676 resultados para PURINE NUCLEOSIDE PHOSPHORYLASE
Filtro por publicador
- ABACUS. Repositorio de Producción Científica - Universidad Europea (1)
- Academic Archive On-line (Stockholm University; Sweden) (1)
- Adam Mickiewicz University Repository (1)
- AMS Tesi di Dottorato - Alm@DL - Università di Bologna (4)
- AMS Tesi di Laurea - Alm@DL - Università di Bologna (1)
- ArchiMeD - Elektronische Publikationen der Universität Mainz - Alemanha (9)
- Aston University Research Archive (20)
- Biblioteca de Teses e Dissertações da USP (2)
- Biblioteca Digital | Sistema Integrado de Documentación | UNCuyo - UNCUYO. UNIVERSIDAD NACIONAL DE CUYO. (1)
- Biblioteca Digital da Produção Intelectual da Universidade de São Paulo (17)
- Biblioteca Digital da Produção Intelectual da Universidade de São Paulo (BDPI/USP) (57)
- Biblioteca Virtual del Sistema Sanitario Público de Andalucía (BV-SSPA), Junta de Andalucía. Consejería de Salud y Bienestar Social, Spain (7)
- Bioline International (2)
- BORIS: Bern Open Repository and Information System - Berna - Suiça (97)
- Brock University, Canada (2)
- Bucknell University Digital Commons - Pensilvania - USA (1)
- CentAUR: Central Archive University of Reading - UK (11)
- Cochin University of Science & Technology (CUSAT), India (6)
- Consorci de Serveis Universitaris de Catalunya (CSUC), Spain (23)
- Cor-Ciencia - Acuerdo de Bibliotecas Universitarias de Córdoba (ABUC), Argentina (1)
- CORA - Cork Open Research Archive - University College Cork - Ireland (1)
- Digital Commons - Michigan Tech (2)
- Digital Commons at Florida International University (7)
- Digital Knowledge Repository of Central Drug Research Institute (1)
- DigitalCommons@The Texas Medical Center (28)
- Doria (National Library of Finland DSpace Services) - National Library of Finland, Finland (7)
- DRUM (Digital Repository at the University of Maryland) (1)
- Duke University (2)
- eResearch Archive - Queensland Department of Agriculture; Fisheries and Forestry (3)
- Glasgow Theses Service (2)
- Instituto Politécnico de Bragança (1)
- Instituto Politécnico do Porto, Portugal (11)
- Lume - Repositório Digital da Universidade Federal do Rio Grande do Sul (1)
- Memorial University Research Repository (1)
- National Center for Biotechnology Information - NCBI (78)
- Plymouth Marine Science Electronic Archive (PlyMSEA) (2)
- QUB Research Portal - Research Directory and Institutional Repository for Queen's University Belfast (3)
- Repositório da Produção Científica e Intelectual da Unicamp (1)
- Repositório do Centro Hospitalar de Lisboa Central, EPE - Centro Hospitalar de Lisboa Central, EPE, Portugal (3)
- Repositório Institucional da Universidade Estadual de São Paulo - UNESP (1)
- Repositório Institucional da Universidade Federal do Rio Grande do Norte (1)
- Repositório Institucional UNESP - Universidade Estadual Paulista "Julio de Mesquita Filho" (84)
- RUN (Repositório da Universidade Nova de Lisboa) - FCT (Faculdade de Cienecias e Technologia), Universidade Nova de Lisboa (UNL), Portugal (3)
- Savoirs UdeS : plateforme de diffusion de la production intellectuelle de l’Université de Sherbrooke - Canada (2)
- Scielo Saúde Pública - SP (37)
- Universidad del Rosario, Colombia (1)
- Universidad Politécnica de Madrid (1)
- Universidade do Minho (5)
- Universidade Federal do Pará (2)
- Universidade Federal do Rio Grande do Norte (UFRN) (4)
- Université de Lausanne, Switzerland (69)
- Université de Montréal (1)
- Université de Montréal, Canada (9)
- University of Canberra Research Repository - Australia (1)
- University of Queensland eSpace - Australia (36)
Resumo:
McArdle disease is an autosomal recessive disorder caused by inherited deficiency of the muscle isoform of glycogen phosphorylase (or ‘myophosphorylase´), which catalyzes the first step of glycogen catabolism, releasing glucose-1-phosphate from glycogen deposits. As a result, muscle metabolism is impaired, leading to different degrees of exercise intolerance. Patients range from asymptomatic to severely affected, including in some cases limitations in activities of daily living. The PYGM gene codifies myophosphoylase and to date 147 pathogenic mutations and 39 polymorphisms have been reported. Exon 1 and 17 are mutational hot-spots in PYGM and 50% of the described mutations are missense.