Author

L. N. Anderson

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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Microbiology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 3 Approach:experimental assay· 2 Assay:proteomics· 2 Organism:bacteria (other)· 1 Organism:human· 1 Assay:imaging· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

W. C. Nelson· 2 shared A. Bhattacharjee· 1 shared A. D. McNaughton· 1 shared A. J. Wilson· 1 shared A. Jumpponen· 1 shared A. R. Frank· 1 shared A. T. Wright· 1 shared B.-J. M. Webb-Robertson· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBiochemistry

W. C. Nelson

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Profiling sorghum-microbe interactions with a specialized photoaffinity probe identifies key sorgoleone binders in Acinetobacter pittii

J. O. Kroll, E. M. Van Fossen, L. N. Anderson, A. D. McNaughton, D. Herrera, Y. Oda, A. J. Wilson, W. C. Nelson, N. Kumar, A. R. Frank, J. R. Elmore, P. Handakumbura, V. S. Lin, R. G. Egbert

This paper uses a sorgoleone-based photoaffinity probe to identify proteins in Acinetobacter pittii that bind sorgoleone, revealing potential pathways for microbial interaction with this plant metabolite.

bioRxiv · May 31, 2023Biochemistry

Fungal Mineral Weathering Mechanisms Revealed Through Direct Molecular Visualization

A. Bhattacharjee, O. Qafoku, J. A. Richardson, L. N. Anderson, K. Schwarz, L. M. Bramer, G. X. Lomas, D. J. Orton, Z. Zhu, M. H. Engelhard, M. E. Bowden, W. C. Nelson, A. Jumpponen, J. K. Jansson, K. S. Hofmockel, C. R. Anderton

This study visualizes fungal nutrient acquisition and transport through mineral interfaces in a soil micromodel, revealing mechanosensory responses and specific transport mechanisms.

bioRxiv · Oct 1, 2021 · PreprintMicrobiology

Proximity-dependent proteomics of the Chlamydia trachomatis inclusion membrane reveals functional interactions with endoplasmic reticulum exit sites

M. S. Dickinson, L. N. Anderson, B.-J. M. Webb-Robertson, J. R. Hansen, R. D. Smith, A. T. Wright, K. Hybiske

This study uses proximity-dependent biotinylation to identify inclusion membrane proteins of Chlamydia trachomatis and reveals a novel interaction with endoplasmic reticulum exit sites.

bioRxiv · Mar 19, 2018Microbiology