
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:
Microbial functional amyloids serve diverse purposes for structure, adhesion and defence
Nirukshan Shanmugam, Max O.D.G. Baker, Sarah R. Ball, et al.
Biophysical Reviews (2019) Vol. 11, Iss. 3, pp. 287-302
Open Access | Times Cited: 70
Nirukshan Shanmugam, Max O.D.G. Baker, Sarah R. Ball, et al.
Biophysical Reviews (2019) Vol. 11, Iss. 3, pp. 287-302
Open Access | Times Cited: 70
Showing 1-25 of 70 citing articles:
The role of gut dysbiosis in Parkinson’s disease: mechanistic insights and therapeutic options
Qing Wang, Yuqi Luo, К. Ray Chaudhuri, et al.
Brain (2021) Vol. 144, Iss. 9, pp. 2571-2593
Open Access | Times Cited: 187
Qing Wang, Yuqi Luo, К. Ray Chaudhuri, et al.
Brain (2021) Vol. 144, Iss. 9, pp. 2571-2593
Open Access | Times Cited: 187
Action Mechanisms of Effectors in Plant-Pathogen Interaction
Zhang Shiyi, Cong Li, Jinping Si, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 12, pp. 6758-6758
Open Access | Times Cited: 118
Zhang Shiyi, Cong Li, Jinping Si, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 12, pp. 6758-6758
Open Access | Times Cited: 118
Neurotoxic amyloidogenic peptides in the proteome of SARS-COV2: potential implications for neurological symptoms in COVID-19
Mirren Charnley, Saba Islam, Guneet K. Bindra, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 71
Mirren Charnley, Saba Islam, Guneet K. Bindra, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 71
The manifold roles of microbial ribosomal peptide–based natural products in physiology and ecology
Yanyan Li, Sylvie Rebuffat
Journal of Biological Chemistry (2019) Vol. 295, Iss. 1, pp. 34-54
Open Access | Times Cited: 115
Yanyan Li, Sylvie Rebuffat
Journal of Biological Chemistry (2019) Vol. 295, Iss. 1, pp. 34-54
Open Access | Times Cited: 115
Computational methods to predict protein aggregation
Susanna Navarro, Salvador Ventura
Current Opinion in Structural Biology (2022) Vol. 73, pp. 102343-102343
Open Access | Times Cited: 61
Susanna Navarro, Salvador Ventura
Current Opinion in Structural Biology (2022) Vol. 73, pp. 102343-102343
Open Access | Times Cited: 61
Cell wall–associated effectors of plant-colonizing fungi
Shigeyuki TANAKA, Regine Kahmann
Mycologia (2021) Vol. 113, Iss. 2, pp. 247-260
Open Access | Times Cited: 49
Shigeyuki TANAKA, Regine Kahmann
Mycologia (2021) Vol. 113, Iss. 2, pp. 247-260
Open Access | Times Cited: 49
Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils
Eri Chatani, Keisuke Yuzu, Yumiko Ohhashi, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 9, pp. 4349-4349
Open Access | Times Cited: 45
Eri Chatani, Keisuke Yuzu, Yumiko Ohhashi, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 9, pp. 4349-4349
Open Access | Times Cited: 45
A mechanistic survey of Alzheimer's disease
Yijing Tang, Dong Zhang, Xiong Gong, et al.
Biophysical Chemistry (2021) Vol. 281, pp. 106735-106735
Open Access | Times Cited: 45
Yijing Tang, Dong Zhang, Xiong Gong, et al.
Biophysical Chemistry (2021) Vol. 281, pp. 106735-106735
Open Access | Times Cited: 45
Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly
Karin Taş, Beatrice Dalla Volta, Christina Lindner, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 36
Karin Taş, Beatrice Dalla Volta, Christina Lindner, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 36
Ribosomally synthesized peptides, foreground players in microbial interactions: recent developments and unanswered questions
Sylvie Rebuffat
Natural Product Reports (2021) Vol. 39, Iss. 2, pp. 273-310
Closed Access | Times Cited: 34
Sylvie Rebuffat
Natural Product Reports (2021) Vol. 39, Iss. 2, pp. 273-310
Closed Access | Times Cited: 34
Catalytic amyloids
Elad Arad, Raz Jelinek
Trends in Chemistry (2022) Vol. 4, Iss. 10, pp. 907-917
Closed Access | Times Cited: 28
Elad Arad, Raz Jelinek
Trends in Chemistry (2022) Vol. 4, Iss. 10, pp. 907-917
Closed Access | Times Cited: 28
The Cryo-EM structures of two amphibian antimicrobial cross-β amyloid fibrils
Robert Bücker, Carolin Seuring, Cornelia Cazey, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 23
Robert Bücker, Carolin Seuring, Cornelia Cazey, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 23
A Coumarin-Based Array for the Discrimination of Amyloids
Natalie Trinh, Kaustubh R. Bhuskute, Nikhil R. Varghese, et al.
ACS Sensors (2024) Vol. 9, Iss. 2, pp. 615-621
Open Access | Times Cited: 5
Natalie Trinh, Kaustubh R. Bhuskute, Nikhil R. Varghese, et al.
ACS Sensors (2024) Vol. 9, Iss. 2, pp. 615-621
Open Access | Times Cited: 5
Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation
Casper Bøjer Rasmussen, Gunna Christiansen, Brian S. Vad, et al.
Protein Science (2018) Vol. 28, Iss. 3, pp. 633-642
Open Access | Times Cited: 42
Casper Bøjer Rasmussen, Gunna Christiansen, Brian S. Vad, et al.
Protein Science (2018) Vol. 28, Iss. 3, pp. 633-642
Open Access | Times Cited: 42
Strategies for the Molecular Imaging of Amyloid and the Value of a Multimodal Approach
Amandeep Kaur, Elizabeth J. New, Margaret Sunde
ACS Sensors (2020) Vol. 5, Iss. 8, pp. 2268-2282
Closed Access | Times Cited: 35
Amandeep Kaur, Elizabeth J. New, Margaret Sunde
ACS Sensors (2020) Vol. 5, Iss. 8, pp. 2268-2282
Closed Access | Times Cited: 35
Antimicrobial α-defensins as multi-target inhibitors against amyloid formation and microbial infection
Yanxian Zhang, Yonglan Liu, Yijing Tang, et al.
Chemical Science (2021) Vol. 12, Iss. 26, pp. 9124-9139
Open Access | Times Cited: 31
Yanxian Zhang, Yonglan Liu, Yijing Tang, et al.
Chemical Science (2021) Vol. 12, Iss. 26, pp. 9124-9139
Open Access | Times Cited: 31
The Hunt for Ancient Prions: Archaeal Prion-Like Domains Form Amyloid-Based Epigenetic Elements
Tomasz Zajkowski, Michael Lee, Shamba S. Mondal, et al.
Molecular Biology and Evolution (2021) Vol. 38, Iss. 5, pp. 2088-2103
Open Access | Times Cited: 27
Tomasz Zajkowski, Michael Lee, Shamba S. Mondal, et al.
Molecular Biology and Evolution (2021) Vol. 38, Iss. 5, pp. 2088-2103
Open Access | Times Cited: 27
The Pga59 cell wall protein is an amyloid forming protein involved in adhesion and biofilm establishment in the pathogenic yeast Candida albicans
Thierry Mourer, Mennat El Ghalid, Gérard Péhau‐Arnaudet, et al.
npj Biofilms and Microbiomes (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 12
Thierry Mourer, Mennat El Ghalid, Gérard Péhau‐Arnaudet, et al.
npj Biofilms and Microbiomes (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 12
The Intricate Interplay: Microbial Metabolites and the Gut‐Liver‐Brain Axis in Parkinson's Disease
Dayamrita Kollaparampil Kishanchand, Athira Krishnan K. A., Krishnapriya Chandrababu, et al.
Journal of Neuroscience Research (2025) Vol. 103, Iss. 1
Closed Access
Dayamrita Kollaparampil Kishanchand, Athira Krishnan K. A., Krishnapriya Chandrababu, et al.
Journal of Neuroscience Research (2025) Vol. 103, Iss. 1
Closed Access
De Novo Amyloid Peptide–Polymer Blends with Enhanced Mechanical and Biological Properties
Xianjun Wang, Malay Mondal, Penelope E. Jankoski, et al.
ACS Applied Polymer Materials (2025) Vol. 7, Iss. 6, pp. 3739-3751
Open Access
Xianjun Wang, Malay Mondal, Penelope E. Jankoski, et al.
ACS Applied Polymer Materials (2025) Vol. 7, Iss. 6, pp. 3739-3751
Open Access
Repurposing Antimicrobial Protegrin-1 as a Dual-Function Amyloid Inhibitor via Cross-seeding
Yijing Tang, Dong Zhang, Jie Zheng
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 17, pp. 3143-3155
Closed Access | Times Cited: 9
Yijing Tang, Dong Zhang, Jie Zheng
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 17, pp. 3143-3155
Closed Access | Times Cited: 9
Staphylococcus aureus functional amyloids catalyze degradation of β-lactam antibiotics
Elad Arad, Kasper B. Pedersen, Orit Malka, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 9
Elad Arad, Kasper B. Pedersen, Orit Malka, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 9
Hydrophobin Rodlets on the Fungal Cell Wall
Sarah R. Ball, Ann H. Kwan, Margaret Sunde
Current topics in microbiology and immunology (2019), pp. 29-51
Closed Access | Times Cited: 28
Sarah R. Ball, Ann H. Kwan, Margaret Sunde
Current topics in microbiology and immunology (2019), pp. 29-51
Closed Access | Times Cited: 28
Enhanced purification coupled with biophysical analyses shows cross-β structure as a core building block for Streptococcus mutans functional amyloids
Ana L. Barrán-Berdón, Sebastian Ocampo, Momin Haider, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 26
Ana L. Barrán-Berdón, Sebastian Ocampo, Momin Haider, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 26
Herpes simplex virus encoded ICP6 protein forms functional amyloid assemblies with necroptosis-associated host proteins
Nirukshan Shanmugam, Max O.D.G. Baker, Máximo Sanz-Hernández, et al.
Biophysical Chemistry (2020) Vol. 269, pp. 106524-106524
Closed Access | Times Cited: 25
Nirukshan Shanmugam, Max O.D.G. Baker, Máximo Sanz-Hernández, et al.
Biophysical Chemistry (2020) Vol. 269, pp. 106524-106524
Closed Access | Times Cited: 25