Limited proteolysis as a tool to probe the tertiary conformation of dysferlin and structural consequences of patient missense variant L344P.

Woolger, Natalie; Bournazos, Adam; Sophocleous, Reece A; Evesson, Frances J; Lek, Angela; Driemer, Birgit; Sutton, R Bryan; Cooper, Sandra T

Woolger, Natalie; Bournazos, Adam; Sophocleous, Reece A; Evesson, Frances J; Lek, Angela; Driemer, Birgit; Sutton, R Bryan; Cooper, Sandra T.

Afiliación

Woolger N; From the Institute for Neuroscience and Muscle Research, Kids Research Institute, The Children's Hospital at Westmead, Locked Bag 4001, Westmead 2145, Australia.
Bournazos A; Discipline of Child and Adolescent Health, Faculty of Medicine, University of Sydney, Sydney 2006, Australia, and.
Sophocleous RA; From the Institute for Neuroscience and Muscle Research, Kids Research Institute, The Children's Hospital at Westmead, Locked Bag 4001, Westmead 2145, Australia.
Evesson FJ; Discipline of Child and Adolescent Health, Faculty of Medicine, University of Sydney, Sydney 2006, Australia, and.
Lek A; From the Institute for Neuroscience and Muscle Research, Kids Research Institute, The Children's Hospital at Westmead, Locked Bag 4001, Westmead 2145, Australia.
Driemer B; Discipline of Child and Adolescent Health, Faculty of Medicine, University of Sydney, Sydney 2006, Australia, and.
Sutton RB; From the Institute for Neuroscience and Muscle Research, Kids Research Institute, The Children's Hospital at Westmead, Locked Bag 4001, Westmead 2145, Australia.
Cooper ST; Discipline of Child and Adolescent Health, Faculty of Medicine, University of Sydney, Sydney 2006, Australia, and.

J Biol Chem ; 292(45): 18577-18591, 2017 11 10.

Article en En | MEDLINE | ID: mdl-28904177

Asunto(s)

Disferlina/genética; Músculo Esquelético/metabolismo; Distrofias Musculares/genética; Mutación Missense; Complejo de la Endopetidasa Proteasomal/metabolismo; Sustitución de Aminoácidos; Biopsia; Dominios C2; Calpaína/genética; Calpaína/metabolismo; Células Cultivadas; Disferlina/química; Disferlina/metabolismo; Células HEK293; Humanos; Peso Molecular; Fibras Musculares Esqueléticas/metabolismo; Fibras Musculares Esqueléticas/patología; Músculo Esquelético/patología; Distrofias Musculares/metabolismo; Distrofias Musculares/patología; Fragmentos de Péptidos/química; Fragmentos de Péptidos/genética; Fragmentos de Péptidos/metabolismo; Conformación Proteica; Pliegue de Proteína; Dominios y Motivos de Interacción de Proteínas; Estructura Terciaria de Proteína; Proteolisis; Proteínas Recombinantes de Fusión/química; Proteínas Recombinantes de Fusión/metabolismo; Proteínas Recombinantes/química; Proteínas Recombinantes/metabolismo

Palabras clave

conformational change; dysferlin; patient missense variant; protein conformation; protein domain; proteolysis; tertiary structure

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Texto completo: 1 Base de datos: MEDLINE Asunto principal: Músculo Esquelético / Mutación Missense / Complejo de la Endopetidasa Proteasomal / Disferlina / Distrofias Musculares Idioma: En Revista: J Biol Chem Año: 2017 Tipo del documento: Article

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