OpenAlex Citation Counts

OpenAlex Citations Logo

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:

A closer look at amyloid ligands, and what they tell us about protein aggregates
Timothy S. Chisholm, Christopher A. Hunter
Chemical Society Reviews (2023) Vol. 53, Iss. 3, pp. 1354-1374
Open Access | Times Cited: 13

Showing 13 citing articles:

Automated microscopic measurement of fibrinaloid microclots and their degradation by nattokinase, the main natto protease
Justine M. Grixti, Chrispian W. Theron, J. Enrique Salcedo-Sora, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 6

Chemical Synthesis Reveals Pathogenic Role of N-Glycosylation in Microtubule-Associated Protein Tau
Wyatt C. Powell, Ruiheng Jing, Morgane Herlory, et al.
Journal of the American Chemical Society (2025)
Closed Access

Luminescent iridium(iii)–peptide bioconjugates for bioanalytical and biomedical applications
Shaozhen Jing, Xiaolei Wu, Daniel Shiu‐Hin Chan, et al.
Inorganic Chemistry Frontiers (2024) Vol. 11, Iss. 12, pp. 3400-3417
Closed Access | Times Cited: 3

Thioflavin T─a Reporter of Microviscosity in Protein Aggregation Process: The Study Case of α-Synuclein
Konstantin Rusakov, Aadil El-Turabi, Lasse Reimer, et al.
The Journal of Physical Chemistry Letters (2024) Vol. 15, Iss. 25, pp. 6685-6690
Open Access | Times Cited: 3

Methods for high throughput discovery of fluoroprobes that recognize tau fibril polymorphs
Emma C. Carroll, Hyunjun Yang, Julia P. G. Jones, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 3

Nickel catalyzed C-N coupling of haloarenes with B2N4 reagents
Qianqian Chang, Qini Li, Yi-Hui Deng, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access

Ligands for Protein Fibrils of Amyloid-β, α-Synuclein, and Tau
Timothy S. Chisholm, Christopher A. Hunter
Chemical Reviews (2025)
Open Access

Proteomic evidence for amyloidogenic cross-seeding in fibrinaloid microclots
Douglas B. Kell, Etheresia Pretorius
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access | Times Cited: 2

Ligand Profiling as a Diagnostic Tool to Differentiate Patient-Derived α-Synuclein Polymorphs
Timothy S. Chisholm, Ronald Melki, Christopher A. Hunter
ACS Chemical Neuroscience (2024) Vol. 15, Iss. 10, pp. 2080-2088
Open Access | Times Cited: 1

Archimedean heterologous helixes in Ti10Cd6-oxo nanoclusters: double-helical self-assembly and therapeutic application in Parkinson's disease
Ling-Cui Meng, Junyi Chen, Feng Zhiming, et al.
Inorganic Chemistry Frontiers (2024) Vol. 11, Iss. 12, pp. 3527-3537
Closed Access | Times Cited: 1

Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots
Douglas B. Kell, Etheresia Pretorius
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 19, pp. 10809-10809
Open Access | Times Cited: 1

The clots removed from ischaemic stroke patients by mechanical thrombectomy are amyloid in nature
Justine M. Grixti, Arun Chandran, Johann Pretorius, et al.
medRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Metabolic Perturbations associated with hIAPP-induced insulin resistance in Skeletal Muscles: Implications to the Development of Type 2 Diabetes
Arya R. Naik, Shreyada N. Save, Soumya Swaroop Sahoo, et al.
The International Journal of Biochemistry & Cell Biology (2024), pp. 106665-106665
Closed Access

Page 1

Scroll to top