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:

Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains
Lin Guo, Hong Joo Kim, Hejia Wang, et al.
Cell (2018) Vol. 173, Iss. 3, pp. 677-692.e20
Open Access | Times Cited: 427

Showing 51-75 of 427 citing articles:

Loss of Dynamic RNA Interaction and Aberrant Phase Separation Induced by Two Distinct Types of ALS/FTD-Linked FUS Mutations
Amirhossein Ghanbari Niaki, Jaya Sarkar, Xinyi Cai, et al.
Molecular Cell (2019) Vol. 77, Iss. 1, pp. 82-94.e4
Open Access | Times Cited: 143
Stress granule mediated protein aggregation and underlying gene defects in the FTD-ALS spectrum
Yalda Baradaran‐Heravi, Christine Van Broeckhoven, Julie van der Zee
Neurobiology of Disease (2019) Vol. 134, pp. 104639-104639
Open Access | Times Cited: 138
Liquid–liquid phase separation in autophagy
Nobuo N. Noda, Zheng Wang, Hong Zhang
The Journal of Cell Biology (2020) Vol. 219, Iss. 8
Open Access | Times Cited: 136
RNA Droplets
Kevin Rhine, Velinda Vidaurre, Sua Myong
Annual Review of Biophysics (2020) Vol. 49, Iss. 1, pp. 247-265
Open Access | Times Cited: 126
A unified mechanism for LLPS of ALS/FTLD-causing FUS as well as its modulation by ATP and oligonucleic acids
Jian Kang, Liangzhong Lim, Yimei Lu, et al.
PLoS Biology (2019) Vol. 17, Iss. 6, pp. e3000327-e3000327
Open Access | Times Cited: 125
C9orf72 arginine-rich dipeptide repeat proteins disrupt karyopherin-mediated nuclear import
Lindsey R. Hayes, Lauren Duan, Kelly Bowen, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 119
Ubiquilin 2 modulates ALS/FTD-linked FUS–RNA complex dynamics and stress granule formation
Elizabeth J. Alexander, Amirhossein Ghanbari Niaki, Tao Zhang, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 49
Open Access | Times Cited: 118
Cytoplasmic functions of TDP-43 and FUS and their role in ALS
Nicol Birsa, Matthew P. Bentham, Pietro Fratta
Seminars in Cell and Developmental Biology (2019) Vol. 99, pp. 193-201
Open Access | Times Cited: 106
Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formation
Rachel L. French, Zachary R. Grese, Himani Aligireddy, et al.
Journal of Biological Chemistry (2019) Vol. 294, Iss. 17, pp. 6696-6709
Open Access | Times Cited: 105
Physiological, Pathological, and Targetable Membraneless Organelles in Neurons
Veronica H. Ryan, Nicolas L. Fawzi
Trends in Neurosciences (2019) Vol. 42, Iss. 10, pp. 693-708
Open Access | Times Cited: 105
Biomolecular condensates in neurodegeneration and cancer
Stephanie Spannl, Maria Tereshchenko, Giovanni J. Mastromarco, et al.
Traffic (2019) Vol. 20, Iss. 12, pp. 890-911
Open Access | Times Cited: 101
Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions
Saskia Hutten, Sinem Usluer, Benjamin Bourgeois, et al.
Cell Reports (2020) Vol. 33, Iss. 12, pp. 108538-108538
Open Access | Times Cited: 99
Phase Separation, Transition, and Autophagic Degradation of Proteins in Development and Pathogenesis
Zheng Wang, Hong Zhang
Trends in Cell Biology (2019) Vol. 29, Iss. 5, pp. 417-427
Closed Access | Times Cited: 98
Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase
James Shorter, Daniel R. Southworth
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 8, pp. a034033-a034033
Open Access | Times Cited: 97
CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
Jiahui Lu, Qin Cao, Michael P. Hughes, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 97
Cellular stress leads to the formation of membraneless stress assemblies in eukaryotic cells
Wessel van Leeuwen, Cathérine Rabouille
Traffic (2019) Vol. 20, Iss. 9, pp. 623-638
Open Access | Times Cited: 94
Hsp40 proteins phase separate to chaperone the assembly and maintenance of membraneless organelles
Jinge Gu, Zhenying Liu, Shengnan Zhang, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 49, pp. 31123-31133
Open Access | Times Cited: 94
A Comprehensive Analysis of the Role of hnRNP A1 Function and Dysfunction in the Pathogenesis of Neurodegenerative Disease
Joseph-Patrick W. E. Clarke, Patricia A. Thibault, Hannah E. Salapa, et al.
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 93
Differences between acute and chronic stress granules, and how these differences may impact function in human disease
Lucas C. Reineke, Joel R. Neilson
Biochemical Pharmacology (2018) Vol. 162, pp. 123-131
Open Access | Times Cited: 92
Molecular Dissection of FUS Points at Synergistic Effect of Low-Complexity Domains in Toxicity
Elke Bogaert, Steven Boeynaems, Masato Kato, et al.
Cell Reports (2018) Vol. 24, Iss. 3, pp. 529-537.e4
Open Access | Times Cited: 89
Stress granule subtypes: an emerging link to neurodegeneration
Vivek M. Advani, Pavel Ivanov
Cellular and Molecular Life Sciences (2020) Vol. 77, Iss. 23, pp. 4827-4845
Open Access | Times Cited: 89
Surface tension and viscosity of protein condensates quantified by micropipette aspiration
Huan Wang, Fleurie M. Kelley, Dragomir Milovanović, et al.
Biophysical Reports (2021) Vol. 1, Iss. 1, pp. 100011-100011
Open Access | Times Cited: 87
Regulation of liquid–liquid phase separation with focus on post-translational modifications
Yun-Yi Luo, Jun Wu, Yanmei Li
Chemical Communications (2021) Vol. 57, Iss. 98, pp. 13275-13287
Closed Access | Times Cited: 87
Biomolecular Condensates and Their Links to Cancer Progression
Danfeng Cai, Zhe Liu, Jennifer Lippincott‐Schwartz
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 7, pp. 535-549
Closed Access | Times Cited: 82
Splicing repression is a major function of TDP-43 in motor neurons
Aneesh Donde, Mingkuan Sun, Jonathan P. Ling, et al.
Acta Neuropathologica (2019) Vol. 138, Iss. 5, pp. 813-826
Open Access | Times Cited: 81

Scroll to top