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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:

The amyloid state and its association with protein misfolding diseases
Tuomas P. J. Knowles, Michele Vendruscolo, Christopher M. Dobson
Nature Reviews Molecular Cell Biology (2014) Vol. 15, Iss. 6, pp. 384-396
Closed Access | Times Cited: 2205

Showing 1-25 of 2205 citing articles:

Considerations and Challenges in Studying Liquid-Liquid Phase Separation and Biomolecular Condensates
Simon Alberti, Amy Gladfelter, Tanja Mittag
Cell (2019) Vol. 176, Iss. 3, pp. 419-434
Open Access | Times Cited: 2353
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Fabrizio Chiti, Christopher M. Dobson
Annual Review of Biochemistry (2017) Vol. 86, Iss. 1, pp. 27-68
Closed Access | Times Cited: 2330
Supramolecular Helical Systems: Helical Assemblies of Small Molecules, Foldamers, and Polymers with Chiral Amplification and Their Functions
Eiji Yashima, Naoki Ousaka, Daisuke Taura, et al.
Chemical Reviews (2016) Vol. 116, Iss. 22, pp. 13752-13990
Open Access | Times Cited: 1689
The Biology of Proteostasis in Aging and Disease
Johnathan Labbadia, Richard I. Morimoto
Annual Review of Biochemistry (2015) Vol. 84, Iss. 1, pp. 435-464
Open Access | Times Cited: 1287
The Amyloid-β Pathway in Alzheimer’s Disease
Harald Hampel, John Hardy, Kaj Blennow, et al.
Molecular Psychiatry (2021) Vol. 26, Iss. 10, pp. 5481-5503
Open Access | Times Cited: 1041
Fibril structure of amyloid-β(1–42) by cryo–electron microscopy
Lothar Gremer, Daniel Schölzel, C. Schenk, et al.
Science (2017) Vol. 358, Iss. 6359, pp. 116-119
Open Access | Times Cited: 913
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: 860
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
Supramolecular Polymers in Aqueous Media
Elisha Krieg, Maartje M. C. Bastings, Pol Besenius, et al.
Chemical Reviews (2016) Vol. 116, Iss. 4, pp. 2414-2477
Closed Access | Times Cited: 689
EHRA/HRS/APHRS/SOLAECE expert consensus on atrial cardiomyopathies: Definition, characterization, and clinical implication
Andreas Goette, Jonathan M. Kalman, Luis Aguinaga, et al.
Heart Rhythm (2016) Vol. 14, Iss. 1, pp. e3-e40
Open Access | Times Cited: 687
Biomimetic peptide self-assembly for functional materials
Aviad Levin, Tuuli A. Hakala, Lee Schnaider, et al.
Nature Reviews Chemistry (2020) Vol. 4, Iss. 11, pp. 615-634
Closed Access | Times Cited: 641
EHRA/HRS/APHRS/SOLAECE expert consensus on atrial cardiomyopathies: definition, characterization, and clinical implication
Andreas Goette, Jonathan M. Kalman, Luis Aguinaga, et al.
EP Europace (2016) Vol. 18, Iss. 10, pp. 1455-1490
Open Access | Times Cited: 612
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
Céline Galvagnion, Alexander K. Buell, Georg Meisl, et al.
Nature Chemical Biology (2015) Vol. 11, Iss. 3, pp. 229-234
Open Access | Times Cited: 597
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: 548
Widespread Proteome Remodeling and Aggregation in Aging C. elegans
Dirk Walther, Prasad Kasturi, Min Zheng, et al.
Cell (2015) Vol. 161, Iss. 4, pp. 919-932
Open Access | Times Cited: 546
Drug self-delivery systems for cancer therapy
Si‐Yong Qin, Aiqing Zhang, Si‐Xue Cheng, et al.
Biomaterials (2016) Vol. 112, pp. 234-247
Closed Access | Times Cited: 495
Half a century of amyloids: past, present and future
Pu Chun Ke, Ruhong Zhou, Louise C. Serpell, et al.
Chemical Society Reviews (2020) Vol. 49, Iss. 15, pp. 5473-5509
Open Access | Times Cited: 476
Update on Alzheimer's Disease Therapy and Prevention Strategies
W. Vallen Graham, Alessandra Bonito‐Oliva, Thomas P. Sakmar
Annual Review of Medicine (2017) Vol. 68, Iss. 1, pp. 413-430
Open Access | Times Cited: 463
The activities of amyloids from a structural perspective
Roland Riek, David Eisenberg
Nature (2016) Vol. 539, Iss. 7628, pp. 227-235
Closed Access | Times Cited: 453
Structure, Dynamics, Assembly, and Evolution of Protein Complexes
Joseph A. Marsh, Sarah A. Teichmann
Annual Review of Biochemistry (2014) Vol. 84, Iss. 1, pp. 551-575
Closed Access | Times Cited: 435
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation
Serene W. Chen, Srdja Drakulić, Emma Deas, et al.
Proceedings of the National Academy of Sciences (2015) Vol. 112, Iss. 16
Open Access | Times Cited: 433
Secondary nucleation in amyloid formation
Mattias Törnquist, Thomas C. T. Michaels, Kalyani Sanagavarapu, et al.
Chemical Communications (2018) Vol. 54, Iss. 63, pp. 8667-8684
Open Access | Times Cited: 411
Serum amyloid A – a review
George H. Sack
Molecular Medicine (2018) Vol. 24, Iss. 1
Open Access | Times Cited: 410
Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy
Yaowang Li, Chunyu Zhao, Feng Luo, et al.
Cell Research (2018) Vol. 28, Iss. 9, pp. 897-903
Open Access | Times Cited: 395
Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo
Sarah K. Kaufman, David W. Sanders, Talitha L. Thomas, et al.
Neuron (2016) Vol. 92, Iss. 4, pp. 796-812
Open Access | Times Cited: 393
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