Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
about
The human protein disulfide isomerase gene familyMolecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcriptsCloning, 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 subunitCytosolic thyroid hormone-binding protein is a monomer of pyruvate kinaseERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylaseProlyl 4-hydroxylaseMutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease ASulfate reduction in higher plants: molecular evidence for a novel 5'-adenylylsulfate reductaseNuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomeraseAssignment of the gene coding for the alpha-subunit of prolyl 4-hydroxylase to human chromosome region 10q21.3-23.1Orchestration of secretory protein folding by ER chaperonesEfficient class II major histocompatibility complex presentation of endogenously synthesized hepatitis C virus core protein by Epstein-Barr virus-transformed B-lymphoblastoid cell lines to CD4(+) T cellsCrystal Structure of Prolyl 4-Hydroxylase from Bacillus anthracisHuman Protein-disulfide Isomerase Is a Redox-regulated Chaperone Activated by Oxidation of Domain a′Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein foldingCharacterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system.Site-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 cellsIs protein disulfide isomerase a redox-dependent molecular chaperone?The Protein Disulfide Isomerase gene family in bread wheat (T. aestivum L.)Catalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule MimicsIdentification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylaseThe 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.Protein-electroblotting and -microsequencing strategies in generating protein data bases from two-dimensional gelsTranscriptional regulation of rat liver protein disulphide-isomerase gene by insulin and in diabetes.Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C.The protein disulphide-isomerase family: unravelling a string of folds.Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide.Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: identification of a nucleoside diphosphatase in the endoplasmic reticulumProlyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegansProlyl 4-hydroxylase: molecular cloning and the primary structure of the alpha subunit from chicken embryoA Salmonella typhimurium genetic locus which confers copper tolerance on copper-sensitive mutants of Escherichia coli.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.Molecular characterization and expression profiling of the protein disulfide isomerase gene family in Brachypodium distachyon L.Chromosomal localization of the gene for a human thyroid hormone-binding protein.Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegansNucleotide sequence of a full-length cDNA clone encoding a mouse cellular thyroid hormone binding protein (p55) that is homologous to protein disulfide isomerase and the beta-subunit of prolyl-4-hydroxylase.Regulatory functions of glutathione S-transferase P1-1 unrelated to detoxificationData base analysis of protein expression patterns during T-cell ontogeny and activationDiverse biological functions of extracellular collagen processing enzymes
P2860
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P2860
Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
description
1987 nî lūn-bûn
@nan
1987 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի մարտին 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
Molecular cloning of the beta- ...... are products of the same gene
@ast
Molecular cloning of the beta- ...... are products of the same gene
@en
Molecular cloning of the beta- ...... are products of the same gene
@nl
type
label
Molecular cloning of the beta- ...... are products of the same gene
@ast
Molecular cloning of the beta- ...... are products of the same gene
@en
Molecular cloning of the beta- ...... are products of the same gene
@nl
prefLabel
Molecular cloning of the beta- ...... are products of the same gene
@ast
Molecular cloning of the beta- ...... are products of the same gene
@en
Molecular cloning of the beta- ...... are products of the same gene
@nl
P2093
P2860
P1433
P1476
Molecular cloning of the beta- ...... are products of the same gene
@en
P2093
K I Kivirikko
M L Huhtala
T Helaakoski
T Pihlajaniemi
P2860
P407
P577
1987-03-01T00:00:00Z