about
Flexibility in HIV-1 Assembly Subunits: Solution Structure of the Monomeric C-Terminal Domain of the Capsid ProteinFlexibility of the major antigenic loop of foot-and-mouth disease virus bound to a Fab fragment of a neutralising antibody: structure and neutralisation.Viral genome segmentation can result from a trade-off between genetic content and particle stability.Resolving structure and mechanical properties at the nanoscale of viruses with frequency modulation atomic force microscopy.Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loopA single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid resistance.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.Insights into RNA virus mutant spectrum and lethal mutagenesis events: replicative interference and complementation by multiple point mutants.Amino Acid Side Chains Buried along Intersubunit Interfaces in a Viral Capsid Preserve Low Mechanical Stiffness Associated with Virus Infectivity.In vitro disassembly of a parvovirus capsid and effect on capsid stability of heterologous peptide insertions in surface loops.Mutational analysis of discontinuous epitopes of foot-and-mouth disease virus using an unprocessed capsid protomer precursor.Quantification and modification of the equilibrium dynamics and mechanics of a viral capsid lattice self-assembled as a protein nanocoating.Identification of the structural basis of thermal lability of a virus provides a rationale for improved vaccines.Dendrimers as potential inhibitors of the dimerization of the capsid protein of HIV-1.A tetraguanidinium ligand binds to the surface of the tetramerization domain of protein P53.Emerging foot-and-mouth disease virus variants with antigenically critical amino acid substitutions predicted by model studies using reference viruses.Crystallization and preliminary X-ray diffraction studies of a monoclonal antibody Fab fragment against foot-and-mouth disease virus and of its complex with the main antigenic site peptide.Direct evaluation of the immunodominance of a major antigenic site of foot-and-mouth disease virus in a natural host.Antibodies raised in a natural host and monoclonal antibodies recognize similar antigenic features of foot-and-mouth disease virus.Cyclic disulfide model of the major antigenic site of serotype-C foot-and-mouth disease virus. Synthetic, conformational and immunochemical studies.Extensive antigenic heterogeneity of foot-and-mouth disease virus of serotype C.Two mechanisms of antigenic diversification of foot-and-mouth disease virus.Non-additive effects of multiple amino acid substitutions on antigen-antibody recognitionStudies on antigenic variability of C strains of foot-and-mouth disease virus by means of synthetic peptides and monoclonal antibodiesThermostability of the Foot-and-Mouth Disease Virus Capsid Is Modulated by Lethal and Viability-Restoring Compensatory Amino Acid Substitutions
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description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Mauricio G. Mateu
@ast
Mauricio G. Mateu
@en
Mauricio G. Mateu
@es
Mauricio G. Mateu
@nl
Mauricio G. Mateu
@sl
type
label
Mauricio G. Mateu
@ast
Mauricio G. Mateu
@en
Mauricio G. Mateu
@es
Mauricio G. Mateu
@nl
Mauricio G. Mateu
@sl
altLabel
Mateu MG
@en
Mauricio Garcia Mateu
@en
prefLabel
Mauricio G. Mateu
@ast
Mauricio G. Mateu
@en
Mauricio G. Mateu
@es
Mauricio G. Mateu
@nl
Mauricio G. Mateu
@sl
P108
P106
P1153
7007069387
P21
P31
P496
0000-0002-2915-1529