Author

A. V. Chandran

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 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 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

M. Hensen· 3 shared N. Zitzmann· 3 shared S. Vasiljevic· 3 shared A. Lia· 2 shared A. Santino· 2 shared C. P. Modenutti· 2 shared D. S. Alonzi· 2 shared J. C. Hill· 2 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiochemistry

M. Hensen

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Author profile →

3 papers

Recent·Most cited

A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint

K. P. Guay, R. Ibba, J. L. Kiappes, M. De Benedictis, I. Zeni, J. D. Le Cornu, M. Hensen, A. V. Chandran, A. L. Kantsadi, A. T. Caputo, J. I. Blanco Capurro, Y. Bayo, J. C. Hill, K. Hudson, A. Lia, , P. Roversi

This paper identifies a small molecule inhibitor of UGGT, a key enzyme in ER glycoprotein folding, and demonstrates its inhibitory effects in vitro and in cell culture.

bioRxiv · Jun 21, 2022Biochemistry

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

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