Global conserved RBD fraction of SARS-CoV-2 S-protein with T500S mutation in silico significantly blocks ACE2 and rejects viral spike

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2396-832X

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Global conserved RBD fraction of SARS-CoV-2 S-protein with T500S mutation in silico significantly blocks ACE2 and rejects viral spike ; volume:7 ; number:1 ; day:4 ; month:2 ; year:2022 ; pages:1-11 ; date:12.2022
Translational medicine communications ; 7, Heft 1 (4.2.2022), 1-11, 12.2022

Creator: Banerjee, Amrita
Kanwar, Mehak
Santra, Dipannita
Maiti, Smarajit

Contributor: SpringerLink (Online service)

DOI: 10.1186/s41231-022-00109-5

URN: urn:nbn:de:101:1-2022051320253991623322

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:24 AM CEST

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Banerjee, Amrita
Kanwar, Mehak
Santra, Dipannita
Maiti, Smarajit
SpringerLink (Online service)

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Global conserved RBD fraction of SARS-CoV-2 S-protein with T500S mutation in silico significantly blocks ACE2 and rejects viral spike

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Other Objects (12)

Spike residue 403 affects binding of coronavirus spikes to human ACE2

Spike residue 403 affects binding of coronavirus spikes to human ACE2

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Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level

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

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Recombinant ACE2 protein protects against acute lung injury induced by SARS-CoV-2 spike RBD protein

Spike residue 403 affects binding of coronavirus spikes to human ACE2

Spike residue 403 affects binding of coronavirus spikes to human ACE2

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

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

Plastic Antibodies Mimicking the ACE2 Receptor for Selective Binding of SARS‐CoV‐2 Spike

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A Novel Therapeutic Peptide Blocks SARS-CoV-2 Spike Protein Binding with Host Cell ACE2 Receptor

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Spike residue 403 affects binding of coronavirus spikes to human ACE2

Spike residue 403 affects binding of coronavirus spikes to human ACE2

Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike

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Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level

Substitution of T403R allows efficient utilization of human ACE2 by Spike proteins of bat coronaviruses

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