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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:

Modulation of the Aβ peptide aggregation pathway by KP1019 limits Aβ-associated neurotoxicity
Michael R. Jones, Changhua Mu, Michael C. P. Wang, et al.
Metallomics (2014) Vol. 7, Iss. 1, pp. 129-135
Open Access | Times Cited: 41

Showing 1-25 of 41 citing articles:

Encyclopedia of Inorganic and Bioinorganic Chemistry

Wiley eBooks (2011)
Open Access | Times Cited: 1486
Development of Multifunctional Molecules as Potential Therapeutic Candidates for Alzheimer’s Disease, Parkinson’s Disease, and Amyotrophic Lateral Sclerosis in the Last Decade
Masha G. Savelieff, Geewoo Nam, Juhye Kang, et al.
Chemical Reviews (2018) Vol. 119, Iss. 2, pp. 1221-1322
Closed Access | Times Cited: 482
Recent advances in Alzheimer’s disease: Mechanisms, clinical trials and new drug development strategies
Jifa Zhang, Yinglu Zhang, Jiaxing Wang, et al.
Signal Transduction and Targeted Therapy (2024) Vol. 9, Iss. 1
Open Access | Times Cited: 135
Metallobiology and therapeutic chelation of biometals (copper, zinc and iron) in Alzheimer’s disease: Limitations, and current and future perspectives
Kehinde D. Fasae, Amos O. Abolaji, Tolulope R. Faloye, et al.
Journal of Trace Elements in Medicine and Biology (2021) Vol. 67, pp. 126779-126779
Open Access | Times Cited: 108
Metal complexes that bind to the amyloid-β peptide of relevance to Alzheimer’s disease
Luiza M. F. Gomes, Janaina C. Bataglioli, Tim Storr
Coordination Chemistry Reviews (2020) Vol. 412, pp. 213255-213255
Closed Access | Times Cited: 73
Redox-Active Metal Ions and Amyloid-Degrading Enzymes in Alzheimer’s Disease
Namdoo Kim, Hyuck Jin Lee
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 14, pp. 7697-7697
Open Access | Times Cited: 43
Targeting misfolding and aggregation of the amyloid-β peptide and mutant p53 protein using multifunctional molecules
Lauryn Grcic, Grace Leech, Kalvin Kwan, et al.
Chemical Communications (2024) Vol. 60, Iss. 11, pp. 1372-1388
Closed Access | Times Cited: 7
Amyloid β-Targeted Metal Complexes for Potential Applications in Alzheimer's Disease
Hao Liu, Yunwei Qu, Xiaohui Wang
Future Medicinal Chemistry (2018) Vol. 10, Iss. 6, pp. 679-701
Closed Access | Times Cited: 59
A catalytic antioxidant for limiting amyloid-beta peptide aggregation and reactive oxygen species generation
Luiza M. F. Gomes, Atif Mahammed, Kathleen E. Prosser, et al.
Chemical Science (2018) Vol. 10, Iss. 6, pp. 1634-1643
Open Access | Times Cited: 55
Recent Developments in Metal-Based Drugs and Chelating Agents for Neurodegenerative Diseases Treatments
Thaís Aparecida Sales, Ingrid G. Prandi, Alexandre A. de Castro, et al.
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 8, pp. 1829-1829
Open Access | Times Cited: 54
Sensitivity towards the GRP78 inhibitor KP1339/IT-139 is characterized by apoptosis induction via caspase 8 upon disruption of ER homeostasis
Beatrix Schoenhacker‐Alte, Thomas Mohr, Christine Pirker, et al.
Cancer Letters (2017) Vol. 404, pp. 79-88
Closed Access | Times Cited: 52
Platinum(II) O,S Complexes Inhibit the Aggregation of Amyloid Model Systems
Daniele Florio, Anna Maria Malfitano, Sarah Di Somma, et al.
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 4, pp. 829-829
Open Access | Times Cited: 44
Advantageous Reactivity of Unstable Metal Complexes: Potential Applications of Metal-Based Anticancer Drugs for Intratumoral Injections
Aviva Levina, Debbie C. Crans, Peter A. Lay
Pharmaceutics (2022) Vol. 14, Iss. 4, pp. 790-790
Open Access | Times Cited: 27
Advances of metallodrug-amyloid β aggregation inhibitors for therapeutic intervention in neurodegenerative diseases: Evaluation of their mechanistic insights and neurotoxicity
Huzaifa Yasir Khan, Azeem Ahmad, Md Nadir Hassan, et al.
Coordination Chemistry Reviews (2023) Vol. 501, pp. 215580-215580
Closed Access | Times Cited: 15
Luminescent Ru(II) Phenanthroline Complexes as a Probe for Real-Time Imaging of Aβ Self-Aggregation and Therapeutic Applications in Alzheimer’s Disease
Débora E.S. Silva, Mariana P. Cali, Wallance Moreira Pazin, et al.
Journal of Medicinal Chemistry (2016) Vol. 59, Iss. 19, pp. 9215-9227
Closed Access | Times Cited: 47
Importance of Hydrogen Bonding: Structure–Activity Relationships of Ruthenium(III) Complexes with Pyridine-Based Ligands for Alzheimer’s Disease Therapy
Brendan J. Wall, Mark F. Will, Gideon K. Yawson, et al.
Journal of Medicinal Chemistry (2021) Vol. 64, Iss. 14, pp. 10124-10138
Closed Access | Times Cited: 30
Role of organometallic complexes in targeted therapies of different diseases: Infectious diseases, Cancer and Neurodegenerative Diseases
Nitin Verma, Tanmay Anand, Chandra Kant Singh, et al.
Journal of Organometallic Chemistry (2024), pp. 123389-123389
Closed Access | Times Cited: 4
Design and synthesis of piano-stool ruthenium(II) complexes and their studies on the inhibition of amyloid β (1–42) peptide aggregation
Sain Singh, Govinda R. Navale, Sonia Agrawal, et al.
International Journal of Biological Macromolecules (2023) Vol. 239, pp. 124197-124197
Closed Access | Times Cited: 10
Transition Metal Complexes as Therapeutics: A New Frontier in Combatting Neurodegenerative Disorders through Protein Aggregation Modulation
Govinda R. Navale, Imtiaz Ahmed, Mi Hee Lim, et al.
Advanced Healthcare Materials (2024)
Closed Access | Times Cited: 3
Ruthenium(iii) complexes containing thiazole-based ligands that modulate amyloid-β aggregation
Samantha E. Huffman, Gideon K. Yawson, Samuel S. Fisher, et al.
Metallomics (2020) Vol. 12, Iss. 4, pp. 491-503
Open Access | Times Cited: 24
A Dual-Pronged Approach: A Ruthenium(III) Complex That Modulates Amyloid-β Aggregation and Disrupts Its Formed Aggregates
Gideon K. Yawson, Mark F. Will, Samantha E. Huffman, et al.
Inorganic Chemistry (2022) Vol. 61, Iss. 6, pp. 2733-2744
Closed Access | Times Cited: 14
Metals and Metal-Nanoparticles in Human Pathologies: From Exposure to Therapy
Joanna Izabela Lachowicz, Luigi Isaia Lecca, Federico Meloni, et al.
Molecules (2021) Vol. 26, Iss. 21, pp. 6639-6639
Open Access | Times Cited: 19
Highly Efficient Singlet Oxygen Generation by BODIPY–Ruthenium(II) Complexes for Promoting Neurite Outgrowth and Suppressing Tau Protein Aggregation
Cheng-Yun Wu, Hsin-Jou Chen, Yun-Chin Wu, et al.
Inorganic Chemistry (2023) Vol. 62, Iss. 3, pp. 1102-1112
Closed Access | Times Cited: 7
A systematic assessment of chemical, genetic, and epigenetic factors influencing the activity of anticancer drug KP1019 (FFC14A)
Upendarrao Golla, Swati Swagatika, Sakshi Chauhan, et al.
Oncotarget (2017) Vol. 8, Iss. 58, pp. 98426-98454
Open Access | Times Cited: 23
A Metallo Pro‐Drug to Target CuII in the Context of Alzheimer's Disease
Amandine Conte‐Daban, Vinita Ambike, Régis Guillot, et al.
Chemistry - A European Journal (2018) Vol. 24, Iss. 20, pp. 5095-5099
Open Access | Times Cited: 21
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