About: Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models

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About: Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models Goto Sponge NotDistinct Permalink

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scientific article published on 04 December 2007

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rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 2007 (ast) наукова стаття, опублікована в грудні 2007 (uk) مقالة علمية نشرت في 04 ديسمبر 2007 (ar) scientific article published on 04 December 2007 (en)
publication date	wds:Q37335428-646EB99A-B421-4E37-B7D5-8C87DC81C97D
publication date	2007-12-04 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37335428-4EEEE765-CF92-415F-99C4-C87E06807BFC
language of work or name	English
cites work	wds:Q37335428-0406688C-27FD-4172-AE5D-C38DAC492BF4 wds:Q37335428-059B4921-1047-4B91-953D-D05BEB32B786 wds:Q37335428-07D5B2F7-B225-4EA7-BDAA-62150644E00D wds:Q37335428-08B75DE4-B151-4FF4-AE6C-4A3855C72F56 wds:Q37335428-0C3D9D26-FCED-41E4-8CCB-0F4C801340C1 wds:Q37335428-128BD7FF-DA76-425A-8284-FF41112F1C58 wds:Q37335428-16C3199F-E738-4162-BD86-5E18B23462B4 wds:Q37335428-1A1680EE-86B6-4FBC-81E5-6871F4A87A3A wds:Q37335428-26E4E334-6961-403F-9725-2CA9CA3F3250 wds:Q37335428-4F872A26-CE11-4710-BD77-C76ADB066B4A wds:Q37335428-5A8935AD-7EAD-44A5-A66D-A524F5E96622 wds:Q37335428-63FCD62B-5E4D-45F0-A99F-F316C00070F3 wds:Q37335428-696E85DC-D111-4260-9062-321BFFC63D01 wds:Q37335428-6C01EF1D-A942-4B70-9F41-FEBFEBF5EC9E wds:Q37335428-708047F5-D71F-467B-8747-88830BA896C6 wds:Q37335428-7644F05D-0B65-4E5B-95A0-037172F8A3F8 wds:Q37335428-7ACD7910-9BE5-4740-B521-E1D07B5261D9 wds:Q37335428-8713CFDE-32F6-41DB-8BFA-DC9E01934DAA wds:Q37335428-8C5EF17F-8674-4F4D-934C-057BAF7BB783 wds:Q37335428-978BC5EF-E023-42E7-8A8E-97D92A8B6D5E wds:Q37335428-A0D0DD59-A484-457E-8649-8D1B59415DCE wds:Q37335428-BCF149D5-504F-448D-A9C0-5EFA9C304DAD wds:Q37335428-C36C3F4D-D098-483C-A732-F4508C93C480 wds:Q37335428-CC3D64B3-1086-4D91-9DEA-2FBE5F8E9595 wds:Q37335428-E4052BC8-6E4B-48FF-B900-14381FD562AE wds:Q37335428-EB84661E-5C16-40ED-8E01-13AEC4B5305F wds:Q37335428-FD82245D-CADD-44AB-9187-99E949DD9FA3 wds:Q37335428-FE223D1E-D1B9-4A56-BFD3-8F84F4883333
cites work	NMRPipe: a multidimensional spectral processing system based on UNIX pipes Role of COL4A1 in small-vessel disease and hemorrhagic stroke. Alport's syndrome, Goodpasture's syndrome, and type IV collagen. NMR View: A computer program for the visualization and analysis of NMR data Collagens, modifying enzymes and their mutations in humans, flies and worms Molecular structure of the collagen triple helix Structure validation by Calpha geometry: phi,psi and Cbeta deviation Collagen XXVIII, a novel von Willebrand factor A domain-containing protein with many imperfections in the collagenous domain Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans. Structures and functions associated with the group of mammalian lectins containing collagen-like sequences Temperature dependence of 1H chemical shifts in proteins Complete primary structure of the human type IV collagen alpha 4(IV) chain. Comparison with structure and expression of the other alpha (IV) chains X-linked Alport syndrome: natural history in 195 families and genotype- phenotype correlations in males. Type IV collagen of the glomerular basement membrane. Evidence that the chain specificity of network assembly is encoded by the noncollagenous NC1 domains Identification of a distinct type IV collagen alpha chain with restricted kidney distribution and assignment of its gene to the locus of X chromosome-linked Alport syndrome Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering The molecular structure of collagen Epidermolysis bullosa. II. Type VII collagen mutations and phenotype-genotype correlations in the dystrophic subtypes Genetic linkage of recessive dystrophic epidermolysis bullosa to the type VII collagen gene Equilibrium thermal transitions of collagen model peptides Characterization of collagen-like peptides containing interruptions in the repeating Gly-X-Y sequence Differential susceptibility of type X collagen to cleavage by two mammalian interstitial collagenases and 72-kDa type IV collagenase Conformational effects of Gly-X-Gly interruptions in the collagen triple helix. Cleavage of collagen type X by human synovial collagenase and neutrophil elastase. Atypical Gly-X-Y sequences surround interruptions in the repeating tripeptide pattern of basement membrane collagen Conformational features of a natural break in the type IV collagen Gly-X-Y repeat NMR shows hydrophobic interactions replace glycine packing in the triple helix at a natural break in the (Gly-X-Y)n repeat
author name string	wds:Q37335428-0145A6B2-6631-4A2E-B7CF-99055CBD623B wds:Q37335428-0FF3C848-3D97-42A7-B2D4-79000EE106A8 wds:Q37335428-1BC1C96E-8C2A-47CC-94BD-02D6EFAA4DC8 wds:Q37335428-59D0F379-2DB5-41C0-A434-74B2099952CC wds:Q37335428-7124DDDF-279F-4AD1-842D-B83BACE51E2F wds:Q37335428-943FD0BC-D73C-4239-A731-01DC9AF49E3E wds:Q37335428-E7972CB9-11D4-47CD-8695-1C268B529687
author name string	Yingjie Li Jean Baum Barbara Brodsky Angela Mohs Christopher Strafaci Geetha Thiagarajan Magdalena Popiel
rdfs:label	Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models (en) Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models (nl) Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models (ast)
skos:prefLabel	Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models (en) Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models (nl) Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models (ast)
name	Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models (en) Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models (nl) Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models (ast)

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