Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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 1-25 of 141 citing articles:

PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
Noriyuki Matsuda, Shigeto Sato, Kahori Shiba, et al.
The Journal of Cell Biology (2010) Vol. 189, Iss. 2, pp. 211-221
Open Access | Times Cited: 1787
Loss of PINK1 Function Promotes Mitophagy through Effects on Oxidative Stress and Mitochondrial Fission
Ruben K. Dagda, Salvatore J. Cherra, Scott Kulich, et al.
Journal of Biological Chemistry (2009) Vol. 284, Iss. 20, pp. 13843-13855
Open Access | Times Cited: 900
The PINK1/Parkin pathway regulates mitochondrial morphology
Angela C. Poole, Ruth E. Thomas, Laurie A. Andrews, et al.
Proceedings of the National Academy of Sciences (2008) Vol. 105, Iss. 5, pp. 1638-1643
Open Access | Times Cited: 848
Parkinson's disease
Bobby Thomas, M. Flint Beal
Human Molecular Genetics (2007) Vol. 16, Iss. R2, pp. R183-R194
Open Access | Times Cited: 684
Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
Clément Gautier, Tohru Kitada, Jie Shen
Proceedings of the National Academy of Sciences (2008) Vol. 105, Iss. 32, pp. 11364-11369
Open Access | Times Cited: 657
PINK1 Protects against Oxidative Stress by Phosphorylating Mitochondrial Chaperone TRAP1
Julia W. Pridgeon, James A. Olzmann, Lih‐Shen Chin, et al.
PLoS Biology (2007) Vol. 5, Iss. 7, pp. e172-e172
Open Access | Times Cited: 589
PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
Kei Okatsu, Toshihiko Oka, Masahiro Iguchi, et al.
Nature Communications (2012) Vol. 3, Iss. 1
Open Access | Times Cited: 540
PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy
Kahori Shiba‐Fukushima, Yuzuru Imai, Shigeharu Yoshida, et al.
Scientific Reports (2012) Vol. 2, Iss. 1
Open Access | Times Cited: 536
Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update
Karen Nuytemans, Jessie Theuns, Marc Cruts, et al.
Human Mutation (2010) Vol. 31, Iss. 7, pp. 763-780
Open Access | Times Cited: 511
The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
Hélène Plun‐Favreau, Kristina Klupsch, Nicoleta Moisoi, et al.
Nature Cell Biology (2007) Vol. 9, Iss. 11, pp. 1243-1252
Closed Access | Times Cited: 467
PINK1 cleavage at position A103 by the mitochondrial protease PARL
Emma Deas, Hélène Plun‐Favreau, Sonia Gandhi, et al.
Human Molecular Genetics (2010) Vol. 20, Iss. 5, pp. 867-879
Open Access | Times Cited: 447
PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
Yong Sung Kim, Jeehye Park, Sunhong Kim, et al.
Biochemical and Biophysical Research Communications (2008) Vol. 377, Iss. 3, pp. 975-980
Closed Access | Times Cited: 354
PINK1 Is Necessary for Long Term Survival and Mitochondrial Function in Human Dopaminergic Neurons
Alison Wood‐Kaczmar, Sonia Gandhi, Zhi Yao, et al.
PLoS ONE (2008) Vol. 3, Iss. 6, pp. e2455-e2455
Open Access | Times Cited: 309
Deciphering the role of heterozygous mutations in genes associated with parkinsonism
Christine Klein, K. Lohmann-Hedrich, Ekaterina Rogaeva, et al.
The Lancet Neurology (2007) Vol. 6, Iss. 7, pp. 652-662
Closed Access | Times Cited: 309
PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy
Sumihiro Kawajiri, Shinji Saiki, Shigeto Sato, et al.
FEBS Letters (2010) Vol. 584, Iss. 6, pp. 1073-1079
Open Access | Times Cited: 234
Characterization of PINK1 processing, stability, and subcellular localization
William Lin, Un Jung Kang
Journal of Neurochemistry (2008) Vol. 106, Iss. 1, pp. 464-474
Open Access | Times Cited: 233
Parkinson disease, 10 years after its genetic revolution: Multiple clues to a complex disorder
Christine Klein, Michael G. Schlossmacher
Neurology (2007) Vol. 69, Iss. 22, pp. 2093-2104
Closed Access | Times Cited: 208
Silencing of PINK1 Expression Affects Mitochondrial DNA and Oxidative Phosphorylation in DOPAMINERGIC Cells
Matthew E. Gegg, Jonathan M. Cooper, Anthony H.V. Schapira, et al.
PLoS ONE (2009) Vol. 4, Iss. 3, pp. e4756-e4756
Open Access | Times Cited: 192
Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF- B signaling
Dan Sha, Lih‐Shen Chin, Lian Li
Human Molecular Genetics (2009) Vol. 19, Iss. 2, pp. 352-363
Open Access | Times Cited: 180
Loss of PINK1 Function Affects Development and Results in Neurodegeneration in Zebrafish
Oleg Anichtchik, Heike Diekmann, Angeleen Fleming, et al.
Journal of Neuroscience (2008) Vol. 28, Iss. 33, pp. 8199-8207
Open Access | Times Cited: 168
Structure of PINK1 in complex with its substrate ubiquitin
Alexander F. Schubert, Christina Gladkova, Els Pardon, et al.
Nature (2017) Vol. 552, Iss. 7683, pp. 51-56
Open Access | Times Cited: 157
Oxidative modifications, mitochondrial dysfunction, and impaired protein degradation in Parkinson's disease: how neurons are lost in the Bermuda triangle
Kristen Malkus, Elpida Tsika, Harry Ischiropoulos
Molecular Neurodegeneration (2009) Vol. 4, Iss. 1
Open Access | Times Cited: 135
Lipid rafts: Keys to neurodegeneration
Cara‐Lynne Schengrund
Brain Research Bulletin (2010) Vol. 82, Iss. 1-2, pp. 7-17
Closed Access | Times Cited: 128
Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection
Jean‐François Trempe, Edward A. Fon
Frontiers in Neurology (2013) Vol. 4
Open Access | Times Cited: 127
PARK6 PINK1 mutants are defective in maintaining mitochondrial membrane potential and inhibiting ROS formation of substantia nigra dopaminergic neurons
Hung‐Li Wang, An-Hsun Chou, Ai-Shun Wu, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2011) Vol. 1812, Iss. 6, pp. 674-684
Open Access | Times Cited: 120
Page 1 - Next Page

Scroll to top