Characterization of biotinylated human ACE2 and SARS-CoV-2 Omicron BA.4/5 spike protein reference materials

to related objects

Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: 1 Online-Ressource.

Language: Englisch

Bibliographic citation: Characterization of biotinylated human ACE2 and SARS-CoV-2 Omicron BA.4/5 spike protein reference materials ; volume:416 ; number:22 ; day:28 ; month:6 ; year:2024 ; pages:4861-4872 ; date:9.2024
Analytical and bioanalytical chemistry ; 416, Heft 22 (28.6.2024), 4861-4872, 9.2024

Creator: Stocks, Bradley B.
Thibeault, Marie-Pier
L’Abbé, Denis
Umer, Muhammad
Liu, Yali
Stuible, Matthew
Durocher, Yves
Melanson, Jeremy E.

Contributor: SpringerLink (Online service)

DOI: 10.1007/s00216-024-05413-7

URN: urn:nbn:de:101:1-2411042109443.892330493175

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

Last update: 15.08.2025, 7:37 AM CEST

Data provider

This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.

Show original at data provider

Associated

Stocks, Bradley B.
Thibeault, Marie-Pier
L’Abbé, Denis
Umer, Muhammad
Liu, Yali
Stuible, Matthew
Durocher, Yves
Melanson, Jeremy E.
SpringerLink (Online service)

Other Objects (12)

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

Structures of ACE2–SIT1 recognized by Omicron variants of SARS-CoV-2

Analyzing the interaction of human ACE2 and RBD of spike protein of SARS-CoV-2 in perspective of Omicron variant

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

SARS‐CoV ‐2 spike protein enhances MAP4K3/GLK ‐induced ACE2 stability in COVID ‐19

SARS-CoV-2 spike protein induces endothelial inflammation via ACE2 independently of viral replication

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

SARS-CoV-2 Spike Protein Exacerbates Thromboembolic Cerebrovascular Complications in Humanized ACE2 Mouse Model

Broadly potent spike-specific human monoclonal antibodies inhibit SARS-CoV-2 Omicron sub-lineages

The SARS-CoV-2 Omicron BA.1 spike G446S mutation potentiates antiviral T-cell recognition

Structural bioinformatics analysis of SARS-CoV-2 variants reveals higher hACE2 receptor binding affinity for Omicron B.1.1.529 spike RBD compared to wild type reference

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

Structures of ACE2–SIT1 recognized by Omicron variants of SARS-CoV-2

Analyzing the interaction of human ACE2 and RBD of spike protein of SARS-CoV-2 in perspective of Omicron variant

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

SARS‐CoV ‐2 spike protein enhances MAP4K3/GLK ‐induced ACE2 stability in COVID ‐19

SARS-CoV-2 spike protein induces endothelial inflammation via ACE2 independently of viral replication

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

SARS-CoV-2 Spike Protein Exacerbates Thromboembolic Cerebrovascular Complications in Humanized ACE2 Mouse Model

Broadly potent spike-specific human monoclonal antibodies inhibit SARS-CoV-2 Omicron sub-lineages

The SARS-CoV-2 Omicron BA.1 spike G446S mutation potentiates antiviral T-cell recognition

Structural bioinformatics analysis of SARS-CoV-2 variants reveals higher hACE2 receptor binding affinity for Omicron B.1.1.529 spike RBD compared to wild type reference

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

Structures of ACE2–SIT1 recognized by Omicron variants of SARS-CoV-2

Analyzing the interaction of human ACE2 and RBD of spike protein of SARS-CoV-2 in perspective of Omicron variant

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

SARS‐CoV ‐2 spike protein enhances MAP4K3/GLK ‐induced ACE2 stability in COVID ‐19

SARS-CoV-2 spike protein induces endothelial inflammation via ACE2 independently of viral replication

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

SARS-CoV-2 Spike Protein Exacerbates Thromboembolic Cerebrovascular Complications in Humanized ACE2 Mouse Model

Broadly potent spike-specific human monoclonal antibodies inhibit SARS-CoV-2 Omicron sub-lineages

The SARS-CoV-2 Omicron BA.1 spike G446S mutation potentiates antiviral T-cell recognition

Structural bioinformatics analysis of SARS-CoV-2 variants reveals higher hACE2 receptor binding affinity for Omicron B.1.1.529 spike RBD compared to wild type reference

Cultural heritage institutions wishing to register will find more information here.

Fields marked * need to be filled in.

Username*

Please enter your username

Email*

Please enter your email address

Please do not fill this field

First name

Last name

Password*

Please enter your password

Confirm password*

Please enter the same password

I have read the terms of use and the privacy policy for the collection of personal data and accept them. *

This field is required.

I would like to subscribe to the newsletter of the Deutsche Digitale Bibliothek. See newsletter subscription info.

Account created

Your "My DDB" account has been successfully created. Before you can log in to your account, you must click the confirmation link in the message we just sent to the email address you provided.

Characterization of biotinylated human ACE2 and SARS-CoV-2 Omicron BA.4/5 spike protein reference materials

Object Details

References and Relationships

Contributors, Places and Time

Further information

Data provider

Associated

Other Objects (12)

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

Structures of ACE2–SIT1 recognized by Omicron variants of SARS-CoV-2

Analyzing the interaction of human ACE2 and RBD of spike protein of SARS-CoV-2 in perspective of Omicron variant

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

SARS‐CoV ‐2 spike protein enhances MAP4K3/GLK ‐induced ACE2 stability in COVID ‐19

SARS-CoV-2 spike protein induces endothelial inflammation via ACE2 independently of viral replication

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

SARS-CoV-2 Spike Protein Exacerbates Thromboembolic Cerebrovascular Complications in Humanized ACE2 Mouse Model

Broadly potent spike-specific human monoclonal antibodies inhibit SARS-CoV-2 Omicron sub-lineages

The SARS-CoV-2 Omicron BA.1 spike G446S mutation potentiates antiviral T-cell recognition

Structural bioinformatics analysis of SARS-CoV-2 variants reveals higher hACE2 receptor binding affinity for Omicron B.1.1.529 spike RBD compared to wild type reference

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

Structures of ACE2–SIT1 recognized by Omicron variants of SARS-CoV-2

Analyzing the interaction of human ACE2 and RBD of spike protein of SARS-CoV-2 in perspective of Omicron variant

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

SARS‐CoV ‐2 spike protein enhances MAP4K3/GLK ‐induced ACE2 stability in COVID ‐19

SARS-CoV-2 spike protein induces endothelial inflammation via ACE2 independently of viral replication

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

SARS-CoV-2 Spike Protein Exacerbates Thromboembolic Cerebrovascular Complications in Humanized ACE2 Mouse Model

Broadly potent spike-specific human monoclonal antibodies inhibit SARS-CoV-2 Omicron sub-lineages

The SARS-CoV-2 Omicron BA.1 spike G446S mutation potentiates antiviral T-cell recognition

Structural bioinformatics analysis of SARS-CoV-2 variants reveals higher hACE2 receptor binding affinity for Omicron B.1.1.529 spike RBD compared to wild type reference

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

Structures of ACE2–SIT1 recognized by Omicron variants of SARS-CoV-2

Analyzing the interaction of human ACE2 and RBD of spike protein of SARS-CoV-2 in perspective of Omicron variant

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

SARS‐CoV ‐2 spike protein enhances MAP4K3/GLK ‐induced ACE2 stability in COVID ‐19

SARS-CoV-2 spike protein induces endothelial inflammation via ACE2 independently of viral replication

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

SARS-CoV-2 Spike Protein Exacerbates Thromboembolic Cerebrovascular Complications in Humanized ACE2 Mouse Model

Broadly potent spike-specific human monoclonal antibodies inhibit SARS-CoV-2 Omicron sub-lineages

The SARS-CoV-2 Omicron BA.1 spike G446S mutation potentiates antiviral T-cell recognition

Structural bioinformatics analysis of SARS-CoV-2 variants reveals higher hACE2 receptor binding affinity for Omicron B.1.1.529 spike RBD compared to wild type reference

Related objects

Reset password