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:

Structural Dynamics of Amyloid-β Protofibrils and Actions of Anti-Amyloid-β Antibodies as Observed by High-Speed Atomic Force Microscopy
Takahiro Watanabe‐Nakayama, Mayumi Tsuji, Kenichi Umeda, et al.
Nano Letters (2023) Vol. 23, Iss. 13, pp. 6259-6268
Closed Access | Times Cited: 12

Showing 12 citing articles:

Lecanemab‐Associated Amyloid‐β Protofibril in Cerebrospinal Fluid Correlates with Biomarkers of Neurodegeneration in Alzheimer's Disease
Moeko Noguchi‐Shinohara, Kazuyoshi Shuta, Hidetomo Murakami, et al.
Annals of Neurology (2025) Vol. 97, Iss. 5, pp. 993-1006
Open Access | Times Cited: 1

The Mechanisms of the Roles of α-Synuclein, Amyloid-β, and Tau Protein in the Lewy Body Diseases: Pathogenesis, Early Detection, and Therapeutics
Moeko Noguchi‐Shinohara, Kenjiro Ono
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 12, pp. 10215-10215
Open Access | Times Cited: 11

ALZ‐801 prevents amyloid β‐protein assembly and reduces cytotoxicity: A preclinical experimental study
Daiki Muramatsu, Takahiro Watanabe‐Nakayama, Mayumi Tsuji, et al.
The FASEB Journal (2025) Vol. 39, Iss. 3
Open Access

Nano-Scale Video Imaging of Motility Machinery by High-Speed Atomic Force Microscopy
Steven John McArthur, Kenichi Umeda, Noriyuki Kodera
Biomolecules (2025) Vol. 15, Iss. 2, pp. 257-257
Open Access

Lecanemab preferentially binds to smaller aggregates present at early Alzheimer's disease
Emre Fertan, Jeff Y. L. Lam, Giulia Albertini, et al.
Alzheimer s & Dementia (2025) Vol. 21, Iss. 4
Open Access

The basis of anti-Aβ antibody therapy: The toxicity of Aβ aggregates and the mechanism of action of anti-Aβ antibodies
Kenjiro Ono, Moeko Noguchi‐Shinohara, Takahiro Watanabe‐Nakayama
Internal Medicine (2024)
Open Access | Times Cited: 2

Direct observation of secondary nucleation in huntingtin amyloid formation by High-Speed Atomic Force Microscopy
Chris van Ewijk, Gaurav Jain, Yari Katar Knelissen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2

Neuroprotective Potential of Raloxifene via G-Protein-Coupled Estrogen Receptors in Aβ-Oligomer-Induced Neuronal Injury
Tetsuhito Nohara, Mayumi Tsuji, Tatsunori Oguchi, et al.
Biomedicines (2023) Vol. 11, Iss. 8, pp. 2135-2135
Open Access | Times Cited: 5

Distinct Effects of Aducanumab and Lecanemab on Intraneuronal Endogenous Aβ42 and Phosphorylated Tau in Alzheimer’s Disease Treatment
Mingjie Liu, Long Zhu, Fuyun Li, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Molecular Dynamics Mappings of the CCT/TRiC Complex-Mediated Protein Folding Cycle Using Diffracted X-ray Tracking
Kazutaka Araki, Takahiro Watanabe‐Nakayama, Daisuke Sasaki, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 19, pp. 14850-14850
Open Access | Times Cited: 2

Globular-shaped Aβ oligomers have diverse mechanisms for promoting Aβ aggregations with the facilitation of fibril elongation
Hiroto Nakano, Sadao Hikishima, Makoto Mori, et al.
Neurobiology of Disease (2024), pp. 106775-106775
Open Access

Synthesis of Symmetrical and Unsymmetrical Tetrahydroxybiphenyls and their Evaluation as Amyloid-β Aggregation Inhibitors
Sarah L. Wicks, Jake A. Roberts, Matthew J. Hurtt, et al.
Letters in Organic Chemistry (2024) Vol. 21, Iss. 11, pp. 964-972
Closed Access

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