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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:

Cryo-EM of amyloid fibrils and cellular aggregates
Anthony Fitzpatrick, Helen R. Saibil
Current Opinion in Structural Biology (2019) Vol. 58, pp. 34-42
Open Access | Times Cited: 126

Showing 1-25 of 126 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: 546
Phase Separation and Neurodegenerative Diseases: A Disturbance in the Force
Aurélie Zbinden, Manuela Pérez‐Berlanga, Pierre De Rossi, et al.
Developmental Cell (2020) Vol. 55, Iss. 1, pp. 45-68
Open Access | Times Cited: 384
Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains
Tamta Arakhamia, Christina E. Lee, Yari Carlomagno, et al.
Cell (2020) Vol. 180, Iss. 4, pp. 633-644.e12
Open Access | Times Cited: 348
Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation
Carolina Alquézar, Shruti Arya, Aimee W. Kao
Frontiers in Neurology (2021) Vol. 11
Open Access | Times Cited: 247
A central role for amyloid fibrin microclots in long COVID/PASC: origins and therapeutic implications
Douglas B. Kell, Gert Jacobus Laubscher, Etheresia Pretorius
Biochemical Journal (2022) Vol. 479, Iss. 4, pp. 537-559
Open Access | Times Cited: 216
Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods
María Florencia Pignataro, María Georgina Herrera, Verónica I. Dodero
Molecules (2020) Vol. 25, Iss. 20, pp. 4854-4854
Open Access | Times Cited: 160
Parkinson’s disease-related phosphorylation at Tyr39 rearranges α-synuclein amyloid fibril structure revealed by cryo-EM
Kun Zhao, Yeh‐Jun Lim, Zhenying Liu, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 33, pp. 20305-20315
Open Access | Times Cited: 155
Extracellular protein components of amyloid plaques and their roles in Alzheimer’s disease pathology
M. Mahafuzur Rahman, Christofer Lendel
Molecular Neurodegeneration (2021) Vol. 16, Iss. 1
Open Access | Times Cited: 154
Protein fibrils from different food sources: A review of fibrillation conditions, properties, applications and research trends
Meng Yuan, Zihao Wei, Changhu Xue
Trends in Food Science & Technology (2022) Vol. 121, pp. 59-75
Closed Access | Times Cited: 124
Homotypic fibrillization of TMEM106B across diverse neurodegenerative diseases
Andrew Chang, Xinyu Xiang, Jing Wang, et al.
Cell (2022) Vol. 185, Iss. 8, pp. 1346-1355.e15
Open Access | Times Cited: 111
2.7 Å cryo-EM structure of ex vivo RML prion fibrils
Szymon W. Manka, Wenjuan Zhang, Adam Wenborn, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 108
Recent advances of interfacial and rheological property based techno-functionality of food protein amyloid fibrils
Jianxiong Yue, Xiaolin Yao, Qingxia Gou, et al.
Food Hydrocolloids (2022) Vol. 132, pp. 107827-107827
Closed Access | Times Cited: 72
An overview on glycation: molecular mechanisms, impact on proteins, pathogenesis, and inhibition
Ana Belén Uceda, Laura Mariño, Rodrigo Casasnovas, et al.
Biophysical Reviews (2024) Vol. 16, Iss. 2, pp. 189-218
Open Access | Times Cited: 23
Parkinson’s disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure
Kun Zhao, Yaowang Li, Zhenying Liu, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 114
Guidelines for Regulated Cell Death Assays: A Systematic Summary, A Categorical Comparison, A Prospective
Xi‐min Hu, Zhixin Li, Ruihan Lin, et al.
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 96
Looking Beyond the Core: The Role of Flanking Regions in the Aggregation of Amyloidogenic Peptides and Proteins
Sabine M. Ulamec, David J. Brockwell, Sheena E. Radford
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 92
Antibody semorinemab reduces tau pathology in a transgenic mouse model and engages tau in patients with Alzheimer’s disease
Gai Ayalon, Seung-Hye Lee, Oskar Adolfsson, et al.
Science Translational Medicine (2021) Vol. 13, Iss. 593
Closed Access | Times Cited: 82
Hierarchical chemical determination of amyloid polymorphs in neurodegenerative disease
Dan Li, Cong Liu
Nature Chemical Biology (2021) Vol. 17, Iss. 3, pp. 237-245
Closed Access | Times Cited: 81
Biomolecular and Biological Applications of Solid-State NMR with Dynamic Nuclear Polarization Enhancement
Wing Ying Chow, Gaël De Paëpe, Sabine Hediger
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9795-9847
Open Access | Times Cited: 65
De novo designed protein inhibitors of amyloid aggregation and seeding
Kevin A. Murray, Carolyn J. Hu, Sarah L. Griner, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 34
Open Access | Times Cited: 52
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: 41
Protein amyloid aggregate: Structure and function
Qianhui Xu, Yeyang Ma, Yunpeng Sun, et al.
Aggregate (2023) Vol. 4, Iss. 4
Open Access | Times Cited: 30
Research progress of protein fibrils: A review of formation mechanism, characterization and applications in the food field
Yixin Zhang, Xiaohui Lv, Adil M. Abker, et al.
Food Hydrocolloids (2024) Vol. 155, pp. 110199-110199
Closed Access | Times Cited: 16
Probing protein aggregation through spectroscopic insights and multimodal approaches: A comprehensive review for counteracting neurodegenerative disorders
Sania Bashir, Ayesha Aiman, Anis Ahmad Chaudhary, et al.
Heliyon (2024) Vol. 10, Iss. 7, pp. e27949-e27949
Open Access | Times Cited: 10
A brief history of amyloid aggregation simulations
Hebah Fatafta, Mohammed Khaled, Batuhan Kav, et al.
Wiley Interdisciplinary Reviews Computational Molecular Science (2024) Vol. 14, Iss. 1
Closed Access | Times Cited: 9
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