thomas Frosio, Luiza Mendonça, et al.
Nature Protocols (2022) Vol. 17, Iss. 2, pp. 421-444
Open Access | Times Cited: 69
Structures of the eukaryotic ribosome and its translational states in situ
Patrick C. Hoffmann, Jan Philipp Kreysing, Iskander Khusainov, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 69
Ciliary central apparatus structure reveals mechanisms of microtubule patterning
Miao Gui, Xiangli Wang, Susan K. Dutcher, et al.
Nature Structural & Molecular Biology (2022) Vol. 29, Iss. 5, pp. 483-492
Open Access | Times Cited: 63
Conformation and dynamics of the kinase domain drive subcellular location and activation of LRRK2
Sven H. Schmidt, Jui-Hung Weng, Phillip C. Aoto, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 23
Open Access | Times Cited: 60
Challenges and triumphs in cryo-electron tomography
Ryan Hylton, Matthew T. Swulius
iScience (2021) Vol. 24, Iss. 9, pp. 102959-102959
Open Access | Times Cited: 59
Nanobodies as allosteric modulators of Parkinson’s disease–associated LRRK2
Ranjan K. Singh, Ahmed Soliman, Giambattista Guaitoli, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 9
Open Access | Times Cited: 44
Structural basis of human LRRK2 membrane recruitment and activation
Hanwen Zhu, Francesca Tonelli, Dario R. Alessi, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 39
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