about
Redox regulation in the endoplasmic reticulum.PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta.A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cellsCytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER.The membrane topology of vitamin K epoxide reductase is conserved between human isoforms and the bacterial enzyme.Spatial separation of HLA-DM/HLA-DR interactions within MIIC and phagosome-induced immune escape.Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins.Stable expression of MHC class I heavy chain/HLA-DO complexes at the plasma membrane.Modulation of the major histocompatibility complex class II-associated peptide repertoire by human histocompatibility leukocyte antigen (HLA)-DO.Inhibition of IRE1α-mediated XBP1 mRNA cleavage by XBP1 reveals a novel regulatory process during the unfolded protein response.Two essential Thioredoxins mediate apicoplast biogenesis, protein import, and gene expression in Toxoplasma gondii.Activation of the unfolded protein response and alternative splicing of ATF6α in HLA-B27 positive lymphocytesThe DM and DM Chain Cooperate in the Oxidation and Folding of HLA-DMNovel polymorphisms in HLA-DOA and HLA-DOB in B-cell malignancies
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description
researcher
@en
wetenschapper
@nl
name
Marcel van Lith
@en
Marcel van Lith
@nl
type
label
Marcel van Lith
@en
Marcel van Lith
@nl
prefLabel
Marcel van Lith
@en
Marcel van Lith
@nl
P106
P31
P496
0000-0003-0225-5501