Author

R. Milligan

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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Biophysics· 1 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Approach:statistical model· 1

Frequent Co-Authors

A. D. Davidson· 2 shared A. Alfieri· 1 shared A. E. Firth· 1 shared A. F. Thompson· 1 shared A. P. Beltrami· 1 shared A. Valpadashi· 1 shared C. Sindelar· 1 shared D. A. Matthews· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersMicrobiology

A. D. Davidson

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

The SARS-CoV-2 protein ORF3c is a mitochondrial modulator of innate immunity

H. Stewart, Y. Lu, S. O'Keefe, A. Valpadashi, L. D. Cruz-Zaragoza, H. A. Michel, S. K. Nguyen, G. W. Carnell, N. Lukhovitskaya, R. Milligan, I. Jungreis, V. Lulla, A. D. Davidson, D. A. Matthews, S. High, , A. E. Firth

This study identifies ORF3c as a SARS-CoV-2 protein that localizes to mitochondria and inhibits IFN-β production without affecting NF-κB or JAK-STAT signaling.

bioRxiv · Nov 15, 2022Microbiology

The SARS-CoV-2 Spike protein disrupts human cardiac pericytes function through CD147-receptor-mediated signalling: a potential non-infective mechanism of COVID-19 microvascular disease

E. Avolio, M. Carrabba, R. Milligan, M. Kavanagh Williamson, A. P. Beltrami, K. Gupta, K. T. Elvers, M. Gamez, R. Foster, K. Gillespie, F. Hamilton, D. Arnold, I. Berger, M. Caputo, A. D. Davidson, , P. Madeddu

This paper shows that SARS-CoV-2 Spike protein causes cardiac pericyte dysfunction through CD147-mediated signaling, without infecting the cells.

bioRxiv · Dec 21, 2020Cell Biology

The Kinesin-5 Tail Domain Directly Modulates the Mechanochemical Cycle of the Motor for Anti-Parallel Microtubule Sliding

T. Bodrug, E. Wilson-Kubalek, S. Nithianantham, A. F. Thompson, A. Alfieri, I. Gaska, J. Major, G. Debs, S. Inagaki, P. Gutierrez, L. Gheber, R. McKenney, C. Sindelar, R. Milligan, J. Stumpff, , J. Al-Bassam

This study shows the kinesin-5 tail domain regulates motor activity by modulating ATP hydrolysis and microtubule sliding, leading to slow motility and force generation.

bioRxiv · Aug 8, 2019Biophysics