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

Flexibility and intrinsic disorder are conserved features of hepatitis C virus E2 glycoprotein

28 Feb 2020

Abstract excerpt

The glycoproteins of hepatitis C virus, E1E2, are unlike any other viral fusion machinery yet described, and are the current focus of immunogen design in HCV vaccine development; thus, making E1E2 both scientifically and medically important.We used pre-existing, but fragmentary, structures to model a complete ectodomain of the major glycoprotein E2 from three strains of HCV.We then performed molecular dynamic...

Read the complete abstract on PubMed

Topics

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

Share to Glycosylation and Glycoproteins Research
Share to Hepatitis C virus research
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 32109245
DOI: 10.1371/journal.pcbi.1007710

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

Flexibility and intrinsic disorder are conserved features of hepatitis C virus E2 glycoproteinPMID 32109245Read ↗

Hepatitis C Virus Envelope Glycoproteins: A Balancing Act of Order and DisorderSemantic proximity Read ↗

A Biologically-validated HCV E1E2 Heterodimer Structural Model.Semantic proximity Read ↗

Structural flexibility at a major conserved antibody target on hepatitis C virus E2 antigenSemantic proximity Read ↗

Structure of engineered hepatitis C virus E1E2 ectodomain in complex with neutralizing antibodiesSemantic proximity Read ↗

Structure of the hepatitis C virus E1E2 glycoprotein complexSemantic proximity Read ↗

Unexpected Structural Features of the Hepatitis C Virus Envelope Protein 2 EctodomainSemantic proximity Read ↗

Genetic Diversity Underlying the Envelope Glycoproteins of Hepatitis C Virus: Structural and Functional Consequences and the Implications for Vaccine Design.Semantic proximity Read ↗

Identification of new functional regions in hepatitis C virus envelope glycoprotein E2.Semantic proximity Read ↗

Sites of vulnerability in HCV E1E2 identified by comprehensive functional screeningSemantic proximity Read ↗

Computational Prediction of the Heterodimeric and Higher-Order Structure of gpE1/gpE2 Envelope Glycoproteins Encoded by Hepatitis C VirusSemantic proximity Read ↗

Identifying immunologically-vulnerable regions of the HCV E2 glycoprotein and broadly neutralizing antibodies that target themSemantic proximity Read ↗

A protein coevolution method uncovers critical features of the Hepatitis C Virus fusion mechanismSemantic proximity Read ↗

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