메뉴 건너뛰기




Volumn 21, Issue 3, 2011, Pages 278-285

Dystroglycanopathies: Coming into focus

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA DYSTROGLYCAN; DOLICHYL PHOSPHATE MANNOSYLTRANSFERASE POLYPEPTIDE 2; DOLICHYL PHOSPHATE MANNOSYLTRANSFERASE POLYPEPTIDE 3; FUKUTIN; FUKUTIN RELATED PROTEIN; GLYCOSYLTRANSFERASE; LIKE GLYCOSYLTRANSFERASE; MANNOSYLTRANSFERASE; N ACETYLGLUCOSAMINYLTRANSFERASE; PROTEIN O LINKED MANNOSE BETA 1,2 N ACETYLGLUCOSAMINYLTRANSFERASE; PROTEIN O MANNOSYLTRANSFERASE 1; PROTEIN O MANNOSYLTRANSFERASE 2; UNCLASSIFIED DRUG;

EID: 79957622998     PISSN: 0959437X     EISSN: 18790380     Source Type: Journal    
DOI: 10.1016/j.gde.2011.02.001     Document Type: Review
Times cited : (209)

References (48)
  • 5
    • 0035212037 scopus 로고    scopus 로고
    • Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan
    • Brockington M., Blake D.J., Prandini P., Brown S.C., Torelli S., Benson M.A., Ponting C.P., Estournet B., Romero N.B., Mercuri E., et al. Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan. Am J Hum Genet 2001, 69:1198-1209.
    • (2001) Am J Hum Genet , vol.69 , pp. 1198-1209
    • Brockington, M.1    Blake, D.J.2    Prandini, P.3    Brown, S.C.4    Torelli, S.5    Benson, M.A.6    Ponting, C.P.7    Estournet, B.8    Romero, N.B.9    Mercuri, E.10
  • 8
    • 10744226857 scopus 로고    scopus 로고
    • Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan
    • Longman C., Brockington M., Torelli S., Jimenez-Mallebrera C., Kennedy C., Khalil N., Feng L., Saran R.K., Voit T., Merlini L., et al. Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan. Hum Mol Genet 2003, 12:2853-2861.
    • (2003) Hum Mol Genet , vol.12 , pp. 2853-2861
    • Longman, C.1    Brockington, M.2    Torelli, S.3    Jimenez-Mallebrera, C.4    Kennedy, C.5    Khalil, N.6    Feng, L.7    Saran, R.K.8    Voit, T.9    Merlini, L.10
  • 13
    • 69949154343 scopus 로고    scopus 로고
    • A comparative study of alpha-dystroglycan glycosylation in dystroglycanopathies suggests that the hypoglycosylation of alpha-dystroglycan does not consistently correlate with clinical severity
    • Jimenez-Mallebrera C., Torelli S., Feng L., Kim J., Godfrey C., Clement E., Mein R., Abbs S., Brown S.C., Campbell K.P., et al. A comparative study of alpha-dystroglycan glycosylation in dystroglycanopathies suggests that the hypoglycosylation of alpha-dystroglycan does not consistently correlate with clinical severity. Brain Pathol 2009, 19:596-611.
    • (2009) Brain Pathol , vol.19 , pp. 596-611
    • Jimenez-Mallebrera, C.1    Torelli, S.2    Feng, L.3    Kim, J.4    Godfrey, C.5    Clement, E.6    Mein, R.7    Abbs, S.8    Brown, S.C.9    Campbell, K.P.10
  • 22
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti J.M., Campbell K.P. Membrane organization of the dystrophin-glycoprotein complex. Cell 1991, 66:1121-1131.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 23
    • 34548506985 scopus 로고    scopus 로고
    • Pinpointing the candidate region for muscular dystrophy in chickens with an abnormal muscle gene
    • Matsumoto H., Yoshizawa M.H., Sasazaki K., Fujiwara S., Kikuchi A.T. Pinpointing the candidate region for muscular dystrophy in chickens with an abnormal muscle gene. Anim Sci J 2007, 78:476-483.
    • (2007) Anim Sci J , vol.78 , pp. 476-483
    • Matsumoto, H.1    Yoshizawa, M.H.2    Sasazaki, K.3    Fujiwara, S.4    Kikuchi, A.T.5
  • 25
    • 32244440192 scopus 로고    scopus 로고
    • Dystroglycan: from biosynthesis to pathogenesis of human disease
    • Barresi R., Campbell K.P. Dystroglycan: from biosynthesis to pathogenesis of human disease. J Cell Sci 2006, 119:199-207.
    • (2006) J Cell Sci , vol.119 , pp. 199-207
    • Barresi, R.1    Campbell, K.P.2
  • 26
    • 0023410821 scopus 로고
    • Cranin: a laminin-binding protein of cell membranes
    • Smalheiser N.R., Schwartz N.B. Cranin: a laminin-binding protein of cell membranes. Proc Natl Acad Sci USA 1987, 84:6457-6461.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6457-6461
    • Smalheiser, N.R.1    Schwartz, N.B.2
  • 27
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function
    • Michele D.E., Campbell K.P. Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function. J Biol Chem 2003, 278:15457-15460.
    • (2003) J Biol Chem , vol.278 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 29
  • 33
    • 77955440095 scopus 로고    scopus 로고
    • Characterization of site-specific O-glycan structures within the mucin-like domain of alpha-dystroglycan from human skeletal muscle
    • Nilsson J., Nilsson J., Larson G., Grahn A. Characterization of site-specific O-glycan structures within the mucin-like domain of alpha-dystroglycan from human skeletal muscle. Glycobiology 2010, 20:1160-1169.
    • (2010) Glycobiology , vol.20 , pp. 1160-1169
    • Nilsson, J.1    Nilsson, J.2    Larson, G.3    Grahn, A.4
  • 35
    • 70349101617 scopus 로고    scopus 로고
    • Abnormal glycosylation of dystroglycan in human genetic disease
    • Hewitt J.E. Abnormal glycosylation of dystroglycan in human genetic disease. Biochim Biophys Acta 2009, 1792:853-861.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 853-861
    • Hewitt, J.E.1
  • 36
    • 44949102241 scopus 로고    scopus 로고
    • Developmental defects in a zebrafish model for muscular dystrophies associated with the loss of fukutin-related protein (FKRP)
    • Thornhill P., Bassett D., Lochmuller H., Bushby K., Straub V. Developmental defects in a zebrafish model for muscular dystrophies associated with the loss of fukutin-related protein (FKRP). Brain 2008, 131:1551-1561.
    • (2008) Brain , vol.131 , pp. 1551-1561
    • Thornhill, P.1    Bassett, D.2    Lochmuller, H.3    Bushby, K.4    Straub, V.5
  • 38
    • 60149086623 scopus 로고    scopus 로고
    • Reduced expression of fukutin related protein in mice results in a model for fukutin related protein associated muscular dystrophies
    • Ackroyd M.R., Skordis L., Kaluarachchi M., Godwin J., Prior S., Fidanboylu M., Piercy R.J., Muntoni F., Brown S.C. Reduced expression of fukutin related protein in mice results in a model for fukutin related protein associated muscular dystrophies. Brain 2009, 132:439-451.
    • (2009) Brain , vol.132 , pp. 439-451
    • Ackroyd, M.R.1    Skordis, L.2    Kaluarachchi, M.3    Godwin, J.4    Prior, S.5    Fidanboylu, M.6    Piercy, R.J.7    Muntoni, F.8    Brown, S.C.9
  • 39
  • 41
    • 78650845413 scopus 로고    scopus 로고
    • Transgenic overexpression of LARGE induces alpha-dystroglycan hyperglycosylation in skeletal and cardiac muscle
    • Brockington M., Torelli S., Sharp P.S., Liu K., Cirak S., Brown S.C., Wells D.J., Muntoni F. Transgenic overexpression of LARGE induces alpha-dystroglycan hyperglycosylation in skeletal and cardiac muscle. PLoS One 2010, 5:e14434.
    • (2010) PLoS One , vol.5
    • Brockington, M.1    Torelli, S.2    Sharp, P.S.3    Liu, K.4    Cirak, S.5    Brown, S.C.6    Wells, D.J.7    Muntoni, F.8
  • 44
    • 0034819780 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation type Ia and IIa are associated with different primary haemostatic complications
    • Van Geet C., Jaeken J., Freson K., Lenaerts T., Arnout J., Vermylen J., Hoylaerts M.F. Congenital disorders of glycosylation type Ia and IIa are associated with different primary haemostatic complications. J Inherit Metab Dis 2001, 24:477-492.
    • (2001) J Inherit Metab Dis , vol.24 , pp. 477-492
    • Van Geet, C.1    Jaeken, J.2    Freson, K.3    Lenaerts, T.4    Arnout, J.5    Vermylen, J.6    Hoylaerts, M.F.7
  • 46
    • 20144388364 scopus 로고    scopus 로고
    • An autosomal recessive limb girdle muscular dystrophy (LGMD2) with mild mental retardation is allelic to Walker-Warburg syndrome (WWS) caused by a mutation in the POMT1 gene
    • Balci B., Uyanik G., Dincer P., Gross C., Willer T., Talim B., Haliloglu G., Kale G., Hehr U., Winkler J., et al. An autosomal recessive limb girdle muscular dystrophy (LGMD2) with mild mental retardation is allelic to Walker-Warburg syndrome (WWS) caused by a mutation in the POMT1 gene. Neuromuscul Disord 2005, 15:271-275.
    • (2005) Neuromuscul Disord , vol.15 , pp. 271-275
    • Balci, B.1    Uyanik, G.2    Dincer, P.3    Gross, C.4    Willer, T.5    Talim, B.6    Haliloglu, G.7    Kale, G.8    Hehr, U.9    Winkler, J.10
  • 47
    • 18244375299 scopus 로고    scopus 로고
    • Mutations in the fukutin-related protein gene (FKRP) identify limb girdle muscular dystrophy 2I as a milder allelic variant of congenital muscular dystrophy MDC1C
    • Brockington M., Yuva Y., Prandini P., Brown S.C., Torelli S., Benson M.A., Herrmann R., Anderson L.V., Bashir R., Burgunder J.M., et al. Mutations in the fukutin-related protein gene (FKRP) identify limb girdle muscular dystrophy 2I as a milder allelic variant of congenital muscular dystrophy MDC1C. Hum Mol Genet 2001, 10:2851-2859.
    • (2001) Hum Mol Genet , vol.10 , pp. 2851-2859
    • Brockington, M.1    Yuva, Y.2    Prandini, P.3    Brown, S.C.4    Torelli, S.5    Benson, M.A.6    Herrmann, R.7    Anderson, L.V.8    Bashir, R.9    Burgunder, J.M.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.