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

Influences on viral replication and sensitivity to GLS4, a HAP compound, of naturally occurring T109/V124 mutations in hepatitis B virus core protein.

Journal of medical virology - 1 Oct 2017

Wang Jianghua, Zhang Haiying, Zhang Yingjun, Jiang Dong, Li Jing, Goldmann Siegfried, Ren Qingyun, Fei Ran, Wang Xueyan, Wei Lai

Abstract excerpt

Heteroaryldihydropyrimidine (HAP) compounds inhibit HBV replication by binding to a hydrophobic pocket at the interface between hepatitis B virus core protein (HBcAg) dimer, which interrupts capsid assembly by changing the kinetics and thermodynamics during this process. Structure biological studies have identified several amino acids in HBcAg crucial for compound binding. Here, we investigated the polymorphisms...

Read the complete abstract on PubMed

Topics

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

Share to Drug Resistance, Viral
Share to Hep G2 Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hepatitis B Core Antigens

Share to Hepatitis B virus

Share to Hepatitis C Antigens

Share to Pyrimidines

Share to Thiazoles

Share to Virus Replication

Source

Identifiers

PMID: 28401569
DOI: 10.1002/jmv.24830

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Influences on viral replication and sensitivity to GLS4, a HAP compound, of naturally occurring T109/V124 mutations in hepatitis B virus core protein.PMID 28401569Read ↗

Assembly Properties of Hepatitis B Virus Core Protein Mutants Correlate with Their Resistance to Assembly-Directed Antivirals.Semantic proximity Read ↗

Heteroaryldihydropyrimidine (HAP) and Sulfamoylbenzamide (SBA) Inhibit Hepatitis B Virus Replication by Different Molecular Mechanisms.Semantic proximity Read ↗

Antiviral profiling of the capsid assembly modulator BAY41-4109 on full-length HBV genotype A-H clinical isolates and core site-directed mutants in vitro.Semantic proximity Read ↗

Preclinical Profile and Characterization of the Hepatitis B Virus Core Protein Inhibitor ABI-H0731Semantic proximity Read ↗

Prevalence of S gene mutations within the major hydrophilic region of hepatitis B virus in patients in Dongguan, southern China.Semantic proximity Read ↗

Hepatitis B Virus Core Protein Dephosphorylation Occurs during Pregenomic RNA EncapsidationSemantic proximity Read ↗

Anti-HBV activity of the HBV capsid assembly modulator JNJ-56136379 across full-length genotype A-H clinical isolates and core site-directed mutants in vitro.Semantic proximity Read ↗

Biological impacts of "hot-spot" mutations of hepatitis B virus X proteins are genotype B and C differentiated.Semantic proximity Read ↗

Basal core promoter and precore mutations in the hepatitis B virus genome enhance replication efficacy of Lamivudine-resistant mutants.Semantic proximity Read ↗

Antivirals interacting with hepatitis B virus core protein and core mutations may misdirect capsid assembly in a similar fashion.Semantic proximity Read ↗

Novel non-HAP class A HBV capsid assembly modulators have distinct in vitro and in vivo profilesSemantic proximity Read ↗

Implications of seven NTCP mutations for receptor stability and Hepatitis B Virus infectivity: A computational analysis.Semantic proximity Read ↗

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