Author

R. A. Dunstan

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 Microbiology· 1

Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 2 Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Organism:Arabidopsis· 1 Research Focus:cell signaling & trafficking· 1 Approach:machine learning (classical)· 1 Assay:protein structure· 1 Assay:structural biology· 1

Frequent Co-Authors

T. Lithgow· 3 shared C. J. Stubenrauch· 2 shared R. S. Bamert· 2 shared A. Rocker· 1 shared A. Y. Peleg· 1 shared C. Greening· 1 shared C. Huang· 1 shared C. T. Webb· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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3 shared papersBiochemistry

T. Lithgow

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Dual Recognition of Multiple Signals in Bacterial Outer Membrane Proteins Enhance Assembly and Maintain Membrane Integrity

E. M. Germany, N. Thewasano, K. Imai, Y. Maruno, R. S. Bamert, C. J. Stubenrauch, R. A. Dunstan, Y. Ding, Y. Nakajima, X. Lai, C. T. Webb, K. Hidaka, K. S. Tan, H.-H. Shen, T. Lithgow, T. Shiota

The paper identifies an additional signal in bacterial outer membrane proteins that enhances assembly efficiency and maintains membrane integrity through interaction with BamD.

bioRxiv · Oct 29, 2021Biochemistry

The component parts of bacteriophage virions accurately defined by a machine-learning approach built on evolutionary features.

T. Y. Thung, M. E. White, W. Dai, J. J. Wilksch, R. S. Bamert, A. Rocker, C. J. Stubenrauch, D. Williams, C. Huang, R. B. Schittelhelm, J. J. Barr, E. Jameson, S. McGowan, Y. Zhang, J. Wang, , T. Lithgow

This paper develops a machine learning tool called STEP3 to accurately define bacteriophage virion components using evolutionary features, validated with mass spectrometry.

mSystems · Jun 29, 2021Peer-reviewedMicrobiology

BonA from Acinetobacter baumannii forms a divisome-localized decamer that supports outer envelope function

R. Grinter, F. C. Morris, R. A. Dunstan, P. M. Leung, M. Belousoff, S. D. Gunasinghe, S. Beckham, A. Y. Peleg, C. Greening, J. Li, E. Heinz, T. Lithgow

This study identifies BonA as an outer membrane protein in Acinetobacter baumannii that forms a transient decamer, supports outer envelope function, and is involved in cell division and motility.

bioRxiv · Sep 1, 2020Biochemistry