Author

M. A. Jarva

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· 3 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Organism:mouse· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

A. John· 2 shared E. D. Goddard-Borger· 2 shared J. P. Lingford· 2 shared A. Schmitt· 1 shared G. M. Dunny· 1 shared H. Hirt· 1 shared J. ter Beek· 1 shared K. Jarman· 1 shared

Activity by Year

2019-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersBiochemistry

A. John

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Author profile →

3 papers

Recent·Most cited

Enterococcal PrgA extends far outside the cell and provides surface exclusion to protect against unwanted conjugation

A. Schmitt, H. Hirt, M. A. Jarva, W.-S. Sun, J. ter Beek, G. M. Dunny, R. P.-A. Berntsson

This paper reports the structure and function of Enterococcus faecalis PrgA, showing it extends outside the cell to provide surface exclusion and reduce plasmid uptake.

bioRxiv · Jun 18, 2020Biochemistry

Structural basis of substrate recognition and catalysis by fucosyltransferase 8

M. A. Jarva, M. Dramicanin, J. P. Lingford, R. Mao, A. John, K. Jarman, R. W. Grinter, E. D. Goddard-Borger

This study determines the structural basis of substrate recognition and catalysis by FUT8 through crystal structures and simulations, revealing conformational changes and dimerization roles in substrate binding.

bioRxiv · Feb 14, 2020Biochemistry

Trefoil factors share a lectin activity that defines their role in mucus

M. A. Jarva, J. P. Lingford, A. John, N. E. Scott, E. D. Goddard-Borger

This study identifies trefoil factors as divalent lectins that bind GlcNAc--1,4-Gal disaccharides, contributing to mucus viscoelasticity through non-covalent glycoprotein cross-linking.

bioRxiv · Nov 29, 2019Biochemistry