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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:

Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage
Sonia Ciudad, Eduard Puig, Thomas Botzanowski, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 202

Showing 26-50 of 202 citing articles:

Internalisation and toxicity of amyloid‐β 1‐42 are influenced by its conformation and assembly state rather than size
Devkee M. Vadukul, Mahmoud Bukar Maina, Hannah Franklin, et al.
FEBS Letters (2020) Vol. 594, Iss. 21, pp. 3490-3503
Open Access | Times Cited: 40
Quantification of N-terminal amyloid-β isoforms reveals isomers are the most abundant form of the amyloid-β peptide in sporadic Alzheimer’s disease
Soumya Mukherjee, Keyla Perez, Larissa Lago, et al.
Brain Communications (2021) Vol. 3, Iss. 2
Open Access | Times Cited: 35
Ultrasmall Molybdenum Disulfide Quantum Dots Cage Alzheimer’s Amyloid Beta to Restore Membrane Fluidity
Yuhuan Li, Huayuan Tang, Houjuan Zhu, et al.
ACS Applied Materials & Interfaces (2021) Vol. 13, Iss. 25, pp. 29936-29948
Open Access | Times Cited: 34
A unifying framework for amyloid-mediated membrane damage: The lipid-chaperone hypothesis
Carmelo Tempra, Federica Scollo, Martina Pannuzzo, et al.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2022) Vol. 1870, Iss. 4, pp. 140767-140767
Open Access | Times Cited: 24
Thermodynamic analysis of amyloid fibril structures reveals a common framework for stability in amyloid polymorphs
Rob van der Kant, Nikolaos Louros, Joost Schymkowitz, et al.
Structure (2022) Vol. 30, Iss. 8, pp. 1178-1189.e3
Open Access | Times Cited: 24
Flanking regions, amyloid cores, and polymorphism: the potential interplay underlying structural diversity
Anukool A. Bhopatkar, Rakez Kayed
Journal of Biological Chemistry (2023) Vol. 299, Iss. 9, pp. 105122-105122
Open Access | Times Cited: 16
Protein Oligomer Engineering: A New Frontier for Studying Protein Structure, Function, and Toxicity
Chang Liu, Jinghui Luo
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 23
Open Access | Times Cited: 15
In Vivo Near-Infrared Fluorescence Imaging Selective for Soluble Amyloid β Aggregates Using y-Shaped BODIPY Derivative
Takahiro Akasaka, Hiroyuki Watanabe, Masahiro Ono
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 20, pp. 14029-14046
Closed Access | Times Cited: 14
A Peptide‐Polyphenol Coated Polypyrrole Nanoparticle for Synergetic Attenuation of Aggregation and Cytotoxicity of Amyloid‐β Fibrils
Zhuo Zhang, Mingchen Lv, Yaping Liu, et al.
Advanced Functional Materials (2024) Vol. 34, Iss. 36
Closed Access | Times Cited: 5
TRIM21-dependent ultrasmall chiral gold nanoparticles for preventing microglia senescence against Alzheimer’s disease
Meiru Lu, Changlong Hao, Liguang Xu, et al.
Science China Chemistry (2024) Vol. 67, Iss. 4, pp. 1360-1372
Closed Access | Times Cited: 5
Amyloid-independent pathogenesis for Alzheimer’s disease: implications for drug design
Michael S. Wolfe
Medicinal Chemistry Research (2024) Vol. 33, Iss. 8, pp. 1330-1338
Closed Access | Times Cited: 5
Secondary structure determines electron transport in peptides
Rajarshi Samajdar, Moeen Meigooni, Hao Yang, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 32
Open Access | Times Cited: 5
Physical mechanisms of amyloid nucleation on fluid membranes
Johannes Krausser, Tuomas P. J. Knowles, Anđela Šarić
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 52, pp. 33090-33098
Open Access | Times Cited: 39
Pushing the limits of native MS: Online SEC-native MS for structural biology applications
Evolène Deslignière, Marie Ley, Maxime Bourguet, et al.
International Journal of Mass Spectrometry (2020) Vol. 461, pp. 116502-116502
Open Access | Times Cited: 39
Strategies for the Molecular Imaging of Amyloid and the Value of a Multimodal Approach
Amandeep Kaur, Elizabeth J. New, Margaret Sunde
ACS Sensors (2020) Vol. 5, Iss. 8, pp. 2268-2282
Closed Access | Times Cited: 36
Amentoflavone: A Bifunctional Metal Chelator that Controls the Formation of Neurotoxic Soluble Aβ42 Oligomers
Liang Sun, Anuj K. Sharma, Byung-Hee Han, et al.
ACS Chemical Neuroscience (2020) Vol. 11, Iss. 17, pp. 2741-2752
Open Access | Times Cited: 33
Structural details of amyloid β oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy
Anna König, Nadine S. Rösener, Lothar Gremer, et al.
Journal of Biological Chemistry (2021) Vol. 296, pp. 100499-100499
Open Access | Times Cited: 32
Interactions of Amyloid-β with Membrane Proteins
Benita Wiatrak, Janusz Piasny, Amadeusz Kuźniarski, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 11, pp. 6075-6075
Open Access | Times Cited: 32
Distinct types of amyloid‐β oligomers displaying diverse neurotoxicity mechanisms in Alzheimer's disease
Priyanka Madhu, Samrat Mukhopadhyay
Journal of Cellular Biochemistry (2021) Vol. 122, Iss. 11, pp. 1594-1608
Closed Access | Times Cited: 31
Exploring amyloid oligomers with peptide model systems
Tuan D. Samdin, Adam G. Kreutzer, James S. Nowick
Current Opinion in Chemical Biology (2021) Vol. 64, pp. 106-115
Open Access | Times Cited: 29
Amyloid Prefibrillar Oligomers: The Surprising Commonalities in Their Structure and Activity
Marco Diociaiuti, Roberto Bonanni, Ida Cariati, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 12, pp. 6435-6435
Open Access | Times Cited: 28
Molecular dynamics simulations reveal the importance of amyloid-beta oligomer β-sheet edge conformations in membrane permeabilization
Dirk Matthes, Bert L. de Groot
Journal of Biological Chemistry (2023) Vol. 299, Iss. 4, pp. 103034-103034
Open Access | Times Cited: 13
Understanding the Molecular Mechanisms of Polyphenol Inhibition of Amyloid β Aggregation
Yin-Lei Han, Huanhuan Yin, Xiao Chao, et al.
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 22, pp. 4051-4061
Closed Access | Times Cited: 13
Parthenolide alleviates cognitive dysfunction and neurotoxicity via regulation of AMPK/GSK3β(Ser9)/Nrf2 signaling pathway
Jinfeng Sun, Liwei Li, Xiong Li, et al.
Biomedicine & Pharmacotherapy (2023) Vol. 169, pp. 115909-115909
Open Access | Times Cited: 12
Probing differences among Aβ oligomers with two triangular trimers derived from Aβ
Adam G. Kreutzer, Gretchen Guaglianone, Stan Yoo, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 22
Open Access | Times Cited: 11

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