R
Rudolf K. F. Beran
Researcher at Yale University
Publications - 31
Citations - 2212
Rudolf K. F. Beran is an academic researcher from Yale University. The author has contributed to research in topics: Virus & Viral replication. The author has an hindex of 18, co-authored 26 publications receiving 1932 citations. Previous affiliations of Rudolf K. F. Beran include University of California, Los Angeles & National Institutes of Health.
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Journal ArticleDOI
Hepatitis B virus X protein identifies the Smc5/6 complex as a host restriction factor
Adrien Decorsiere,Henrik Mueller,Pieter C van Breugel,Fabien Abdul,Laetitia Gerossier,Rudolf K. F. Beran,Christine M. Livingston,Congrong Niu,Simon P. Fletcher,Olivier Hantz,Michel Strubin +10 more
TL;DR: A novel role for the Smc5/6 complex as a restriction factor selectively blocking extrachromosomal DNA transcription is uncovered, and HBx relieves the inhibition to allow productive hepatitis B virus gene expression.
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RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP
Sophie Dumont,Wei Cheng,Victor Serebrov,Rudolf K. F. Beran,Ignacio Tinoco,Anna Marie Pyle,Carlos Bustamante +6 more
TL;DR: This work follows in real time, at a resolution of two base pairs and 20 ms, the RNA translocation and unwinding cycles of a hepatitis C virus helicase (NS3) monomer, a representative superfamily-2 helicase essential for viral replication, and therefore a potentially important drug target.
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Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome'.
Annie Prud’Homme-Genereux,Rudolf K. F. Beran,Isabelle Iost,C. Shane Ramey,George A. Mackie,Robert W. Simons +5 more
TL;DR: It is demonstrated that one member of this family, CsdA, whose expression is induced by cold shock, interacts physically and functionally with RNase E, and is shown to be a flexible macromolecular machine capable of adapting to altered environmental conditions.
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Hepatitis C Virus NS2 Protein Contributes to Virus Particle Assembly via Opposing Epistatic Interactions with the E1-E2 Glycoprotein and NS3-NS4A Enzyme Complexes
TL;DR: A reverse genetic analysis of NS2 in the context of a chimeric genotype 2a infectious cell culture system reveals a complex network of interactions involving NS2 and other viral structural and nonstructural proteins during virus assembly.
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The C Terminus of Hepatitis C Virus NS4A Encodes an Electrostatic Switch That Regulates NS5A Hyperphosphorylation and Viral Replication
Brett D. Lindenbach,Béla M. Prágai,Roland Montserret,Rudolf K. F. Beran,Anna Marie Pyle,François Penin,Charles M. Rice +6 more
TL;DR: The structure and function of the C-terminal acidic region of NS4A is examined through site-directed mutagenesis of a Con1 subgenomic replicon and through biophysical characterization of a synthetic peptide corresponding to this region, indicating that this region can adopt an alpha-helical conformation but that this folding requires neutralization of a cluster of acidic residues.