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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:

Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA
Andreas C. Woerner, Frédéric Frottin, Daniel Hornburg, et al.
Science (2015) Vol. 351, Iss. 6269, pp. 173-176
Open Access | Times Cited: 372

Showing 1-25 of 372 citing articles:

In vivo aspects of protein folding and quality control
David Balchin, Manajit Hayer‐Hartl, F. Ulrich Hartl
Science (2016) Vol. 353, Iss. 6294
Open Access | Times Cited: 1308
The proteostasis network and its decline in ageing
Mark S. Hipp, Prasad Kasturi, F. Ulrich Hartl
Nature Reviews Molecular Cell Biology (2019) Vol. 20, Iss. 7, pp. 421-435
Open Access | Times Cited: 1211
A new era for understanding amyloid structures and disease
M.G. Iadanza, Matthew P. Jackson, Eric W. Hewitt, et al.
Nature Reviews Molecular Cell Biology (2018) Vol. 19, Iss. 12, pp. 755-773
Closed Access | Times Cited: 863
Pathways of cellular proteostasis in aging and disease
Courtney L. Klaips, Gopal Gunanathan Jayaraj, F. Ulrich Hartl
The Journal of Cell Biology (2017) Vol. 217, Iss. 1, pp. 51-63
Open Access | Times Cited: 706
Protein misfolding in neurodegenerative diseases: implications and strategies
Patrick Sweeney, Hyunsun Park, Marc Baumann, et al.
Translational Neurodegeneration (2017) Vol. 6, Iss. 1
Open Access | Times Cited: 555
TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD
Ching-Chieh Chou, Yi Zhang, Mfon Umoh, et al.
Nature Neuroscience (2018) Vol. 21, Iss. 2, pp. 228-239
Open Access | Times Cited: 511
Protein Misfolding Diseases
F. Ulrich Hartl
Annual Review of Biochemistry (2017) Vol. 86, Iss. 1, pp. 21-26
Closed Access | Times Cited: 487
The nucleolus functions as a phase-separated protein quality control compartment
Frédéric Frottin, Florian Schueder, Shivani Tiwary, et al.
Science (2019) Vol. 365, Iss. 6451, pp. 342-347
Open Access | Times Cited: 441
Stress Granule Assembly Disrupts Nucleocytoplasmic Transport
Ke Zhang, J. Gavin Daigle, Kathleen M. Cunningham, et al.
Cell (2018) Vol. 173, Iss. 4, pp. 958-971.e17
Open Access | Times Cited: 384
Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimer’s Disease
Bahareh Eftekharzadeh, J. Gavin Daigle, Larisa E. Kapinos, et al.
Neuron (2018) Vol. 99, Iss. 5, pp. 925-940.e7
Open Access | Times Cited: 377
In Situ Architecture and Cellular Interactions of PolyQ Inclusions
Felix J.B. Bäuerlein, Itika Saha, Archana Mishra, et al.
Cell (2017) Vol. 171, Iss. 1, pp. 179-187.e10
Open Access | Times Cited: 339
Mutant Huntingtin Disrupts the Nuclear Pore Complex
Jonathan C. Grima, J. Gavin Daigle, Nicolas Arbez, et al.
Neuron (2017) Vol. 94, Iss. 1, pp. 93-107.e6
Open Access | Times Cited: 331
Physiological functions and pathobiology of TDP‐43 and FUS/TLS proteins
Antonia Ratti, Emanuele Buratti
Journal of Neurochemistry (2016) Vol. 138, Iss. S1, pp. 95-111
Open Access | Times Cited: 325
Phase Separation: Linking Cellular Compartmentalization to Disease
Adriano Aguzzi, Matthias Altmeyer
Trends in Cell Biology (2016) Vol. 26, Iss. 7, pp. 547-558
Closed Access | Times Cited: 323
A Liquid to Solid Phase Transition Underlying Pathological Huntingtin Exon1 Aggregation
Thomas R. Peskett, Fredérique Rau, Jonathan O’Driscoll, et al.
Molecular Cell (2018) Vol. 70, Iss. 4, pp. 588-601.e6
Open Access | Times Cited: 317
C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins
Yong‐Jie Zhang, Tania F. Gendron, Jonathan C. Grima, et al.
Nature Neuroscience (2016) Vol. 19, Iss. 5, pp. 668-677
Open Access | Times Cited: 300
Are aberrant phase transitions a driver of cellular aging?
Simon Alberti, Anthony A. Hyman
BioEssays (2016) Vol. 38, Iss. 10, pp. 959-968
Open Access | Times Cited: 283
Mechanisms and Functions of Spatial Protein Quality Control
Emily M. Sontag, Rahul S. Samant, Judith Frydman
Annual Review of Biochemistry (2017) Vol. 86, Iss. 1, pp. 97-122
Closed Access | Times Cited: 266
Polyglutamine Repeats in Neurodegenerative Diseases
Andrew P. Lieberman, Vikram G. Shakkottai, Roger L. Albin
Annual Review of Pathology Mechanisms of Disease (2018) Vol. 14, Iss. 1, pp. 1-27
Open Access | Times Cited: 260
Architecture of the symmetric core of the nuclear pore
Daniel H. Lin, T. Stuwe, S. Schilbach, et al.
Science (2016) Vol. 352, Iss. 6283
Open Access | Times Cited: 257
Lost in Transportation: Nucleocytoplasmic Transport Defects in ALS and Other Neurodegenerative Diseases
Hong Joo Kim, J. Paul Taylor
Neuron (2017) Vol. 96, Iss. 2, pp. 285-297
Open Access | Times Cited: 246
Polyglutamine-Expanded Huntingtin Exacerbates Age-Related Disruption of Nuclear Integrity and Nucleocytoplasmic Transport
F. Gasset-Rosa, Carlos Chillón-Marinas, Alexander Goginashvili, et al.
Neuron (2017) Vol. 94, Iss. 1, pp. 48-57.e4
Open Access | Times Cited: 231
Soluble Oligomers of PolyQ-Expanded Huntingtin Target a Multiplicity of Key Cellular Factors
Yujin Kim, Fabian Hosp, Frédéric Frottin, et al.
Molecular Cell (2016) Vol. 63, Iss. 6, pp. 951-964
Open Access | Times Cited: 221
Recent Insights into the Role of Unfolded Protein Response in ER Stress in Health and Disease
Dan Lindholm, Laura Korhonen, Ove Eriksson, et al.
Frontiers in Cell and Developmental Biology (2017) Vol. 5
Open Access | Times Cited: 200
The expanding biology of the C9orf72 nucleotide repeat expansion in neurodegenerative disease
Aaron R. Haeusler, Christopher J. Donnelly, Jeffrey D. Rothstein
Nature reviews. Neuroscience (2016) Vol. 17, Iss. 6, pp. 383-395
Open Access | Times Cited: 183
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