ArticleNucleic acids research2008
Solution structure of stem-loop alpha of the hepatitis B virus post-transcriptional regulatory element.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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Who cites it
21 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The Post-Transcriptional Regulatory Element of Hepatitis B Virus: From Discovery to Therapy.Viruses · 2024Pooled it
- Application of ddPCR for diagnosis and treatment monitoring of visceral leishmaniasis patients: addition of an ultrasensitive tool to the diagnostic arsenal.Microbiology spectrum · 2026Article
- Hepatitis B virus genotypes A1 and A2 have distinct replication phenotypes due to polymorphisms in the HBx gene.PLoS pathogens · 2025Article
- The host geneActa biochimica et biophysica Sinica · 2024Article
- The role of structure in regulatory RNA elements.Bioscience reports · 2024Review
- Host Poly(A) Polymerases PAPD5 and PAPD7 Provide Two Layers of Protection That Ensure the Integrity and Stability of Hepatitis B Virus RNA.Journal of virology · 2021Article
- Prevalence and Risk Factors Associated with Hepatitis B and Hepatitis C Infections among Patients Undergoing Hemodialysis: A Single-Centre Study in Somalia.International journal of nephrology · 2021Article
- Scorpion-Derived Antiviral Peptides with a Special Focus on Medically Important Viruses: An Update.BioMed research international · 2021Review
- The Dihydroquinolizinone Compound RG7834 Inhibits the Polyadenylase Function of PAPD5 and PAPD7 and Accelerates the Degradation of Matured Hepatitis B Virus Surface Protein mRNA.Antimicrobial agents and chemotherapy · 2020Article
- Viral interactions with non-homologous end-joining: a game of hide-and-seek.The Journal of general virology · 2020Review
- Viral hijacking of the TENT4-ZCCHC14 complex protects viral RNAs via mixed tailing.Nature structural & molecular biology · 2020Article
- Virological Basis for the Cure of Chronic Hepatitis B.ACS infectious diseases · 2019Review
- Spatiotemporal patterns and risk factors concerning hepatitis B virus infections in the Beijing-Tianjin-Hebei area of China.Epidemiology and infection · 2019Article
- Application of droplet digital PCR to detect the pathogens of infectious diseases.Bioscience reports · 2018Review
- Deep sequencing of HBV pre-S region reveals high heterogeneity of HBV genotypes and associations of word pattern frequencies with HCC.PLoS genetics · 2018Article
- Revisiting GNRA and UNCG folds: U-turns versus Z-turns in RNA hairpin loops.RNA (New York, N.Y.) · 2017Article
- Hepatitis B virus nuclear export elements: RNA stem-loop α and β, key parts of the HBV post-transcriptional regulatory element.RNA biology · 2016Review
- Oncogenes and RNA splicing of human tumor viruses.Emerging microbes & infections · 2014Review
- Prospects for inhibiting the post-transcriptional regulation of gene expression in hepatitis B virus.World journal of gastroenterology · 2014Review
- Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chronic hepatitis B virus (HBV) infections may lead to severe diseases like liver cirrhosis or hepatocellular carcinoma (HCC). The HBV post-transcriptional regulatory element (HPRE) facilitates the nuclear export of unspliced viral mRNAs, contains a splicing regulatory element and resides in the 3'-region of all viral transcripts. The HPRE consists of three sub-elements alpha (nucleotides 1151-1346), beta1 (nucleotides 1347-1457) and beta2 (nucleotides 1458-1582), which confer together full export competence. Here, we present the NMR solution structure (pdb 2JYM) of the stem-loop alpha (SLalpha, nucleotides 1292-1321) located in the sub-element alpha. The SLalpha contains a CAGGC pentaloop highly conserved in hepatoviruses, which essentially adopts a CUNG-like tetraloop conformation. Furthermore, the SLalpha harbours a single bulged G residue flanked by A-helical regions. The structure is highly suggestive of serving two functions in the context of export of unspliced viral RNA: binding sterile alpha motif (SAM-) domain containing proteins and/or preventing the utilization of a 3'-splice site contained within SLalpha.
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