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pro vyhledávání: '"Kenneth E. Murray"'
Publikováno v:
Virology. 375:412-423
Genome replication of mammalian orthoreovirus (MRV) occurs in cytoplasmic inclusion bodies called viral factories. Nonstructural protein microNS, encoded by genome segment M3, is a major constituent of these structures. When expressed without other v
Autor:
Max L. Nibert, Kenneth E. Murray
Publikováno v:
Journal of Virology. 81:4572-4584
Millimolar concentrations of guanidine hydrochloride (GuHCl) are known to inhibit the replication of many plant and animal viruses having positive-sense RNA genomes. For example, GuHCl reversibly interacts with the nucleotide-binding region of poliov
Publikováno v:
Journal of Virology. 78:1393-1402
cis -acting RNA sequences and structures in the 5′ and 3′ nontranslated regions of poliovirus RNA interact with host translation machinery and viral replication proteins to coordinately regulate the sequential translation and replication of polio
Autor:
Kenneth E. Murray, David J. Barton
Publikováno v:
Journal of Virology. 77:4739-4750
The cis -acting replication element (CRE) is a 61-nucleotide stem-loop RNA structure found within the coding sequence of poliovirus protein 2C. Although the CRE is required for viral RNA replication, its precise role(s) in negative- and positive-stra
Publikováno v:
Journal of Virology
Chimeric poliovirus RNAs, possessing the 5′ nontranslated region (NTR) of hepatitis C virus in place of the 5′ NTR of poliovirus, were used to examine the role of the poliovirus 5′ NTR in viral replication. The chimeric viral RNAs were incubate
Autor:
Kenneth E. Murray, Vidya Sagar
Publikováno v:
Virus research. 183
Mammalian orthoreovirus mRNAs possess short 5′ UTR, lack 3′ poly(A) tails, and may lack 5′ cap structures at late times post-infection. As such, the mechanisms by which these viral mRNAs recruit ribosomes remain completely unknown. Toward addre
Publikováno v:
The Journal of biological chemistry. 279(6)
The mammalian Orthoreovirus (mORV) core particle is an icosahedral multienzyme complex for viral mRNA synthesis and provides a delimited system for mechanistic studies of that process. Previous genetic results have identified the mORV mu2 protein as
Publikováno v:
RNA (New York, N.Y.). 7(8)
The 5'-terminal 88 nt of poliovirus RNA fold into a cloverleaf RNA structure and form ribonucleoprotein complexes with poly(rC) binding proteins (PCBPs; AV Gamarnik, R Andino, RNA, 1997, 3:882-892; TB Parsley, JS Towner, LB Blyn, E Ehrenfeld, BL Seml
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