Hepatitis Delta Virus

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  Subject Areas on Research

  • A circular trans-acting hepatitis delta virus ribozyme. 
  • A conserved bulged adenosine in a peripheral duplex of the antigenomic HDV self-cleaving RNA reduceskinetic trapping of inactive conformations. 
  • A nested double pseudoknot is required for self-cleavage activity of both the genomic and antigenomic hepatitis delta virus ribozymes. 
  • A pH-sensitive RNA tertiary interaction affects self-cleavage activity of the HDV ribozymes in the absence of added divalent metal ion. 
  • A pseudoknot-like structure required for efficient self-cleavage of hepatitis delta virus RNA. 
  • A single nucleotide linked to a switch in metal ion reactivity preference in the HDV ribozymes. 
  • A toggle duplex in hepatitis delta virus self-cleaving RNA that stabilizes an inactive and a salt-dependent pro-active ribozyme conformation. 
  • Assessment of disparate structural features in three models of the hepatitis delta virus ribozyme. 
  • Catalytic strategies of the hepatitis delta virus ribozymes. 
  • Chemical rescue, multiple ionizable groups, and general acid-base catalysis in the HDV genomic ribozyme. 
  • Circular ribozymes generated in Escherichia coli using group I self-splicing permuted intron-exon sequences. 
  • Cis- and trans-acting ribozymes from a human pathogen, hepatitis delta virus. 
  • Cleavage of oligoribonucleotides by a ribozyme derived from the hepatitis delta virus RNA sequence. 
  • Core sequences and a cleavage site wobble pair required for HDV antigenomic ribozyme self-cleavage. 
  • Core-associated non-duplex sequences distinguishing the genomic and antigenomic self-cleaving RNAs of hepatitis delta virus. 
  • Energetic contribution of non-essential 5' sequence to catalysis in a hepatitis delta virus ribozyme. 
  • Epidemiology of hepatitis B in eastern Kenya. 
  • Evidence that genomic and antigenomic RNA self-cleaving elements from hepatitis delta virus have similar secondary structures. 
  • Experimental evidence for the secondary structure of the hepatitis delta virus ribozyme. 
  • HDV ribozyme activity in monovalent cations. 
  • HDV ribozymes. 
  • Hepatitis delta virus ribozymes fold to generate a solvent-inaccessible core with essential nucleotides near the cleavage site phosphate. 
  • Imidazole rescue of a cytosine mutation in a self-cleaving ribozyme. 
  • Increasing utilization of human T-cell lymphotropic virus (+) donors in liver transplantation: is it safe? 
  • Involvement of a cytosine side chain in proton transfer in the rate-determining step of ribozyme self-cleavage. 
  • Kinetic scheme for intermolecular RNA cleavage by a ribozyme derived from hepatitis delta virus RNA. 
  • Molecular biology. Versatility of self-cleaving ribozymes. 
  • New tools provide a second look at HDV ribozyme structure, dynamics and cleavage. 
  • Optimal self-cleavage activity of the hepatitis delta virus RNA is dependent on a homopurine base pair in the ribozyme core. 
  • Reversible cross-linking combined with immunoprecipitation to study RNA-protein interactions in vivo. 
  • Ribozyme activity in the genomic and antigenomic RNA strands of hepatitis delta virus. 
  • Ribozyme cleavage of a 2,5-phosphodiester linkage: mechanism and a restricted divalent metal-ion requirement. 
  • Secondary structure of the self-cleaving RNA of hepatitis delta virus: applications to catalytic RNA design. 
  • Self-cleavage of hepatitis delta virus genomic strand RNA is enhanced under partially denaturing conditions. 
  • Self-cleaving ribozymes of hepatitis delta virus RNA. 
  • The hepatitis delta virus large antigen is farnesylated both in vitro and in animal cells. 
  • The poly(A) site sequence in HDV RNA alters both extent and rate of self-cleavage of the antigenomic ribozyme. 
  • The self-cleaving domain from the genomic RNA of hepatitis delta virus: sequence requirements and the effects of denaturant. 
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  Keywords of People

  • Been, Michael Douglas, Professor Emeritus of Biochemistry, Biochemistry
  • Richardson, David C., Professor of Biochemistry, Duke Cancer Institute