Substitutions for arginine at position 780 in triple helical domain of the &#945;1(I) chain alter folding of the type I procollagen molecule and cause osteogenesis imperfecta.

Makareeva, Elena; Sun, Guoli; Mirigian, Lynn S; Mertz, Edward L; Vera, Juan C; Espinoza, Nydea A; Yang, Kathleen; Chen, Diana; Klein, Teri E; Byers, Peter H; Leikin, Sergey

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.

Makareeva, Elena; Sun, Guoli; Mirigian, Lynn S; Mertz, Edward L; Vera, Juan C; Espinoza, Nydea A; Yang, Kathleen; Chen, Diana; Klein, Teri E; Byers, Peter H; Leikin, Sergey.

Afiliação

Makareeva E; Section on Physical Biochemistry, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America.
Sun G; Department of Pathology, University of Washington, Seattle, Washington, United States of America.
Mirigian LS; Section on Physical Biochemistry, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America.
Mertz EL; Section on Physical Biochemistry, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America.
Vera JC; Section on Physical Biochemistry, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America.
Espinoza NA; Section on Physical Biochemistry, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America.
Yang K; Department of Pathology, University of Washington, Seattle, Washington, United States of America.
Chen D; Department of Pathology, University of Washington, Seattle, Washington, United States of America.
Klein TE; Department of Genetics, Stanford University, Palo Alto, California, United States of America.
Byers PH; Department of Pathology, University of Washington, Seattle, Washington, United States of America.
Leikin S; Department of Medicine, Division of Medical Genetics, University of Washington, Seattle, Washington, United States of America.

PLoS One ; 13(7): e0200264, 2018.

Article em En | MEDLINE | ID: mdl-29990383

Assuntos

Arginina/metabolismo; Colágeno Tipo I/metabolismo; Osteogênese Imperfeita/metabolismo; Pró-Colágeno/metabolismo; Dicroísmo Circular; Colágeno Tipo I/genética; Humanos; Mutação; Osteogênese Imperfeita/genética; Pró-Colágeno/genética; Dobramento de Proteína

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Osteogênese Imperfeita / Arginina / Pró-Colágeno / Colágeno Tipo I Limite: Humans Idioma: En Revista: PLoS One Ano de publicação: 2018 Tipo de documento: Article

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