Author

M. J. Plevin

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· 1 Microbiology· 1 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Organism:chicken / avian· 1 Assay:long-read sequencing· 1 Organism:plant (other)· 1

Frequent Co-Authors

C. Degut· 3 shared A. Bateman· 1 shared A. J. McCormick· 1 shared A. Lafita· 1 shared A. N. St John· 1 shared A. Salter· 1 shared C. G. Baumann· 1 shared E. Paci· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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3 shared papersPlant Biology

C. Degut

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

A promiscuous mechanism to phase separate eukaryotic carbon fixation in the green lineage

J. Barrett, M. I. S. Naduthodi, Y. Mao, C. Degut, S. Musial, A. Salter, M. C. Leake, M. J. Plevin, A. J. McCormick, J. N. Blaza, L. Mackinder

The paper identifies a conserved linker protein from Chlorella that can phase separate Rubisco in Chlamydomonas and some plants, enabling cross-species pyrenoid formation.

bioRxiv · Apr 9, 2024Plant Biology

Fundamental steps in Minichromosome Maintenance complex assembly are conserved from archaea to eukaryotes

O. W. Noble, C. Degut, M. R. Hodgkinson, J. P. Chong, M. J. Plevin

This study identifies a conserved MCM assembly mechanism in archaea and eukaryotes by analyzing the structure and assembly pathway of a mesophilic archaeal MCM.

bioRxiv · Aug 11, 2023 · PreprintBiochemistry

Periscope Proteins are variable length regulators of bacterial cell surface interactions

F. Whelan, A. Lafita, J. Gilburt, C. Degut, S. C. Griffiths, H. T. Jenkins, A. N. St John, E. Paci, J. W. B. Moir, M. J. Plevin, C. G. Baumann, A. Bateman, J. R. Potts

The paper identifies Periscope Proteins as variable-length bacterial surface regulators that influence host interactions through domain number variation.

bioRxiv · Dec 24, 2020Microbiology