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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:

Pathogenic effects of novel mutations in the P‐type ATPase ATP13A2 ( PARK9 ) causing Kufor‐Rakeb syndrome, a form of early‐onset parkinsonism
Jin‐Sung Park, Prachi Mehta, Antony A. Cooper, et al.
Human Mutation (2011) Vol. 32, Iss. 8, pp. 956-964
Open Access | Times Cited: 113

Showing 1-25 of 113 citing articles:

Alpha-synuclein: Pathology, mitochondrial dysfunction and neuroinflammation in Parkinson’s disease
Emily M. Rocha, Briana De Miranda, Laurie H. Sanders
Neurobiology of Disease (2017) Vol. 109, pp. 249-257
Closed Access | Times Cited: 627
Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration
Benjamin Dehay, Alfredo Ramı́rez, Marta Martínez‐Vicente, et al.
Proceedings of the National Academy of Sciences (2012) Vol. 109, Iss. 24, pp. 9611-9616
Open Access | Times Cited: 347
At the end of the autophagic road: an emerging understanding of lysosomal functions in autophagy
Han‐Ming Shen, Noboru Mizushima
Trends in Biochemical Sciences (2013) Vol. 39, Iss. 2, pp. 61-71
Closed Access | Times Cited: 328
“Manganese-induced neurotoxicity: a review of its behavioral consequences and neuroprotective strategies”
Tanara V. Peres, Maria Rosa Chitolina Schetinger, Pan Chen, et al.
BMC Pharmacology and Toxicology (2016) Vol. 17, Iss. 1
Open Access | Times Cited: 325
Lysosomal impairment in Parkinson's disease
Benjamin Dehay, Marta Martínez‐Vicente, Guy A. Caldwell, et al.
Movement Disorders (2013) Vol. 28, Iss. 6, pp. 725-732
Open Access | Times Cited: 302
Autophagy in Parkinson's Disease
Xu Hou, Jens O. Watzlawik, Fabienne C. Fiesel, et al.
Journal of Molecular Biology (2020) Vol. 432, Iss. 8, pp. 2651-2672
Open Access | Times Cited: 280
Deficiency of ATP13A2 Leads to Lysosomal Dysfunction, α-Synuclein Accumulation, and Neurotoxicity
Marija Usenovic, Emilie Tresse, Joseph R. Mazzulli, et al.
Journal of Neuroscience (2012) Vol. 32, Iss. 12, pp. 4240-4246
Open Access | Times Cited: 267
Activation of -Glucocerebrosidase Reduces Pathological -Synuclein and Restores Lysosomal Function in Parkinson's Patient Midbrain Neurons
Joseph R. Mazzulli, Friederike Zunke, Taiji Tsunemi, et al.
Journal of Neuroscience (2016) Vol. 36, Iss. 29, pp. 7693-7706
Open Access | Times Cited: 251
Parkinson's disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes α-Synuclein externalization via exosomes
Stephanie M.Y. Kong, Brian K.K. Chan, Jin‐Sung Park, et al.
Human Molecular Genetics (2014) Vol. 23, Iss. 11, pp. 2816-2833
Open Access | Times Cited: 212
The Parkinson’s disease-associated genes ATP13A2 and SYT11 regulate autophagy via a common pathway
Carla F. Bento, Avraham Ashkenazi, María Jiménez-Sánchez, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 174
The emerging roles of vacuolar-type ATPase-dependent Lysosomal acidification in neurodegenerative diseases
Qiao‐Yun Song, Bo Meng, Haidong Xu, et al.
Translational Neurodegeneration (2020) Vol. 9, Iss. 1
Open Access | Times Cited: 148
Mechanisms of autophagy–lysosome dysfunction in neurodegenerative diseases
Ralph A. Nixon, David C. Rubinsztein
Nature Reviews Molecular Cell Biology (2024) Vol. 25, Iss. 11, pp. 926-946
Closed Access | Times Cited: 54
An ERcentric view of Parkinson's disease
Gabriela Mercado, Pamela Valdés, Claudio Hetz
Trends in Molecular Medicine (2013) Vol. 19, Iss. 3, pp. 165-175
Closed Access | Times Cited: 180
The role of Ca2+ signaling in Parkinson's disease
Sofia Zaichick, Kaitlyn M. McGrath, Gabriela Caraveo
Disease Models & Mechanisms (2017) Vol. 10, Iss. 5, pp. 519-535
Open Access | Times Cited: 165
Cell biology of the NCL proteins: What they do and don't do
Jaime Cárcel‐Trullols, Attila Kovács, David A. Pearce
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2015) Vol. 1852, Iss. 10, pp. 2242-2255
Open Access | Times Cited: 165
Iron dysregulation in movement disorders
Petr Dušek, Joseph Jankovic, Weidong Le
Neurobiology of Disease (2012) Vol. 46, Iss. 1, pp. 1-18
Closed Access | Times Cited: 163
ATP13A2/PARK9 Regulates Secretion of Exosomes and α-Synuclein
Taiji Tsunemi, Kana Hamada, Dimitri Krainc
Journal of Neuroscience (2014) Vol. 34, Iss. 46, pp. 15281-15287
Open Access | Times Cited: 157
PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity
David Ramonet, Agata Podhajska, Klodjan Stafa, et al.
Human Molecular Genetics (2011) Vol. 21, Iss. 8, pp. 1725-1743
Open Access | Times Cited: 156
The role of ATP13A2 in Parkinson's disease: Clinical phenotypes and molecular mechanisms
Jin‐Sung Park, Nicholas Blair, Carolyn M. Sue
Movement Disorders (2015) Vol. 30, Iss. 6, pp. 770-779
Closed Access | Times Cited: 154
Loss-of-function mutations in theATP13A2/PARK9 gene cause complicated hereditary spastic paraplegia (SPG78)
Alejandro Estrada‐Cuzcano, Shaun Martin, Teodora Chamova, et al.
Brain (2016) Vol. 140, Iss. 2, pp. 287-305
Open Access | Times Cited: 148
Zn2+ dyshomeostasis caused by loss of ATP13A2/PARK9 leads to lysosomal dysfunction and alpha-synuclein accumulation
Taiji Tsunemi, Dimitri Krainc
Human Molecular Genetics (2013) Vol. 23, Iss. 11, pp. 2791-2801
Open Access | Times Cited: 144
Endocytic membrane trafficking and neurodegenerative disease
Andrea M. A. Schreij, Edward A. Fon, Peter S. McPherson
Cellular and Molecular Life Sciences (2015) Vol. 73, Iss. 8, pp. 1529-1545
Open Access | Times Cited: 143
Glucocerebrosidase gene therapy prevents α-synucleinopathy of midbrain dopamine neurons
Emily M. Rocha, Gaynor A. Smith, Eric Park, et al.
Neurobiology of Disease (2015) Vol. 82, pp. 495-503
Open Access | Times Cited: 139
Whispering dysphonia (DYT4 dystonia) is caused by a mutation in the TUBB4 gene
Katja Lohmann, Robert A. Wilcox, Susen Winkler, et al.
Annals of Neurology (2012) Vol. 73, Iss. 4, pp. 537-545
Open Access | Times Cited: 139
Parkinson's disease-associated human ATP13A2 (PARK9) deficiency causes zinc dyshomeostasis and mitochondrial dysfunction
Jin-Sung Park, Brianada Koentjoro, David Veivers, et al.
Human Molecular Genetics (2014) Vol. 23, Iss. 11, pp. 2802-2815
Open Access | Times Cited: 137
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