File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Characterization of three osteogenesis imperfecta collagen α1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity

TitleCharacterization of three osteogenesis imperfecta collagen α1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity
Authors
Issue Date1992
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 1992, v. 288 n. 1, p. 131-135 How to Cite?
AbstractType I collagen α1(I) glycine to serine substitutions, resulting from G-to-A mutations, were defined in three cases of osteogenesis imperfecta (OI). The Gly substitutions displayed a gradient of phenotypic severity according to the location of the mutation in the collagen triple helix. The most C-terminal of these, Gly565 to Ser, led to the lethal perinatal (type II) form of OI, whereas the more N-terminal mutations, Gly415 and Gly352 to Ser, led to severe OI (type III/IV) and moderate OI (type IVB) respectively. These data support the notion that glycine substitutions towards the C-terminus of the α1(I) or α2(I) chains will be more clinically severe than those towards the N-terminus. This results from the more disruptive effect of the mutations at the C-terminus on helix initiation and C- and N-terminal helix directional propagation. This generalization must be modified by considering the nature of the glycine substitution and the surrounding amino acid sequence, since the helix is composed of subdomains of differing stability which will affect the ability of helix re-nucleation and propagation.
Persistent Identifierhttp://hdl.handle.net/10722/147366
ISSN
2015 Impact Factor: 3.562
2015 SCImago Journal Rankings: 2.582
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBateman, JFen_US
dc.contributor.authorMoeller, Ien_US
dc.contributor.authorHannagan, Men_US
dc.contributor.authorChan, Den_US
dc.contributor.authorCole, WGen_US
dc.date.accessioned2012-05-29T06:03:12Z-
dc.date.available2012-05-29T06:03:12Z-
dc.date.issued1992en_US
dc.identifier.citationBiochemical Journal, 1992, v. 288 n. 1, p. 131-135en_US
dc.identifier.issn0264-6021en_US
dc.identifier.urihttp://hdl.handle.net/10722/147366-
dc.description.abstractType I collagen α1(I) glycine to serine substitutions, resulting from G-to-A mutations, were defined in three cases of osteogenesis imperfecta (OI). The Gly substitutions displayed a gradient of phenotypic severity according to the location of the mutation in the collagen triple helix. The most C-terminal of these, Gly565 to Ser, led to the lethal perinatal (type II) form of OI, whereas the more N-terminal mutations, Gly415 and Gly352 to Ser, led to severe OI (type III/IV) and moderate OI (type IVB) respectively. These data support the notion that glycine substitutions towards the C-terminus of the α1(I) or α2(I) chains will be more clinically severe than those towards the N-terminus. This results from the more disruptive effect of the mutations at the C-terminus on helix initiation and C- and N-terminal helix directional propagation. This generalization must be modified by considering the nature of the glycine substitution and the surrounding amino acid sequence, since the helix is composed of subdomains of differing stability which will affect the ability of helix re-nucleation and propagation.en_US
dc.languageengen_US
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.orgen_US
dc.relation.ispartofBiochemical Journalen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshChilden_US
dc.subject.meshCollagen - Chemistry - Geneticsen_US
dc.subject.meshFemaleen_US
dc.subject.meshGlycine - Geneticsen_US
dc.subject.meshHot Temperatureen_US
dc.subject.meshHumansen_US
dc.subject.meshInfanten_US
dc.subject.meshInfant, Newbornen_US
dc.subject.meshMaleen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMutationen_US
dc.subject.meshNucleic Acid Heteroduplexesen_US
dc.subject.meshOsteogenesis Imperfecta - Geneticsen_US
dc.subject.meshPhenotypeen_US
dc.subject.meshProtein Denaturationen_US
dc.subject.meshRna, Messenger - Chemistryen_US
dc.subject.meshSerine - Geneticsen_US
dc.titleCharacterization of three osteogenesis imperfecta collagen α1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severityen_US
dc.typeArticleen_US
dc.identifier.emailChan, D:chand@hkucc.hku.hken_US
dc.identifier.authorityChan, D=rp00540en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid1445258-
dc.identifier.scopuseid_2-s2.0-0026492532en_US
dc.identifier.volume288en_US
dc.identifier.issue1en_US
dc.identifier.spage131en_US
dc.identifier.epage135en_US
dc.identifier.isiWOS:A1992JY71200019-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US
dc.identifier.scopusauthoridMoeller, I=7004124283en_US
dc.identifier.scopusauthoridHannagan, M=6507095190en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats