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

Differentiation-dependent interpentameric disulfide bond stabilizes native human papillomavirus type 16.

PloS one - 1 Jan 2011

Conway Michael J, Cruz Linda, Alam Samina, Christensen Neil D, Meyers Craig

Abstract excerpt

Genetic and biochemical analyses of human papillomavirus type 16 (HPV16) capsids have shown that certain conserved L1 cysteine residues are critical for capsid assembly, integrity, and maturation. Since previous studies utilized HPV capsids produced in monolayer culture-based protein expression systems, the ascribed roles for these cysteine residues were not placed in the temporal context of the natural host...

Read the complete abstract on PubMed

Topics

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

Share to Capsid
Share to Capsid Proteins
Share to Disulfides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genome, Viral

Share to Human papillomavirus 16

Share to Oncogene Proteins, Viral

Share to Protein Multimerization

Share to Virion

Source

Open in PubMed Open full text

Identifiers

PMID: 21811610
DOI: 10.1371/journal.pone.0022427
PMCID: PMC3139651

Genes

SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Differentiation-dependent interpentameric disulfide bond stabilizes native human papillomavirus type 16.PMID 21811610Read ↗

Two Highly Conserved Cysteine Residues in HPV16 L2 Form an Intramolecular Disulfide Bond and Are Critical for Infectivity in Human KeratinocytesSemantic proximity Read ↗

Mutational analysis of human papillomavirus type 16 major capsid protein L1: the cysteines affecting the intermolecular bonding and structure of L1-capsids.Semantic proximity Read ↗

Mutations in HPV18 E1^E4 Impact Virus Capsid Assembly, Infectivity Competence, and Maturation.Semantic proximity Read ↗

Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines.Semantic proximity Read ↗

Arrangement of L2 within the Papillomavirus CapsidSemantic proximity Read ↗

Papillomavirus capsid mutation to escape dendritic cell-dependent innate immunity in cervical cancer.Semantic proximity Read ↗

Susceptibility of naturally human papillomavirus type 16 major capsid protein L1 variants to vaccines and predictions of future evolutionary trends.Semantic proximity Read ↗

Study of infectious virus production from HPV18/16 capsid chimeras.Semantic proximity Read ↗

DNA-Induced Structural Changes in the Papillomavirus CapsidSemantic proximity Read ↗

Human papillomavirus 16 minor capsid protein L2 helps capsomeres assemble independently of intercapsomeric disulfide bonding.Semantic proximity Read ↗

Genetic analysis of the vaccinia virus I6 telomere-binding protein uncovers a key role in genome encapsidation.Semantic proximity Read ↗

Naturally Occurring Single Amino Acid Substitution in the L1 Major Capsid Protein of Human Papillomavirus Type 16: Alteration of Susceptibility to Antibody-Mediated Neutralization.Semantic proximity Read ↗

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