about
A common fold mediates vertebrate defense and bacterial attackEpitope-specific TCR repertoire diversity imparts no functional advantage on the CD8+ T cell response to cognate viral peptidesStructural and biological basis of CTL escape in coronavirus-infected micePrevention of Cytotoxic T Cell Escape Using a Heteroclitic Subdominant Viral T Cell DeterminantConstraints within major histocompatibility complex class I restricted peptides: Presentation and consequences for T-cell recognitionThe type III effectors NleE and NleB from enteropathogenic E. coli and OspZ from Shigella block nuclear translocation of NF-kappaB p65.Crystal structure of HLA-G: a nonclassical MHC class I molecule expressed at the fetal-maternal interface.The cellular redox environment alters antigen presentationCrystal structure of the human T cell receptor CD3 epsilon gamma heterodimer complexed to the therapeutic mAb OKT3.Stonefish toxin defines an ancient branch of the perforin-like superfamily.Specificity on a knife-edge: the alphabeta T cell receptor.Enzymatic properties of an ecto-nucleoside triphosphate diphosphohydrolase from Legionella pneumophila: substrate specificity and requirement for virulence.Cryo-electron tomography: an ideal method to study membrane-associated proteins.The mystery behind membrane insertion: a review of the complement membrane attack complexFunctional and structural characteristics of NY-ESO-1-related HLA A2-restricted epitopes and the design of a novel immunogenic analogue.The production and purification of the human T-cell receptors, the CD3epsilongamma and CD3epsilondelta heterodimers: complex formation and crystallization with OKT3, a therapeutic monoclonal antibody.Lack of prominent peptide-major histocompatibility complex features limits repertoire diversity in virus-specific CD8+ T cell populations.The structure of H-2K(b) and K(bm8) complexed to a herpes simplex virus determinant: evidence for a conformational switch that governs T cell repertoire selection and viral resistance.Antigen ligation triggers a conformational change within the constant domain of the alphabeta T cell receptor.The first transmembrane region of complement component-9 acts as a brake on its self-assembly
P50
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P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Michelle A Dunstone
@ast
Michelle A Dunstone
@en
Michelle A Dunstone
@es
Michelle A Dunstone
@nl
type
label
Michelle A Dunstone
@ast
Michelle A Dunstone
@en
Michelle A Dunstone
@es
Michelle A Dunstone
@nl
prefLabel
Michelle A Dunstone
@ast
Michelle A Dunstone
@en
Michelle A Dunstone
@es
Michelle A Dunstone
@nl
P106
P1153
6602164085
P21
P31
P496
0000-0002-6026-648X