Author

Maria Sandkvist

University of MichiganORCID 0000-0001-6605-4720Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Assay:proteomics· 2 Organism:Arabidopsis· 1 Research Focus:cell type annotation· 1 Research Focus:protein folding & dynamics· 1 Organism:virus· 1

Frequent Co-Authors

Cameron S. RobertsiD· 2 shared Colby GuraiD· 1 shared Eliese Potocek· 1 shared Kwame Kannatey-Asibu· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

4 top collaborators · 4 mutual co-author links

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2 shared papersMicrobiology

Cameron S. RobertsORCID

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2 papers

Recent·Most cited

MicrobiologyJournal of BacteriologyPeer-reviewedJun 12, 2026

The GlyGly-CTERM domain functions as an independent motif that targets proteins to rhombosortase in Vibrio cholerae

Cameron S. Roberts, Kwame Kannatey-Asibu, Eliese Potocek, Maria Sandkvist

The paper investigates the GlyGly-CTERM motif's role in targeting proteins to rhombosortase in V. cholerae, showing it enables membrane association but requires a secondary signal for outer membrane translocation.

1 citation

virusproteomics

𝕏 PostBluesky

MicrobiologybioRxivPreprintSep 9, 2025

The Type II Secretion System Utilizes AsmA-like Protein GspN to Facilitate Transport of Lipoproteins to the Cell Surface of Acinetobacter baumannii

Cameron S. Roberts, Colby Gura, Maria Sandkvist

This paper identifies GspN as a key component of the T2SS required for the outer membrane translocation and surface localization of lipoproteins in A. baumannii.

DOI 10.1101/2025.09.09.675180

Arabidopsisproteomics

𝕏 PostBluesky