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:

Protein aggregation diseases: pathogenicity and therapeutic perspectives
Adriano Aguzzi, Tracy O’Connor
Nature Reviews Drug Discovery (2010) Vol. 9, Iss. 3, pp. 237-248
Closed Access | Times Cited: 714

Showing 1-25 of 714 citing articles:

Delivery of siRNA to the mouse brain by systemic injection of targeted exosomes
Lydia Álvarez-Erviti, Yiqi Seow, HaiFang Yin, et al.
Nature Biotechnology (2011) Vol. 29, Iss. 4, pp. 341-345
Closed Access | Times Cited: 4200
The Amyloid State of Proteins in Human Diseases
David Eisenberg, Mathias Jucker
Cell (2012) Vol. 148, Iss. 6, pp. 1188-1203
Open Access | Times Cited: 1640
Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
Han‐Xiang Deng, Wenjie Chen, Seong‐Tshool Hong, et al.
Nature (2011) Vol. 477, Iss. 7363, pp. 211-215
Open Access | Times Cited: 1112
ER stress and the unfolded protein response in neurodegeneration
Claudio Hetz, Smita Saxena
Nature Reviews Neurology (2017) Vol. 13, Iss. 8, pp. 477-491
Closed Access | Times Cited: 811
Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology
Gang Wei, Zhiqiang Su, Nicholas P. Reynolds, et al.
Chemical Society Reviews (2017) Vol. 46, Iss. 15, pp. 4661-4708
Open Access | Times Cited: 792
Molecular mechanisms of protein aggregation from global fitting of kinetic models
Georg Meisl, Julius B. Kirkegaard, Paolo Arosio, et al.
Nature Protocols (2016) Vol. 11, Iss. 2, pp. 252-272
Closed Access | Times Cited: 661
Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity
Zachary Monahan, Veronica H. Ryan, Abigail M. Janke, et al.
The EMBO Journal (2017) Vol. 36, Iss. 20, pp. 2951-2967
Open Access | Times Cited: 632
Gain of function of mutant p53 by coaggregation with multiple tumor suppressors
Jie Xu, Joke Reumers, José R. Couceiro, et al.
Nature Chemical Biology (2011) Vol. 7, Iss. 5, pp. 285-295
Closed Access | Times Cited: 505
Fragmented mitochondria released from microglia trigger A1 astrocytic response and propagate inflammatory neurodegeneration
Amit U. Joshi, Paras S. Minhas, Shane A. Liddelow, et al.
Nature Neuroscience (2019) Vol. 22, Iss. 10, pp. 1635-1648
Open Access | Times Cited: 467
From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation
Samuel I. A. Cohen, Michele Vendruscolo, Christopher M. Dobson, et al.
Journal of Molecular Biology (2012) Vol. 421, Iss. 2-3, pp. 160-171
Closed Access | Times Cited: 459
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides
Georg Meisl, Xiaoting Yang, Erik Hellstrand, et al.
Proceedings of the National Academy of Sciences (2014) Vol. 111, Iss. 26, pp. 9384-9389
Open Access | Times Cited: 451
A Method for the Acute and Rapid Degradation of Endogenous Proteins
Dean Clift, William A. McEwan, Larisa I. Labzin, et al.
Cell (2017) Vol. 171, Iss. 7, pp. 1692-1706.e18
Open Access | Times Cited: 426
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
Samuel I. A. Cohen, Paolo Arosio, Jenny Presto, et al.
Nature Structural & Molecular Biology (2015) Vol. 22, Iss. 3, pp. 207-213
Open Access | Times Cited: 385
Prions in Yeast
Susan W. Liebman, Yury O. Chernoff
Genetics (2012) Vol. 191, Iss. 4, pp. 1041-1072
Open Access | Times Cited: 377
Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments
Samuel I. A. Cohen, Michele Vendruscolo, Mark E. Welland, et al.
The Journal of Chemical Physics (2011) Vol. 135, Iss. 6
Open Access | Times Cited: 335
Autophagy in neurodegenerative diseases: pathogenesis and therapy
Fang Guo, Xinyao Liu, Huaibin Cai, et al.
Brain Pathology (2017) Vol. 28, Iss. 1, pp. 3-13
Open Access | Times Cited: 333
Ubiquitin-independent function of optineurin in autophagic clearance of protein aggregates
Jelena Korać-Prlić, Véronique Schaeffer, Igor Kovačević, et al.
Journal of Cell Science (2012) Vol. 126, Iss. 2, pp. 580-592
Open Access | Times Cited: 308
Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases
Daniel W. Neef, Alex M. Jaeger, Dennis J. Thiele
Nature Reviews Drug Discovery (2011) Vol. 10, Iss. 12, pp. 930-944
Open Access | Times Cited: 288
Liquid-liquid phase separation in biology: mechanisms, physiological functions and human diseases
Hong Zhang, Ji Xiong, Pilong Li, et al.
Science China Life Sciences (2020) Vol. 63, Iss. 7, pp. 953-985
Closed Access | Times Cited: 254
A Seeding Reaction Recapitulates Intracellular Formation of Sarkosyl-insoluble Transactivation Response Element (TAR) DNA-binding Protein-43 Inclusions
Yoshiaki Furukawa, Kumi Kaneko, Shôji Watanabe, et al.
Journal of Biological Chemistry (2011) Vol. 286, Iss. 21, pp. 18664-18672
Open Access | Times Cited: 232
Manganese-Induced Neurotoxicity: New Insights Into the Triad of Protein Misfolding, Mitochondrial Impairment, and Neuroinflammation
Dilshan S. Harischandra, Shivani Ghaisas, Gary Zenitsky, et al.
Frontiers in Neuroscience (2019) Vol. 13
Open Access | Times Cited: 230
Aβ neurotoxicity depends on interactions between copper ions, prion protein, and N -methyl- d -aspartate receptors
Haitao You, Shigeki Tsutsui, Shahid Hameed, et al.
Proceedings of the National Academy of Sciences (2012) Vol. 109, Iss. 5, pp. 1737-1742
Open Access | Times Cited: 225
Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity
Pin‐Nan Cheng, Cong Liu, Minglei Zhao, et al.
Nature Chemistry (2012) Vol. 4, Iss. 11, pp. 927-933
Open Access | Times Cited: 222
Function and toxicity of amyloid beta and recent therapeutic interventions targeting amyloid beta in Alzheimer's disease
Kolla Rajasekhar, Malabika Chakrabarti, Thimmaiah Govindaraju
Chemical Communications (2015) Vol. 51, Iss. 70, pp. 13434-13450
Closed Access | Times Cited: 220
Matter over mind: Liquid phase separation and neurodegeneration
Shana Elbaum‐Garfinkle
Journal of Biological Chemistry (2019) Vol. 294, Iss. 18, pp. 7160-7168
Open Access | Times Cited: 217
Page 1 - Next Page

Scroll to top