Inhibition of transfer to secondary receptors by heparan sulfate-binding drug or antibody induces noninfectious uptake of human papillomavirus. - Wikidata - wikimedia - TriplyDB

Inhibition of transfer to secondary receptors by heparan sulfate-binding drug or antibody induces noninfectious uptake of human papillomavirus.

Inhibition of transfer to secondary receptors by heparan sulfate-binding drug or antibody induces noninfectious uptake of human papillomavirus.

http://www.wikidata.org/entity/Q36099326

about

The S100A10 subunit of the annexin A2 heterotetramer facilitates L2-mediated human papillomavirus infection Two highly conserved cysteine residues in HPV16 L2 form an intramolecular disulfide bond and are critical for infectivity in human keratinocytes Cutaneous and mucosal human papillomaviruses differ in net surface charge, potential impact on tropism Tetraspanin CD151 mediates papillomavirus type 16 endocytosis Current understanding of the mechanism of HPV infection Papillomavirus Infectious Pathways: A Comparison of Systems The cytoskeleton in papillomavirus infection Concepts of papillomavirus entry into host cells Human papillomavirus type 16 entry: retrograde cell surface transport along actin-rich protrusions Large scale RNAi reveals the requirement of nuclear envelope breakdown for nuclear import of human papillomaviruses Entry of human papillomavirus type 16 by actin-dependent, clathrin- and lipid raft-independent endocytosis Subunit interactions in bovine papillomavirus Structural Basis of Oligosaccharide Receptor Recognition by Human Papillomavirus Target cell cyclophilins facilitate human papillomavirus type 16 infection Differential dependence on host cell glycosaminoglycans for infection of epithelial cells by high-risk HPV types Clathrin- and caveolin-independent entry of human papillomavirus type 16--involvement of tetraspanin-enriched microdomains (TEMs)Identification of neutralizing conformational epitopes on the human papillomavirus type 31 major capsid protein and functional implications Potential anti-HPV and related cancer agents from marine resources: an overview.A central region in the minor capsid protein of papillomaviruses facilitates viral genome tethering and membrane penetration for mitotic nuclear entry.Mechanisms of cell entry by human papillomaviruses: an overview.The role of furin in papillomavirus infection.HPV16 infection of HaCaTs is dependent on β4 integrin, and α6 integrin processing.Differential binding patterns to host cells associated with particles of several human alphapapillomavirus types.The nuclear retention signal of HPV16 L2 protein is essential for incoming viral genome to transverse the trans-Golgi network.Inhibition of SARS pseudovirus cell entry by lactoferrin binding to heparan sulfate proteoglycans.In vivo mechanisms of vaccine-induced protection against HPV infection.Essential roles for soluble virion-associated heparan sulfonated proteoglycans and growth factors in human papillomavirus infections.Binding and neutralization characteristics of a panel of monoclonal antibodies to human papillomavirus 58.The role of inflammation in HPV infection of the Oesophagus.Human papillomavirus species-specific interaction with the basement membrane-resident non-heparan sulfate receptor.The HPV16 and MusPV1 papillomaviruses initially interact with distinct host components on the basement membrane Interaction of human tumor viruses with host cell surface receptors and cell entry Kallikrein-8 Proteolytically Processes Human Papillomaviruses in the Extracellular Space To Facilitate Entry into Host Cells Opposing effects of bacitracin on human papillomavirus type 16 infection: enhancement of binding and entry and inhibition of endosomal penetration Topography of the Human Papillomavirus Minor Capsid Protein L2 during Vesicular Trafficking of Infectious Entry.Cyclophilins facilitate dissociation of the human papillomavirus type 16 capsid protein L1 from the L2/DNA complex following virus entry.Proteoglycans in host-pathogen interactions: molecular mechanisms and therapeutic implications The U4 Antibody Epitope on Human Papillomavirus 16 Identified by Cryo-electron Microscopy Use of an in vivo animal model for assessing the role of integrin α(6)β(4) and syndecan-1 in early steps in papillomavirus infection.Interaction of human papillomavirus type 16 particles with heparan sulfate and syndecan-1 molecules in the keratinocyte extracellular matrix plays an active role in infection.

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P2860

Inhibition of transfer to secondary receptors by heparan sulfate-binding drug or antibody induces noninfectious uptake of human papillomavirus.

http://www.wikidata.org/entity/Q36099326

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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Inhibition of transfer to seco ...... ptake of human papillomavirus.

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Inhibition of transfer to seco ...... ptake of human papillomavirus.

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type

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Inhibition of transfer to seco ...... ptake of human papillomavirus.

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Inhibition of transfer to seco ...... ptake of human papillomavirus.

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Inhibition of transfer to seco ...... ptake of human papillomavirus.

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Inhibition of transfer to seco ...... ptake of human papillomavirus.

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Journal of Virology

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Inhibition of transfer to seco ...... ptake of human papillomavirus.

@en

P2093

Hans-Christoph Selinka

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Hetal D Patel

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Kirsten Freitag

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Luise Florin

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Martin Sapp

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Michaela Schmidtke

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Vadim A Makarov

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P2860

Carrageenan is a potent inhibitor of papillomavirus infection

Human papillomavirus infection requires cell surface heparan sulfate.

Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection

A membrane-destabilizing peptide in capsid protein L2 is required for egress of papillomavirus genomes from endosomes.

Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression

Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells

Animal cell mutants defective in glycosaminoglycan biosynthesis

Characterization of a heparan sulfate octasaccharide that binds to herpes simplex virus type 1 glycoprotein D.

Maturation of papillomavirus capsids.

The L1 major capsid protein of human papillomavirus type 11 recombinant virus-like particles interacts with heparin and cell-surface glycosaminoglycans on human keratinocytes.

P304

10970-10980

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scholarly article

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10.1128/JVI.00998-07

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20

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81

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17686860

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2045555

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