Evidence map›Paper›PMID 41617687›Full record

ArticleNature communications2026

Multistep receptor binding of the hepatitis B virus preS1 domain.

Chisa Kobayashi, Toru Ekimoto, Koji Ooka, Junki Mifune, Kayo Matsuzawa, Lusheng Que, Yingfang Li, Atsuto Kusunoki, Takeshi Morita, Kaho Shionoya and 11 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. 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

21 authors.

Chisa Kobayashi *Department of Drug Development, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.
Toru Ekimoto *Computational Life Science Laboratory, Graduate School of Medical Life Science, Yokohama City University, Yokohama, Japan.
Koji OokaKomaba Organization for Educational Excellence, College of Arts and Sciences, The University of Tokyo, Tokyo, Japan.ORCID http://orcid.org/0000-0002-0833-8853
Junki MifuneDepartment of Drug Development, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.
Kayo MatsuzawaDepartment of Drug Development, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.
Lusheng QueDepartment of Virology II, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.
Yingfang LiDepartment of Virology II, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.
Atsuto KusunokiDepartment of Drug Development, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.
Takeshi MoritaDepartment of Drug Development, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.
Kaho ShionoyaDepartment of Drug Development, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.
Makoto NaganoDepartment of Drug Development, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.
Kousho WakaeDepartment of Virology II, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.
Masanori IsogawaDepartment of Virology II, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.ORCID http://orcid.org/0000-0001-8730-4303
Masamichi MuramatsuDepartment of Virology II, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan.
Umeharu OhtoGraduate School of Frontier Sciences, The University of Tokyo, Chiba, Japan.
Norimichi NomuraDepartment of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.ORCID http://orcid.org/0000-0002-6330-2239
Sam-Yong ParkDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Yokohama, Japan.ORCID http://orcid.org/0000-0001-6164-8896
Camille SureauINSERM, Université de Tours, Tours, France.
Munehito AraiKomaba Organization for Educational Excellence, College of Arts and Sciences, The University of Tokyo, Tokyo, Japan.ORCID http://orcid.org/0000-0002-1223-2242
Mitsunori IkeguchiComputational Life Science Laboratory, Graduate School of Medical Life Science, Yokohama City University, Yokohama, Japan.
Koichi WatashiDepartment of Drug Development, National Institute of Infectious Diseases, Japan Institute for Health Security, Tokyo, Japan. watashi.k@jihs.go.jp.

Funding

Japan Agency for Medical Research and Development (AMED) JP23ama121007Japan Agency for Medical Research and Development (AMED) JP23ama121023Japan Agency for Medical Research and Development (AMED) JP23fk0310517Japan Agency for Medical Research and Development (AMED) JP25ak0101271Japan Agency for Medical Research and Development (AMED) JP25fk0310525Japan Agency for Medical Research and Development (AMED) JP25fk0310533Japan Agency for Medical Research and Development (AMED) JP25fk0310547MEXT | Japan Science and Technology Agency (JST) JPMJMI22G1MEXT | Japan Science and Technology Agency (JST) JPMJSP2151MEXT | Japan Society for the Promotion of Science (JSPS) JP23H02724MEXT | Japan Society for the Promotion of Science (JSPS) JP24K02290MEXT | Japan Society for the Promotion of Science (JSPS) JP24K18078MEXT | Japan Society for the Promotion of Science (JSPS) JP25H00976MEXT | Japan Society for the Promotion of Science (JSPS) JP25H01280MEXT | Japan Society for the Promotion of Science (JSPS) JP25K21767MEXT | Japan Society for the Promotion of Science (JSPS) JP25K21782MEXT | Japan Society for the Promotion of Science (JSPS) JP25KJ2119Takeda Science Foundation N/A
6 · The paper itself

Abstract

The preS1 domain present on hepatitis B and D virus particles is an intrinsically disordered peptide (IDP) essential for recognizing the host receptor, sodium taurocholate co-transporting polypeptide (NTCP). However, it remains poorly understood how the disordered preS1 peptide achieves high-affinity binding through its conformational change. Here, we reveal a stepwise binding process through which multiple regions within preS1 cooperate to establish the stable binding to NTCP. By combining structure-based molecular simulations with virological assays, we show that Asn9

Indexed as

Hepatitis B Surface AntigensHepatitis B virusOrganic Anion Transporters, Sodium-DependentProtein PrecursorsReceptors, VirusSymportersAnimalsHumansMiceModels, MolecularMutationProtein BindingProtein DomainsHepatitis B Surface AntigensOrganic Anion Transporters, Sodium-Dependentpresurface protein 1, hepatitis B surface antigenProtein PrecursorsReceptors, Virussodium-bile acid cotransporterSymporters

Identifiers

PMID41617687
PMCPMC12858840

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.