Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly.
about
ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp5719F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b'x from human protein disulphide isomerase (hPDI).Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution.Substrate recognition by the protein disulfide isomerases.A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cellsERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations.ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activityGenerating an unfoldase from thioredoxin-like domainsA structural overview of the PDI family of proteins.Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway.Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction.Co-expression of recombinant human prolyl with human collagen α1 (III) chains in two yeast systems.Catalysis of protein disulfide bond isomerization in a homogeneous substrateCombined ligand-observe (19)F and protein-observe (15)N,(1)H-HSQC NMR suggests phenylalanine as the key Δ-somatostatin residue recognized by human protein disulfide isomerase.Crystal and solution structures of human protein disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity.Biochemical evidence for the presence of mixed membrane topologies of the severe acute respiratory syndrome coronavirus envelope protein expressed in mammalian cells
P2860
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P2860
Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年學術文章
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name
Three binding sites in protein ...... hydroxylase tetramer assembly.
@en
type
label
Three binding sites in protein ...... hydroxylase tetramer assembly.
@en
prefLabel
Three binding sites in protein ...... hydroxylase tetramer assembly.
@en
P2093
P2860
P356
P1476
Three binding sites in protein ...... hydroxylase tetramer assembly.
@en
P2093
Johanna Myllyharju
Kirsi E H Salo
Lloyd W Ruddock
Peppi Koivunen
P2860
P304
P356
10.1074/JBC.M412480200
P407
P577
2004-12-07T00:00:00Z