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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:

N-Terminal Modified Aβ Variants Enable Modulations to the Structures and Cytotoxicity Levels of Wild-Type Aβ Fibrils through Cross-Seeding
Zhiwen Hu, Dan Fai Au, Letticia Cruceta, et al.
ACS Chemical Neuroscience (2020) Vol. 11, Iss. 14, pp. 2058-2065
Open Access | Times Cited: 11

Showing 11 citing articles:

Pyroglutamate Aβ cascade as drug target in Alzheimer’s disease
Thomas A. Bayer
Molecular Psychiatry (2021) Vol. 27, Iss. 4, pp. 1880-1885
Open Access | Times Cited: 57
Early stage β-amyloid-membrane interactions modulate lipid dynamics and influence structural interfaces and fibrillation
June M. Kenyaga, Qinghui Cheng, Wei Qiang
Journal of Biological Chemistry (2022) Vol. 298, Iss. 10, pp. 102491-102491
Open Access | Times Cited: 22
Insights into Cerebral Amyloid Angiopathy Type 1 and Type 2 from Comparisons of the Fibrillar Assembly and Stability of the Aβ40-Iowa and Aβ40-Dutch Peptides
Jitika Rajpoot, Elliot J. Crooks, Brandon A. Irizarry, et al.
Biochemistry (2022) Vol. 61, Iss. 12, pp. 1181-1198
Open Access | Times Cited: 16
In-cell 31P solid-state NMR measurements of the lipid dynamics and influence of exogeneous β-amyloid peptides on live neuroblastoma neuro-2a cells
June M. Kenyaga, Sarah A. Oteino, Yan Sun, et al.
Biophysical Chemistry (2023) Vol. 297, pp. 107008-107008
Open Access | Times Cited: 7
The Hidden Role of Non-Canonical Amyloid β Isoforms in Alzheimer’s Disease
Lukas Busch, Simone Eggert, Kristina Endres, et al.
Cells (2022) Vol. 11, Iss. 21, pp. 3421-3421
Open Access | Times Cited: 10
Effect of Cross-Seeding of Wild-Type Amyloid-β1–40 Peptides with Post-translationally Modified Fibrils on Internal Dynamics of the Fibrils Using Deuterium Solid-State NMR
Aryana Rodgers, Matthew Sawaged, Dmitry Ostrovsky, et al.
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 13, pp. 2887-2899
Closed Access | Times Cited: 5
Modulation of aggregation and structural polymorphisms of β-amyloid fibrils in cellular environments by pyroglutamate-3 variant cross-seeding
Letticia Cruceta, Yan Sun, June M. Kenyaga, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 10, pp. 105196-105196
Open Access | Times Cited: 4
How Single Site Mutations Can Help Understanding Structure Formation of Amyloid β1−40
Benedikt Schwarze, Daniel Huster
Macromolecular Bioscience (2023) Vol. 23, Iss. 5
Open Access | Times Cited: 3
Modulation of the Activity of the Insulin-Degrading Enzyme by Aβ Peptides
Merc M. Kemeh, Noel D. Lazo
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 16, pp. 2935-2943
Closed Access | Times Cited: 2
The Features of Beta-Amyloid Phosphorylation in Alzheimer’s Disease
Polina A. Strelnikova, А. Е. Бугрова, Natalia V. Zakharova, et al.
Acta Naturae (2024) Vol. 16, Iss. 3, pp. 93-101
Open Access
Comparative Hydrophobic Core Dynamics Between Wild‐Type Amyloid‐β Fibrils, Glutamate‐3 Truncation, and Serine‐8 Phosphorylation
Liliya Vugmeyster, Dan Fai Au, Matthew C. Smith, et al.
ChemPhysChem (2021) Vol. 23, Iss. 3
Open Access | Times Cited: 3
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