A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase
about
Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcriptsProlyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complexCloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunitERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylaseAssignment of the gene coding for the alpha-subunit of prolyl 4-hydroxylase to human chromosome region 10q21.3-23.1The Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible MoleculeCharacterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system.Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradationSite-directed mutagenesis of human protein disulphide isomerase: effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cellsBrain tissue banking for stem cells for our futureCatalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule MimicsProteomic characterization of an isolated fraction of synthetic proteasome inhibitor (PSI)-induced inclusions in PC12 cells might offer clues to aggresomes as a cellular defensive response against proteasome inhibition by PSI.The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells.Conformational preferences of substrates for human prolyl 4-hydroxylaseLemon protein disulfide isomerase: cDNA cloning and biochemical characterization.Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide.Prolyl 4-hydroxylase: molecular cloning and the primary structure of the alpha subunit from chicken embryoRab GTPase mediated procollagen trafficking in ascorbic acid stimulated osteoblasts.Small molecule-induced oxidation of protein disulfide isomerase is neuroprotective.dpy-18 encodes an alpha-subunit of prolyl-4-hydroxylase in caenorhabditis elegans.Glucose-stimulated translation regulation of insulin by the 5' UTR-binding proteins.Expression of growth factors and remodelling of the airway wall in bronchial asthma.Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegansA developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cellsTranscriptome-wide identification of preferentially expressed genes in the hypothalamus and pituitary glandProteomic profiling of endorepellin angiostatic activity on human endothelial cellsERp57 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 activityGlycosylation site-binding protein is not required for N-linked glycoprotein synthesis.Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast.Protein disulfide-isomerase interacts with soluble guanylyl cyclase via a redox-based mechanism and modulates its activity.Identification of a novel saturable endoplasmic reticulum localization mechanism mediated by the C-terminus of a Dictyostelium protein disulfide isomerase.Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins.Extracellular Alix regulates integrin-mediated cell adhesions and extracellular matrix assembly.Cell-free synthesis and assembly of prolyl 4-hydroxylase: the role of the beta-subunit (PDI) in preventing misfolding and aggregation of the alpha-subunit.Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylaseCo-expression of the alpha subunit of human prolyl 4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes. Soluble alpha-subunit-BiP complexes have no prolyl 4-hydroxylase activity.Modification of vertebrate and algal prolyl 4-hydroxylases and vertebrate lysyl hydroxylase by diethyl pyrocarbonate. Evidence for histidine residues in the catalytic site of 2-oxoglutarate-coupled dioxygenases.The catalytic mechanism of the hydroxylation reaction of peptidyl proline and lysine does not require protein disulphide-isomerase activity.Minoxidil specifically decreases the expression of lysine hydroxylase in cultured human skin fibroblasts.Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit.
P2860
Q24307638-ECBDE29A-0F0D-49B6-B3B3-012617062231Q24309419-0F4AC8D5-812C-4644-A6C9-4A3C961BBF31Q24318327-A9107706-5980-4980-A78E-B26121F4CC90Q24534312-2BC5A497-20E2-43DB-A3DB-4CA88E7EFF6CQ24677837-AF613F88-F3E9-4364-B93A-E12C6F2B0FBEQ27652283-4BFE2FA3-A3FB-42A0-BBF6-F5B24B97A7BEQ27919642-1B0D0FE4-A77F-4F1C-A9CD-29C856F2B60AQ27934273-67CCBE6F-7297-4873-A93A-F21AB3D959F6Q28212078-7FA50F52-0940-4AA1-B2F1-EF2D51B5529BQ28817010-9E929094-46D8-4624-AB05-CA3752D3A73AQ29999427-13A042F5-68DB-420E-90B1-734870E40F1EQ30479870-89185734-6812-4AA4-8C04-0DFDC8C6E8CAQ30982469-002C51D9-C01B-4261-BE04-666C512A3CB0Q33605183-6C8730DB-5789-4AA1-BD44-19A53D138A12Q33690852-454B061F-505C-46C5-B3C3-3A598739CC53Q33835861-C156B0E7-6A93-44A1-91EA-300CA1C94A46Q34306686-4170D382-22BE-450B-8353-BDFF301C8AE5Q34438696-2620C2BA-BDCA-4D36-924D-AAF550D266D3Q34470561-F148AC56-F8BF-4871-B596-BAE24FC7115EQ34609789-87142FCD-2AB5-4B1B-8407-C52F60CFE3B6Q34800126-041B9DC1-E3D1-4ECB-888F-9A73596C6F86Q35563890-328C4308-4003-454D-BCC0-B5B5FEBA8562Q35692955-4458E47A-153F-4A54-994A-A15781340A16Q35942438-41D1CD3B-D8A0-45B0-A713-8AD28F651788Q35971350-2C3A7D8A-5E11-4350-8C47-688EE03F67EAQ36509450-C9C3F0B0-0638-4B11-A7BB-8024594C844CQ37149513-7ECCA5E8-031C-47B0-B226-E458717DAC01Q37422638-A8B3CFC9-4C36-48B3-9F89-42BE1CB5A296Q37516246-25A1DF4A-C8C5-453E-897A-D42F1821487BQ37712434-8839FBFA-134F-49AF-A56E-DC9055676D02Q38488336-20022BD3-D5B7-4C27-9692-56C8E54C2D2CQ39779420-68C8130F-46F9-4FC4-A8EA-228A1B45528FQ39960034-D586AB07-04AB-4EDC-9B79-320DFDC9552CQ40872620-9CCA5B7C-DCBA-4A3A-B380-521751C2E6E0Q41120528-9172772C-A7E1-486E-B7AC-97FD89C53F0FQ41205782-D3217017-FDA2-4C08-8732-006397FF4989Q41789005-62A15CF0-EFF1-4398-8545-510799A03E1FQ41850887-E510B13E-0459-4F77-AA0E-D27E53472C73Q41917280-A830BC64-BD5F-4153-9424-47F2814DB967Q42063969-D8D9A82B-A3A9-47B9-9A3B-9B495C626DEB
P2860
A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase
description
1987 nî lūn-bûn
@nan
1987 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
A single polypeptide acts both ...... a protein disulfide-isomerase
@ast
A single polypeptide acts both ...... a protein disulfide-isomerase
@en
A single polypeptide acts both ...... a protein disulfide-isomerase
@nl
type
label
A single polypeptide acts both ...... a protein disulfide-isomerase
@ast
A single polypeptide acts both ...... a protein disulfide-isomerase
@en
A single polypeptide acts both ...... a protein disulfide-isomerase
@nl
prefLabel
A single polypeptide acts both ...... a protein disulfide-isomerase
@ast
A single polypeptide acts both ...... a protein disulfide-isomerase
@en
A single polypeptide acts both ...... a protein disulfide-isomerase
@nl
P2093
P1476
A single polypeptide acts both ...... a protein disulfide-isomerase
@en
P2093
K I Kivirikko
T Helaakoski
T Pihlajaniemi
P304
P407
P577
1987-05-15T00:00:00Z