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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:

C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1
Chou Hung Sim, Daisy Lio, Su San Mok, et al.
Human Molecular Genetics (2006) Vol. 15, Iss. 21, pp. 3251-3262
Open Access | Times Cited: 141

Showing 26-50 of 141 citing articles:

S-Nitrosylation of PINK1 Attenuates PINK1/Parkin-Dependent Mitophagy in hiPSC-Based Parkinson’s Disease Models
Chang-ki Oh, Abdullah Sultan, Joseph Platzer, et al.
Cell Reports (2017) Vol. 21, Iss. 8, pp. 2171-2182
Open Access | Times Cited: 113
PINK1 Kinase Catalytic Activity Is Regulated by Phosphorylation on Serines 228 and 402
Liesbeth Aerts, Katleen Craessaerts, Bart De Strooper, et al.
Journal of Biological Chemistry (2014) Vol. 290, Iss. 5, pp. 2798-2811
Open Access | Times Cited: 109
PINK 1 autophosphorylation is required for ubiquitin recognition
Shafqat Rasool, Naoto Soya, Luc Truong, et al.
EMBO Reports (2018) Vol. 19, Iss. 4
Open Access | Times Cited: 103
Regulation of mitochondrial functions by protein phosphorylation and dephosphorylation
Sangbin Lim, Kelly Smith, Ssang‐Taek Lim, et al.
Cell & Bioscience (2016) Vol. 6, Iss. 1
Open Access | Times Cited: 91
Mechanisms of PINK1, ubiquitin and Parkin interactions in mitochondrial quality control and beyond
Andrew N. Bayne, Jean‐François Trempe
Cellular and Molecular Life Sciences (2019) Vol. 76, Iss. 23, pp. 4589-4611
Closed Access | Times Cited: 89
PINK1-dependent phosphorylation of PINK1 and Parkin is essential for mitochondrial quality control
Na Zhuang, Lin Li, She Chen, et al.
Cell Death and Disease (2016) Vol. 7, Iss. 12, pp. e2501-e2501
Open Access | Times Cited: 86
Mitochondria in Aging and Alzheimer’s Disease: Focus on Mitophagy
Jangampalli Adi Pradeepkiran, Javaria Baig, Ann Seman, et al.
The Neuroscientist (2023) Vol. 30, Iss. 4, pp. 440-457
Closed Access | Times Cited: 29
Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1
Andreas Weihofen, Beth L. Ostaszewski, Yasufumi Minami, et al.
Human Molecular Genetics (2007) Vol. 17, Iss. 4, pp. 602-616
Closed Access | Times Cited: 142
Review: Familial Parkinson's disease – genetics, clinical phenotype and neuropathology in relation to the common sporadic form of the disease
Carola Schiesling, Nicole Kieper, Kay Seidel, et al.
Neuropathology and Applied Neurobiology (2008) Vol. 34, Iss. 3, pp. 255-271
Closed Access | Times Cited: 134
Effect of endogenous mutant and wild-type PINK1 on Parkin in fibroblasts from Parkinson disease patients
Aleksandar Raković, Anne Grünewald, Philip Seibler, et al.
Human Molecular Genetics (2010) Vol. 19, Iss. 16, pp. 3124-3137
Closed Access | Times Cited: 123
Cytoplasmic localization and proteasomal degradation of N-terminally cleaved form of PINK1
Sho Takatori, Genta Ito, Takeshi Iwatsubo
Neuroscience Letters (2007) Vol. 430, Iss. 1, pp. 13-17
Closed Access | Times Cited: 114
A critical evaluation of the ubiquitin–proteasome system in Parkinson's disease
Casey Cook, Leonard Petrucelli
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2009) Vol. 1792, Iss. 7, pp. 664-675
Open Access | Times Cited: 111
Mitochondrial Respiratory Dysfunction in Familiar Parkinsonism Associated with PINK1 Mutation
Cláudia Piccoli, Anna Maria Sardanelli, Rosella Scrima, et al.
Neurochemical Research (2008) Vol. 33, Iss. 12, pp. 2565-2574
Closed Access | Times Cited: 109
Impact of recent genetic findings in Parkinson??s disease
Christine Klein, K. Lohmann-Hedrich
Current Opinion in Neurology (2007) Vol. 20, Iss. 4, pp. 453-464
Closed Access | Times Cited: 106
Kinases and kinase signaling pathways: Potential therapeutic targets in Parkinson's disease
Gang Wang, Jing Pan, Shengdi Chen
Progress in Neurobiology (2012) Vol. 98, Iss. 2, pp. 207-221
Closed Access | Times Cited: 102
Pathogenesis of familial Parkinson’s disease: new insights based on monogenic forms of Parkinson’s disease
Taku Hatano, Shinichiro Kubo, Shigeto Sato, et al.
Journal of Neurochemistry (2009) Vol. 111, Iss. 5, pp. 1075-1093
Open Access | Times Cited: 97
Neural stem cells in Parkinson’s disease: a role for neurogenesis defects in onset and progression
Jaclyn Nicole Le Grand, Laura González-Cano, Maria Angeliki S. Pavlou, et al.
Cellular and Molecular Life Sciences (2014) Vol. 72, Iss. 4, pp. 773-797
Closed Access | Times Cited: 94
The effects of pdr1, djr1.1 and pink1 loss in manganese-induced toxicity and the role of α-synuclein in C. elegans
Julia Bornhorst, Sudipta Chakraborty, Sören Meyer, et al.
Metallomics (2013) Vol. 6, Iss. 3, pp. 476-490
Open Access | Times Cited: 92
Pink1 deficiency attenuates astrocyte proliferation through mitochondrial dysfunction, reduced akt and increased p38 mapk activation, and downregulation of egfr
Insup Choi, Jun Kim, Hey‐Kyeong Jeong, et al.
Glia (2013) Vol. 61, Iss. 5, pp. 800-812
Open Access | Times Cited: 86
Genetic mutations and functions of PINK1
Sumihiro Kawajiri, Shinji Saiki, Shigeto Sato, et al.
Trends in Pharmacological Sciences (2011) Vol. 32, Iss. 10, pp. 573-580
Closed Access | Times Cited: 80
Characterization of PINK1 (PTEN-induced Putative Kinase 1) Mutations Associated with Parkinson Disease in Mammalian Cells and Drosophila*
Saera Song, Seoyeon Jang, Jeehye Park, et al.
Journal of Biological Chemistry (2013) Vol. 288, Iss. 8, pp. 5660-5672
Open Access | Times Cited: 74
Akt Phosphorylates NQO1 and Triggers its Degradation, Abolishing Its Antioxidative Activities in Parkinson's Disease
Shilin Luo, Seong Su Kang, Zhi-Hao Wang, et al.
Journal of Neuroscience (2019) Vol. 39, Iss. 37, pp. 7291-7305
Open Access | Times Cited: 65
The multi‐faceted role of mitochondria in the pathology of Parkinson’s disease
Dennison Trinh, Ahmad R. Israwi, Lindsay R. Arathoon, et al.
Journal of Neurochemistry (2020) Vol. 156, Iss. 6, pp. 715-752
Open Access | Times Cited: 61
Autophagy regulation by RNA alternative splicing and implications in human diseases
Patricia González-Rodríguez, Daniel J. Klionsky, Bertrand Joseph
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 28
Mitochondrial protein dysfunction in pathogenesis of neurological diseases
Liang Wang, Ziyun Yang, Xiumei He, et al.
Frontiers in Molecular Neuroscience (2022) Vol. 15
Open Access | Times Cited: 28

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