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:
Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils
Einav Tayeb-Fligelman, Jeannette T. Bowler, Christen E. Tai, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 14
Einav Tayeb-Fligelman, Jeannette T. Bowler, Christen E. Tai, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 14
Showing 14 citing articles:
Protein misfolding and amyloid nucleation through liquid–liquid phase separation
S. Mukherjee, Manisha Poudyal, K. Dave, et al.
Chemical Society Reviews (2024) Vol. 53, Iss. 10, pp. 4976-5013
Closed Access | Times Cited: 20
S. Mukherjee, Manisha Poudyal, K. Dave, et al.
Chemical Society Reviews (2024) Vol. 53, Iss. 10, pp. 4976-5013
Closed Access | Times Cited: 20
Protein–protein interactions regulating α-synuclein pathology
Jiannan Wang, Lijun Dai, Sichun Chen, et al.
Trends in Neurosciences (2024) Vol. 47, Iss. 3, pp. 209-226
Closed Access | Times Cited: 7
Jiannan Wang, Lijun Dai, Sichun Chen, et al.
Trends in Neurosciences (2024) Vol. 47, Iss. 3, pp. 209-226
Closed Access | Times Cited: 7
Phosphorylation in the Ser/Arg-rich region of the nucleocapsid of SARS-CoV-2 regulates phase separation by inhibiting self-association of a distant helix
Hannah Stuwe, Patrick N. Reardon, Zhen Yu, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 6, pp. 107354-107354
Open Access | Times Cited: 7
Hannah Stuwe, Patrick N. Reardon, Zhen Yu, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 6, pp. 107354-107354
Open Access | Times Cited: 7
Promising Strategies to Reduce the SARS-CoV-2 Amyloid Deposition in the Brain and Prevent COVID-19-Exacerbated Dementia and Alzheimer’s Disease
Nikita Navolokin, Viktoria Adushkina, Daria Zlatogorskaya, et al.
Pharmaceuticals (2024) Vol. 17, Iss. 6, pp. 788-788
Open Access | Times Cited: 3
Nikita Navolokin, Viktoria Adushkina, Daria Zlatogorskaya, et al.
Pharmaceuticals (2024) Vol. 17, Iss. 6, pp. 788-788
Open Access | Times Cited: 3
Viral amyloids: New opportunities for antiviral therapeutic strategies
Frank Gondelaud, Pierre‐Yves Lozach, Sonia Longhi
Current Opinion in Structural Biology (2023) Vol. 83, pp. 102706-102706
Open Access | Times Cited: 8
Frank Gondelaud, Pierre‐Yves Lozach, Sonia Longhi
Current Opinion in Structural Biology (2023) Vol. 83, pp. 102706-102706
Open Access | Times Cited: 8
SARS-CoV-2 amyloid, is COVID-19-exacerbated dementia an amyloid disorder in the making?
Nathaniel G.N. Milton
Frontiers in Dementia (2023) Vol. 2
Open Access | Times Cited: 7
Nathaniel G.N. Milton
Frontiers in Dementia (2023) Vol. 2
Open Access | Times Cited: 7
Brain-wide alterations revealed by spatial transcriptomics and proteomics in COVID-19 infection
Ting Zhang, Yunfeng Li, Liuliu Pan, et al.
Nature Aging (2024) Vol. 4, Iss. 11, pp. 1598-1618
Closed Access | Times Cited: 1
Ting Zhang, Yunfeng Li, Liuliu Pan, et al.
Nature Aging (2024) Vol. 4, Iss. 11, pp. 1598-1618
Closed Access | Times Cited: 1
SARS-CoV-2 Spike amyloid fibrils specifically and selectively accelerates amyloid fibril formation of human prion protein and the amyloid β peptide
Johan N. K. Larsson, Ebba Hellstrand, Per Hammarström, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 3
Johan N. K. Larsson, Ebba Hellstrand, Per Hammarström, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 3
Binding of SARS-CoV-2 nucleocapsid protein to uninfected epithelial cells induces antibody-mediated complement deposition
Jamal Fahoum, Maria Billan, Julia K. Varga, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Jamal Fahoum, Maria Billan, Julia K. Varga, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Amyloidogenesis of SARS-CoV-2 Delta Plus and Omicron Variants Receptor-Binding Domain (RBD): Impact of SUMO Fusion Tag
Sadegh Zargan, Hasan Jalili, Bahareh Dabirmanesh, et al.
Research Square (Research Square) (2024)
Open Access
Sadegh Zargan, Hasan Jalili, Bahareh Dabirmanesh, et al.
Research Square (Research Square) (2024)
Open Access
Amyloidogenesis of SARS-CoV-2 delta plus and omicron variants receptor-binding domain (RBD): impact of SUMO fusion tag
Sadegh Zargan, Hasan Jalili, Bahareh Dabirmanesh, et al.
Biotechnology Letters (2024) Vol. 46, Iss. 6, pp. 1037-1048
Open Access
Sadegh Zargan, Hasan Jalili, Bahareh Dabirmanesh, et al.
Biotechnology Letters (2024) Vol. 46, Iss. 6, pp. 1037-1048
Open Access
Cell invasive amyloid assemblies from SARS-CoV-2 peptides can form multiple polymorphs with varying neurotoxicity
Oana Sanislav, Rina Tetaj, Metali, et al.
Nanoscale (2024)
Closed Access
Oana Sanislav, Rina Tetaj, Metali, et al.
Nanoscale (2024)
Closed Access
Cell invasive amyloid assemblies from SARS-CoV-2 peptides can form multiple polymorphs with varying neurotoxicity
Oana Sanislav, Rina Tetaj, Metali, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Oana Sanislav, Rina Tetaj, Metali, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Designed inhibitors to reduce amyloid virulence and cytotoxicity and combat neurodegenerative and infectious diseases
Rinat Yona Indig, Meytal Landau
Current Opinion in Chemical Biology (2023) Vol. 75, pp. 102318-102318
Open Access
Rinat Yona Indig, Meytal Landau
Current Opinion in Chemical Biology (2023) Vol. 75, pp. 102318-102318
Open Access
