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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:

Linking hnRNP Function to ALS and FTD Pathology
Maria D. Purice, J. Paul Taylor
Frontiers in Neuroscience (2018) Vol. 12
Open Access | Times Cited: 109

Showing 1-25 of 109 citing articles:

The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum
G Elif Karagöz, Diego Acosta‐Alvear, Peter Walter
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 9, pp. a033886-a033886
Open Access | Times Cited: 266
Karyopherin-mediated nucleocytoplasmic transport
Casey E. Wing, Ho Yee Joyce Fung, Yuh Min Chook
Nature Reviews Molecular Cell Biology (2022) Vol. 23, Iss. 5, pp. 307-328
Open Access | Times Cited: 190
Tau activates microglia via the PQBP1-cGAS-STING pathway to promote brain inflammation
Meihua Jin, Hiroki Shiwaku, Hikari Tanaka, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 134
Recent progress of the genetics of amyotrophic lateral sclerosis and challenges of gene therapy
Hui Wang, Liping Guan, Min Deng
Frontiers in Neuroscience (2023) Vol. 17
Open Access | Times Cited: 44
Cellular consequences of arginine methylation
Benjamin M. Lorton, David Shechter
Cellular and Molecular Life Sciences (2019) Vol. 76, Iss. 15, pp. 2933-2956
Open Access | Times Cited: 132
RNA-Binding Proteins in Amyotrophic Lateral Sclerosis.
Melody Zhao, Jihye Rachel Kim, Rebekah van Bruggen, et al.
PubMed (2018) Vol. 41, Iss. 9, pp. 818-829
Closed Access | Times Cited: 123
Structural Insights Into TDP-43 and Effects of Post-translational Modifications
Liberty François‐Moutal, Samantha Perez‐Miller, David D. Scott, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 123
The roles of hnRNP A2/B1 in RNA biology and disease
Yu Liu, Songlin Shi
Wiley Interdisciplinary Reviews - RNA (2020) Vol. 12, Iss. 2
Closed Access | Times Cited: 115
Molecular and Cellular Mechanisms Affected in ALS
Laura Le Gall, Ekene Anakor, Owen Connolly, et al.
Journal of Personalized Medicine (2020) Vol. 10, Iss. 3, pp. 101-101
Open Access | Times Cited: 112
The Nuclear SUMO-Targeted Ubiquitin Quality Control Network Regulates the Dynamics of Cytoplasmic Stress Granules
Jan Keiten‐Schmitz, Kristina Wagner, Tanja Piller, et al.
Molecular Cell (2020) Vol. 79, Iss. 1, pp. 54-67.e7
Closed Access | Times Cited: 102
The role of hnRNPs in frontotemporal dementia and amyotrophic lateral sclerosis
Alexander Bampton, Lauren M. Gittings, Pietro Fratta, et al.
Acta Neuropathologica (2020) Vol. 140, Iss. 5, pp. 599-623
Open Access | Times Cited: 97
ALS/FTD mutant CHCHD10 mice reveal a tissue-specific toxic gain-of-function and mitochondrial stress response
Corey J. Anderson, Kirsten Bredvik, Suzanne R. Burstein, et al.
Acta Neuropathologica (2019) Vol. 138, Iss. 1, pp. 103-121
Open Access | Times Cited: 87
Rare deleterious mutations of HNRNP genes result in shared neurodevelopmental disorders
Madelyn A. Gillentine, Tianyun Wang, Kendra Hoekzema, et al.
Genome Medicine (2021) Vol. 13, Iss. 1
Open Access | Times Cited: 85
Molecular Mechanisms Underlying TDP-43 Pathology in Cellular and Animal Models of ALS and FTLD
Alistair Wood, Yuval Gurfinkel, Nicole Polain, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 9, pp. 4705-4705
Open Access | Times Cited: 70
Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD
Bilal Khalil, Miriam Linsenmeier, Courtney L. Smith, et al.
Molecular Neurodegeneration (2024) Vol. 19, Iss. 1
Open Access | Times Cited: 15
Nuclear pore dysfunction and disease: a complex opportunity
Charlotte M. Fare, Jeffrey D. Rothstein
Nucleus (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 11
Implications of Selective Autophagy Dysfunction for ALS Pathology
Emiliano Vicencio, Sebastián Beltrán, Luis Labrador, et al.
Cells (2020) Vol. 9, Iss. 2, pp. 381-381
Open Access | Times Cited: 53
The proteome of granulovacuolar degeneration and neurofibrillary tangles in Alzheimer’s disease
David Hondius, Frank Koopmans, Conny Leistner, et al.
Acta Neuropathologica (2021) Vol. 141, Iss. 3, pp. 341-358
Open Access | Times Cited: 53
The overexpression of TDP-43 in astrocytes causes neurodegeneration via a PTP1B-mediated inflammatory response
Shinrye Lee, Seyeon Kim, Ha‐Young Kang, et al.
Journal of Neuroinflammation (2020) Vol. 17, Iss. 1
Open Access | Times Cited: 52
Stage-specific control of oligodendrocyte survival and morphogenesis by TDP-43
Dongeun Heo, Jonathan P. Ling, Gian C Molina-Castro, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 30
Cryo-EM structure of hnRNPDL-2 fibrils, a functional amyloid associated with limb-girdle muscular dystrophy D3
Javier García‐Pardo, Andrea Bartolomé-Nafría, Antonio Chaves-Sanjuán, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 21
Mutant UBQLN2 promotes toxicity by modulating intrinsic self-assembly
Lisa M. Sharkey, Nathaniel Safren, Amit S. Pithadia, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 44
Open Access | Times Cited: 57
A Chemical Chaperone Decouples TDP-43 Disordered Domain Phase Separation from Fibrillation
Kyoung‐Jae Choi, Phoebe S. Tsoi, Mahdi Muhammad Moosa, et al.
Biochemistry (2018) Vol. 57, Iss. 50, pp. 6822-6826
Open Access | Times Cited: 56
Pleiotropic requirements for human TDP-43 in the regulation of cell and organelle homeostasis
Agnes Roczniak-Ferguson, Shawn M. Ferguson
Life Science Alliance (2019) Vol. 2, Iss. 5, pp. e201900358-e201900358
Open Access | Times Cited: 50
The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure
Yunpeng Sun, Kun Zhao, Wencheng Xia, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 48
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