Author

D. S. Alonzi

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

Biology Disciplines

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Biochemistry· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Assay:structural biology· 2 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

N. Zitzmann· 3 shared A. V. Chandran· 2 shared M. Hensen· 2 shared S. Vasiljevic· 2 shared A. J. Thompson· 1 shared A. Kumar· 1 shared A. Lia· 1 shared A. Santino· 1 shared

Activity by Year

2019-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersBiochemistry

N. Zitzmann

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Author profile →

3 papers

Recent·Most cited

Analysis of SARS-CoV-2 spike glycosylation reveals shedding of a vaccine candidate

J. Brun, S. Vasiljevic, B. Gangadharan, M. Hensen, A. V. Chandran, M. L. Hill, J. L. Kiappes, R. A. Dwek, D. S. Alonzi, W. B. Struwe, N. Zitzmann

The paper compares glycosylation patterns between SARS-CoV-2 viral spikes and a vaccine candidate, showing differences in secretion pathways and potential implications for immune response and vaccine design.

bioRxiv · Nov 16, 2020 · PreprintBiochemistry

Structure of human endo-α-1,2-mannosidase (MANEA), an antiviral host-glycosylation target

L. F. Sobala, P. Z. Fernandes, Z. Hakki, A. J. Thompson, J. D. Howe, M. Hill, N. Zitzmann, S. Davies, Z. Stamataki, T. D. Butters, D. S. Alonzi, S. J. Williams, G. J. Davies

The paper reports the structure of human MANEA and inhibitor complexes, revealing its mechanism and informing the development of antiviral agents against bovine viral diarrhea and dengue viruses.

bioRxiv · Jun 30, 2020Biochemistry

Clamping, bending, and twisting inter-domain motions in the misfold-recognising portion of UDP glucose:glycoprotein glucosyl-transferase.

C. P. Modenutti, J. I. Blanco Capurro, R. Ibba, S. Vasiljevic, M. Hensen, D. S. Alonzi, A. V. Chandran, J. C. Hill, J. Rushton, A. Kumar, S. Rubichi, A. Lia, G. Tax, L. Marti, A. Santino, , P. Roversi

This study uses molecular dynamics simulations and structural analysis to characterize inter-domain motions in UGGT, revealing conformational flexibility and a proposed Parodi limit for substrate recognition.

bioRxiv · Dec 25, 2019Biochemistry