Author

A. J. Domma

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 4 Assay:proteomics· 4 Research Focus:host-pathogen & immune response· 3 Research Focus:cell type annotation· 1

Frequent Co-Authors

J. P. Kamil· 4 shared H. Zhang· 3 shared C. C. Nguyen· 2 shared F. Goodrum· 2 shared M. N. A. Siddiquey· 1 shared N. J. Moorman· 1 shared N. Moorman· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

7 top collaborators · 13 mutual co-author links

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4 shared papersMicrobiology

J. P. Kamil

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4 papers

Recent·Most cited

Human cytomegalovirus attenuates AKT activity by destabilizing insulin receptor substrate proteins

A. J. Domma, F. Goodrum, N. J. Moorman, J. P. Kamil

This study shows that human cytomegalovirus (HCMV) inactivates AKT by using UL38 to degrade IRS1, which is necessary for AKT activation during infection.

bioRxiv · Apr 17, 2023Microbiology

The AKT Forkhead box O transcription factor axis regulates human cytomegalovirus replication

H. Zhang, A. J. Domma, F. Goodrum, N. Moorman, J. P. Kamil

This study shows that HCMV inactivates AKT to promote FOXO3a nuclear localization, which is required for efficient viral replication.

bioRxiv · Apr 14, 2022Microbiology

ER reorganization and intracellular retention of CD58 are functionally independent properties of the human cytomegalovirus ER resident glycoprotein UL148

C. C. Nguyen, A. J. Domma, H. Zhang, J. P. Kamil

This study shows that ER reorganization and CD58 retention by HCMV UL148 are independent functions, as mutations affecting one do not impact the other.

bioRxiv · Aug 27, 2019Microbiology

The human cytomegalovirus ER resident glycoprotein UL148 activates the unfolded protein response

M. N. A. Siddiquey, H. Zhang, C. C. Nguyen, A. J. Domma, J. P. Kamil

This paper identifies UL148, a human cytomegalovirus glycoprotein, as an activator of the unfolded protein response (UPR) in both infected and uninfected cells.

bioRxiv · May 23, 2018Microbiology