about
Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stagesRibophorin I acts as a substrate-specific facilitator of N-glycosylationBiosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulumSignal recognition particle mediates post-translational targeting in eukaryotesRibophorin I regulates substrate delivery to the oligosaccharyltransferase coreEeyarestatin 1 interferes with both retrograde and anterograde intracellular trafficking pathwaysThe pathogenic mechanism of the Mycobacterium ulcerans virulence factor, mycolactone, depends on blockade of protein translocation into the ERSolution structure of the SGTA dimerisation domain and investigation of its interactions with the ubiquitin-like domains of BAG6 and UBL4ASGTA antagonizes BAG6-mediated protein triageOST4 is a subunit of the mammalian oligosaccharyltransferase required for efficient N-glycosylationThe oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as ubiquitous and selective modulators of mammalian N-glycosylationThe Charcot Marie Tooth disease protein LITAF is a zinc-binding monotopic membrane protein.Formation and turnover of NSF- and SNAP-containing "fusion" complexes occur on undocked, clathrin-coated vesicle-derived membranes.Membrane-protein biosynthesis at the endoplasmic reticulum.Disease-associated mutations cause premature oligomerization of myelin proteolipid protein in the endoplasmic reticulum.Early events in glycosylphosphatidylinositol anchor addition. substrate proteins associate with the transamidase subunit gpi8p.Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.Elevation of proteasomal substrate levels sensitizes cells to apoptosis induced by inhibition of proteasomal deubiquitinases.The oligomeric state of Derlin-1 is modulated by endoplasmic reticulum stress.The association of BAG6 with SGTA and tail-anchored proteinsThe signal sequence influences post-translational ER translocation at distinct stages.Protein targeting and translocation at the endoplasmic reticulum membrane--through the eye of a needle?Role of calnexin in the glycan-independent quality control of proteolipid protein.Membrane protein insertion into the endoplasmic reticulum--another channel tunnel?Mechanisms that determine the transmembrane disposition of proteins.Making membrane proteins at the mammalian endoplasmic reticulum.Polytopic membrane protein folding and assembly in vitro and in vivo.Tail-anchored protein biosynthesis at the endoplasmic reticulum: the same but different.Polytopic proteins: preventing aggregation in the membrane.TRC40 can deliver short secretory proteins to the Sec61 translocon.Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocationDeubiquitinases regulate the activity of caspase-1 and interleukin-1β secretion via assembly of the inflammasomeGet3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked.Differences in endoplasmic-reticulum quality control determine the cellular response to disease-associated mutants of proteolipid protein.Delivering proteins for export from the cytosol.Ca2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane.Reorientation of the first signal-anchor sequence during potassium channel biogenesis at the Sec61 complex.Biogenesis of tail-anchored proteins: the beginning for the end?Structure and function of signal recognition particle (SRP).
P50
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P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Stephen High
@ast
Stephen High
@en
Stephen High
@es
Stephen High
@fr
Stephen High
@nl
Stephen High
@sl
type
label
Stephen High
@ast
Stephen High
@en
Stephen High
@es
Stephen High
@fr
Stephen High
@nl
Stephen High
@sl
prefLabel
Stephen High
@ast
Stephen High
@en
Stephen High
@es
Stephen High
@fr
Stephen High
@nl
Stephen High
@sl
P106
P21
P31
P496
0000-0002-4532-8152