About: The crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix

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About: The crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix Goto Sponge NotDistinct Permalink

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scientific article published on 23 June 2006

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) article scientifique publié en 2006 (fr) наукова стаття, опублікована в червні 2006 (uk) scientific article published on 23 June 2006 (en) artículu científicu espublizáu en xunu de 2006 (ast)
publication date	wds:Q79785484-5769694B-64E2-42A3-B25C-477705412C8E
publication date	2006-06-23 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q79785484-1AAF5D50-37D4-4AF7-BF27-860A71A76500
language of work or name	English
cites work	wds:Q79785484-6DB4A761-C29D-4905-BE9A-3DB7C803ED4A
cites work	Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
author name string	wds:Q79785484-7C3DBCFE-2655-473E-88A9-0CF0D02EB175 wds:Q79785484-8059F6CE-9716-4FDD-8EC0-EE447B9B4A17
author name string	Hans Peter Bächinger Maria A Schumacher
rdfs:label	The crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix (en) The crystal structure of a collagen-like polypeptide with 3 (nl)
skos:prefLabel	The crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix (en) The crystal structure of a collagen-like polypeptide with 3 (nl)
name	The crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix (en) The crystal structure of a collagen-like polypeptide with 3 (nl)
author	wds:Q79785484-418B9B88-EAC5-4E33-919B-B8D195C59477
author	Kazunori Mizuno
title	wds:Q79785484-31A1BB7C-73F9-4211-99F1-0F47D85A5E25
title	The crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix (en)
page(s)	wds:Q79785484-3445BE32-5CD9-4F78-B66F-898468C83947
page(s)	27566-27574
instance of	wds:Q79785484-0D24F38B-31EA-4D59-A016-40E02F64E1D3
instance of	scholarly article
PubMed ID	wds:Q79785484-E604921C-8833-4753-81CC-F8950C25754B
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16798737
PubMed ID	16798737
published in	wds:Q79785484-16BC1EAF-3CBB-418E-A6C8-83EEA02263D0
published in	Journal of Biological Chemistry
issue	wds:Q79785484-2B6F10C3-21D6-4314-B63F-F8D3B9C6BA00
volume	wds:Q79785484-68AD0E12-2141-48A0-8B0D-3C89618437F4
issue	37
volume	281
DOI	wds:Q79785484-4C9AF0EB-D180-48CA-AF37-B92A1B106E0D
DOI	http://dx.doi.org/10.1074/JBC.M602797200
DOI	10.1074/JBC.M602797200
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q79785484
is cites work of	Bone collagen: new clues to its mineralization mechanism from recessive osteogenesis imperfecta Differential effects of collagen prolyl 3-hydroxylation on skeletal tissues Peptidyl 3-hydroxyproline binding properties of type I collagen suggest a function in fibril supramolecular assembly Mineralization of the metre-long biosilica structures of glass sponges is templated on hydroxylated collagen A novel 3-hydroxyproline (3Hyp)-rich motif marks the triple-helical C terminus of tendon type I collagen Characterization of recombinant human prolyl 3-hydroxylase isoenzyme 2, an enzyme modifying the basement membrane collagen IV Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta Location of 3-hydroxyproline residues in collagen types I, II, III, and V/XI implies a role in fibril supramolecular assembly Collagen structure and stability Comprehensive mass spectrometric mapping of the hydroxylated amino acid residues of the α1(V) collagen chain Structural Insights into Charge Pair Interactions in Triple Helical Collagen-like Proteins Collagen prolyl 3-hydroxylation: a major role for a minor post-translational modification? Fibrillar Collagens
is cites work of	wds:Q27316988-B56AE442-72DD-413A-BCA2-3CB209378A0A wds:Q24314388-C5600A58-FF8A-44F6-AA75-D6630C9E9316 wds:Q24295351-0665C0EA-6EB3-4A83-941C-10488B0D8356 wds:Q34624077-7CC7A3CE-8636-44C5-A946-1FD4FA19515D wds:Q39013213-35DFE661-737A-49AF-BF64-F54E4108D682 wds:Q36418901-40745052-5789-494E-BBE6-376AE4CBF0B6 wds:Q27676290-9401EF05-01A1-4F2F-BA09-E06B2136A326 wds:Q26862184-E3695E71-0386-43C4-BA90-FBF7B9E3291E wds:Q35858452-628C6479-53A9-48F2-A67C-72556ED8DE04 wds:Q24610632-47A6ED83-3BE4-44D1-8ECF-B865497675A4 wds:Q37716768-0E2FADE8-B276-4232-8C15-D3A9630D5D75 wds:Q33593978-D4C08FFE-C2DE-467F-B658-61740D860F55 wds:Q42792464-93D00EA9-C9C0-4CC6-985E-4F911E2AF69E

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