Journal ArticleDOI
Characterization of rotavirus replication intermediates: a model for the assembly of single-shelled particles.
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TLDR
Analysis of the formation and turnover of RIs in infected cells pulse-labeled with 35S-amino acids supports a hypothesis that rotavirus single-shelled particles are assembled in vivo by the sequential addition of VP2 and VP6 to precore RIs consisting of VP1, VP3, VP9, NS35, and NS34.About:
This article is published in Virology.The article was published on 1989-10-01. It has received 144 citations till now. The article focuses on the topics: RNA-dependent RNA polymerase & RNA.read more
Citations
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Journal ArticleDOI
A conserved double-stranded RNA-binding domain.
TL;DR: On the basis of the binding studies and computer analysis, a consensus sequence is derived that defines a 65- to 68-amino acid dsRNA-binding domain, the minimal region that binds ds RNA.
Journal ArticleDOI
Reassortment in segmented RNA viruses: mechanisms and outcomes.
TL;DR: Recent studies that examined the mechanisms and outcomes of reassortment for three well-studied viral families are discussed and how these findings provide new perspectives on the replication and evolution of segmented RNA viruses are discussed.
Journal ArticleDOI
Rotavirus Replication: Plus-Sense Templates for Double-Stranded RNA Synthesis Are Made in Viroplasms
TL;DR: It is proposed that plus-strand RNAs synthesized within viroplasms are the primary source of templates for genome replication and that trafficking pathways do not exist within the cytosol that transport plus-strate RNAs to viroPLasms.
Journal ArticleDOI
Expression of rotavirus VP2 produces empty corelike particles.
TL;DR: The results definitively show the existence of an innermost protein shell in rotavirus which is formed independently of other rotav virus proteins, and have implications for schemes ofRotavirus morphogenesis.
Journal ArticleDOI
Mechanism of interferon action: Identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2α protein kinase
TL;DR: Computer analysis revealed that the human protein P1 sequence corresponding to amino acid residues within the N-terminal RNA binding domain displays high homology with two animal virus proteins which possess RNA binding activity and two proteins of unknown function, but which are likely RNA binding proteins.
References
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Journal ArticleDOI
Interactions between small nuclear ribonucleoprotein particles in formation of spliceosomes
TL;DR: Electrophoretic separation of ribonucleoprotein particles in a nondenaturing gel was used to analyze the splicing of mRNA precursors and surprisingly, U4 snRNP was not part of the intron-containing complex, suggesting that U4/6 snR NP disassembles and assembles during splicing.
Journal ArticleDOI
Tables for estimating sedimentation through linear concentration gradients of sucrose solution
TL;DR: A set of tables is presented for use in the design and interpretation of centrifuge experiments involving sedimentation in linear sucrose density gradients that can be used to predict the position of a material of given sedimentation coefficient and density.
Journal ArticleDOI
Proteolytic enhancement of rotavirus infectivity: molecular mechanisms.
TL;DR: The polypeptide compositions of single- shelled and double-shelled simian rotavirus particles were modified by exposure to proteolytic enzymes, and the role of cleavage activation in other virus-specific biological functions (e.g., hemagglutination and virulence).
Journal ArticleDOI
Three-dimensional structure of rotavirus.
TL;DR: The three-dimensional structures of double and single-shelled simian rotavirus have been determined to a resolution of 40 A by image processing electron micrographs of unstained, unfixed virus particles embedded in vitreous ice and it is demonstrated that the icosahedral surface lattices in these structures have a triangulation number of 13 in a left-handed configuration.
Book ChapterDOI
Rotaviruses: A Review
TL;DR: The Rotavirus genus of the Reoviridae consists of a number of antigenically related and morphologically identical viruses that cause enteritis, primarily in young mammals and avians.