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26
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0029958839
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Alternative splicing of agrin alters its binding to heparin, dystroglycan and the putative agrin receptor
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See annotation [28]. of special interest
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Gesemann M, Cavalli V, Denzer AJ, Brancaccio A, Schumacher B, Ruegg MA. Alternative splicing of agrin alters its binding to heparin, dystroglycan and the putative agrin receptor. Neuron. 16:1996;755-767 See annotation [28]. of special interest.
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Gesemann, M.1
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0029887301
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See annotation [28]. of special interest
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Meier, T.1
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28
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0029670148
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Agrin binding to α-dystroglycan
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These three recent papers [26-28] call into question, through mutational analysis of agrin, whether the binding of agrin to dystroglycan is relevant to formation of the NMJ. of special interest
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Hopf C, Hoch W. Agrin binding to α-dystroglycan. J Biol Chem. 271:1996;5231-5236 These three recent papers [26-28] call into question, through mutational analysis of agrin, whether the binding of agrin to dystroglycan is relevant to formation of the NMJ. of special interest.
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Defective neuromuscular synaptogenesis in agrin-deficient mutant mice
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This paper details the recent finding that agrin is necessary for both pre- and postsynaptic differentiation of the NMJ, a finding strikingly similar to that for the receptor MuSK (see also [34]). of outstanding interest
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Gautam M, Noakes PG, Moscoso L, Rupp F, Scheller RH, Merlie JP, Sanes JR. Defective neuromuscular synaptogenesis in agrin-deficient mutant mice. Cell. 85:1986;525-535 This paper details the recent finding that agrin is necessary for both pre- and postsynaptic differentiation of the NMJ, a finding strikingly similar to that for the receptor MuSK (see also [34]). of outstanding interest.
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Gautam, M.1
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34
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15844417385
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The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo
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Demonstration that MuSK is required for NMJ formation. The similarity of the phenotype to the agrin-deficient phenotype (see [33]) gave the first clue that MuSK is the agrin receptor. of outstanding interest
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DeChiara TM, Bowen DC, Valenzuela DM, Simmons MV, Poueymirou WT, Thomas S, Kinetz E, Compton DL, Rojas E, Park JS, et al. The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo. Cell. 85:1996;501-512 Demonstration that MuSK is required for NMJ formation. The similarity of the phenotype to the agrin-deficient phenotype (see [33]) gave the first clue that MuSK is the agrin receptor. of outstanding interest.
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Dechiara, T.M.1
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35
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15844380040
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Agrin acts via a MuSK receptor complex
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This paper provides biochemical evidence that agrin can phosphorylate MuSK, and that agrin binds to MuSK in muscle cells. It also provides evidence for a MuSK-accessory component, MASC. of outstanding interest
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Glass DJ, Bowen DC, Stitt TN, Radziejewski C, Bruno J, Ryan TE, Gies DR, Shah S, Mattsson K, Burden SJ, et al. Agrin acts via a MuSK receptor complex. Cell. 85:1996;513-523 This paper provides biochemical evidence that agrin can phosphorylate MuSK, and that agrin binds to MuSK in muscle cells. It also provides evidence for a MuSK-accessory component, MASC. of outstanding interest.
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Cell
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Glass, D.J.1
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15844418441
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Treanor, J.1
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38
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15844365303
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GDNF-induced activation of the ret protein tyrosine kinase is mediated by GDNFR-alpha, a novel receptor for GDNF
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These two papers [37,38] provide an additional example, besides the MuSK system, of an 'alpha' component for an RTK. Jing et al.'s paper [38] is the first instance in which an RTK-associated alpha component has been cloned. of outstanding interest
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