Fibrillin-1 mutations causing Weill-Marchesani syndrome and acromicric and geleophysic dysplasias disrupt heparan sulfate interactions.

Cain, Stuart A; McGovern, Amanda; Baldwin, Andrew K; Baldock, Clair; Kielty, Cay M

Cain, Stuart A; McGovern, Amanda; Baldwin, Andrew K; Baldock, Clair; Kielty, Cay M.

Affiliation

Cain SA; Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester, United Kingdom. stuart.a.cain@manchester.ac.uk

PLoS One ; 7(11): e48634, 2012.

Article in En | MEDLINE | ID: mdl-23133647

Subject(s)

Bone Diseases, Developmental/genetics; Heparitin Sulfate/metabolism; Limb Deformities, Congenital/genetics; Microfilament Proteins/genetics; Mutation; Weill-Marchesani Syndrome/genetics; Binding Sites; Cell Line; Fibrillin-1; Fibrillin-2; Fibrillins; Fibroblasts/cytology; Gene Deletion; HEK293 Cells; Humans; Mutagenesis; Oligosaccharides/chemistry; Protein Isoforms; Protein Structure, Tertiary; Recombinant Proteins/chemistry

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bone Diseases, Developmental / Limb Deformities, Congenital / Weill-Marchesani Syndrome / Heparitin Sulfate / Microfilament Proteins / Mutation Limits: Humans Language: En Journal: PLoS One Journal subject: CIENCIA / MEDICINA Year: 2012 Document type: Article Affiliation country: United kingdom

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