J
Janet M. Rozovics
Researcher at University of California, Irvine
Publications - 9
Citations - 673
Janet M. Rozovics is an academic researcher from University of California, Irvine. The author has contributed to research in topics: Picornavirus & RNA. The author has an hindex of 8, co-authored 9 publications receiving 546 citations. Previous affiliations of Janet M. Rozovics include Loma Linda University.
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Journal ArticleDOI
SARS Coronavirus nsp1 Protein Induces Template-Dependent Endonucleolytic Cleavage of mRNAs: Viral mRNAs Are Resistant to nsp1-Induced RNA Cleavage
Cheng Huang,Kumari G. Lokugamage,Janet M. Rozovics,Krishna Narayanan,Bert L. Semler,Shinji Makino +5 more
TL;DR: It is revealed that the nsp1 induced endonucleolytic RNA cleavage mainly near the 5′ untranslated region of capped mRNA templates, which may be an important strategy by which the virus circumvents the action of nsp 1 leading to the efficient accumulation of viral mRNAs and viral proteins during infection.
Journal ArticleDOI
An RNA virus hijacks an incognito function of a DNA repair enzyme
Richard Virgen-Slane,Janet M. Rozovics,Kerry D. Fitzgerald,Tuan Ngo,Wayne Chou,Gerbrand J. van der Heden van Noort,Dmitri V. Filippov,Paul D. Gershon,Bert L. Semler +8 more
TL;DR: The purification and identification of VPg unlinkase as the DNA repair enzyme, 5′-tyrosyl–DNA phosphodiesterase-2 (TDP2) is reported, revealing a unique RNA repair-like function for TDP2 and suggesting an unusual role in host–pathogen interactions for this cellular enzyme.
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Alphacoronavirus Transmissible Gastroenteritis Virus nsp1 Protein Suppresses Protein Translation in Mammalian Cells and in Cell-Free HeLa Cell Extracts but Not in Rabbit Reticulocyte Lysate
Cheng Huang,Kumari G. Lokugamage,Janet M. Rozovics,Krishna Narayanan,Bert L. Semler,Shinji Makino +5 more
TL;DR: The data suggested that HeLa cell extracts and cultured host cells, but not RRL, contain a host factor(s) that is essential for TGEV nsp1-induced translational suppression.
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Cellular mRNA Decay Protein AUF1 Negatively Regulates Enterovirus and Human Rhinovirus Infections
TL;DR: It is demonstrated that all four isoforms of AUF1 bind directly to stem-loop IV of the poliovirus 5′ NCR, an interaction that is inhibited through proteolytic cleavage ofAUF1 by the viral proteinase 3CD.
Journal ArticleDOI
Picornavirus Modification of a Host mRNA Decay Protein
Janet M. Rozovics,Amanda J. Chase,Andrea L. Cathcart,Wayne Chou,Paul D. Gershon,Saiprasad G. Palusa,Jeffrey Wilusz,Bert L. Semler +7 more
TL;DR: Experiments suggest that AUF1, a host RNA binding protein involved in mRNA decay, plays a role in the infectious cycle of picornaviruses such as poliovirus and human rhinovirus and how small RNA viruses manipulate the activities of host cell RNA binding proteins to ensure a faithful intracellular replication cycle is illuminated.