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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:

Catalytic amyloids: Is misfolding folding?
Liam R. Marshall, Ivan V. Korendovych
Current Opinion in Chemical Biology (2021) Vol. 64, pp. 145-153
Open Access | Times Cited: 24

Showing 24 citing articles:

Histidine as a key modulator of molecular self-assembly: Peptide-based supramolecular materials inspired by biological systems
Yu Chen, Kai Tao, Wei Ji, et al.
Materials Today (2022) Vol. 60, pp. 106-127
Open Access | Times Cited: 51
Asymmetric Michael addition catalysed by copper–amyloid complexes
Nobutaka Fujieda, Atsushi Tonomura, Tomofumi Mochizuki, et al.
RSC Advances (2024) Vol. 14, Iss. 1, pp. 206-210
Open Access | Times Cited: 6
Catalytic amyloids
Elad Arad, Raz Jelinek
Trends in Chemistry (2022) Vol. 4, Iss. 10, pp. 907-917
Closed Access | Times Cited: 26
Self-assembly of the de novo designed peptides to produce supramolecular catalysts with built-in enzyme-like active sites: a review of structure–activity relationship
Yi Lou, Baoli Zhang, Xiangyu Ye, et al.
Materials Today Nano (2023) Vol. 21, pp. 100302-100302
Open Access | Times Cited: 17
Design of Functional Globular β‐Sheet Miniproteins
Truc Lam Pham, Franziska Thomas
ChemBioChem (2024) Vol. 25, Iss. 7
Open Access | Times Cited: 5
EMBER multidimensional spectral microscopy enables quantitative determination of disease- and cell-specific amyloid strains
Hyunjun Yang, Peng Yuan, Yibing Wu, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 12
Open Access | Times Cited: 11
Metal Ions Can Modulate the Self-Assembly and Activity of Catalytic Peptide Amyloids
Eva Duran-Meza, Raúl Araya-Secchi, Patricio Romero-Hasler, et al.
Langmuir (2024) Vol. 40, Iss. 12, pp. 6094-6106
Closed Access | Times Cited: 3
Peptides and metal ions: A successful marriage for developing artificial metalloproteins
Linda Leone, Maria De Fenza, Alessandra Esposito, et al.
Journal of Peptide Science (2024)
Closed Access | Times Cited: 3
Supramolecular enzyme-mimicking catalysts self-assembled from peptides
Qing Liu, Akinori Kuzuya, Zhen‐Gang Wang
iScience (2022) Vol. 26, Iss. 1, pp. 105831-105831
Open Access | Times Cited: 17
Small Peptides in the Detection of Mycotoxins and Their Potential Applications in Mycotoxin Removal
Zitong Zhao, Zhenzhen Zhang, Haoxiang Zhang, et al.
Toxins (2022) Vol. 14, Iss. 11, pp. 795-795
Open Access | Times Cited: 15
Amyloids of α-Synuclein Promote Chemical Transformations of Neuronal Cell Metabolites
István Horváth, Khadra A. Mohamed, Ranjeet Kumar, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 16, pp. 12849-12849
Open Access | Times Cited: 6
Chemical catalysis by biological amyloids
Pernilla Wittung‐Stafshede
Biochemical Society Transactions (2023) Vol. 51, Iss. 5, pp. 1967-1974
Open Access | Times Cited: 6
Elucidating Conformational Dynamics and Thermostability of Designed Aromatic Clusters by Using Protein Cages
Yuki Hishikawa, Hiroki Noya, Satoru Nagatoishi, et al.
Chemistry - A European Journal (2023) Vol. 29, Iss. 34
Closed Access | Times Cited: 3
Crystalline Metal‐Peptide Networks: Structures, Applications, and Future Outlook
Seoneun Jeong, Kwonjung Lee, Sung Hyun Yoo, et al.
ChemBioChem (2022) Vol. 24, Iss. 2
Closed Access | Times Cited: 5
Intracellular artificial supramolecular architectures based on de novo designed peptides
Takayuki Miki, Mitsunori Hashimoto, Hideyuki Takahashi, et al.
Royal Society of Chemistry eBooks (2024), pp. 64-85
Closed Access
Simulating chemical reactions promoted by self-assembled peptides with catalytic properties
Yuqin Yang, Xiaoyu Wang, Hao Dong
Methods in enzymology on CD-ROM/Methods in enzymology (2024), pp. 321-343
Closed Access
Screening of oxidative behavior in catalytic amyloid assemblies
Liam R. Marshall, Ivan V. Korendovych
Methods in enzymology on CD-ROM/Methods in enzymology (2024), pp. 15-33
Closed Access
Stopped-flow measurement of CO2 hydration activity by catalytic amyloids
Liam R. Marshall, Olga V. Makhlynets
Methods in enzymology on CD-ROM/Methods in enzymology (2024), pp. 35-49
Closed Access
Structural characterization of amyloid aggregates with spatially resolved infrared spectroscopy
Divya Baghel, Ana Pacheco de Oliveira, Saumya Satyarthy, et al.
Methods in enzymology on CD-ROM/Methods in enzymology (2024), pp. 113-150
Closed Access
Avoiding common pitfalls in designing kinetic protocols for catalytic amyloid studies
Liam R. Marshall, Ivan V. Korendovych
Methods in enzymology on CD-ROM/Methods in enzymology (2024), pp. 1-13
Closed Access
Catalytic Nanomaterials by Conjugation of an Artificial Heme-Peroxidase to Amyloid Fibrils
Alessandra Esposito, Linda Leone, Alfonso De Simone, et al.
ACS Applied Materials & Interfaces (2024) Vol. 16, Iss. 34, pp. 45371-45382
Closed Access
Amyloids. Evolutionary Past and Biotechnological Future
O. V. Nevzglyadova, Е. В. Михайлова, Soĭdla Tr
Cell and Tissue Biology (2024) Vol. 18, Iss. 6, pp. 587-601
Closed Access
EMBER multi-dimensional spectral microscopy enables quantitative determination of disease- and cell-specific amyloid strains
Hyunjun Yang, Peng Yuan, Yibing Wu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Short Peptides for Hydrolase Supramolecular Mimicry and Their Potential Applications
Paola Alletto, Ana M. García, Silvia Marchesan
Gels (2023) Vol. 9, Iss. 9, pp. 678-678
Open Access
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