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 1-25 of 202 citing articles:

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis
Phuong H. Nguyen, Ayyalusamy Ramamoorthy, Bikash R. Sahoo, et al.
Chemical Reviews (2021) Vol. 121, Iss. 4, pp. 2545-2647
Open Access | Times Cited: 545

Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids
Dieter Willbold, Birgit Strodel, Gunnar F. Schröder, et al.
Chemical Reviews (2021) Vol. 121, Iss. 13, pp. 8285-8307
Open Access | Times Cited: 154

A guide to studying protein aggregation
Joëlle A.J. Housmans, Guiqin Wu, Joost Schymkowitz, et al.
FEBS Journal (2021) Vol. 290, Iss. 3, pp. 554-583
Open Access | Times Cited: 129

Aβ-oligomers: A potential therapeutic target for Alzheimer's disease
Sudeshna Ghosh, Rafat Ali, Sandeep Verma
International Journal of Biological Macromolecules (2023) Vol. 239, pp. 124231-124231
Closed Access | Times Cited: 44

Lipidic folding pathway of α-Synuclein via a toxic oligomer
Vrinda Sant, Dirk Matthes, Hisham Mazal, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 2

Visualizing and trapping transient oligomers in amyloid assembly pathways
Emma E. Cawood, Theodoros K. Karamanos, Andrew J. Wilson, et al.
Biophysical Chemistry (2020) Vol. 268, pp. 106505-106505
Open Access | Times Cited: 116

Natural Compounds as Inhibitors of Aβ Peptide Aggregation: Chemical Requirements and Molecular Mechanisms
Katiuscia Pagano, Simona Tomaselli, Henriette Molinari, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 93

The role of surfaces on amyloid formation
Fulvio Grigolato, Paolo Arosio
Biophysical Chemistry (2021) Vol. 270, pp. 106533-106533
Open Access | Times Cited: 71

Amphiphilic Distyrylbenzene Derivatives as Potential Therapeutic and Imaging Agents for Soluble and Insoluble Amyloid β Aggregates in Alzheimer’s Disease
Liang Sun, Hong-Jun Cho, Soumyo Sen, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 27, pp. 10462-10476
Open Access | Times Cited: 69

Cholesterol as a key player in amyloid β-mediated toxicity in Alzheimer’s disease
Vladimı́r Rudajev, Jiřı́ Novotný
Frontiers in Molecular Neuroscience (2022) Vol. 15
Open Access | Times Cited: 50

Studying protein structure and function by native separation–mass spectrometry
Guusje van Schaick, Rob Haselberg, Govert W. Somsen, et al.
Nature Reviews Chemistry (2022) Vol. 6, Iss. 3, pp. 215-231
Open Access | Times Cited: 47

Imaging Amyloid‐β Membrane Interactions: Ion‐Channel Pores and Lipid‐Bilayer Permeability in Alzheimer's Disease
John H. Viles
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 25
Open Access | Times Cited: 40

A Hairpin Motif in the Amyloid-β Peptide Is Important for Formation of Disease-Related Oligomers
Mohammed Khaled, Isabel Rönnbäck, Leopold L. Ilag, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 33, pp. 18340-18354
Open Access | Times Cited: 36

Evidence that Alzheimer’s Disease Is a Disease of Competitive Synaptic Plasticity Gone Awry
Zhen Huang
Journal of Alzheimer s Disease (2024) Vol. 99, Iss. 2, pp. 447-470
Open Access | Times Cited: 15

A NIR iridium(III) complex-based reversible probe for assessing AD progression and screening anti-AD drugs through visualization of the “Cu2+-H2S seesaw” phenomenon in Alzheimer’s disease
Chaolong Liu, Meichun Qin, Shouheng Xu, et al.
Sensors and Actuators B Chemical (2024) Vol. 407, pp. 135509-135509
Closed Access | Times Cited: 10

Neuroprotective Effects of Catechins by Differentially Affecting the Binding of Beta-amyloid and Its Aggregates to the Target Cells
He Li, Changxin Zheng, Zhenxing Wang, et al.
Molecular Neurobiology (2025)
Closed Access | Times Cited: 1

Cryo‐electron Microscopy Imaging of Alzheimer's Amyloid‐beta 42 Oligomer Displayed on a Functionally and Structurally Relevant Scaffold
Jinming Wu, Thorsten B. Blum, Daniel P. Farrell, et al.
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 34, pp. 18680-18687
Open Access | Times Cited: 51

3D-visualization of amyloid-β oligomer interactions with lipid membranes by cryo-electron tomography
Yao Tian, Ruina Liang, Amit Kumar, et al.
Chemical Science (2021) Vol. 12, Iss. 20, pp. 6896-6907
Open Access | Times Cited: 42

Structural basis of FPR2 in recognition of Aβ42 and neuroprotection by humanin
Ya Zhu, Xiaowen Lin, Xin Zong, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 37

Zinc–Epigallocatechin-3-gallate Network-Coated Nanocomposites against the Pathogenesis of Amyloid-Beta
Nikolaos K. Andrikopoulos, Yuhuan Li, Aparna Nandakumar, et al.
ACS Applied Materials & Interfaces (2023) Vol. 15, Iss. 6, pp. 7777-7792
Open Access | Times Cited: 20

Effect of the Lipid Landscape on the Efficacy of Cell-Penetrating Peptides
Florina Zákány, István M. Mándity, Zoltán Varga, et al.
Cells (2023) Vol. 12, Iss. 13, pp. 1700-1700
Open Access | Times Cited: 19

The structure of tyrosine-10 favors ionic conductance of Alzheimer’s disease-associated full-length amyloid-β channels
Abhijith G. Karkisaval, Rowan Hassan, Andrew Nguyen, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 8

Lipids shape brain function through ion channel and receptor modulations: physiological mechanisms and clinical perspectives
Salvatore Incontro, Maria Laura Musella, Malika Sammari, et al.
Physiological Reviews (2024) Vol. 105, Iss. 1, pp. 137-207
Closed Access | Times Cited: 7

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