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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:

Amyloid formation as a protein phase transition
Thomas C. T. Michaels, Daoyuan Qian, Anđela Šarić, et al.
Nature Reviews Physics (2023) Vol. 5, Iss. 7, pp. 379-397
Closed Access | Times Cited: 81

Showing 1-25 of 81 citing articles:

Protein-based bioactive coatings: from nanoarchitectonics to applications
Chengyu Fu, Zhengge Wang, Xingyu Zhou, et al.
Chemical Society Reviews (2024) Vol. 53, Iss. 3, pp. 1514-1551
Closed Access | Times Cited: 24
Protein misfolding and amyloid nucleation through liquid–liquid phase separation
S. Mukherjee, Manisha Poudyal, K. Dave, et al.
Chemical Society Reviews (2024) Vol. 53, Iss. 10, pp. 4976-5013
Closed Access | Times Cited: 24
Self‐Assembled Nanocarrier Delivery Systems for Bioactive Compounds
Yafei Zhang, Yuning Zhang, Rui Ding, et al.
Small (2024) Vol. 20, Iss. 26
Closed Access | Times Cited: 17
RNA modulates hnRNPA1A amyloid formation mediated by biomolecular condensates
Chiara Morelli, Lenka Faltova, Umberto Capasso Palmiero, et al.
Nature Chemistry (2024) Vol. 16, Iss. 7, pp. 1052-1061
Open Access | Times Cited: 14
Supersaturation, a Critical Factor Underlying Proteostasis of Amyloid Fibril Formation
Yuji Goto, Kichitaro Nakajima, Suguru Yamamoto, et al.
Journal of Molecular Biology (2024) Vol. 436, Iss. 14, pp. 168475-168475
Closed Access | Times Cited: 11
Metastable condensates suppress conversion to amyloid fibrils
Tapojyoti Das, Fatima Zaidi, Mina Farag, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 10
Peristaltic pump-triggered amyloid formation suggests shear stresses are in vivo risks for amyloid nucleation
Yuji Goto, Tomoki Ota, Wenlou Yuan, et al.
Deleted Journal (2025) Vol. 2, Iss. 1
Open Access | Times Cited: 1
Binary peptide coacervates as an active model for biomolecular condensates
Shoupeng Cao, Peng Zhou, Guizhi Shen, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
Pathologic polyglutamine aggregation begins with a self-poisoning polymer crystal
Tej Kandola, Shriram Venkatesan, Jiahui Zhang, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 16
Tau forms synaptic nano-biomolecular condensates controlling the dynamic clustering of recycling synaptic vesicles
Shanley F. Longfield, Mahdie Mollazade, Tristan P. Wallis, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 16
Fibrinaloid Microclots and Atrial Fibrillation
Douglas B. Kell, Gregory Y.H. Lip, Etheresia Pretorius
Biomedicines (2024) Vol. 12, Iss. 4, pp. 891-891
Open Access | Times Cited: 5
Adsorption mechanism of soy protein amyloid fibrils with different morphological structures at the interface of oil-in-water emulsion
Jingwen Zhao, Baoyue Chang, Yigang Hu, et al.
Food Hydrocolloids (2024), pp. 110899-110899
Closed Access | Times Cited: 5
Fibrinaloid Microclots and Atrial Fibrillation
Douglas B. Kell, Gregory Y.H. Lip, Etheresia Pretorius
(2024)
Open Access | Times Cited: 4
Invited review: Modeling milk stability
Carl Holt, John A. Carver
Journal of Dairy Science (2024) Vol. 107, Iss. 8, pp. 5259-5279
Open Access | Times Cited: 4
Molecular mechanism of α-synuclein aggregation on lipid membranes revealed
Alexander J. Dear, Xiangyu Teng, Sarah R. Ball, et al.
Chemical Science (2024) Vol. 15, Iss. 19, pp. 7229-7242
Open Access | Times Cited: 4
Biomolecular condensates and disease pathogenesis
Ke Ruan, Ge Bai, Yanshan Fang, et al.
Science China Life Sciences (2024) Vol. 67, Iss. 9, pp. 1792-1832
Closed Access | Times Cited: 4
On the reversibility of amyloid fibril formation
Tinna Pálmadóttir, Josef Getachew, Lei Ortigosa-Pascual, et al.
Biophysics Reviews (2025) Vol. 6, Iss. 1
Open Access
Mechanism of amyloid fibril formation triggered by breakdown of supersaturation
Keiichi Yamaguchi, Kichitaro Nakajima, Hirotsugu Ogi, et al.
Deleted Journal (2025) Vol. 2, Iss. 1
Open Access
Effects of Sup35 overexpression on the formation, morphology, and physiological functions of intracellular Sup35 assemblies
Jianhui Feng, Ekaterina Osmekhina, Jaakko V. I. Timonen, et al.
Applied and Environmental Microbiology (2025)
Open Access
Decoding biomolecular condensate dynamics: an energy landscape approach
Subhadip Biswas, Davit A. Potoyan
PLoS Computational Biology (2025) Vol. 21, Iss. 2, pp. e1012826-e1012826
Open Access
Time‐resolved Photoluminescence Determined the Dynamic Self‐Assembly for the Interactions Between Nanofibers and Proteins
Ruijia Zhang, Hanlin Xu, Chao Ren, et al.
Small (2025) Vol. 21, Iss. 11
Closed Access
Thiocyanate Ion (SCN–) Offers a Major Impact in Rapid Protein Amyloidosis: A Salient Role Played by Protein Solvation
Ria Saha, Indrani Bhattacharya, Sumana Pyne, et al.
The Journal of Physical Chemistry B (2025)
Closed Access
Zinc ions trigger the prion protein liquid-liquid phase separation.
Mariana Juliani do Amaral, Luís Guilherme de Oliveira, Yraima Cordeiro
Biochemical and Biophysical Research Communications (2025) Vol. 753, pp. 151489-151489
Closed Access
1000 fold Ultra‐Photosensitized Fluorescent Protein Mimics Toward Photocatalytic Proximity Labeling and Proteomic Profiling Functions
Rui Sun, Yanan Huang, Huan Feng, et al.
Advanced Science (2025)
Open Access
β-Lactoglobulin Forms a Conserved Fibril Core That Assembles into Diverse Fibril Polymorphs
Yongyi Xu, Danni Li, Yiling Zhang, et al.
Nano Letters (2025) Vol. 25, Iss. 9, pp. 3653-3661
Closed Access
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