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First demonstration of a repulsive action of a netrin in Drosophila and of the combinatorial effects of netrins, semaphorins and Ig superfamily members in motor axon targeting.
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Provides a detailed phenotypic analysis of mice carrying a mutation in the Unc5h3/Rcm gene that supports the hypothesis that UNC5H3 may function as a repulsive netrin receptor in guiding pre-cerebellar neurons.
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This paper provides the first direct evidence that vertebrate UNC-5 family proteins have a conserved role in axonal repulsion. Conversion of the effect of netrin-1 from attraction to repulsion is shown to be mediated by the formation of a receptor complex of DCC and UNC-5 family proteins, with association of their cytoplasmic domains.
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Presents a phenotypic analysis of olivary neuron migration in netrin-1 knockout mice that supports the hypothesis that netrin-1 guides cell migrations in vertebrates.
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Demonstrates that the netrin receptor frazzled in Drosophila is required for retinal axon targeting, and describes the surprising discovery that it is required in the target, not the neurons. This result suggests that frazzled is functioning in a capacity other than as a receptor, perhaps as a ligand detected by some other axonal receptor.
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Describes the cloning of three mammalian Slit genes, and demonstrates that both Drosophila and vertebrate Slit proteins bind Robo receptors. In addition, the authors provide evidence of a conserved function for Slit proteins in repelling axons in vertebrates. They report that a mammalian Slit protein binds to netrin-1
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Brose K, Bland KS, Wang KH, Arnott D, Henzel W, Goodman CS, Tessier-Lavigne M, Kidd T Slit proteins bind Robo receptors and have an evolutionarily conserved role in repulsive axon guidance. Cell. 96:1999;795-806. Describes the cloning of three mammalian Slit genes, and demonstrates that both Drosophila and vertebrate Slit proteins bind Robo receptors. In addition, the authors provide evidence of a conserved function for Slit proteins in repelling axons in vertebrates. They report that a mammalian Slit protein binds to netrin-1.
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Description of several vertebrate Slit proteins. This study also demonstrates the repulsive activity of a Slit protein on olfactory bulb axons and its binding to a Robo receptor.
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Using a clever set of inferences, the authors identify Slit as the midline repellent functioning via the Robo receptor in Drosophila. Slit is also shown to function in repulsion of mesodermal cells away from the midline.
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Kidd T, Bland KS, Goodman CS Slit is the midline repellent for the robo receptor in Drosophila. Cell. 96:1999;785-794. Using a clever set of inferences, the authors identify Slit as the midline repellent functioning via the Robo receptor in Drosophila. Slit is also shown to function in repulsion of mesodermal cells away from the midline.
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Midline crossing in Drosophila is controlled by the repulsive Robo receptor, whose expression on axons is shown to be downregulated by the Commissureless protein, allowing axonal passage across the midline.
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Kidd T, Russell C, Goodman CS, Tear G Dosage-sensitive and complementary functions of roundabout and commissureless control axon crossing of the CNS midline. Neuron. 20:1998;25-33. Midline crossing in Drosophila is controlled by the repulsive Robo receptor, whose expression on axons is shown to be downregulated by the Commissureless protein, allowing axonal passage across the midline.
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Provides confirmation of the repulsive role of Drosophila Slit, with the demonstration that ectopic expression of Slit redirects axons away from the site of Slit expression.
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A genetic screen for axon guidance mutants in C. elegans identified the conserved Robo family member SAX-3 as a receptor controlling multiple axon guidance events.
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Reports that Slit-2 repels axons in the forebrain (olfactory bulb and hippocampal axons). This is the first demonstration that a Slit protein also has collapse-inducing activity (in addition to repulsive activity).
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Nguyen Ba-Charvet KT, Brose K, Marillat V, Kidd T, Goodman CS, Tessier-Lavigne M, Sotelo C, Chedotal A Slit2-mediated chemorepulsion and collapse of developing forebrain axons. Neuron. 22:1999;463-473. Reports that Slit-2 repels axons in the forebrain (olfactory bulb and hippocampal axons). This is the first demonstration that a Slit protein also has collapse-inducing activity (in addition to repulsive activity).
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Structure/function analysis and domain-swapping experiments are used to show that the 'sign' of the repulsive Slit receptor Robo and the attractive netrin receptor frazzled is dictated by their cytoplasmic domains.
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Bashaw GJ, Goodman CS Chimeric axon guidance receptors: the cytoplasmic domains of slit and netrin receptors specify attraction versus repulsion. Cell. 97:1999;917-926. Structure/function analysis and domain-swapping experiments are used to show that the 'sign' of the repulsive Slit receptor Robo and the attractive netrin receptor frazzled is dictated by their cytoplasmic domains.
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A mammalian Slit protein is shown to function in repulsion of migrating neurons, providing a molecular basis for a previously described chemorepulsive activity.
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Jiang, Z.-H.4
Dupuis, S.5
Wu, J.Y.6
Rao, Y.7
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40
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0033166879
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Cellular and molecular guidance of GABAergic neuronal migration from an extracortical origin to the neocortex
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••], but on a different population of neurons.
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••], but on a different population of neurons.
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Zhu, Y.1
Li, H.2
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Wu, J.Y.4
Rao, Y.5
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41
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0033180233
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Chemorepulsion of neuronal migration by slit-2 in the developing mammalian forebrain
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•], this paper describes the repulsive action of a Slit protein on migrating neurons. The paper is notable for the fact that the author (who first described chemorepulsion of migrating neurons) actually purified the Slit protein using a bioassay for chemorepulsion.
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•], this paper describes the repulsive action of a Slit protein on migrating neurons. The paper is notable for the fact that the author (who first described chemorepulsion of migrating neurons) actually purified the Slit protein using a bioassay for chemorepulsion.
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Neuron
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Hu, H.1
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43
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Biochemical purification of a mammalian slit protein as a positive regulator of sensory axon elongation and branching
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The authors demonstrate the existence of an activity in brain that can stimulate the branching and elongation of sensory axons. They purified the factor and found that it is an amino-terminal fragment of Slit-2. The study is the first to identify a factor that can stimulate interstitial axon branching, and also demonstrates that Slit proteins are bifunctional.
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Wang KH, Brose K, Arnott D, Kidd T, Goodman CS, Henzel W, Tessier-Lavigne M Biochemical purification of a mammalian slit protein as a positive regulator of sensory axon elongation and branching. Cell. 96:1999;771-784. The authors demonstrate the existence of an activity in brain that can stimulate the branching and elongation of sensory axons. They purified the factor and found that it is an amino-terminal fragment of Slit-2. The study is the first to identify a factor that can stimulate interstitial axon branching, and also demonstrates that Slit proteins are bifunctional.
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Cell
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Wang, K.H.1
Brose, K.2
Arnott, D.3
Kidd, T.4
Goodman, C.S.5
Henzel, W.6
Tessier-Lavigne, M.7
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44
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0033360412
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Neuronal growth cone collapse triggers lateral extensions along trailing axons
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Provides the remarkable demonstration of a link between growth cone repulsion and axonal branching. Collapse of retinal axons in response to ephrins or mechanical probing leads to lateral extesion of filopodia and lamellipodia hundreds of microns behind the lead growth cone. [Published erratum appears in Nat Neurosci 1999
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Davenport RW, Thies E, Cohen ML Neuronal growth cone collapse triggers lateral extensions along trailing axons. Nat Neurosci. 2:1999;254-259. [Published erratum appears in Nat Neurosci 1999, 2(5):485]. Provides the remarkable demonstration of a link between growth cone repulsion and axonal branching. Collapse of retinal axons in response to ephrins or mechanical probing leads to lateral extesion of filopodia and lamellipodia hundreds of microns behind the lead growth cone.
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Nat Neurosci
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Davenport, R.W.1
Thies, E.2
Cohen, M.L.3
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45
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0031922119
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The ephrins and Eph receptors in neural development
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Flanagan JG, Vanderhaeghen P The ephrins and Eph receptors in neural development. Annu Rev Neurosci. 21:1998;309-345.
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O'Leary DD, Wilkinson DG Eph receptors and ephrins in neural development. Curr Opin Neurobiol. 9:1999;65-73.
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Wilkinson, D.G.2
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0033016108
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Eph receptors and ephrins: Effectors of morphogenesis
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An excellent and comprehensive review of the functions of ephrins in axon guidance and in other tissues.
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Holder N, Klein R Eph receptors and ephrins: effectors of morphogenesis. Development. 126:1999;2033-2044. An excellent and comprehensive review of the functions of ephrins in axon guidance and in other tissues.
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Holder, N.1
Klein, R.2
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48
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In vitro guidance of retinal ganglion cell axons by RAGS, a 25 kDa tectal protein related to ligands for Eph receptor tyrosine kinases
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Drescher U, Kremoser C, Handwerker C, Loschinger J, Noda M, Bonhoeffer F In vitro guidance of retinal ganglion cell axons by RAGS, a 25 kDa tectal protein related to ligands for Eph receptor tyrosine kinases. Cell. 82:1995;359-370.
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Drescher, U.1
Kremoser, C.2
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Noda, M.5
Bonhoeffer, F.6
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49
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0033587129
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In vivo cell sorting in complementary segmental domains mediated by Eph receptors and ephrins
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An exciting report showing that bidirectional signaling across rhombomere boundaries between EphB receptors and their ephrin-B ligands can result in cell sorting to prevent intermixing between adjacent rhombomeres.
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Xu Q, Mellitzer G, Robinson V, Wilkinson DG In vivo cell sorting in complementary segmental domains mediated by Eph receptors and ephrins. Nature. 399:1999;267-271. An exciting report showing that bidirectional signaling across rhombomere boundaries between EphB receptors and their ephrin-B ligands can result in cell sorting to prevent intermixing between adjacent rhombomeres.
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Nature
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Xu, Q.1
Mellitzer, G.2
Robinson, V.3
Wilkinson, D.G.4
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50
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0033082959
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Roles of ephrinB ligands and EphB receptors in cardiovascular development: Demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis
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Adams RH, Wilkinson GA, Weiss C, Diella F, Gale NW, Deutsch U, Risau W, Klein R Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis. Genes Dev. 13:1999;295-306.
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Adams, R.H.1
Wilkinson, G.A.2
Weiss, C.3
Diella, F.4
Gale, N.W.5
Deutsch, U.6
Risau, W.7
Klein, R.8
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51
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0033560751
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Surface densities of ephrin-B1 determine EphB1-coupled activation of cell attachment through alphavbeta3 and alpha5beta1 integrins
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Huynh-Do U, Stein E, Lane AA, Liu H, Cerretti DP, Daniel TO Surface densities of ephrin-B1 determine EphB1-coupled activation of cell attachment through alphavbeta3 and alpha5beta1 integrins. EMBO J. 18:1999;2165-2173.
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EMBO J
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Huynh-Do, U.1
Stein, E.2
Lane, A.A.3
Liu, H.4
Cerretti, D.P.5
Daniel, T.O.6
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52
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0032489430
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The VAB-1 Eph receptor tyrosine kinase functions in neural and epithelial morphogenesis in C. elegans
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Describes the genetic and molecular analysis of a C. elegans Eph receptor, VAB-1. Mutations in vab-1 were isolated on the basis of morphogenetic defects in epidermal cells. Expression and genetic mosaic analyses show that VAB-1 function is required non-autonomously in underlying neuronal precursors for epidermal morphogenesis. Analysis of a large set of partialloss-of-function mutations in vab-1 suggests that VAB-1 may have both kinase-dependent and kinase-independent functions in signalling.
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George SE, Simokat K, Hardin J, Chisholm AD The VAB-1 Eph receptor tyrosine kinase functions in neural and epithelial morphogenesis in C. elegans. Cell. 92:1998;633-643. Describes the genetic and molecular analysis of a C. elegans Eph receptor, VAB-1. Mutations in vab-1 were isolated on the basis of morphogenetic defects in epidermal cells. Expression and genetic mosaic analyses show that VAB-1 function is required non-autonomously in underlying neuronal precursors for epidermal morphogenesis. Analysis of a large set of partialloss-of-function mutations in vab-1 suggests that VAB-1 may have both kinase-dependent and kinase-independent functions in signalling.
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(1998)
Cell
, vol.92
, pp. 633-643
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George, S.E.1
Simokat, K.2
Hardin, J.3
Chisholm, A.D.4
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53
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0032993165
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Isolation and characterization of Dek, a Drosophila Eph receptor tyrosine kinase
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Scully A, McKeown M, Thomas J Isolation and characterization of Dek, a Drosophila Eph receptor tyrosine kinase. Mol Cell Neurosci. 13:1999;337-347.
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Mol Cell Neurosci
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Scully, A.1
McKeown, M.2
Thomas, J.3
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54
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0033035138
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Extensive gene duplication in the early evolution of animals before the parazoan-eumetazoan split demonstrated by G proteins and protein tyrosine kinases from sponge and hydra
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Suga H, Koyanagi M, Hoshiyama D, Ono K, Iwabe N, Kuma K, Miyata T Extensive gene duplication in the early evolution of animals before the parazoan-eumetazoan split demonstrated by G proteins and protein tyrosine kinases from sponge and hydra. J Mol Evol. 48:1999;646-653.
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J Mol Evol
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Suga, H.1
Koyanagi, M.2
Hoshiyama, D.3
Ono, K.4
Iwabe, N.5
Kuma, K.6
Miyata, T.7
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55
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0032103082
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Signaling by Eph receptors and their ephrin ligands
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Bruckner K, Klein R Signaling by Eph receptors and their ephrin ligands. Curr Opin Neurobiol. 8:1998;375-382.
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Curr Opin Neurobiol
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Bruckner, K.1
Klein, R.2
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56
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0033103887
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EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains
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An important paper that addresses the mechanism of reverse signaling by transmembrane ephrins. Ephrin-Bs were found to localise to membrane rafts in cell culture and to bind PDZ-domain-containing proteins at their carboxyl termini, thereby recruiting an as yet unidentified serine/threonine kinase. Stimulation by EphB receptors caused coalescence of these rafts into large membrane patches, potentially acting as signaling centers.
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Bruckner K, Pablo Labrador J, Scheiffele P, Herb A, Seeburg PH, Klein R EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains. Neuron. 22:1999;511-524. An important paper that addresses the mechanism of reverse signaling by transmembrane ephrins. Ephrin-Bs were found to localise to membrane rafts in cell culture and to bind PDZ-domain-containing proteins at their carboxyl termini, thereby recruiting an as yet unidentified serine/threonine kinase. Stimulation by EphB receptors caused coalescence of these rafts into large membrane patches, potentially acting as signaling centers.
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(1999)
Neuron
, vol.22
, pp. 511-524
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Bruckner, K.1
Pablo Labrador, J.2
Scheiffele, P.3
Herb, A.4
Seeburg, P.H.5
Klein, R.6
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57
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0032408173
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PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands
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Demonstrates that both Eph receptors and ephrin-Bs can bind PDZ domain proteins, and makes the striking observation that both receptors, ligands and PDZ proteins colocalise at synapses in cultured neurons, suggesting novel roles for Eph signaling in synaptogenesis.
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Torres R, Firestein BL, Dong H, Staudinger J, Olson EN, Huganir RL, Bredt DS, Gale NW, Yancopoulos GD PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands. Neuron. 21:1998;1453-1463. Demonstrates that both Eph receptors and ephrin-Bs can bind PDZ domain proteins, and makes the striking observation that both receptors, ligands and PDZ proteins colocalise at synapses in cultured neurons, suggesting novel roles for Eph signaling in synaptogenesis.
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(1998)
Neuron
, vol.21
, pp. 1453-1463
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Torres, R.1
Firestein, B.L.2
Dong, H.3
Staudinger, J.4
Olson, E.N.5
Huganir, R.L.6
Bredt, D.S.7
Gale, N.W.8
Yancopoulos, G.D.9
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58
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0033525063
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The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif
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Demonstrates that ephrin-Bs can bind several PDZ-domain-containing proteins, including syntenin.
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Lin D, Gish GD, Songyang Z, Pawson T The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif. J Biol Chem. 274:1999;3726-3733. Demonstrates that ephrin-Bs can bind several PDZ-domain-containing proteins, including syntenin.
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(1999)
J Biol Chem
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, pp. 3726-3733
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Lin, D.1
Gish, G.D.2
Songyang, Z.3
Pawson, T.4
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59
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0032849015
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Genes required for axon pathfinding and extension in the C. elegans nerve ring
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Describes genetic analysis of several new genes identified through their roles in sensory neuron axon guidance. The authors used double-mutant analysis to show that the C. elegans Eph (VAB-1), SAX-3, and netrin pathways appear to act (at least partly) in parallel to direct axon guidance.
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Zallen JA, Kirch SA, Bargmann CI Genes required for axon pathfinding and extension in the C. elegans nerve ring. Development. 126:1999;3679-3692. Describes genetic analysis of several new genes identified through their roles in sensory neuron axon guidance. The authors used double-mutant analysis to show that the C. elegans Eph (VAB-1), SAX-3, and netrin pathways appear to act (at least partly) in parallel to direct axon guidance.
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(1999)
Development
, vol.126
, pp. 3679-3692
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Zallen, J.A.1
Kirch, S.A.2
Bargmann, C.I.3
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60
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0031001812
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Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells
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Holland SJ, Gale NW, Gish GD, Roth RA, Songyang Z, Cantley LC, Henkemeyer M, Yancopoulos GD, Pawson T Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells. EMBO J. 16:1997;3877-3888.
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EMBO J
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Holland, S.J.1
Gale, N.W.2
Gish, G.D.3
Roth, R.A.4
Songyang, Z.5
Cantley, L.C.6
Henkemeyer, M.7
Yancopoulos, G.D.8
Pawson, T.9
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61
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0031893255
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Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase
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Stein E, Huynh-Do U, Lane AA, Cerretti DP, Daniel TO Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase. J Biol Chem. 273:1998;1303-1308.
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J Biol Chem
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Stein, E.1
Huynh-Do, U.2
Lane, A.A.3
Cerretti, D.P.4
Daniel, T.O.5
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62
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0029943447
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Drosophila photoreceptor axon guidance and targeting requires the dreadlocks SH2/SH3 adapter protein
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Garrity PA, Rao Y, Salecker I, McGlade J, Pawson T, Zipursky SL Drosophila photoreceptor axon guidance and targeting requires the dreadlocks SH2/SH3 adapter protein. Cell. 85:1996;639-650.
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Cell
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Garrity, P.A.1
Rao, Y.2
Salecker, I.3
McGlade, J.4
Pawson, T.5
Zipursky, S.L.6
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63
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0033603254
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Pak functions downstream of dock to regulate photoreceptor axon guidance in Drosophila
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An elegant and comprehensive analysis of the role of the Pak (p21-activated) kinase in signaling downstream of Dock/Nck in Drosophila axon guidance.
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Hing H, Xiao J, Harden N, Lim L, Zipursky SL Pak functions downstream of dock to regulate photoreceptor axon guidance in Drosophila. Cell. 97:1999;853-863. An elegant and comprehensive analysis of the role of the Pak (p21-activated) kinase in signaling downstream of Dock/Nck in Drosophila axon guidance.
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Cell
, vol.97
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Hing, H.1
Xiao, J.2
Harden, N.3
Lim, L.4
Zipursky, S.L.5
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64
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0000969241
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Unified nomenclature for the semaphorins/collapsins
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Unified nomenclature for the semaphorins/collapsins. Cell. 97:1999;551-552.
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Cell
, vol.97
, pp. 551-552
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65
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Surround repulsion of spinal sensory axons in higher vertebrate embryos
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Keynes R, Tannahill D, Morgenstern DA, Johnson AR, Cook GM, Pini A Surround repulsion of spinal sensory axons in higher vertebrate embryos. Neuron. 18:1997;889-897.
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Neuron
, vol.18
, pp. 889-897
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Keynes, R.1
Tannahill, D.2
Morgenstern, D.A.3
Johnson, A.R.4
Cook, G.M.5
Pini, A.6
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66
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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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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.
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Neuron
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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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67
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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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Genetic analysis of Sema-1a in Drosophila provides direct and convincing evidence that Sema-1a functions as a repellent that drives axon defasciculation.
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Yu HH, 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. Genetic analysis of Sema-1a in Drosophila provides direct and convincing evidence that Sema-1a functions as a repellent that drives axon defasciculation.
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Neuron
, vol.20
, pp. 207-220
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Yu, H.H.1
Araj, H.H.2
Ralls, S.A.3
Kolodkin, A.L.4
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68
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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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[Published erratum appears in Neuron 1997
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Chen H, Chedotal 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. [Published erratum appears in Neuron 1997, 19(3):559].
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Neuron
, vol.19
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Chen, H.1
Chedotal, A.2
He, Z.3
Goodman, C.S.4
Tessier-Lavigne, M.5
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69
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0032176852
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Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors \[see comments]
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Provides direct evidence, through expression of ectopic neuropilin, to support the model that the specificity of neuronal responses to class 3 semaphorins is dictated by the complement of neuropilins expresed by the neurons.
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Takahashi T, Nakamura F, Jin Z, Kalb RG, Strittmatter SM Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors \[see comments]. Nat Neurosci. 1:1998;487-493. Provides direct evidence, through expression of ectopic neuropilin, to support the model that the specificity of neuronal responses to class 3 semaphorins is dictated by the complement of neuropilins expresed by the neurons.
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Nat Neurosci
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Takahashi, T.1
Nakamura, F.2
Jin, Z.3
Kalb, R.G.4
Strittmatter, S.M.5
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70
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0032215144
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Neuropilin-2 is a receptor for semaphorin IV: Insight into the structural basis of receptor function and specificity [see comments]
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Presents structure/function analysis of neuropilins and evidence in support of the hypothesis that neuropilin-2 is a necessary receptor for semaphorin IV (Sema3F).
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Giger RJ, Urquhart ER, Gillespie SK, Levengood DV, Ginty DD, Kolodkin AL Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity [see comments]. Neuron. 21:1998;1079-1092. Presents structure/function analysis of neuropilins and evidence in support of the hypothesis that neuropilin-2 is a necessary receptor for semaphorin IV (Sema3F).
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(1998)
Neuron
, vol.21
, pp. 1079-1092
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Giger, R.J.1
Urquhart, E.R.2
Gillespie, S.K.3
Levengood, D.V.4
Ginty, D.D.5
Kolodkin, A.L.6
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71
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0032215735
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Neuropilin-1 extracellular domains mediate semaphorin D/III-induced growth cone collapse [see comments]
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Demonstrates that the cytoplasmic domain of neuropilin-1 is not required for its function as a semaphorin receptor, supporting the existence of a distinct signaling receptor that mediates class 3 semaphorin effects.
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Nakamura F, Tanaka M, Takahashi T, Kalb RG, Strittmatter SM Neuropilin-1 extracellular domains mediate semaphorin D/III-induced growth cone collapse [see comments]. Neuron. 21:1998;1093-1100. Demonstrates that the cytoplasmic domain of neuropilin-1 is not required for its function as a semaphorin receptor, supporting the existence of a distinct signaling receptor that mediates class 3 semaphorin effects.
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(1998)
Neuron
, vol.21
, pp. 1093-1100
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Nakamura, F.1
Tanaka, M.2
Takahashi, T.3
Kalb, R.G.4
Strittmatter, S.M.5
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72
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0032408496
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Semaphorin-neuropilin interactions underlying sympathetic axon responses to class III semaphorins
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Presents structure/function and loss-of-function data supporting the hypothesis that the responses of neurons to class 3 semaphorins are dictated by the complement of neuropilin receptors expressed by the neurons.
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Chen H, He Z, Bagri A, Tessier-Lavigne M Semaphorin-neuropilin interactions underlying sympathetic axon responses to class III semaphorins. Neuron. 21:1998;1283-1290. Presents structure/function and loss-of-function data supporting the hypothesis that the responses of neurons to class 3 semaphorins are dictated by the complement of neuropilin receptors expressed by the neurons.
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(1998)
Neuron
, vol.21
, pp. 1283-1290
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Chen, H.1
He, Z.2
Bagri, A.3
Tessier-Lavigne, M.4
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73
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0032433853
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Plexin A is a neuronal semaphorin receptor that controls axon guidance
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Demonstrates that a plexin protein, plexin A, is the receptor that mediates the axon guidance functions of the transmembrane semaphorin Sema-1a in Drosophila.
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Winberg ML, Noordermeer JN, Tamagnone L, Comoglio PM, Spriggs MK, Tessier-Lavigne M, Goodman CS Plexin A is a neuronal semaphorin receptor that controls axon guidance. Cell. 95:1998;903-916. Demonstrates that a plexin protein, plexin A, is the receptor that mediates the axon guidance functions of the transmembrane semaphorin Sema-1a in Drosophila.
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(1998)
Cell
, vol.95
, pp. 903-916
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Winberg, M.L.1
Noordermeer, J.N.2
Tamagnone, L.3
Comoglio, P.M.4
Spriggs, M.K.5
Tessier-Lavigne, M.6
Goodman, C.S.7
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74
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0032055098
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A poxvirus-encoded semaphorin induces cytokine production from monocytes and binds to a novel cellular semaphorin receptor, VESPR
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••].
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(1998)
Immunity
, vol.8
, pp. 473-482
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Comeau, M.R.1
Johnson, R.2
Dubose, R.F.3
Petersen, M.4
Gearing, P.5
Vandenbos, T.6
Park, L.7
Farrah, T.8
Buller, R.M.9
Cohen, J.I.10
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75
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0032549799
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Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor
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Presents surprising finding that neuropilin-1 and -2, receptors for class 3 semaphorins, are also receptors for a specific heparin-binding isoform of vascular endothelial growth factor (VEGF), apparently cooperating with the signal VEGF receptor KDR, a receptor tyrosine kinase.
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