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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:

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

Showing 1-25 of 92 citing articles:

Mechanisms and pathology of protein misfolding and aggregation
Nikolaos Louros, Joost Schymkowitz, Frédéric Rousseau
Nature Reviews Molecular Cell Biology (2023) Vol. 24, Iss. 12, pp. 912-933
Closed Access | Times Cited: 116
TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP
Diana Arseni, Renren Chen, Alexey G. Murzin, et al.
Nature (2023) Vol. 620, Iss. 7975, pp. 898-903
Open Access | Times Cited: 72
Transient interactions between the fuzzy coat and the cross-β core of brain-derived Aβ42 filaments
Maria Milanesi, Z. Faidon Brotzakis, Michele Vendruscolo
Science Advances (2025) Vol. 11, Iss. 3
Open Access | Times Cited: 2
Computational methods to predict protein aggregation
Susanna Navarro, Salvador Ventura
Current Opinion in Structural Biology (2022) Vol. 73, pp. 102343-102343
Open Access | Times Cited: 62
Functional amyloids from bacterial biofilms – structural properties and interaction partners
Ümit Akbey, Maria Andreasen
Chemical Science (2022) Vol. 13, Iss. 22, pp. 6457-6477
Open Access | Times Cited: 45
General Principles Underpinning Amyloid Structure
Taylor AIP, Rosemary A. Staniforth
Frontiers in Neuroscience (2022) Vol. 16
Open Access | Times Cited: 39
Structural evolution of fibril polymorphs during amyloid assembly
Martin Wilkinson, Yong Xu, Dev Thacker, et al.
Cell (2023) Vol. 186, Iss. 26, pp. 5798-5811.e26
Open Access | Times Cited: 37
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
Multifaceted interactions mediated by intrinsically disordered regions play key roles in alpha synuclein aggregation
Sagar D. Khare, Priscilla Chinchilla, Jean Baum
Current Opinion in Structural Biology (2023) Vol. 80, pp. 102579-102579
Open Access | Times Cited: 23
Structures of AT8 and PHF1 phosphomimetic tau: Insights into the posttranslational modification code of tau aggregation
Nadia El Mammeri, Aurelio J. Dregni, Pu Duan, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 10
Open Access | Times Cited: 13
Selective Detection of Intermediate-Amplitude Motion by Solid-State NMR
Pu Duan, Mei Hong
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 10, pp. 2293-2303
Closed Access | Times Cited: 10
The folding and misfolding of multidomain proteins
Stefano Gianni, Maurizio Brunori
Molecular Aspects of Medicine (2025) Vol. 101, pp. 101337-101337
Closed Access | Times Cited: 1
NMR unveils an N-terminal interaction interface on acetylated-α-synuclein monomers for recruitment to fibrils
Xue Yang, Baifan Wang, Cody L. Hoop, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 18
Open Access | Times Cited: 51
Single residue modulators of amyloid formation in the N-terminal P1-region of α-synuclein
Sabine M. Ulamec, Roberto Maya‐Martinez, Emily J. Byrd, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 37
How do protein aggregates escape quality control in neurodegeneration?
Margreet B. Koopman, Luca Ferrari, Stefan Rüdiger
Trends in Neurosciences (2022) Vol. 45, Iss. 4, pp. 257-271
Open Access | Times Cited: 33
Solid-state nuclear magnetic resonance in the structural study of polyglutamine aggregation
Patrick C.A. van der Wel
Biochemical Society Transactions (2024) Vol. 52, Iss. 2, pp. 719-731
Open Access | Times Cited: 8
Disease-relevant β2-microglobulin variants share a common amyloid fold
Martin Wilkinson, Rodrigo Gallardo, Roberto Maya‐Martinez, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 16
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
Architectonic principles of polyproline II helix bundle protein domains
Cristian Segura Rodríguez, Douglas V. Laurents
Archives of Biochemistry and Biophysics (2024) Vol. 756, pp. 109981-109981
Open Access | Times Cited: 6
Cleaved TMEM106B forms amyloid aggregates in central and peripheral nervous systems
Mehtap Bacioglu, Manuel Schweighauser, Derrick Gray, et al.
Acta Neuropathologica Communications (2024) Vol. 12, Iss. 1
Open Access | Times Cited: 6
Modulation of Alzheimer’s Disease Aβ40 Fibril Polymorphism by the Small Heat Shock Protein αB-Crystallin
Natalia P. Rodina, Simon Hornung, Riddhiman Sarkar, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 28, pp. 19077-19087
Open Access | Times Cited: 6
Determination of the Structure and Dynamics of the Fuzzy Coat of an Amyloid Fibril of IAPP Using Cryo-Electron Microscopy
Z. Faidon Brotzakis, Thomas Löhr, Steven Truong, et al.
Biochemistry (2023) Vol. 62, Iss. 16, pp. 2407-2416
Open Access | Times Cited: 12
In cell NMR reveals cells selectively amplify and structurally remodel amyloid fibrils
Shoyab Ansari, Dominique Lagasca, Rania Dumarieh, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Investigating the Sequence Determinants of the Curling of Amyloid Fibrils Using Ovalbumin as a Case Study
Joëlle A.J. Housmans, Bert Houben, Margarita Monge‐Morera, et al.
Biomacromolecules (2022) Vol. 23, Iss. 9, pp. 3779-3797
Open Access | Times Cited: 18
Amyloids in bladder cancer hijack cancer-related proteins and are positive correlated to tumor stage
Diego Alem, César X. García-Laviña, Francisco Garagorry, et al.
Scientific Reports (2025) Vol. 15, Iss. 1
Open Access
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