Free Access
Issue |
Med Sci (Paris)
Volume 24, Number 11, Novembre 2008
|
|
---|---|---|
Page(s) | 912 - 915 | |
Section | Nouvelles | |
DOI | https://doi.org/10.1051/medsci/20082411912 | |
Published online | 15 November 2008 |
- Kobuke K, Piccolo F, Garringer KW, et al. A common disease-associated missense mutation in alphasarcoglycan fails to cause muscular dystrophy in mice. Hum Mol Genet 2008; 17 : 1201–13. [Google Scholar]
- Bartoli M, Gicquel E, Barrault L, et al. Mannosidase I inhibition rescues the human [alpha]-sarcoglycan R77C recurrent mutation. Hum Mol Genet 2008; 17 : 1214–21. [Google Scholar]
- Roberds SL, Anderson RD, Ibraghimov-Beskrovnaya O, Campbell KP. Primary structure and muscle-specific expression of the 50-kDa dystrophin-associated glycoprotein (adhalin). J Biol Chem 1993; 268 : 23739–42. [Google Scholar]
- Roberds SL, Leturcq F, Allamand V, et al. Missense mutations in the adhalin gene linked to autosomal recessive muscular dystrophy. Cell 1994; 78 : 625–33. [Google Scholar]
- Piccolo F, Roberds SL, Jeanpierre M, et al. Primary adhalinopathy : a common cause of autosomal recessive muscular dystrophy of variable severity. Nat Genet 1995; 10 : 243–5. [Google Scholar]
- Carrié A, Piccolo F, Leturcq F, et al. Mutational diversity and hot spots in the alpha-sarcoglycan gene in autosomal recessive muscular dystrophy (LGMD2D). J Med Genet 1997; 34 : 470–5. [Google Scholar]
- Eymard B, Romero NB, Leturcq F, et al. Primary adhalinopathy (alpha-sarcoglycanopathy) : clinical, pathological and genetic correlation in twenty patients with autosomal recessive muscular dystrophy. Neurology 1997; 4 : 1227–34. [Google Scholar]
- Kaplan JC, Beckmann JS, Fardeau M. Limb girdle muscular dystrophies. In : Karpati G, Hilton-Jones D, Griggs R, eds. Disorders of voluntary muscle, chapter 20, 7e ed. Cambridge : Cambridge University Press, 2001 : 433–63. [Google Scholar]
- Ervasti JM, Campbell KP. Membrane organization of the dystrophin-glycoprotein complex. Cell 1991; 66 : 1121–31. [Google Scholar]
- Ozawa E, Mizuno Y, Hagiwara Y, et al . Molecular and cell biology of the sarcoglycan complex. Muscle Nerve 2005; 32 : 563–76. [Google Scholar]
- Holt K, Campbell K. Assembly of the sarcoglycan complex. Insights for muscular dystrophy. J Biol Chem 1998; 23 : 34667–70. [Google Scholar]
- Allikian MJ, McNally EM. Processing and assembly of the dystrophin glycoprotein complex. Traffic 2007; 8 : 177–83. [Google Scholar]
- Lim L, Campbell K. The sarcoglycan complex in limbgirdle muscular dystrophy. Curr Opin Neurol 1998; 11 : 443–52. [Google Scholar]
- Trabelsi M, Kavian N, Daoud F, et al. Revised spectrum of mutations in sarcoglycanopathies. Eur J Hum Genet 2008; 16 : 793–803. [Google Scholar]
- Duclos F, Straub V, Moore SA, et al. Progressive muscular dystrophy in alpha-sarcoglycan-deficient mice. J Cell Biol 1998; 142 : 1461–71. [Google Scholar]
- Durbeej M, Campbell KP. Muscular dystrophies involving the dystrophin-glycoprotein complex : an overview of current mouse models. Curr Opin Genet Dev 2002; 12 : 349–61. [Google Scholar]
- LOVD. Leiden Muscular Dystrophy pages. http://www. dmd.nl/nmdb/home.php [Google Scholar]
- Draviam RA, Wang B, Shand SH, et al. Alphasarcoglycan is recycled from the plasma membrane in the absence of sarcoglycan complex assembly. Traffic 2006; 7 : 793–810. [Google Scholar]
- Hebert DN , Molinari M. In and out of the ER : protein folding, quality control, degradation, and related human diseases. Physiol Rev 2007; 87 : 1377–408. [Google Scholar]
- Roth J, Yam GH, Fan J, et al. Protein quality control : the who’s who, the where’s and therapeutic escapes. Histochem Cell Biol 2008; 129 : 163–77. [Google Scholar]
- Elbein AD, Kerbacher JK, Schwartz CJ, Sprague EA. Kifunensine inhibits glycoprotein processing and the function of the modified LDL receptor in endothelial cells. Arch Biochem Biophys 1991; 288 : 177–84. [Google Scholar]
- Tokunaga F, Brostrom C, Koide T, Arvan P. Endoplasmic reticulum (ER)-associated degradation of misfolded N-linked glycoproteins is suppressed upon inhibition of ER mannosidase I. J Biol Chem 2000; 275 : 40757–64. [Google Scholar]
- Gregersen N, Bross P, Vang S, Christensen JH. Protein misfolding and human disease. Annu Rev Genomics Hum Genet 2006; 7 : 103–24. [Google Scholar]
- Aridor M. Visiting the ER : the endoplasmic reticulum as a target for therapeutics in traffic related diseases. Adv Drug Deliv Rev 2007; 59 : 759–81. [Google Scholar]
- French PJ, van Doorninck JH, Peters RH, et al. A delta F508 mutation in mouse cystic fibrosis transmembrane conductance regulator results in a temperature-sensitive processing defect in vivo. J Clin Invest 1996; 98 : 1304–12. [Google Scholar]
- Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007; 8 : 519–29. [Google Scholar]
- Bernier V, Lagacé M, Bichet DG, Bouvier M. Pharmacological chaperones : potential treatment for conformational diseases. Trends Endocrinol Metab 2004; 15 : 222–8. [Google Scholar]
- Fan JQ. A counterintuitive approach to treat enzyme deficiencies : use of enzyme inhibitors for restoring mutant enzyme activity. Biol Chem 2008; 389 : 1–11. [Google Scholar]
- Hamanaka R, Shinohara T, Yano S, et al. Rescue of mutant alpha-galactosidase A in the endoplasmic reticulum by 1-deoxygalactonojirimycin leads to trafficking to lysosomes. Biochim Biophys Acta 2008; 1782 : 408–13. [Google Scholar]
- Pey AL, Ying M, Cremades N, et al. Identification of pharmacological chaperones as potential therapeutic agents to treat phenylketonuria. J Clin Invest 2008; 118 : 2858–67. [Google Scholar]
- Tropak MB, Mahuran D. Lending a helping hand, screening chemical libraries for compounds that enhance beta-hexosaminidase; A activity in GM2 gangliosidosis cells. FEBS Journal 2007; 274 : 4951–61. [Google Scholar]
- Balch WE, Morimoto RI, Dillin A, Kelly JW. Adapting proteostasis for disease intervention. Science 2008; 319 : 916–9. [Google Scholar]
- Foufelle F, Ferré P. La réponse UPR : son rôle physiologique et physiopathologique. Med Sci (Paris) 2007; 23 : 291–6. [Google Scholar]
- Yon-Kahn J. Repliement des protéines : études in vitro. Med Sci (Paris) 2005; 21 : 601–7. [Google Scholar]
- Goldberg ME. Le repliement des protéines : seconde traduction du message génétique. Med Sci (Paris) 2005; 21 : 563–6. [Google Scholar]
- Kaplan JC, Delpech M. Biologie moléculaire et médecine, 3e ed. Collection De la biologie à la clinique. Paris : Flammarion Médecine-Sciences, 2007 : 820 p. [Google Scholar]
- Chevet E. Inflammation intestinale et stress du réticulum endoplasmique : un lien génétique. Med Sci (Paris) 2008; 24 : 899–900. [Google Scholar]
Current usage metrics show cumulative count of Article Views (full-text article views including HTML views, PDF and ePub downloads, according to the available data) and Abstracts Views on Vision4Press platform.
Data correspond to usage on the plateform after 2015. The current usage metrics is available 48-96 hours after online publication and is updated daily on week days.
Initial download of the metrics may take a while.