Author

M. Kleer

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· 5 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Organism:human· 6 Research Focus:host-pathogen & immune response· 5 Assay:proteomics· 4 Assay:bulk RNA-seq· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

J. A. Corcoran· 4 shared C. McCormick· 2 shared C.-A. Robinson· 2 shared D. A. Khaperskyy· 2 shared E. L. Castle· 2 shared E. S. Pringle· 2 shared M. P. Bui-Marinos· 2 shared P. D. Slaine· 2 shared

Activity by Year

2017-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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4 shared papersMicrobiology

J. A. Corcoran

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Author profile →

6 papers

Recent·Most cited

Nsp1 proteins of human coronaviruses HCoV-OC43 and SARS-CoV2 inhibit stress granule formation

S. M. Dolliver, M. Kleer, M. P. Bui-Marinos, S. Ying, J. A. Corcoran, D. Khaperskyy

This study shows that HCoV-OC43 and SARS-CoV2 inhibit stress granule formation through viral proteins N and Nsp1, with Nsp1 also reducing G3BP1 levels and causing nuclear retention of TIAR.

bioRxiv · May 2, 2022Microbiology

A panel of KSHV mutants in the polycistronic kaposin locus for precise analysis of individual protein products

M. Kleer, G. MacNeil, E. S. Pringle, J. A. Corcoran

The paper creates a panel of KSHV mutants to analyze the individual roles of kaposin proteins in viral replication and pathogenesis.

bioRxiv · Jun 11, 2021Microbiology

Kaposi's sarcoma-associated herpesvirus (KSHV) utilizes the NDP52/CALCOCO2 selective autophagy receptor to disassemble processing bodies

C.-A. Robinson, G. K. Singh, M. Kleer, E. L. Castle, B. Q. Boudreau, J. A. Corcoran

This paper shows KSHV uses the NDP52/CALCOCO2 autophagy receptor to disassemble processing bodies, enhancing inflammation during infection.

bioRxiv · Feb 7, 2021Cell Biology

Human coronaviruses disassemble processing bodies

M. Kleer, R. P. Mulloy, C.-A. Robinson, D. Evseev, M. P. Bui-Marinos, E. L. Castle, A. Banerjee, S. Mubareka, K. Mossman, J. A. Corcoran

This study shows SARS-CoV-2 and related coronaviruses induce processing body disassembly, with SARS-CoV-2's N protein uniquely causing this effect, leading to increased proinflammatory cytokine production.

bioRxiv · Nov 8, 2020Microbiology

Thiopurines activate an antiviral unfolded protein response that blocks viral glycoprotein accumulation in cell culture infection model

P. D. Slaine, M. Kleer, B. Duguay, E. S. Pringle, E. Kadijk, S. Ying, A. D. Balgi, M. Roberge, C. McCormick, D. A. Khaperskyy

This study shows that thiopurines 6-TG and 6-TGo activate the UPR to block viral glycoprotein accumulation in cell culture models of influenza and coronavirus infections.

bioRxiv · Sep 30, 2020Microbiology

Stress granule-inducing eukaryotic translation initiation factor 4A inhibitors block influenza A virus replication

P. D. Slaine, M. Kleer, N. Smith, D. A. Khaperskyy, C. McCormick

This paper shows that eIF4A inhibitors like PatA and silvestrol block influenza A virus replication by inducing stress granules and inhibiting viral protein synthesis.

bioRxiv · Oct 2, 2017Microbiology