Virtual screening and molecular dynamics simulations provide insight into repurposing drugs against SARS-CoV-2 variants Spike protein/ACE2 interface
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2045-2322
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
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online resource.
- Erschienen in
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Virtual screening and molecular dynamics simulations provide insight into repurposing drugs against SARS-CoV-2 variants Spike protein/ACE2 interface ; volume:13 ; number:1 ; day:27 ; month:1 ; year:2023 ; pages:1-15 ; date:12.2023
Scientific reports ; 13, Heft 1 (27.1.2023), 1-15, 12.2023
- Urheber
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Pirolli, Davide
Righino, Benedetta
Camponeschi, Chiara
Ria, Francesco
Sante, Gabriele Di
Rosa, Maria Cristina De
- Beteiligte Personen und Organisationen
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SpringerLink (Online service)
- DOI
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10.1038/s41598-023-28716-8
- URN
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urn:nbn:de:101:1-2023041821252219681231
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:49 MESZ
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Beteiligte
- Pirolli, Davide
- Righino, Benedetta
- Camponeschi, Chiara
- Ria, Francesco
- Sante, Gabriele Di
- Rosa, Maria Cristina De
- SpringerLink (Online service)
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Publisher Correction: Virtual screening and molecular dynamics simulations provide insight into repurposing drugs against SARS-CoV-2 variants Spike protein/ACE2 interface
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Publisher Correction: Virtual screening and molecular dynamics simulations provide insight into repurposing drugs against SARS-CoV-2 variants Spike protein/ACE2 interface
Spike residue 403 affects binding of coronavirus spikes to human ACE2
Spike residue 403 affects binding of coronavirus spikes to human ACE2
Atomistic insight into the essential binding event of ACE2-derived peptides to the SARS-CoV-2 spike protein
Structural insight into the substrate recognition and transport mechanism of amino acid transporter complex ACE2-B0AT1 and ACE2-SIT1
TPC1 mutants provide insight into SV channel function
Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike
Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike
Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level
Mitochondrial DNAs provide insight into trypanosome phylogeny and molecular evolution
Substitution of T403R allows efficient utilization of human ACE2 by Spike proteins of bat coronaviruses
SARS‐CoV ‐2 spike protein enhances MAP4K3/GLK ‐induced ACE2 stability in COVID ‐19
Publisher Correction: Virtual screening and molecular dynamics simulations provide insight into repurposing drugs against SARS-CoV-2 variants Spike protein/ACE2 interface
Spike residue 403 affects binding of coronavirus spikes to human ACE2
Spike residue 403 affects binding of coronavirus spikes to human ACE2
Atomistic insight into the essential binding event of ACE2-derived peptides to the SARS-CoV-2 spike protein
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TPC1 mutants provide insight into SV channel function
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Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike
Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level
Mitochondrial DNAs provide insight into trypanosome phylogeny and molecular evolution
Substitution of T403R allows efficient utilization of human ACE2 by Spike proteins of bat coronaviruses