K
Kathleen Yang
Researcher at University of Washington
Publications - 4
Citations - 767
Kathleen Yang is an academic researcher from University of Washington. The author has contributed to research in topics: Osteogenesis imperfecta & Type I collagen. The author has an hindex of 4, co-authored 4 publications receiving 679 citations.
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Journal ArticleDOI
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
Joan C. Marini,Antonella Forlino,Antonella Forlino,Wayne A. Cabral,Aileen M. Barnes,James D. San Antonio,Sarah A. Milgrom,James C. Hyland,Jarmo Körkkö,Darwin J. Prockop,Anne De Paepe,Paul Coucke,Sofie Symoens,Francis H. Glorieux,Peter J. Roughley,Alan M. Lund,Kaija Kuurila-Svahn,Heini Hartikka,Daniel H. Cohn,Deborah Krakow,Monica Mottes,Ulrike Schwarze,Diana Chen,Kathleen Yang,Christine D Kuslich,James Troendle,Raymond Dalgleish,Peter H. Byers +27 more
TL;DR: The data on genotype–phenotype relationships indicate that the two collagen chains play very different roles in matrix integrity and that phenotype depends on intracellular and extracellular events.
Journal ArticleDOI
Mutation and polymorphism spectrum in osteogenesis imperfecta type II: implications for genotype–phenotype relationships
Dale L. Bodian,Ting-Fung Chan,Annie Poon,Ulrike Schwarze,Kathleen Yang,Peter H. Byers,Pui-Yan Kwok,Teri E. Klein +7 more
TL;DR: The results contribute to the understanding of the etiology of OI by providing data to evaluate and refine current models relating genotype to phenotype and by providing an unbiased indication of the relative frequency of mutations in OI-associated genes.
Journal ArticleDOI
Recurrence of perinatal lethal osteogenesis imperfecta in sibships: Parsing the risk between parental mosaicism for dominant mutations and autosomal recessive inheritance
TL;DR: In most populations, recurrence of lethal osteogenesis imperfecta usually results from parental mosaicism for dominant mutations, but the carrier frequency of recessive forms of osteogenesisperfecta will alter that proportion.
Journal ArticleDOI
Substitutions for arginine at position 780 in triple helical domain of the α1(I) chain alter folding of the type I procollagen molecule and cause osteogenesis imperfecta
Elena Makareeva,Guoli Sun,Lynn S. Mirigian,Edward L. Mertz,Juan Carlos Vera,Nydea A. Espinoza,Kathleen Yang,Diana Chen,Teri E. Klein,Peter H. Byers,Sergey Leikin +10 more
TL;DR: Investigating leucine and cysteine substitutions for one Y-position arginine, p.Arg958, of proα1(I) chains that cause mild OI observed slower triple helix folding and intracellular collagen retention, which disturbed the Endoplasmic Reticulum function and affected matrix deposition.