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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:

Blessings in disguise: biological benefits of prion-like mechanisms
Gregory A. Newby, Susan Lindquist
Trends in Cell Biology (2013) Vol. 23, Iss. 6, pp. 251-259
Closed Access | Times Cited: 141

Showing 1-25 of 141 citing articles:

PLAAC: a web and command-line application to identify proteins with prion-like amino acid composition
Alex K. Lancaster, Andrew Nutter-Upham, Susan Lindquist, et al.
Bioinformatics (2014) Vol. 30, Iss. 17, pp. 2501-2502
Open Access | Times Cited: 537
Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use
John F. Atkins, Gary Loughran, Pramod R. Bhatt, et al.
Nucleic Acids Research (2016), pp. gkw530-gkw530
Open Access | Times Cited: 328
Neurodegenerative Diseases: Expanding the Prion Concept
Lary C. Walker, Mathias Jucker
Annual Review of Neuroscience (2015) Vol. 38, Iss. 1, pp. 87-103
Open Access | Times Cited: 323
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
FUS and TDP-43 Phases in Health and Disease
Bede Portz, Bo Lim Lee, James Shorter
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 7, pp. 550-563
Open Access | Times Cited: 226
Potentiated Hsp104 Variants Antagonize Diverse Proteotoxic Misfolding Events
Meredith E. Jackrel, Morgan E. DeSantis, Bryan Martinez, et al.
Cell (2014) Vol. 156, Iss. 1-2, pp. 170-182
Open Access | Times Cited: 224
Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease
Zachary M. March, Oliver D. King, James Shorter
Brain Research (2016) Vol. 1647, pp. 9-18
Open Access | Times Cited: 212
Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior
Titus M. Franzmann, Simon Alberti
Journal of Biological Chemistry (2018) Vol. 294, Iss. 18, pp. 7128-7136
Open Access | Times Cited: 207
Luminidependens (LD) is an Arabidopsis protein with prion behavior
Sohini Chakrabortee, Can Kayatekin, Gregory A. Newby, et al.
Proceedings of the National Academy of Sciences (2016) Vol. 113, Iss. 21, pp. 6065-6070
Open Access | Times Cited: 186
A bacterial global regulator forms a prion
Andy H. Yuan, Ann Hochschild
Science (2017) Vol. 355, Iss. 6321, pp. 198-201
Open Access | Times Cited: 154
Protein Phase Separation as a Stress Survival Strategy
Titus M. Franzmann, Simon Alberti
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 6, pp. a034058-a034058
Open Access | Times Cited: 145
Controlling entropy to tune the functions of intrinsically disordered regions
Tilman Flock, Robert J. Weatheritt, Natasha S. Latysheva, et al.
Current Opinion in Structural Biology (2014) Vol. 26, pp. 62-72
Closed Access | Times Cited: 144
Cell Biology of Prions and Prionoids: A Status Report
Adriano Aguzzi, Asvin KK Lakkaraju
Trends in Cell Biology (2015) Vol. 26, Iss. 1, pp. 40-51
Closed Access | Times Cited: 137
Self-assembled FUS binds active chromatin and regulates gene transcription
Liuqing Yang, József Gál, Jing Chen, et al.
Proceedings of the National Academy of Sciences (2014) Vol. 111, Iss. 50, pp. 17809-17814
Open Access | Times Cited: 134
Protein aggregates are associated with replicative aging without compromising protein quality control
Juha Saarikangas, Yves Barral
eLife (2015) Vol. 4
Open Access | Times Cited: 133
The CPEB3 Protein Is a Functional Prion that Interacts with the Actin Cytoskeleton
Joseph S. Stephan, Luana Fioriti, Nayan Lamba, et al.
Cell Reports (2015) Vol. 11, Iss. 11, pp. 1772-1785
Open Access | Times Cited: 127
An Evolutionarily Conserved Prion-like Element Converts Wild Fungi from Metabolic Specialists to Generalists
Daniel F. Jarosz, Alex K. Lancaster, Jessica C. S. Brown, et al.
Cell (2014) Vol. 158, Iss. 5, pp. 1072-1082
Open Access | Times Cited: 119
Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104
Elizabeth A. Sweeny, James Shorter
Journal of Molecular Biology (2015) Vol. 428, Iss. 9, pp. 1870-1885
Open Access | Times Cited: 92
Molecular Basis of Orb2 Amyloidogenesis and Blockade of Memory Consolidation
Rubén Hervás, Liying Li, Amitabha Majumdar, et al.
PLoS Biology (2016) Vol. 14, Iss. 1, pp. e1002361-e1002361
Open Access | Times Cited: 89
Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins
Meredith E. Jackrel, James Shorter
Disease Models & Mechanisms (2014)
Open Access | Times Cited: 93
Functional Role of Tia1/Pub1 and Sup35 Prion Domains: Directing Protein Synthesis Machinery to the Tubulin Cytoskeleton
Xiang Li, Joseph B. Rayman, Eric R. Kandel, et al.
Molecular Cell (2014) Vol. 55, Iss. 2, pp. 305-318
Open Access | Times Cited: 82
Yeast and Fungal Prions
Reed B. Wickner
Cold Spring Harbor Perspectives in Biology (2016) Vol. 8, Iss. 9, pp. a023531-a023531
Open Access | Times Cited: 80
Protein aggregation as a mechanism of adaptive cellular responses
Juha Saarikangas, Yves Barral
Current Genetics (2016) Vol. 62, Iss. 4, pp. 711-724
Closed Access | Times Cited: 71
Prions, Chaperones, and Proteostasis in Yeast
Tatiana A. Chernova, Keith D. Wilkinson, Yury O. Chernoff
Cold Spring Harbor Perspectives in Biology (2016) Vol. 9, Iss. 2, pp. a023663-a023663
Open Access | Times Cited: 70
The role of disorder in RNA binding affinity and specificity
Diana S. M. Ottoz, Luke E. Berchowitz
Open Biology (2020) Vol. 10, Iss. 12
Open Access | Times Cited: 68
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