Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit.
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 complexThe prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for epigenetic silencing in breast cancerCloning, 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-hydroxylaseHuman prolyl-4-hydroxylase alpha(I) transcription is mediated by upstream stimulatory factorsStudies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assayPurification and cloning of a proline 3-hydroxylase, a novel enzyme which hydroxylates free L-proline to cis-3-hydroxy-L-prolineAssignment of the gene coding for the alpha-subunit of prolyl 4-hydroxylase to human chromosome region 10q21.3-23.1Characterization 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 cellsSmall changes huge impact: the role of protein posttranslational modifications in cellular homeostasis and diseaseHuman ALKBH4 interacts with proteins associated with transcriptionCharacterization of endoplasmic reticulum-localized UDP-D-galactose: hydroxyproline O-galactosyltransferase using synthetic peptide substrates in Arabidopsis.Conformational preferences of substrates for human prolyl 4-hydroxylaseEnhanced transforming growth factor-beta signaling and fibrogenesis in ovine fetal skeletal muscle of obese dams at late gestation.Identification of Novel Peptidyl Serine α-Galactosyltransferase Gene Family in Plants.Specific inhibition of eIF-5A and collagen hydroxylation by a single agent. Antiproliferative and fibrosuppressive effects on smooth muscle cells from human coronary arteries.Prolyl 4-hydroxylase: molecular cloning and the primary structure of the alpha subunit from chicken embryoUnity in diversity, a systems approach to regulating plant cell physiology by 2-oxoglutarate-dependent dioxygenasesIn vivo imaging of basement membrane movement: ECM patterning shapes Hydra polypsProlyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegansConformational control of Bax localization and apoptotic activity by Pro168.Human prolyl hydroxylase expression in uterine leiomyoma during the menstrual cycle.From collagen chemistry towards cell therapy - a personal journey.Evidence for a role of collagen synthesis in arterial smooth muscle cell migrationBiological messiness vs. biological genius: Mechanistic aspects and roles of protein promiscuity.Transcriptional regulation of secretory capacity by bZip transcription factors.How tubular epithelial cells dictate the rate of renal fibrogenesis?Modulation of fibrosis in systemic sclerosis by nitric oxide and antioxidants.Proteomic analysis of human osteoprogenitor response to disordered nanotopography.The supramolecular structure of bone: X-ray scattering analysis and lateral structure modeling.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.Biosynthesis of recombinant human pro-alpha 1(III) chains in a baculovirus expression system: production of disulphide-bonded and non-disulphide-bonded species containing full-length triple helices.The Roles of Vitamin C in Skin Health.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 translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells.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.
P2860
Q24307638-2E2734A8-8738-43CF-A976-831B64F8B4C8Q24309419-352F271B-EBB8-4E94-ADF4-B56E57D71449Q24310299-552D1294-4182-424D-A7B7-0104A2ADFAE0Q24318327-39CC78FD-8B2D-4104-B88C-3BF42F70DAD1Q24534312-1DC0386E-B2F1-4963-8C16-65B9A59413B7Q24649970-355BF99A-B98F-4F97-B452-903656740149Q24671869-21DC782D-E44F-4162-BD86-8B94FBA2B904Q24676959-0A46A7F8-168C-4223-A9CB-44C99A84D2EAQ24677837-6E579582-8FE4-48D7-BE7F-E25EE76F7727Q27919642-1CECC32D-4553-40FE-B81C-50FC71470316Q28212078-33842DE2-84A6-41D1-9577-0273E2168CD9Q28396109-C5028490-8E91-4179-AA0A-FA204305EDEDQ28485078-2507990C-C6A6-493A-9538-3AFD30177790Q30893296-99A4BE3F-9918-4457-8689-44381A7397FCQ33605183-9429B4A4-CD6C-4FD4-A802-A91C3AF20C28Q33916545-532632C8-AACE-4348-9C79-3BB449EDB239Q33946942-C50C042C-1614-42FA-AE0A-E33E8069CF66Q34198618-47333353-DDF4-4087-8890-757569E36B1DQ34306686-D573ADDB-DFDF-46E5-A775-ECD3DCAD5D9EQ35166815-A2F1DD1A-6D25-4F42-8601-98F293CC5E92Q35630657-0C19589B-D3AE-494E-9C9F-C98C1FFF91EBQ35692955-AADF02CE-0B39-4C8C-A641-9DCA315762D5Q36321947-5C9939B6-3527-4792-96FD-2851D6CF8F2BQ36594429-CC9F6B37-0417-4CF2-8AC5-25D8D3A0108BQ36909454-73769FEB-EC10-4EEF-A2D9-0876E8E5A95FQ37381419-E7D53E7E-5F0D-4868-A9B8-62ED183DF60EQ38248878-61DC5573-0085-41EE-B9C7-6ED2EBEE198EQ38395499-63671204-8767-4AB7-AEFF-D989E454E731Q38545865-79A9A806-74B4-4E62-885F-D4923D7AF2A4Q38909892-EAA481C3-0C2D-405F-8151-EE7211E0D4EDQ39231200-BDC0F330-47E5-4901-8D2F-46952386CF0DQ39418386-EA793E8F-BC7B-4A37-BDAD-CB0B1197E4FEQ41120528-A9E0F6F1-2647-43BA-853C-06AA17A9376CQ41205782-85F21541-56EE-4C08-A766-5F1F377CF53BQ41259159-8B076AFD-3BB5-4B8B-93D3-9E860A5E9D4FQ41584171-86D91A58-44E7-49F8-A142-DC7CF8809141Q41789005-270E9BB8-AA0F-4FDA-82A6-D97051AFEFBEQ41824074-357DB454-527C-4F00-BE11-951568DFC5F6Q41850887-4C424DF8-5165-4B29-AA1B-9CE4C1A1FE32Q41917280-E0A9AE81-5C18-47DA-B659-7339B1304A94
P2860
Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit.
description
1989 nî lūn-bûn
@nan
1989 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի մարտին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Protein hydroxylation: prolyl ...... and a multifunctional subunit.
@ast
Protein hydroxylation: prolyl ...... and a multifunctional subunit.
@en
Protein hydroxylation: prolyl ...... and a multifunctional subunit.
@nl
type
label
Protein hydroxylation: prolyl ...... and a multifunctional subunit.
@ast
Protein hydroxylation: prolyl ...... and a multifunctional subunit.
@en
Protein hydroxylation: prolyl ...... and a multifunctional subunit.
@nl
prefLabel
Protein hydroxylation: prolyl ...... and a multifunctional subunit.
@ast
Protein hydroxylation: prolyl ...... and a multifunctional subunit.
@en
Protein hydroxylation: prolyl ...... and a multifunctional subunit.
@nl
P2093
P1433
P1476
Protein hydroxylation: prolyl ...... and a multifunctional subunit.
@en
P2093
Kivirikko KI
Pihlajaniemi T
P304
P407
P577
1989-03-01T00:00:00Z