Author

K. A. Ciazynska

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 1 Immunology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Assay:protein structure· 2 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

J. A. G. Briggs· 3 shared X. Xiong· 3 shared A. P. Carter· 2 shared K. Qu· 2 shared L. C. James· 2 shared R. Doffinger· 2 shared S. Ebrahimi· 2 shared B. Liu· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersMicrobiology

J. A. G. Briggs

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Engineered disulfide reveals structural dynamics of locked SARS-CoV-2 spike

K. Qu, Q. Chen, K. A. Ciazynska, B. Liu, X. Zhang, J. Wang, Y. He, J. Guan, J. He, T. Liu, A. P. Carter, X. Xiong, J. A. G. Briggs

This study engineers a SARS-CoV-2 spike protein with a disulfide bond to stabilize the locked conformation, revealing structural dynamics and the role of domain D in conformational changes and viral fitness.

PLOS Pathogens · Jul 29, 2022Peer-reviewedMicrobiology

SARS-CoV-2 spike protein arrested in the closed state induces potent neutralizing responses

G. W. Carnell, K. A. Ciazynska, D. A. Wells, X. Xiong, E. T. Aguinam, S. H. McLaughlin, D. Mallery, S. Ebrahimi, L. Ceron-Gutierrez, L. C. James, R. Doffinger, J. L. Heeney, J. A. G. Briggs

This study evaluates closed-state SARS-CoV-2 spike protein immunization in mice, finding it induces potent neutralizing antibodies and T-cell responses, with unique binding properties compared to standard S protein constructs.

bioRxiv · Jan 14, 2021Immunology

A thermostable, closed, SARS-CoV-2 spike protein trimer.

X. Xiong, K. Qu, K. A. Ciazynska, M. Hosmillo, A. P. Carter, S. Ebrahimi, Z. Ke, S. H. W. Scheres, L. Bergamaschi, G. L. Grice, Y. Zhang, The CITIID-NIHR COVID-19 BioResource Collaboration, J. A. Nathan, S. Baker, L. C. James, , J. A. G. Briggs

This paper designs a thermostable, closed SARS-CoV-2 spike protein trimer that remains in the pre-fusion state and can be used in serological assays.

bioRxiv · Jun 15, 2020Biochemistry