About: Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts

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About: Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts Goto Sponge NotDistinct Permalink

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description	wissenschaftlicher Artikel (de) artículu científicu espublizáu en 1981 (ast) vědecký článek publikovaný v roce 1981 (cs) наукова стаття, опублікована в липні 1981 (uk) 1981 թվականի հուլիսին հրատարակված գիտական հոդված (hy) 1981 թուականի Յուլիսին հրատարակուած գիտական յօդուած (hyw) مقالة علمية (نشرت في يوليو 1981) (ar) wetenschappelijk artikel (gepubliceerd op 1981/07/01) (nl) vedecký článok (publikovaný 1981/07/01) (sk) scientific journal article (en)
publication date	wds:Q28608930-C886D8F7-06D3-47BB-B4DC-8D2AB43EA9E5
publication date	1981-07-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q28608930-002E8CD5-12D1-4C14-90EF-DFEDD1CC4729 wds:Q28608930-0FB1F21F-2405-462A-ABFD-F044CD71C3BB wds:Q28608930-1424D3E6-254C-46C6-9A0A-EBA7411FB5A8 wds:Q28608930-2D0B9821-CE46-4763-A4B9-F73E07B4FC9E wds:Q28608930-2E9F8046-6E86-4F08-936A-6A0595224827 wds:Q28608930-49395AD1-18B5-4310-B675-34B9CC0EE3D4 wds:Q28608930-6A58D013-2DE5-42FB-B88E-BA031E5121C9 wds:Q28608930-74CAEEBB-4516-418E-B9FF-B8A4733314E4 wds:Q28608930-753AE50B-867B-43BB-9B5E-F2710CF9FB6F wds:Q28608930-7B0CEB0B-4194-45E1-9ADC-468DD34CAB38 wds:Q28608930-9586C1E2-D5C4-44CA-AC09-233AEDA6A968 wds:Q28608930-97F92721-7494-44FC-AAAF-6A941F585B0D wds:Q28608930-A1857C97-AAB9-40D9-B192-490810D4269B wds:Q28608930-B3CCFD76-FB11-41F6-94A8-96DFDD824008 wds:Q28608930-B71DD41E-0EEE-400D-94B2-E2A0163AC431 wds:Q28608930-B9404918-0C8B-40BC-9823-1F278947AC6E wds:Q28608930-C04CEAF7-D3AF-4546-987D-C107FE37E9C1 wds:Q28608930-C1242F21-5B13-4E6F-BDEC-50E68074DFA5 wds:Q28608930-CB7E0991-7C58-48D7-B0CF-B58838B990AF wds:Q28608930-EEBCB421-BF8C-4C79-B597-97E1959B85FE wds:Q28608930-F1D55BB7-4876-44DA-BE95-E10540F40E03
cites work	Collagen: molecular diversity in the body's protein scaffold A Heritable Disorder of Connective Tissue Collagen Glycosyltransferases Isolation of lysyl hydroxylase, an enzyme of collagen synthesis, from chick embryos as a homogeneous protein Lysyl-protocollagen hydroxylase deficiency in fibroblasts from siblings with hydroxylysine-deficient collagen Abnormal properties of collagen lysyl hydroxylase from skin fibroblasts of siblings with hydroxylysine-deficient collagen Ascorbate Action on Normal and Mutant Human Lysyl Hydroxylases from Cultured Dermal Fibroblasts Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics and related aspects Lysyl hydroxylase. Further purification and characterization of the enzume from chick embryos and chick embryo cartilage Human Prolyl Hydroxylase. Purification, Partial Characterization and Preparation of Antiserum to the Enzyme Assay of protocollagen lysyl hydroxylase activity in the skin of human subjects and changes in the activity with age Partial purification and characterization of protocollagen lysine hydroxylase from chick embryos Intracellular enzymes of collagen biosynthesis in rat liver as a function of age and in hepatic injury induced by dimethylnitrosamine. Changes in prolyl hydroxylase, lysyl hydroxylase, collagen galactosyltransferase and collagen glucosyltransferase Preferential hydroxylation of type IV collagen by lysyl hydroxylase from Ehlers-Danlos syndrome type VI fibroblasts Affinity chromatography of lysyl hydroxylase on concanavalin A-agarose Studies on protocollagen lysine hydroxylase. Hydroxylation of synthetic peptides and the stoichiometric decarboxylation of -ketoglutarate Differences between proline and lysine hydroxylations in their inhibition by zinc or by ascorbate deficiency during collagen synthesis in various cell types Studies on the lysyl hydroxylase reaction. II. Inhibition kinetics and the reaction mechanism Immunological characterization of lysyl hydroxylase, an enzyme of collagen synthesis Purification and enzymatic properties of lysyl hydroxylase from fetal porcine skin Affinity chromatography of collagen glycosyltransferases on collagen linked to agarose
author name string	wds:Q28608930-4E2A4396-289A-4B67-922C-CC07FE489A8D wds:Q28608930-7F3DBFD4-78FC-4018-A285-B73F9A6E6A70 wds:Q28608930-C0A3BF5F-B61C-49D7-9CE9-FA4188FDA256
author name string	K. I. Kivirikko U. Puistola T. M. Turpeenniemi-Hujanen
rdfs:label	Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts (en) Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts (nl) Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts (ast)
skos:prefLabel	Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts (en) Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts (nl) Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts (ast)
name	Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts (en) Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts (nl) Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts (ast)
title	wds:Q28608930-CECBAAAE-701B-4984-B3C0-397F9321F72F
title	Human lysyl hydroxylase: purification to homogeneity, partial characterization and comparison of catalytic properties with those of a mutant enzyme from Ehlers-Danlos syndrome type VI fibroblasts (en)
page(s)	wds:Q28608930-20524566-1DEC-4041-AAF9-2B36CAF75181
page(s)	355–366
instance of	wds:Q28608930-08841A90-496C-4454-AF15-A59D1A923D5E
instance of	scholarly article
main subject	wds:Q28608930-c3110ae4-4bb5-4c68-ab73-667acf849d6c
main subject	Ehlers-Danlos syndrome
PubMed ID	wds:Q28608930-48B640C3-85EB-413A-8CC4-CA43A70EE098
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6809411
PubMed ID	6809411
published in	wds:Q28608930-5DA368F3-1C43-4DF0-BF54-CFE4D54890FA
published in	Matrix Biology
issue	wds:Q28608930-CC357E0D-90FB-40F9-8B04-C5AB7A117835
volume	wds:Q28608930-101C0DF3-6A0A-4F6F-9AD2-13F6FE3E9987
issue	4
volume	1
DOI	wds:Q28608930-7EE48E84-F6A3-4ABB-8CD3-4348A6BBB0F0
DOI	http://dx.doi.org/10.1016/S0174-173X(81)80012-X
DOI	10.1016/S0174-173X(81)80012-X
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28608930
is cites work of	10 Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3----p36.2 Polyclonal and monoclonal antibodies to human lysyl hydroxylase and studies on the molecular heterogeneity of the enzyme Failure of highly purified lysyl hydroxylase to hydroxylate lysyl residues in the non-helical regions of collagen Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity Monoclonal antibodies to human prolyl 4-hydroxylase Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity Deletion of cysteine 369 in lysyl hydroxylase 1 eliminates enzyme activity and causes Ehlers-Danlos syndrome type VI. Disentangling mechanisms involved in collagen pyridinoline cross-linking: The immunophilin FKBP65 is critical for dimerization of lysyl hydroxylase 2

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