about
Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidaseThe structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside bindingCellular proteostasis: degradation of misfolded proteins by lysosomesThe human cytomegalovirus gene product US6 inhibits ATP binding by TAPβ2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHThe ABC-transporter signature motif is required for peptide translocation but not peptide binding by TAPComparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formationSynaptotagmin I-DeltaC2B. A novel synaptotagmin isoform with a single C2 domain in the bovine adrenal medulla.Analysis of familial hemophagocytic lymphohistiocytosis type 4 (FHL-4) mutant proteins reveals that S-acylation is required for the function of syntaxin 11 in natural killer cellsImmunologic human renal allograft injury associates with an altered IL-10/TNF-α expression ratio in regulatory B cells.Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils.Antigen presentation: peptides and proteins scramble for the exit.The MHC class I antigen presentation pathway: strategies for viral immune evasion.An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation.Direct three-dimensional visualization of membrane disruption by amyloid fibrilspH-induced molecular shedding drives the formation of amyloid fibril-derived oligomersVirus subversion of protective immunity.Natural processing sites for human cathepsin E and cathepsin D in tetanus toxin: implications for T cell epitope generation.Di-leucine signals mediate targeting of tyrosinase and synaptotagmin to synaptic-like microvesicles within PC12 cells.Natural killer cell cytotoxicity: how do they pull the trigger?Ligand binding to distinct states diverts aggregation of an amyloid-forming protein.Amyloid Fibres: Inert End-Stage Aggregates or Key Players in Disease?β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomesUbiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation.Dependence of the localization and function of the human cytomegalovirus protein US6 on the transporter associated with antigen processing.Kaposi's sarcoma-associated herpesvirus RTA promotes degradation of the Hey1 repressor protein through the ubiquitin proteasome pathwayFibril fragmentation in amyloid assembly and cytotoxicity: when size matters.Investigation into the role of macrophages in the formation and degradation of beta2-microglobulin amyloid fibrils.Organelle proteomics: identification of the exocytic machinery associated with the natural killer cell secretory lysosome.Aggregation modulators interfere with membrane interactions of β2-microglobulin fibrils.Structural and Functional Dissection of the Human Cytomegalovirus Immune Evasion Protein US6.Fibril fragmentation enhances amyloid cytotoxicity.A complex web of signal-dependent trafficking underlies the triorganellar distribution of P-selectin in neuroendocrine PC12 cells.Powering the peptide pump: TAP crosstalk with energetic nucleotides.Why are Functional Amyloids Non-Toxic in Humans?Specific glycosaminoglycans promote unseeded amyloid formation from beta2-microglobulin under physiological conditions.A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pH.Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid.A new era for understanding amyloid structures and diseaseA Balance of Opposing Signals within the Cytoplasmic Tail Controls the Lysosomal Targeting of P-selectin
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onderzoeker
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Eric W Hewitt
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P185
P106
P1153
7005772889
P21
P31
P496
0000-0002-6238-6303