Evidence map›Paper›PMID 33536177›Full record

ArticleJournal of virology2021

A putative amphipathic alpha helix in hepatitis B virus small envelope protein plays a critical role in the morphogenesis of subviral particles.

Sisi Yang, Zhongliang Shen, Yaoyue Kang, Liren Sun, Usha Viswanathan, Hongying Guo, Tianlun Zhou, Xinghong Dai, Jinhong Chang, Jiming Zhang and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

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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

11 authors at 3 institutions in 2 countries.

Sisi YangDepartment of Infectious Diseases, Huashan Hospital, Fudan University, Shanghai, China.
Zhongliang ShenDepartment of Infectious Diseases, Huashan Hospital, Fudan University, Shanghai, China.
Yaoyue KangDepartment of Infectious Diseases, Huashan Hospital, Fudan University, Shanghai, China.
Liren SunBaruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.
Usha ViswanathanBaruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.
Hongying GuoDepartment of Infectious Diseases, Huashan Hospital, Fudan University, Shanghai, China.
Tianlun ZhouBaruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.ORCID https://orcid.org/0000-0001-5864-0578
Xinghong DaiDepartment of Physiology and Biophysics, Case Western Reserve University, School of Medicine, Cleveland, Ohio, USA.
Jinhong ChangBaruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.
Jiming ZhangDepartment of Infectious Diseases, Huashan Hospital, Fudan University, Shanghai, China jmzhang@fudan.edu.cn ju-tao.guo@bblumberg.org.
Ju-Tao GuoBaruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA jmzhang@fudan.edu.cn ju-tao.guo@bblumberg.org.ORCID https://orcid.org/0000-0001-5335-2788
Fudan University · CNHepatitis B Foundation · USUniversity School · US

Funding

Evaulation of therapeutic benefits of HBV nucleocapsid assembly inhibitorsR01AI113267 · NIAID · DREXEL UNIVERSITY · PI DU, YANMING, GUO, JU-TAO · 2014 to 2018
$2.9M
NIAID NIH HHS R01 AI113267
6 · The paper itself

Abstract

Hepatitis B virus (HBV) small (S) envelope protein has the intrinsic ability to direct the formation of small spherical subviral particles (SVPs) in eukaryotic cells. However, the molecular mechanism underlying the morphogenesis of SVPs from the monomeric S protein initially synthesized at the endoplasmic reticulum (ER) membrane remains largely elusive. Structure prediction and extensive mutagenesis analysis suggested that the amino acid residues spanning W156 to R169 of S protein form an amphipathic alpha helix and play essential roles in SVP production and S protein metabolic stability. Further biochemical analyses showed that the putative amphipathic alpha helix was not required for the disulfide-linked S protein oligomerization, but was essential for SVP morphogenesis. Pharmacological disruption of vesicle trafficking between the ER and Golgi complex in SVP producing cells supported the hypothesis that S protein-directed SVP morphogenesis takes place at the ER-Golgi intermediate compartment (ERGIC). Moreover, it was demonstrated that S protein is degraded in hepatocytes

Identifiers

PMID33536177
PMCPMC8103704
OpenAlexW3126502479

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.