Conformational Control of Fast Asparagine Deamidation in a Norovirus Capsid Protein-Reference-Cited by-同舟云学术

Conformational Control of Fast Asparagine Deamidation in a Norovirus Capsid Protein

Published:2023-02-21 Issue:5 Volume:62 Page:1032-1043
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Creutznacher Robert¹,Schulze-Niemand Eric²,König Patrick¹,Stanojlovic Vesna³,Mallagaray Alvaro¹,Peters Thomas¹^ORCID,Stein Matthias²^ORCID,Schubert Mario³^ORCID

Affiliation:

1. Institute of Chemistry and Metabolomics, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany

2. Molecular Simulations and Design Group, Max Planck Institute for Dynamics of Complex Technical Systems, Sandtorstrasse 1, 39106 Magdeburg, Germany

3. Department of Biosciences and Medical Biology, University of Salzburg, Hellbrunnerstrasse 34, 5020 Salzburg, Austria

Funder

Deutsche Forschungsgemeinschaft

European Cooperation in Science and Technology

European Funds for Regional Development

Max Planck Society for the Advancement of Science and the International Max Planck Research School (IMPRS) for Advanced Methods in Process and Systems Engineering

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.2c00656

Reference57 articles.

1. Controlled Deamidation of Peptides and Proteins: An Experimental Hazard and a Possible Biological Timer

2. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation.

3. Post-Translational Modifications of Protein Backbones: Unique Functions, Mechanisms, and Challenges

4. Asparagine Deamidation in a Complementarity Determining Region of a Recombinant Monoclonal Antibody in Complex with Antigen

5. Identification of multiple sources of charge heterogeneity in a recombinant antibody

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