Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A conserved bulged adenosine in a peripheral duplex of the antigenomic HDV self-cleaving RNA reduceskinetic trapping of inactive conformations.

Nucleic acids research - 1 Feb 1999

Perrotta A T, Nikiforova O, Been M D

Abstract excerpt

In the ribozyme of hepatitis delta virus antigenomic RNA, two short duplexes, P2 and P2a, stabilize the active self-cleaving structure. However, P2a also promotes kinetic trapping of non-native structures. A bulged adenosine (A14) separates P2a and P2; this bulged A is conserved in clinical isolates of HDV but is unlikely to be physically close to the cleavage site phosphate in the ribozyme structure. Removing...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Base Sequence
Share to Kinetics
Share to Membrane Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Nucleic Acid Conformation

Share to RNA, Viral

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 9889275
DOI: 10.1093/nar/27.3.795
PMCID: PMC148249

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A conserved bulged adenosine in a peripheral duplex of the antigenomic HDV self-cleaving RNA reduceskinetic trapping of inactive conformations.PMID 9889275Read ↗

Design of a highly reactive HDV ribozyme sequence uncovers facilitation of RNA folding by alternative pairings and physiological ionic strength.Semantic proximity Read ↗

The folding pathway of the genomic hepatitis delta virus ribozyme is dominated by slow folding of the pseudoknots.Semantic proximity Read ↗

A sequence element necessary for self-cleavage of the antigenomic hepatitis delta RNA in 20 M formamide.Semantic proximity Read ↗

Wobble pairs of the HDV ribozyme play specific roles in stabilization of active site dynamics.Semantic proximity Read ↗

Hepatitis delta antigen requires a flexible quasi-double-stranded RNA structure to bind and condense hepatitis delta virus RNA in a ribonucleoprotein complex.Semantic proximity Read ↗

Self-association of adenine-dependent hairpin ribozymes.Semantic proximity Read ↗

Functional involvement of G8 in the hairpin ribozyme cleavage mechanism.Semantic proximity Read ↗

Wild-type is the optimal sequence of the HDV ribozyme under cotranscriptional conditions.Semantic proximity Read ↗

Mutational studies uncover non-native structure in the dimeric kinetic intermediate of the H2A-H2B heterodimer.Semantic proximity Read ↗

Unbiased in vitro selection reveals the unique character of the self-cleaving antigenomic HDV RNA sequence.Semantic proximity Read ↗

Mutational analysis of the stability of the H2A and H2B histone monomers.Semantic proximity Read ↗

Characterization of the trans Watson-Crick GU base pair located in the catalytic core of the antigenomic HDV ribozyme.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.