ArticleMolecules (Basel, Switzerland)2022
Biochemical and Biophysical Characterisation of the Hepatitis E Virus Guanine-7-Methyltransferase.
Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Viral helicase and methyltransferase promote genotype one-hepatitis e virus internal ribosome entry site-like element activity.Npj viruses · 2025Article
- Methotrexate, an anti-inflammatory drug, inhibits Hepatitis E viral replication.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Inhibition of HEV Replication by FDA-Approved RdRp Inhibitors.ACS omega · 2023Article
- The hepatitis E virus ORF1 hypervariable region confers partial cyclophilin dependency.The Journal of general virology · 2023Article
- Spectroscopic, Thermodynamic and Molecular Docking Studies on Molecular Mechanisms of Drug Binding to Proteins.Molecules (Basel, Switzerland) · 2022Article
- Inhibition of Hepatitis E Virus Replication by Novel Inhibitor Targeting Methyltransferase.Viruses · 2022Article
Corrections and comments
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Authors and funding
14 authors at 5 institutions in 3 countries.
Funding
Abstract
Hepatitis E virus (HEV) is an understudied pathogen that causes infection through fecal contaminated drinking water and is prominently found in South Asian countries. The virus affects ~20 million people annually, leading to ~60,000 infections per year. The positive-stranded RNA genome of the HEV genotype 1 has four conserved open reading frames (ORFs), of which ORF1 encodes a polyprotein of 180 kDa in size, which is processed into four non-structural enzymes: methyltransferase (MTase), papain-like cysteine protease, RNA-dependent RNA polymerase, and RNA helicase. MTase is known to methylate guanosine triphosphate at the 5'-end of viral RNA, thereby preventing its degradation by host nucleases. In the present study, we cloned, expressed, and purified MTase spanning 33-353 amino acids of HEV genotype 1. The activity of the purified enzyme and the conformational changes were established through biochemical and biophysical studies. The binding affinity of MTase with magnesium ions (Mg
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Registered trials
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