about
Tapasin-related protein TAPBPR is an additional component of the MHC class I presentation pathwayHRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradationSelective export of HLA-F by its cytoplasmic tailThe binding of TAPBPR and Tapasin to MHC class I is mutually exclusive.TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalystCellular expression, trafficking, and function of two isoforms of human ULBP5/RAET1G.TAPBPR isoforms exhibit altered association with MHC class I.TAPBPR bridges UDP-glucose:glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway.The recognition of abnormal forms of HLA-B27 by CD4+ T cells.TAPBPR: a new player in the MHC class I presentation pathway.F pocket flexibility influences the tapasin dependence of two differentially disease-associated MHC Class I proteins.Tapasin dependence of major histocompatibility complex class I molecules correlates with their conformational flexibility.Major histocompatibility complex class I-restricted alloreactive CD4+ T cells.NKG2D ligand MICA is retained in the cis-Golgi apparatus by human cytomegalovirus protein UL142.Utilizing TAPBPR to promote exogenous peptide loading onto cell surface MHC I moleculesTAPBPR mediates peptide dissociation from MHC class I using a leucine leverRapid disease progression in a patient with mismatch repair-deficient and cortisol secreting adrenocortical carcinoma treated with pembrolizumab
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description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Louise H Boyle
@ast
Louise H Boyle
@en
Louise H Boyle
@es
Louise H Boyle
@nl
Louise H Boyle
@sl
type
label
Louise H Boyle
@ast
Louise H Boyle
@en
Louise H Boyle
@es
Louise H Boyle
@nl
Louise H Boyle
@sl
prefLabel
Louise H Boyle
@ast
Louise H Boyle
@en
Louise H Boyle
@es
Louise H Boyle
@nl
Louise H Boyle
@sl
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P21
P31
P496
0000-0002-3105-6555