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Inaugural article: The glycosynapse
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Hakomori S. Inaugural article: the glycosynapse. Proc Natl Acad Sci USA. 99:2002;225-232. This paper, together with [4], describes some of the principal conceptual advances of glycosphingolipid function, many of which were made by this author.
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Proc Natl Acad Sci USA
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Identification of active site residue in glucosylceramide synthase. A nucleotide-binding catalytic motif conserved with processive β-glycosyltransferases
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Marks D.L., Dominguez M., Wu K., Pagano R.E. Identification of active site residue in glucosylceramide synthase. A nucleotide-binding catalytic motif conserved with processive β-glycosyltransferases. J Biol Chem. 276:2001;26492-26498.
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Marks, D.L.1
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0035851917
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Glycosphingolipids are required for sorting melanosomal proteins in the Golgi complex
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This work outlines a novel function for glucosylceramide - the intracellular transport of proteins to melanosomes.
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Sprong H., Degroote S., Claessens T., van Drunen J., Oorschot V., Westerink B.H., Hirabayashi Y., Klumperman J., van der Sluijs P., van Meer G. Glycosphingolipids are required for sorting melanosomal proteins in the Golgi complex. J Cell Biol. 155:2001;369-380. This work outlines a novel function for glucosylceramide - the intracellular transport of proteins to melanosomes.
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Sprong, H.1
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0035852635
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Physical and functional association of glycolipid N-acetyl-galactosaminyl and galactosyl transferases in the Golgi apparatus
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Using FRET (fluorescence resonance energy transfer), two glycosyltransferases that function sequentially are found in a physical complex in the Golgi apparatus.
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Giraudo C.G., Daniotti J.L., Maccioni H.J. Physical and functional association of glycolipid N-acetyl-galactosaminyl and galactosyl transferases in the Golgi apparatus. Proc Natl Acad Sci USA. 98:2001;1625-1630. Using FRET (fluorescence resonance energy transfer), two glycosyltransferases that function sequentially are found in a physical complex in the Golgi apparatus.
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Proc Natl Acad Sci USA
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Giraudo, C.G.1
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Functional organization of the Golgi apparatus in glycosphingolipid biosynthesis. Lactosylceramide and subsequent glycosphingolipids are formed in the lumen of the late Golgi
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Lannert H., Gorgas K., Meissner I., Wieland F.T., Jeckel D. Functional organization of the Golgi apparatus in glycosphingolipid biosynthesis. Lactosylceramide and subsequent glycosphingolipids are formed in the lumen of the late Golgi. J Biol Chem. 273:1998;2939-2946.
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Kasahara K., Watanabe K., Takeuchi K., Kaneko H., Oohira A., Yamamoto T., Sanai Y. Involvement of gangliosides in glycosylphosphatidylinositol-anchored neuronal cell adhesion molecule TAG-1 signaling in lipid rafts. J Biol Chem. 275:2000;34701-34709.
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Immunoseparation of sphingolipid-enriched membrane domains enriched in Src family protein tyrosine kinases and in the neuronal adhesion molecule TAG-1 by anti-GD3 ganglioside monoclonal antibody
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Prinetti A., Prioni S., Chigorno V., Karagogeos D., Tettamanti G., Sonnino S. Immunoseparation of sphingolipid-enriched membrane domains enriched in Src family protein tyrosine kinases and in the neuronal adhesion molecule TAG-1 by anti-GD3 ganglioside monoclonal antibody. J Neurochem. 78:2001;1162-1167.
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Werth N., Schuette C.G., Wilkening G., Lemm T., Sandhoff K. Degradation of membrane-bound ganglioside GM2 by β-hexosaminidase A. Stimulation by GM2 activator protein and lysosomal lipids. J Biol Chem. 276:2001;12685-12690.
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Mice with disrupted GM2/GD2 synthase gene lack complex gangliosides but exhibit only subtle defects in their nervous system
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Mice lacking complex gangliosides develop Wallerian degeneration and myelination defects
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Sheikh K.A., Sun J., Liu Y., Kawai H., Crawford T.O., Proia R.L., Griffin J.W., Schnaar R.L. Mice lacking complex gangliosides develop Wallerian degeneration and myelination defects. Proc Natl Acad Sci USA. 96:1999;7532-7537.
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Wu G., Xie X., Lu Z.H., Ledeen R.W. Cerebellar neurons lacking complex gangliosides degenerate in the presence of depolarizing levels of potassium. Proc Natl Acad Sci USA. 98:2001;307-312.
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Mice expressing only monosialoganglioside GM3 exhibit lethal audiogenic seizures
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This paper, together with [27], shows that gangliosides are essential for proper functioning of the nervous system.
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Kawai H., Allende M.L., Wada R., Kono M., Sango K., Deng C., Miyakawa T., Crawley J.N., Werth N., Bierfreund U., et al. Mice expressing only monosialoganglioside GM3 exhibit lethal audiogenic seizures. J Biol Chem. 276:2001;6885-6888. This paper, together with [27], shows that gangliosides are essential for proper functioning of the nervous system.
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Kawai, H.1
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Okada M., Itoh Mi M., Haraguchi M., Okajima T., Inoue M., Oishi H., Matsuda Y., Iwamoto T., Kawano T., Fukumoto S., et al. b-Series ganglioside deficiency exhibits no definite changes in the neurogenesis and the sensitivity to Fas-mediated apoptosis but impairs regeneration of the lesioned hypoglossal nerve. J Biol Chem. 277:2002;1633-1636.
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Refractory skin injury in the complex knock-out mice expressing only GM3 ganglioside
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Epidermal growth factor receptor glycosylation is required for ganglioside GM3 binding and GM3-mediated suppression of activation
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Ganglioside GM3 participates in the pathological conditions of insulin resistance
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This work presents an intriguing link between type 2 diabetes and expression of the GM3 ganglioside.
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Tagami S., Inokuchi Ji J., Kabayama K., Yoshimura H., Kitamura F., Uemura S., Ogawa C., Ishii A., Saito M., Ohtsuka Y., et al. Ganglioside GM3 participates in the pathological conditions of insulin resistance. J Biol Chem. 277:2002;3085-3092. This work presents an intriguing link between type 2 diabetes and expression of the GM3 ganglioside.
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A close association of ganglioside-specific sialidase, Neu 3, with caveolin in membrane microdomains
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Together with [44•], this paper shows an association of a ganglioside-specific sialidase with caveolae (and rafts). The results suggest that dynamic ganglioside changes may occur in microdomains.
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46
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50
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52
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Collins B.E., Ito H., Sawada N., Ishida H., Kiso M., Schnaar R.L. Enhanced binding of the neural siglecs, myelin-associated glycoprotein and Schwann cell myelin protein, to Chol-1 (α-series) gangliosides and novel sulfated Chol-1 analogs. J Biol Chem. 274:1999;37637-37643.
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53
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0031022517
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54
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55
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0037062511
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From the cover: Gangliosides are functional nerve cell ligands for myelin-associated glycoprotein (MAG), an inhibitor of nerve regeneration
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The authors show that gangliosides have an essential function in neuron-glia interactions by mediating the signal from MAG to control neurite growth.
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Vyas A.A., Patel H.V., Fromholt S.E., Heffer-Lauc M., Vyas K.A., Dang J., Schachner M., Schnaar R.L. From the cover: gangliosides are functional nerve cell ligands for myelin-associated glycoprotein (MAG), an inhibitor of nerve regeneration. Proc Natl Acad Sci USA. 99:2002;8412-8417. The authors show that gangliosides have an essential function in neuron-glia interactions by mediating the signal from MAG to control neurite growth.
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Proc Natl Acad Sci USA
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Vyas, A.A.1
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Dang, J.6
Schachner, M.7
Schnaar, R.L.8
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56
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0037071537
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The p75 receptor transduces the signal from myelin-associated glycoprotein to Rho
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NTR, which transmits the MAG signal across the neuronal plasma membrane to RhoA.
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NTR, which transmits the MAG signal across the neuronal plasma membrane to RhoA.
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J Cell Biol
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Yamashita, T.1
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