Author

N. Bulleid

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· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:C. elegans· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

X. Cao· 2 shared A. D. Winter· 1 shared A. P. Page· 1 shared E. Tjahjono· 1 shared I. L. Johnstone· 1 shared L. J. Beltran· 1 shared M. A. Pringle· 1 shared M. van Lith· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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2 shared papersCell Biology

X. Cao

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Author profile →

3 papers

Recent·Most cited

Dietary derived Vitamin B12 protects the nematode Caenorhabditis elegans from thiol reducing agents.

A. D. Winter, E. Tjahjono, L. J. Beltran, I. L. Johnstone, N. Bulleid, A. P. Page

This study identifies RIPS-1, a methyl transferase in C. elegans that protects against thiol reducing agents, highlighting the role of dietary vitamin B12 in metabolic processes and reductive stress resistance.

bioRxiv · May 3, 2022 · PreprintBiochemistry

The Mammalian Cytosolic Thioredoxin Reductase Pathway Acts via a Membrane Protein to Reduce ER-localised Proteins

X. Cao, S. Lilla, Z. Cao, M. A. Pringle, O. B. Oka, P. J. Robinson, T. Szmaja, M. van Lith, S. Zanivan, N. Bulleid

The paper demonstrates that the cytosolic thioredoxin reductase pathway reduces ER-localized proteins via a membrane protein, essential for ER redox homeostasis and protein folding.

Journal of Cell Science · Apr 30, 2020Peer-reviewedCell Biology

Protein secondary structure determines the temporal relationship between folding and disulfide formation

P. Robinson, S. Kanemura, X. Cao, N. Bulleid

This study investigates how protein secondary structure influences disulfide formation during folding, showing that disulfide-driven and folding-driven mechanisms depend on structural features.

bioRxiv · Sep 12, 2019Biochemistry