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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:

Amyloidogenicity, Cytotoxicity, and Receptor Activity of Bovine Amylin: Implications for Xenobiotic Transplantation and the Design of Nontoxic Amylin Variants
Rehana Akter, Rebekah L. Bower, Andisheh Abedini, et al.
ACS Chemical Biology (2018) Vol. 13, Iss. 9, pp. 2747-2757
Open Access | Times Cited: 19

Showing 19 citing articles:

Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes
Danilo Milardi, Ehud Gazit, Sheena E. Radford, et al.
Chemical Reviews (2021) Vol. 121, Iss. 3, pp. 1845-1893
Open Access | Times Cited: 163
The association of circulating amylin with β‐amyloid in familial Alzheimer's disease
Han Ly, Nirmal Verma, Savita Sharma, et al.
Alzheimer s & Dementia Translational Research & Clinical Interventions (2021) Vol. 7, Iss. 1
Open Access | Times Cited: 31
Decoding the Contribution of IAPP Amyloid Aggregation to Beta Cell Dysfunction: A Systematic Review and Epistemic Meta-Analysis of Type 1 Diabetes
Valeria Moya-Gudiño, Nelly Altamirano-Bustamante, M. Revilla, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 2, pp. 767-767
Open Access
Analysis of Baboon IAPP Provides Insight into Amyloidogenicity and Cytotoxicity of Human IAPP
Zachary Ridgway, Kyung-Hoon Lee, Alexander Zhyvoloup, et al.
Biophysical Journal (2020) Vol. 118, Iss. 5, pp. 1142-1151
Open Access | Times Cited: 20
Distinct Modes of Action of IAPP Oligomers on Membranes
Aliasghar Sepehri, Binod Nepal, Themis Lazaridis
Journal of Chemical Information and Modeling (2021) Vol. 61, Iss. 9, pp. 4645-4655
Open Access | Times Cited: 17
Amyloidogenicity of naturally occurring full‐length animal IAPP variants
Larry M. Palato, Shannon M Pilcher, Alissa Oakes, et al.
Journal of Peptide Science (2019) Vol. 25, Iss. 8
Open Access | Times Cited: 18
Analysis of Proline Substitutions Reveals the Plasticity and Sequence Sensitivity of Human IAPP Amyloidogenicity and Toxicity
Zachary Ridgway, Charles Eldrid, Alexander Zhyvoloup, et al.
Biochemistry (2020) Vol. 59, Iss. 6, pp. 742-754
Open Access | Times Cited: 13
Understanding the mechanism of amylin aggregation: From identifying crucial segments to tracing dominant sequential events to modeling potential aggregation suppressors
Ritama Ghosh, Shreyan Ghosh, Atanu Das
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2022) Vol. 1871, Iss. 1, pp. 140866-140866
Closed Access | Times Cited: 7
An environmentally sensitive molecular rotor as a NIR fluorescent probe for the detection of islet amyloid polypeptide
Pin‐Han Lin, Chang-Shun Tsai, Chia-Chien Hsu, et al.
Talanta (2022) Vol. 254, pp. 124130-124130
Closed Access | Times Cited: 7
Amyloidogenicity and cytotoxicity of des-Lys-1 human amylin provides insight into amylin self-assembly and highlights the difficulties of defining amyloidogenicity
Kyunghoon Lee, Alexander Zhyvoloup, Daniel P. Raleigh
Protein Engineering Design and Selection (2019) Vol. 32, Iss. 2, pp. 87-93
Open Access | Times Cited: 10
Analysis of Amylin Consensus Sequences Suggests That Human Amylin Is Not Optimized to Minimize Amyloid Formation and Provides Clues to Factors That Modulate Amyloidogenicity
Daeun Noh, Rebekah L. Bower, Debbie L. Hay, et al.
ACS Chemical Biology (2020) Vol. 15, Iss. 6, pp. 1408-1416
Open Access | Times Cited: 9
Contribution of the 12–17 hydrophobic region of islet amyloid polypeptide in self-assembly and cytotoxicity
Mathilde Fortier, Mélanie Côté‐Cyr, Vy Nguyen, et al.
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 6
Differential Effects of Aromatic Residues on Amyloid Formation and Cytotoxicity of Human IAPP
Lakshan Manathunga, Alexander Zhyvoloup, Aria Baghai, et al.
Biochemistry (2022) Vol. 61, Iss. 21, pp. 2334-2343
Open Access | Times Cited: 6
Analysis of Sheep and Goat IAPP Provides Insight into IAPP Amyloidogenicity and Cytotoxicity
Matthew E.T. Miller, Minghao Li, Aria Baghai, et al.
Biochemistry (2022) Vol. 61, Iss. 22, pp. 2531-2545
Open Access | Times Cited: 6
Synthesis and evaluation of novel two-photon fluorescence probes for in vivo imaging of amylin aggregates in the pancreas
Hiroyuki Watanabe, Yusuke Miki, Yoichi Shimizu, et al.
Dyes and Pigments (2019) Vol. 170, pp. 107615-107615
Closed Access | Times Cited: 8
Human Islet Amyloid Polypeptide Overexpression in INS-1E Cells Influences Amylin Oligomerization under ER Stress and Oxidative Stress
Yeong‐Min Yoo, Seong Soo Joo
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 21, pp. 11341-11341
Open Access | Times Cited: 5
Structural diversity in the membrane-bound hIAPP dimer correlated with distinct membrane disruption mechanisms
Qin Qiao, Guanghong Wei, Zhijian Song
Physical Chemistry Chemical Physics (2024) Vol. 26, Iss. 8, pp. 7090-7102
Open Access
In-silico analysis of islet amyloid polypeptide (IAPP) to predict the potential mutations involved in type II diabetes
Dikpal Reddy, R. Geetha
AIP conference proceedings (2024) Vol. 3193, pp. 020264-020264
Closed Access
Distinct modes of action of IAPP oligomers on membranes
Aliasghar Sepehri, Binod Nepal, Themis Lazaridis
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access
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