A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid lability and confer resistance to acid-dependent uncoating inhibition.

A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid lability and confer resistance to acid-dependent uncoating inhibition.

Item
http://www.wikidata.org/entity/Q39755293
Structure-based energetics of protein interfaces guides foot-and-mouth disease virus vaccine designA single amino acid substitution in the core protein of West Nile virus increases resistance to acidotropic compoundsProtection of a single dose west nile virus recombinant subviral particle vaccine against lineage 1 or 2 strains and analysis of the cross-reactivity with Usutu virus.Establishment of persistent infection with foot-and-mouth disease virus in BHK-21 cells.Virus engineering: functionalization and stabilization.Three-dimensional structure of foot-and-mouth disease virus and its biological functions.An increase in acid resistance of foot-and-mouth disease virus capsid is mediated by a tyrosine replacement of the VP2 histidine previously associated with VP0 cleavage.Adaption of FMDV Asia-1 to Suspension Culture: Cell Resistance Is Overcome by Virus Capsid Alterations.Role of a single amino acid substitution of VP3 H142D for increased acid resistance of foot-and-mouth disease virus serotype A.The pH Stability of Foot-and-Mouth Disease Virus Particles Is Modulated by Residues Located at the Pentameric Interface and in the N Terminus of VP1.Single amino acid substitution of VP1 N17D or VP2 H145Y confers acid-resistant phenotype of type Asia1 foot-and-mouth disease virus.Selection and characterization of an acid-resistant mutant of serotype O foot-and-mouth disease virus.Mutations that hamper dimerization of foot-and-mouth disease virus 3A protein are detrimental for infectivity.Equine Rhinitis A Virus Mutants with Altered Acid Resistance Unveil a Key Role of VP3 and Intrasubunit Interactions in the Control of the pH Stability of the Aphthovirus Capsid.A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid resistance.The pH stability of foot-and-mouth disease virus.Influence of cell type and cell culture media on the propagation of foot-and-mouth disease virus with regard to vaccine quality.
P2860

A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid lability and confer resistance to acid-dependent uncoating inhibition.

Item
http://www.wikidata.org/entity/Q39755293
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
2010年學術文章
@zh
2010年學術文章
@zh-hant
name
A single amino acid substituti ...... ependent uncoating inhibition.
@en
A single amino acid substituti ...... ependent uncoating inhibition.
@nl
type
label
A single amino acid substituti ...... ependent uncoating inhibition.
@en
A single amino acid substituti ...... ependent uncoating inhibition.
@nl
prefLabel
A single amino acid substituti ...... ependent uncoating inhibition.
@en
A single amino acid substituti ...... ependent uncoating inhibition.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P932
P356
P1433
P1476
A single amino acid substituti ...... ependent uncoating inhibition.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P932