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Murine semaphorin D/collapsin is a member of a diverse gene family and creates domains inhibitory for axonal extension
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Püschel AW. The semaphorins: a family of axonal guidance molecules? Eur J Neurosci. 8:1996;1317-1321.
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Culotti JG, Kolodkin AL. Functions of netrins and semaphorins in axon guidance. Curr Opin Neurobiol. 6:1996;81-88.
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Cloning and expression of a novel murine semaphorin with structural similarity to insect semaphorin 1
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Zhou L, White FA, Lentz SL, Wright DE, Fisher DA, Snider WD. Cloning and expression of a novel murine semaphorin with structural similarity to insect semaphorin 1. Mol Cell Neurosci. 9:1997;26-41.
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Snider, W.D.6
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Adams RH, Betz H, Püschel AW. A novel class of murine semaphorins with homology to thrombospondin is differentially expressed during early embryogenesis. Mech Dev. 57:1996;33-45.
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Collapsin: A protein in brain that induces the collapse and paralysis of neuronal growth cones
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Luo Y, Raible D, Raper JA. Collapsin: a protein in brain that induces the collapse and paralysis of neuronal growth cones. Cell. 75:1993;217-227.
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Fan J, Raper JA. Localized collapsing cues can steer growth cones without inducing their full collapse. Neuron. 14:1995;263-274.
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Motor axon subpopulations respond differentially to the chemorepellents netrin-1 and semaphorin D
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Varela-Echavarria A, Tucker A, Püschel AW, Guthrie S. Motor axon subpopulations respond differentially to the chemorepellents netrin-1 and semaphorin D. Neuron. 18:1997;193-207.
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Varela-Echavarria, A.1
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Püschel, A.W.3
Guthrie, S.4
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14
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0026467112
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Fasciclin IV: Sequence, expression, and function during growth cone guidance in the grasshopper embryo
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Kolodkin AL, Matthes DJ, O'Connor TP, Patel NH, Admon A, Bentley D, Goodman CS. Fasciclin IV: sequence, expression, and function during growth cone guidance in the grasshopper embryo. Neuron. 9:1992;831-845.
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Kolodkin, A.L.1
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Bentley, D.6
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15
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Semaphorin II can function as a selective inhibitor of specific synaptic arborizations
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Matthes DJ, Sink H, Kolodkin AL, Goodman CS. Semaphorin II can function as a selective inhibitor of specific synaptic arborizations. Cell. 81:1995;631-639.
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Transmembrane grasshopper Semaphorin I promotes axon outgrowth in vivo
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Wong JTW, Yu WTC, O'Connor TP. Transmembrane grasshopper Semaphorin I promotes axon outgrowth in vivo. Development. 124:1997;3597-3607.
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Wong, J.T.W.1
Yu, W.T.C.2
O'Connor, T.P.3
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0032005462
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The transmembrane semaphorin Sema I is required in Drosophila for embryonic motor and CNS axon guidance
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Yu H-H, Araj HH, Ralls SA, Kolodkin AL. The transmembrane semaphorin Sema I is required in Drosophila for embryonic motor and CNS axon guidance. Neuron. 20:1998;207-220.
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Yu H-H1
Araj, H.H.2
Ralls, S.A.3
Kolodkin, A.L.4
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18
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0030847193
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Neuropilin is a receptor for the axonal chemorepellent semaphorin III
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of outstanding interest. See annotation [19].
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of outstanding interest He Z, Tessier-Lavigne M. Neuropilin is a receptor for the axonal chemorepellent semaphorin III. Cell. 90:1997;739-751 See annotation [19].
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Cell
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He, Z.1
Tessier-Lavigne, M.2
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19
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0030829388
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Neuropilin is a semaphorin III receptor
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of outstanding interest. These two papers [18,19] report expression cloning of Sema III receptors. The cloning strategies adopted in these two studies are basically the same: COS cell cDNA expression libraries constructed using mRNA of E14 rat DRG or spinal cord were screened using an AP-tagged Sema III fusion protein. These two independent approaches have arrived at the same conclusion, namely that Sema III binds to a membrane protein homologous to neuropilin, which was previously isolated in various vertebrate species (see [21-24]).
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of outstanding interest Kolodkin AL, Levengood DV, Rowe EG, Tai Y-T, Giger RJ, Ginty DD. Neuropilin is a semaphorin III receptor. Cell. 90:1997;753-762 These two papers [18,19] report expression cloning of Sema III receptors. The cloning strategies adopted in these two studies are basically the same: COS cell cDNA expression libraries constructed using mRNA of E14 rat DRG or spinal cord were screened using an AP-tagged Sema III fusion protein. These two independent approaches have arrived at the same conclusion, namely that Sema III binds to a membrane protein homologous to neuropilin, which was previously isolated in various vertebrate species (see [21-24]).
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(1997)
Cell
, vol.90
, pp. 753-762
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Kolodkin, A.L.1
Levengood, D.V.2
Rowe, E.G.3
Tai Y-T4
Giger, R.J.5
Ginty, D.D.6
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20
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0030778454
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Neuropilin-semaphorin III/D-mediated chemorepulsive signals play a crucial role in peripheral nerve projection in mice
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of outstanding interest. This paper reports the phenotype of neuropilin-1 null mutant mice, which were generated by targeted disruption of the neuropilin (neuropilin-1) gene. The neuropilin-1 mutant mice were embryonic lethal, probably owing to abnormal development of the vascular system. Live homozygous mutant embryos were observed as late as E12.5, and showed severe abnormalities in the trajectory of the cranial and spinal nerves that expressed neuropilin-1 in normal embryos. The paper also reports that DRG growth cones of the neuropilin-1 mutants are perfectly protected from Sema III-induced collapse in vitro.
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of outstanding interest Kitsukawa T, Shimizu M, Sanbo M, Hirata T, Taniguchi M, Bekku Y, Yagi T, Fujisawa H. Neuropilin-semaphorin III/D-mediated chemorepulsive signals play a crucial role in peripheral nerve projection in mice. Neuron. 19:1997;995-1005 This paper reports the phenotype of neuropilin-1 null mutant mice, which were generated by targeted disruption of the neuropilin (neuropilin-1) gene. The neuropilin-1 mutant mice were embryonic lethal, probably owing to abnormal development of the vascular system. Live homozygous mutant embryos were observed as late as E12.5, and showed severe abnormalities in the trajectory of the cranial and spinal nerves that expressed neuropilin-1 in normal embryos. The paper also reports that DRG growth cones of the neuropilin-1 mutants are perfectly protected from Sema III-induced collapse in vitro.
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(1997)
Neuron
, vol.19
, pp. 995-1005
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Kitsukawa, T.1
Shimizu, M.2
Sanbo, M.3
Hirata, T.4
Taniguchi, M.5
Bekku, Y.6
Yagi, T.7
Fujisawa, H.8
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21
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0023217141
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Specific cell surface labels in the visual centers of Xenopus laevis tadpole identified using monoclonal antibodies
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Takagi S, Tsuji T, Amagai T, Takamatsu T, Fujisawa H. Specific cell surface labels in the visual centers of Xenopus laevis tadpole identified using monoclonal antibodies. Dev Biol. 122:1987;90-100.
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Takagi, S.1
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Amagai, T.3
Takamatsu, T.4
Fujisawa, H.5
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22
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0025866476
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The A5 antigen, a candidate for the neuronal recognition molecule, has homologies to complement components and coagulation factors
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Takagi S, Hirata T, Agata K, Mochii M, Eguchi G, Fujisawa H. The A5 antigen, a candidate for the neuronal recognition molecule, has homologies to complement components and coagulation factors. Neuron. 7:1991;295-307.
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Takagi, S.1
Hirata, T.2
Agata, K.3
Mochii, M.4
Eguchi, G.5
Fujisawa, H.6
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23
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0029093153
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Expression of a cell adhesion molecule, neuropilin, in the developing chick nervous system
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Takagi S, Kasuya Y, Shimizu M, Matsuura T, Tsuboi M, Kawakami A, Fujisawa H. Expression of a cell adhesion molecule, neuropilin, in the developing chick nervous system. Dev Biol. 170:1995;207-222.
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Dev Biol
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Takagi, S.1
Kasuya, Y.2
Shimizu, M.3
Matsuura, T.4
Tsuboi, M.5
Kawakami, A.6
Fujisawa, H.7
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24
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0030032861
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Developmentally regulated expression of a cell surface protein, neuropilin, in the mouse nervous system
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Kawakami A, Kitsukawa T, Takagi S, Fujisawa H. Developmentally regulated expression of a cell surface protein, neuropilin, in the mouse nervous system. J Neurobiol. 29:1996;1-17.
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Kawakami, A.1
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Takagi, S.3
Fujisawa, H.4
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25
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0342872023
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Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III
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of outstanding interest. This paper reports a new member of the neuropilin family, neuropilin-2, in mice. A rat neuropilin-2 homologue was reported in another paper (see [19]). In mice, several isoforms of neuropilin-2 have been isolated: neuropilin-2a, neuropilin-2b, and at least three other neuropilin-2a isoforms with insertions of amino acids. This paper also reports that neuropilin-2a is expressed in embryonic tissues, including neural tissue, and distributes in a mostly complementary manner to neuropilin-1 (see [24]). The paper also shows that neuropilin-1 can bind Sema III, Sema E and Sema IV, whereas neuropilin-2 binds Sema E and Sema IV but not Sema III. On the bases of these findings, the authors propose that the specificity of action of different semaphorin members to different neuron classes is determined by differential expression of neuropilin family members, even though the role of neuropilin-2 in semaphorin signaling has not yet been determined.
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of outstanding interest Chen H, Chédotal A, He Z, Goodman CS, Tessier-Lavigne M. Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III. Neuron. 19:1997;547-559 This paper reports a new member of the neuropilin family, neuropilin-2, in mice. A rat neuropilin-2 homologue was reported in another paper (see [19]). In mice, several isoforms of neuropilin-2 have been isolated: neuropilin-2a, neuropilin-2b, and at least three other neuropilin-2a isoforms with insertions of amino acids. This paper also reports that neuropilin-2a is expressed in embryonic tissues, including neural tissue, and distributes in a mostly complementary manner to neuropilin-1 (see [24]). The paper also shows that neuropilin-1 can bind Sema III, Sema E and Sema IV, whereas neuropilin-2 binds Sema E and Sema IV but not Sema III. On the bases of these findings, the authors propose that the specificity of action of different semaphorin members to different neuron classes is determined by differential expression of neuropilin family members, even though the role of neuropilin-2 in semaphorin signaling has not yet been determined.
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(1997)
Neuron
, vol.19
, pp. 547-559
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Chen, H.1
Chédotal, A.2
He, Z.3
Goodman, C.S.4
Tessier-Lavigne, M.5
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26
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0030730838
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Role of a neuronal cell-surface molecule, neuropilin, in nerve fiber fasciculation and guidance
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Fujisawa H, Kitsukawa T, Kawakami A, Takagi S, Shimizu M, Hirata T. Role of a neuronal cell-surface molecule, neuropilin, in nerve fiber fasciculation and guidance. Cell Tissue Res. 290:1997;465-470.
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Cell Tissue Res
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Fujisawa, H.1
Kitsukawa, T.2
Kawakami, A.3
Takagi, S.4
Shimizu, M.5
Hirata, T.6
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27
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0030930310
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Secreted chick semaphorins bind recombinant neuropilin with similar affinities but different subsets of neurons in situ
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of special interest. The authors produced AP-tagged Coll-1, Coll-2, Coll-3, and Coll-5, and then tested their binding to tissue sections and recombinant neuropilin (neuropilin-1) protein. All of the AP-tagged collapsins bound to recombinant neuropilin-1 protein with similar affinities, whereas each collapsin exhibited a different binding profile in neuronal tissue. The authors also report that the carboxyl tail of each collapsin binds strongly to neuropilin-1 even though the profile of its binding to tissue sections is not specific for each collapsin member. In contrast, the semaphorin domain binds to tissue sections in a pattern specific for each collapsin.
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of special interest Feiner L, Koppel AM, Kobayashi H, Raper J. Secreted chick semaphorins bind recombinant neuropilin with similar affinities but different subsets of neurons in situ. Neuron. 19:1997;539-545 The authors produced AP-tagged Coll-1, Coll-2, Coll-3, and Coll-5, and then tested their binding to tissue sections and recombinant neuropilin (neuropilin-1) protein. All of the AP-tagged collapsins bound to recombinant neuropilin-1 protein with similar affinities, whereas each collapsin exhibited a different binding profile in neuronal tissue. The authors also report that the carboxyl tail of each collapsin binds strongly to neuropilin-1 even though the profile of its binding to tissue sections is not specific for each collapsin member. In contrast, the semaphorin domain binds to tissue sections in a pattern specific for each collapsin.
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(1997)
Neuron
, vol.19
, pp. 539-545
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Feiner, L.1
Koppel, A.M.2
Kobayashi, H.3
Raper, J.4
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28
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0030664097
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Neuronal and non-neuronal collapsin-1 binding sites in developing chick are distinct from other semaphorin binding sites
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Takahashi T, Nakamura F, Strittmatter SM. Neuronal and non-neuronal collapsin-1 binding sites in developing chick are distinct from other semaphorin binding sites. J Neurosci. 17:1997;9183-9193.
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(1997)
J Neurosci
, vol.17
, pp. 9183-9193
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Takahashi, T.1
Nakamura, F.2
Strittmatter, S.M.3
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29
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0030665043
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Structural features of collapsin required for biological activity and distribution of binding sites in the developing chick
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Eickholt BJ, Morrow R, Walsh FS, Doherty P. Structural features of collapsin required for biological activity and distribution of binding sites in the developing chick. Mol Cell Neurosci. 9:1997;358-371.
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Mol Cell Neurosci
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Eickholt, B.J.1
Morrow, R.2
Walsh, F.S.3
Doherty, P.4
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30
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0028973307
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The guidance molecule semaphorin III is expressed in regions of spinal cord and periphery avoided by growing sensory axons
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Wright DE, White FA, Gerfen RW, Silos-Santiago I, Snider WD. The guidance molecule semaphorin III is expressed in regions of spinal cord and periphery avoided by growing sensory axons. J Comp Neurol. 361:1995;321-333.
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Wright, D.E.1
White, F.A.2
Gerfen, R.W.3
Silos-Santiago, I.4
Snider, W.D.5
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31
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0029904748
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Anatomy of rat semaphorin III/collapsin-1 mRNA expression and relationship to developing nerve tracts during neuroembryogenesis
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Giger RJ, Wolfer DP, De Wit MJ, Verhaagen J. Anatomy of rat semaphorin III/collapsin-1 mRNA expression and relationship to developing nerve tracts during neuroembryogenesis. J Comp Neurol. 375:1996;378-392.
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Giger, R.J.1
Wolfer, D.P.2
De Wit, M.J.3
Verhaagen, J.4
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32
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0030987542
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Disruption of semaphorin III/D gene causes severe abnormality in peripheral nerve projection
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of outstanding interest. This paper reports the phenotype of the Sema III mutant mouse, which was generated by targeted disruption of the Sema III gene. Sema III mutant mouse embryos exhibit a similar abnormality in the PNS as that observed in neuropilin-1 mutant mouse embryos (see [20]), even though the Sema III mutant mouse is viable after birth. This paper also reports the production of heterozygous knocked-in lacZ mice in which the lacZ gene was inserted into the Sema III locus, and shows that PNS axons avoid the lacZ-expressing areas. These findings indicate that Sema III is a chemorepulsive guidance signal for PNS axons in vivo.
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of outstanding interest Taniguchi M, Yuasa S, Fujisawa H, Naruse I, Saga S, Mishina M, Yagi T. Disruption of semaphorin III/D gene causes severe abnormality in peripheral nerve projection. Neuron. 19:1997;519-530 This paper reports the phenotype of the Sema III mutant mouse, which was generated by targeted disruption of the Sema III gene. Sema III mutant mouse embryos exhibit a similar abnormality in the PNS as that observed in neuropilin-1 mutant mouse embryos (see [20]), even though the Sema III mutant mouse is viable after birth. This paper also reports the production of heterozygous knocked-in lacZ mice in which the lacZ gene was inserted into the Sema III locus, and shows that PNS axons avoid the lacZ-expressing areas. These findings indicate that Sema III is a chemorepulsive guidance signal for PNS axons in vivo.
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(1997)
Neuron
, vol.19
, pp. 519-530
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-
Taniguchi, M.1
Yuasa, S.2
Fujisawa, H.3
Naruse, I.4
Saga, S.5
Mishina, M.6
Yagi, T.7
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33
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0031898879
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Zebrafish Semaphorin Z1a collapses specific growth cones and alters their pathway in vivo
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Shoji W, Yee CS, Kuwada JY. Zebrafish Semaphorin Z1a collapses specific growth cones and alters their pathway in vivo. Development. 125:1998;1275-1283.
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Shoji, W.1
Yee, C.S.2
Kuwada, J.Y.3
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34
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0030061951
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Positional cues that are strictly localized in the telencephalon induce preferential growth of mitral cell axons
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Sugisaki N, Hirata T, Naruse I, Kawakami A, Kitsukawa T, Fujisawa H. Positional cues that are strictly localized in the telencephalon induce preferential growth of mitral cell axons. J Neurobiol. 29:1996;127-137.
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Hirata, T.2
Naruse, I.3
Kawakami, A.4
Kitsukawa, T.5
Fujisawa, H.6
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35
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0030023741
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The distribution of collapsin-1 mRNA in the developing chick nervous system
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Shepherd I, Luo Y, Raper JA, Chang S. The distribution of collapsin-1 mRNA in the developing chick nervous system. Dev Biol. 173:1996;185-199.
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Dev Biol
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Shepherd, I.1
Luo, Y.2
Raper, J.A.3
Chang, S.4
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A role for collapsin-1 in olfactory and cranial sensory axon guidance
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Kobayashi H, Koppel AM, Luo Y, Raper JA. A role for collapsin-1 in olfactory and cranial sensory axon guidance. J Neurosci. 17:1997;8339-8352.
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Luo, Y.3
Raper, J.A.4
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Many major CNS axon projections develop normally in the absence of semaphorin III
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Catalano SM, Messersmith EK, Goodman CS, Shatz CJ, Chedotal A. Many major CNS axon projections develop normally in the absence of semaphorin III. Mol Cell Neurosci. 11:1998;173-182.
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Goodman, C.S.3
Shatz, C.J.4
Chedotal, A.5
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38
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Semaphorin III can function as a selective chemorepellent to pattern sensory projections in the spinal cord
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Messersmith EK, Leonardo ED, Shatz CJ, Tessier-Lavigne M, Goodman CS, Kolodkin AL. Semaphorin III can function as a selective chemorepellent to pattern sensory projections in the spinal cord. Neuron. 14:1995;949-959.
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Messersmith, E.K.1
Leonardo, E.D.2
Shatz, C.J.3
Tessier-Lavigne, M.4
Goodman, C.S.5
Kolodkin, A.L.6
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39
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The sensory innervation of the mouse spinal cord may be patterned by differential expression of and differential responsiveness to semaphorins
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Püschel AW, Adams RH, Betz H. The sensory innervation of the mouse spinal cord may be patterned by differential expression of and differential responsiveness to semaphorins. Mol Cell Neurosci. 7:1996;419-431.
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