Knowledge Management on the Novel LAGE-Like GlcNAc-Transferase Protein Family
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Publisher
Springer Berlin Heidelberg
Link
http://link.springer.com/content/pdf/10.1007/978-3-642-10616-3_19.pdf
Reference21 articles.
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2. Grewal, P.K., Holzfeind, P.J., Bittner, R.E., Hewitt, J.E.: Mutant glycosyltransferase and altered glycosylation of alpha-dystroglycan in the myodystrophy mouse. Nat. Genet. 28, 151–154 (2001)
3. Holzfeind, P.J., Grewal, P.K., Reitsamer, H.A., Kechvar, J., Lassmann, H., Hoeger, H., Hewitt, J.E., Bittner, R.E.: Skeletal, cardiac and tongue muscle pathology, defective retinal transmission, and neuronal migration defects in the Large(myd) mouse defines a natural model for glycosylation-deficient muscle - eye - brain disorders. Hum. Mol. Genet. 11, 2673–2687 (2002)
4. Longman, C., Brockington, M., Torelli, S., Jimenez-Mallebrera, C., Kennedy, C., Khalil, N., Feng, L., Saran, R.K., Voit, T., Merlini, L., Sewry, C.A., Brown, S.C., Muntoni, F.: 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. 12, 2853–2861 (2003)
5. Busch, C., Hofmann, F., Selzer, J., Munro, S., Jeckel, D., Aktories, K.: A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins. J. Biol. Chem. 273, 19566–19572 (1998)
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