about
The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: surface localization and role in host cell adhesionLaminin receptor initiates bacterial contact with the blood brain barrier in experimental meningitis models.Mapping the laminin receptor binding domains of Neisseria meningitidis PorA and Haemophilus influenzae OmpP2.Identification and characterization of novel antigenic vaccine candidates of Actinobacillus pleuropneumoniae.Phase variation mediates reductions in expression of surface proteins during persistent meningococcal carriage.Characterization of the Campylobacter jejuni heptosyltransferase II gene, waaF, provides genetic evidence that extracellular polysaccharide is lipid A core independent.Prevalence and phase variable expression status of two autotransporters, NalP and MspA, in carriage and disease isolates of Neisseria meningitidis.Optimization of Molecular Approaches to Genogroup Neisseria meningitidis Carriage Isolates and Implications for Monitoring the Impact of New Serogroup B VaccinesNuclear trafficking, histone cleavage and induction of apoptosis by the meningococcal App and MspA autotransporters.A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonizationFructose-1,6-bisphosphate aldolase (FBA)-a conserved glycolytic enzyme with virulence functions in bacteria: 'ill met by moonlight'.Genomic Analysis of Serogroup Y Neisseria meningitidis Isolates Reveals Extensive Similarities Between Carriage-Associated and Disease-Associated Organisms.Fructose-1,6-bisphosphate aldolase of Neisseria meningitidis binds human plasminogen via its C-terminal lysine residue.Rise in Group W Meningococcal Carriage in University Students, United Kingdom.Deciphering the complex three-way interaction between the non-integrin laminin receptor, galectin-3 and Neisseria meningitidis.Carriage of meningococci by university students, United Kingdom.Cloning, mutation and distribution of a putative lipopolysaccharide biosynthesis locus in Campylobacter jejuni.Persistence, replacement, and rapid clonal expansion of meningococcal carriage isolates in a 2008 university student cohort.Human antibody responses to the meningococcal factor H binding protein (LP2086) during invasive disease, colonization and carriage.AasP autotransporter protein of Actinobacillus pleuropneumoniae does not protect pigs against homologous challenge.Limited impact of adolescent meningococcal ACWY vaccination on group W carriage in university students.University vaccine campaign increases meningococcal ACWY vaccine coverage.Localized Hypermutation is the Major Driver of Meningococcal Genetic Variability during Persistent Asymptomatic CarriageUptake of Neisserial autotransporter lipoprotein (NalP) promotes an increase in human brain microvascular endothelial cell metabolic activityThe moonlighting peroxiredoxin-glutaredoxin in Neisseria meningitidis binds plasminogen via a C-terminal lysine residue and contributes to survival in a whole blood modelPotentiation of Phase Variation in Multiple Outer-Membrane Proteins During Spread of the Hyperinvasive Neisseria meningitidis Serogroup W ST-11 LineageVariant Signal Peptides of Vaccine Antigen, FHbp, Impair Processing Affecting Surface Localization and Antibody-Mediated Killing in Most Meningococcal Isolates
P50
Q28903784-D57347A1-11BC-49CA-B03F-BD9BC7FFE385Q30487909-9320C69A-68B9-4705-8032-7C5AB61655F1Q31104611-8A27BA24-463F-4CD1-8A4F-549AEC8D5942Q33323965-4F2BC8EA-DAF0-4770-834D-760794EC178FQ33603065-8FA0B579-B26E-467C-AE55-3222E4D3A948Q34308441-12B2BC5A-3EC9-4092-959F-616955AD4B94Q34921091-4DBDFF2A-DFAB-400E-9AA7-D8783C42F953Q35683382-6FFE043B-DFBD-407B-9DE9-AEFEE885A533Q37257511-AEBC6F19-6B3D-4F63-8D15-0DDA7FE704B8Q37539302-A3798FCC-DAE6-4C3B-986B-A3B3ECE48D02Q38268493-DDD18D5D-7603-4559-8B26-70F7EF01D247Q40126952-83429C79-0E81-4ADE-AC45-6F9788DDEC2BQ40166085-140D11C7-8751-4DD7-B1F2-9D53444090BEQ40197164-E6FE0391-4B02-4E2F-BA6D-410238756FEDQ41719699-613C015C-9A37-4044-9DB9-9B63F766371FQ42553085-47DA82FE-9BE2-4E76-9309-744BE1BE3C78Q42594962-A555B3D5-2B7F-40EC-84C1-B664790361C7Q42625430-92A9C4B1-7F6F-49E8-9D2C-81AC6B31E04FQ43672052-0AB4135A-7DA4-440E-A2E1-70FEE6751D23Q44048265-B3AE241B-5AC0-4A71-898F-4EC37BC98F09Q47212171-FF89AE4D-CA91-483F-B2A5-59DB85550196Q47406523-932DE315-54E3-499C-AB36-0C391407BD6BQ90629856-4F3D8DF9-AEEB-4625-9F32-6EAE08024801Q90776292-00FABA9B-BA3C-4B89-A29F-4A8615437DEFQ91441071-AC2D0133-4108-48B9-8012-ACA122A296C0Q92231104-55D297E3-D4FA-4C29-B544-365117A26DB1Q92537969-3F33E74E-962E-4832-B4B0-36C01AAD3BB2
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Neil J. Oldfield
@ast
Neil J. Oldfield
@en
Neil J. Oldfield
@es
Neil J. Oldfield
@nl
Neil J. Oldfield
@sl
type
label
Neil J. Oldfield
@ast
Neil J. Oldfield
@en
Neil J. Oldfield
@es
Neil J. Oldfield
@nl
Neil J. Oldfield
@sl
prefLabel
Neil J. Oldfield
@ast
Neil J. Oldfield
@en
Neil J. Oldfield
@es
Neil J. Oldfield
@nl
Neil J. Oldfield
@sl
P106
P1153
6603467169
P2038
Neil_Oldfield
P21
P31
P496
0000-0001-7423-8378