Evidence map›Paper›PMID 34705562›Full record

ArticleJournal of virology2022

Core Protein-Directed Antivirals and Importin β Can Synergistically Disrupt Hepatitis B Virus Capsids.

Christine Kim, Lauren F Barnes, Christopher J Schlicksup, Angela J Patterson, Brian Bothner, Martin F Jarrold, Che-Yen Joseph Wang, Adam Zlotnick

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.0field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
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  12. CRISPR/Cas9 for hepatitis B virus infection treatment.Immunity, inflammation and disease · 2023
    Review
  13. Article
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  15. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Christine KimDepartment of Molecular & Cellular Biochemistry, Indiana University, Bloomington, Indiana, USA.
Lauren F BarnesDepartment of Chemistry, Indiana University, Bloomington, Indiana, USA.
Christopher J SchlicksupDepartment of Molecular & Cellular Biochemistry, Indiana University, Bloomington, Indiana, USA.
Angela J PattersonDepartment of Chemistry & Biochemistry, Montana State Universitygrid.41891.35, Bozeman, Montana, USA.
Brian BothnerDepartment of Chemistry & Biochemistry, Montana State Universitygrid.41891.35, Bozeman, Montana, USA.ORCID 0000-0003-1295-9609
Martin F JarroldDepartment of Chemistry, Indiana University, Bloomington, Indiana, USA.
Che-Yen Joseph WangDepartment of Microbiology & Immunology, Pennsylvania State Universitygrid.29857.31 College of Medicine, Hershey, Pennsylvania, USA.
Adam ZlotnickDepartment of Molecular & Cellular Biochemistry, Indiana University, Bloomington, Indiana, USA.ORCID 0000-0001-9945-6267
Indiana University Bloomington · USMontana State University · USPennsylvania State University · US

Funding

Multimode Observation of Virus Capsid AssemblyR01AI118933 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI Adam Zlotnick · 2016 to 2026
$4.0M
The Structural Biology of HBVR01AI144022 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI ZLOTNICK, ADAM · 2019 to 2022
$1.5M
Graduate Program in Quantitative and Chemical Biology at Indiana University BloomT32GM109825 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI GIEDROC, DAVID P. · 2014 to 2018
$926k
HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) R01-AI118933HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) R01-AI144022NIAID NIH HHS R01 AI118933NIAID NIH HHS R01 AI144022NIGMS NIH HHS T32 GM109825
6 · The paper itself

Abstract

Viral structural proteins can have multiple activities. Antivirals that target structural proteins have potential to exhibit multiple antiviral mechanisms. Hepatitis B virus (HBV) core protein (Cp) is involved in most stages of the viral life cycle; it assembles into capsids, packages viral RNA, is a metabolic compartment for reverse transcription, interacts with nuclear trafficking machinery, and disassembles to release the viral genome into the nucleus. During nuclear localization, HBV capsids bind to host importins (e.g., Impβ) via Cp's C-terminal domain (CTD); the CTD is localized to the interior of the capsid and is transiently exposed on the exterior. We used HAP12 as a representative Cp allosteric modulator (CpAM), a class of antivirals that inappropriately stimulates and misdirects HBV assembly and deforms capsids. CpAM impact on other aspects of the HBV life cycle is poorly understood. We investigate how HAP12 influences the interactions between empty or RNA-filled capsids with Impβ and trypsin

Indexed as

Antiviral Agentsbeta KaryopherinsCapsidDose-Response Relationship, DrugDrug SynergismHepatitis B Core AntigensHepatitis B virusProtein BindingProteolysisVirus AssemblyAntiviral Agentsbeta KaryopherinsHepatitis B Core AntigensantiviralassemblycapsidHBVkaryopherin

Identifiers

PMID34705562
PMCPMC8791275
OpenAlexW3211183605

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.