About: A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens

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About: A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens Goto Sponge NotDistinct Permalink

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description	artículu científicu espublizáu en 2011 (ast) vědecký článek publikovaný v roce 2011 (cs) 2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված (hy) 2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована у вересні 2011 (uk) vedecký článok (publikovaný 2011/09/02) (sk) مقالة علمية (نشرت في 2-9-2011) (ar) wetenschappelijk artikel (gepubliceerd op 2011/09/02) (nl) article publié dans la revue scientifique Journal of Biological Chemistry (fr) scientific journal article (en) im September 2011 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28505276-F903CD33-82E9-4495-9277-4D33C834E000
publication date	2011-09-02 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28505276-91DED2DF-FEFE-4675-80FC-16B863944F3F
language of work or name	English
cites work	wds:Q28505276-005F453D-3950-4E1D-8384-74529731CDE5 wds:Q28505276-029ED272-EBA1-41A5-8E89-2DE83E9A3952 wds:Q28505276-05BDBC62-01FD-41F1-96D0-B0C8A232311D wds:Q28505276-0F781A8B-F4E4-4F18-892A-064DD851ABF0 wds:Q28505276-135035EC-BACC-4D16-A444-AA3FAAEB33C2 wds:Q28505276-27089770-2F07-4D3D-973A-89846F98FBCC wds:Q28505276-2790DB07-D2BE-41CE-B40D-1BA61A24BF72 wds:Q28505276-338F8FC4-09AC-4EB6-A824-2791170123E5 wds:Q28505276-33C659FB-B5F5-4B8B-99F4-6BF2A70763FF wds:Q28505276-34D507EC-5FA3-43F9-B69D-C326EB4EA224 wds:Q28505276-45E3E299-867F-4D59-A33C-BD2C8B8B921A wds:Q28505276-495D0401-FFD5-470A-BCCA-1906036A6C61 wds:Q28505276-51191776-E314-4E76-B1F6-10A504F5800F wds:Q28505276-53990570-C819-425E-8857-59BEFB47A32B wds:Q28505276-5422B900-AD54-4659-88A1-435E72DBD303 wds:Q28505276-6EA09A68-73AC-43F7-8CB6-9D12678F5EA5 wds:Q28505276-76447450-6CD9-44E5-AA4B-25B7DEBC86F5 wds:Q28505276-77372B42-8EAF-471A-8B9F-030EAB5DF034 wds:Q28505276-84D01885-0215-4F69-AE91-C4D10D94DE0C wds:Q28505276-86281199-584C-4F81-8B08-BBC3ABD65707 wds:Q28505276-8D1D2EE8-1611-473C-B8EB-17073CF1CA30 wds:Q28505276-90DEC5E0-0CE6-4638-9CC9-2A80775CE054 wds:Q28505276-90F8639D-9DD2-4958-A505-1EB0DFA0CAD0 wds:Q28505276-9FA7E271-CD6A-4F06-A479-FE01770BEF8D wds:Q28505276-A04D8FE5-AACA-47BC-8985-AAC8E9EE26F5 wds:Q28505276-A7C1C511-C0AB-4002-9A00-398F22792B23 wds:Q28505276-B028853A-186B-4A04-B40D-519F1BABAF20 wds:Q28505276-BB8253B2-435F-430C-826D-0FB3E286C76D wds:Q28505276-C2987B75-CB3B-4E51-A0E4-F4F182BB168F wds:Q28505276-CA3584F3-DBF9-42DC-A3F7-A4362F58E122 wds:Q28505276-CD4C524A-239A-4594-9DDA-FB9B1DB8DD92 wds:Q28505276-D56CC28C-6E74-487C-91E0-C41EA695D8AA wds:Q28505276-D588020E-F3A2-4510-BF45-BB62B7ED4324 wds:Q28505276-DAB60518-BB42-4E1C-80C6-9054D187AB34 wds:Q28505276-E08E6362-E11D-4133-B515-27DB8DE156DA wds:Q28505276-EB478E1F-025D-4319-9787-8E6847BA3ADE wds:Q28505276-F868CE8C-6611-4AD6-8016-1A046515D940
cites work	The prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for epigenetic silencing in breast cancer A novel 3-hydroxyproline (3Hyp)-rich motif marks the triple-helical C terminus of tendon type I collagen Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis A role for 14-3-3 tau in E2F1 stabilization and DNA damage-induced apoptosis Characterization of recombinant human prolyl 3-hydroxylase isoenzyme 2, an enzyme modifying the basement membrane collagen IV LEPREL1, a novel ER and Golgi resident member of the Leprecan family Molecular characterization of a novel basement membrane-associated proteoglycan, leprecan Partial purification and characterization of chick-embryo prolyl 3-hydroxylase Covalent structure of mouse type-IV collagen. Isolation, order and partial amino-acid sequence of cyanogen-bromide and tryptic peptides of pepsin fragment P1 from the alpha 1(IV) chain Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes CRTAP and LEPRE1 mutations in recessive osteogenesis imperfecta CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta Location of 3-hydroxyproline residues in collagen types I, II, III, and V/XI implies a role in fibril supramolecular assembly Recessive osteogenesis imperfecta caused by LEPRE1 mutations: clinical documentation and identification of the splice form responsible for prolyl 3-hydroxylation Effect of the -Gly-3(S)-hydroxyprolyl-4(R)-hydroxyprolyl- tripeptide unit on the stability of collagen model peptides. Recombinant procollagen II: Deletion of D period segments identifies sequences that are required for helix stabilization and generates a temperature-sensitive N-proteinase cleavage site. Sp1 family of transcription factors regulates the human alpha2 (XI) collagen gene (COL11A2) in Saos-2 osteoblastic cells Effect of 3-hydroxyproline residues on collagen stability Identification of alternatively spliced variants of type II procollagen in vitreous Incomplete processing of type II procollagen by a rat chondrosarcoma cell line Collagen XI chain misassembly in cartilage of the chondrodysplasia (cho) mouse 3-Hydroxyproline, a new amino acid of collagen Surface-induced aggregation of type I procollagen Insights on the evolution of prolyl 3-hydroxylation sites from comparative analysis of chicken and Xenopus fibrillar collagens Learning how mutations in type I collagen genes cause connective tissue disease. Ehlers-Danlos syndrome type VIIB. Morphology of type I collagen fibrils formed in vivo and in vitro is determined by the conformation of the retained N-propeptide Activities of prolyl hydroxylase, lysyl hydroxylase, collagen galactosyltransferase and collagen glucosyltransferase in the liver of rats with hepatic injury Structure of protocollagen proline hydroxylase from chick embryos Further hydroxylation of lysyl residues in collagen by protocollagen lysyl hydroxylase in vitro. The post-translational phenotype of collagen synthesized by SAOS-2 osteosarcoma cells Regulation of collagen post-translational modification in transformed human and chick-embryo cells Assembly of collagen types II, IX and XI into nascent hetero-fibrils by a rat chondrocyte cell line Conservation of notochord gene expression across chordates: insights from the Leprecan gene family Expression of prolyl 3-hydroxylase genes in embryonic and adult mouse tissues Letter to the Editor: Hyal2, where are you?
author name string	wds:Q28505276-0ECBB5E9-3346-4016-99DE-9D6BDD36F81D wds:Q28505276-39F813EC-2EA1-4C38-B77C-EA593BC04BCB wds:Q28505276-C0742F38-561D-4359-9EE9-0B7A560B2FE2 wds:Q28505276-CFBEDB05-BD42-4ABA-877E-DF59B235DED3 wds:Q28505276-D7280240-D604-4D8E-AAF6-E72C526AA897
OpenCitations bibliographic resource ID	wds:Q28505276-6FC3D823-CC54-4D7A-BB84-CCA59DA760BC
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/650345
author name string	Mary Ann Weis Russell J. Fernandes David R. Eyre

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