메뉴 건너뛰기




Volumn 8, Issue 1, 1998, Pages 87-97

Neural cell recognition molecule L1:From cell biology to human hereditary brain malformations

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; IMMUNOGLOBULIN; NERVE CELL RECOGNITION MOLECULE L1; UNCLASSIFIED DRUG;

EID: 0038405181     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(98)80012-3     Document Type: Article
Times cited : (218)

References (76)
  • 1
    • 0021298675 scopus 로고
    • Immunocytological and biochemical characterization of a new neuronal cell surface component (L1 antigen) which is involved in cell adhesion
    • Rathjen FG, Schachner M. Immunocytological and biochemical characterization of a new neuronal cell surface component (L1 antigen) which is involved in cell adhesion. EMBO J. 3:1984;1-10.
    • (1984) EMBO J , vol.3 , pp. 1-10
    • Rathjen, F.G.1    Schachner, M.2
  • 2
    • 0021046979 scopus 로고
    • L1 mono- And polyclonal antibodies modify cell migration in early postnatal mouse cerebellum
    • Lindner J, Rathjen FG, Schachner M. L1 mono- and polyclonal antibodies modify cell migration in early postnatal mouse cerebellum. Nature. 305:1983;427-430.
    • (1983) Nature , vol.305 , pp. 427-430
    • Lindner, J.1    Rathjen, F.G.2    Schachner, M.3
  • 3
    • 0020967913 scopus 로고
    • Nerve growth factor-inducible large external (NILE) glycoprotein: Studies of a central and peripheral neuronal marker
    • Salton SR, Richter-Landsberg C, Greene LA, Shelanski ML. Nerve growth factor-inducible large external (NILE) glycoprotein: studies of a central and peripheral neuronal marker. J Neurosci. 3:1983;441-454.
    • (1983) J Neurosci , vol.3 , pp. 441-454
    • Salton, S.R.1    Richter-Landsberg, C.2    Greene, L.A.3    Shelanski, M.L.4
  • 4
    • 0021688148 scopus 로고
    • Polypeptide components and binding functions of neuron-glia cell adhesion molecules
    • Grumet M, Hoffman S, Chuong CM, Edelman GM. Polypeptide components and binding functions of neuron-glia cell adhesion molecules. Proc Natl Acad Sci USA. 81:1984;7989-7993.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 7989-7993
    • Grumet, M.1    Hoffman, S.2    Chuong, C.M.3    Edelman, G.M.4
  • 5
    • 0030273263 scopus 로고    scopus 로고
    • The L1 family of neural cell adhesion molecules: Old proteins performing new tricks
    • of special interest. Reviews structure, expression patterns and molecular interactions of L1-like proteins and correlates in vitro functional studies with mutational phenotypes of the L1 gene in humans.
    • Hortsch M. The L1 family of neural cell adhesion molecules: old proteins performing new tricks. of special interest Neuron. 17:1996;587-593 Reviews structure, expression patterns and molecular interactions of L1-like proteins and correlates in vitro functional studies with mutational phenotypes of the L1 gene in humans.
    • (1996) Neuron , vol.17 , pp. 587-593
    • Hortsch, M.1
  • 6
    • 0030273292 scopus 로고    scopus 로고
    • Structure/function relationships of axon-associatied adhesion receptors of the immunoglobulin superfamily
    • of special interest. Reviews the complex interactions of axonal IgSF members and the mapping of ligand-binding sites.
    • Brümmendorf T, Rathjen FG. Structure/function relationships of axon-associatied adhesion receptors of the immunoglobulin superfamily. of special interest Curr Opin Neurobiol. 6:1996;584-593 Reviews the complex interactions of axonal IgSF members and the mapping of ligand-binding sites.
    • (1996) Curr Opin Neurobiol , vol.6 , pp. 584-593
    • Brümmendorf, T.1    Rathjen, F.G.2
  • 7
    • 0029739225 scopus 로고    scopus 로고
    • Structural features of a close homologue of L1 (CHL1) in the mouse - A new member of the L1 family of neural recognition molecules
    • of special interest. Reports the sequence of a novel member of the L1 subfamily, termed CHL1, in the mouse nervous system. CHL1 is primarily expressed in the central nervous system by neurons and glial cells.
    • Holm J, Hillenbrand R, Steuber V, Bartsch U, Moos M, Lubbert H, Montag D, Schachner M. Structural features of a close homologue of L1 (CHL1) in the mouse - a new member of the L1 family of neural recognition molecules. of special interest Eur J Neurosci. 8:1996;1613-1629 Reports the sequence of a novel member of the L1 subfamily, termed CHL1, in the mouse nervous system. CHL1 is primarily expressed in the central nervous system by neurons and glial cells.
    • (1996) Eur J Neurosci , vol.8 , pp. 1613-1629
    • Holm, J.1    Hillenbrand, R.2    Steuber, V.3    Bartsch, U.4    Moos, M.5    Lubbert, H.6    Montag, D.7    Schachner, M.8
  • 8
    • 0030851345 scopus 로고    scopus 로고
    • Differential glycosylation of tractin and leechCAM, two novel Ig superfamily members, regulates neurite extension and fascicle formation
    • of special interest. Reports the cloning and characterization of a L1-like molecule, termed tractin, in hirudinid leech species. Tractin is expressed on axons of the central and peripheral nervous system. In vivo antibody perturbation experiments using an antibody that recognizes a glycoepitope on both tractin and leech-CAM reveal a participation of this epitope in neurite extension and branching.
    • Huang YQ, Jellies J, Johansen KM, Johansen J. Differential glycosylation of tractin and leechCAM, two novel Ig superfamily members, regulates neurite extension and fascicle formation. of special interest J Cell Biol. 138:1997;143-157 Reports the cloning and characterization of a L1-like molecule, termed tractin, in hirudinid leech species. Tractin is expressed on axons of the central and peripheral nervous system. In vivo antibody perturbation experiments using an antibody that recognizes a glycoepitope on both tractin and leech-CAM reveal a participation of this epitope in neurite extension and branching.
    • (1997) J Cell Biol , vol.138 , pp. 143-157
    • Huang, Y.Q.1    Jellies, J.2    Johansen, K.M.3    Johansen, J.4
  • 9
    • 0030938745 scopus 로고    scopus 로고
    • Expression of an L1 related cell adhesion molecule on developing CNS fiber tracts in zebrafish and its functional contribution to axon fasciculation
    • Weiland UM, Ott H, Bastmeyer M, Schaden H, Giordano S, Stuermer CAO. Expression of an L1 related cell adhesion molecule on developing CNS fiber tracts in zebrafish and its functional contribution to axon fasciculation. Mol Cell Neurosci. 9:1997;77-89.
    • (1997) Mol Cell Neurosci , vol.9 , pp. 77-89
    • Weiland, U.M.1    Ott, H.2    Bastmeyer, M.3    Schaden, H.4    Giordano, S.5    Stuermer, C.A.O.6
  • 10
    • 0031014381 scopus 로고    scopus 로고
    • Molecular characterization of E587 antigen: An axonal recognition molecule expressed in the goldfish central nervous system
    • of special interest. Shows that a L1-related molecule, the E587 antigen, that is involved in axon fasciculation and outgrowth in the goldfish is upregulated on regenerating retinal ganglion cell axons.
    • Giordano S, Laessing U, Ankerhold R, Lottspeich F, Stuermer CAO. Molecular characterization of E587 antigen: an axonal recognition molecule expressed in the goldfish central nervous system. of special interest J Comp Neurol. 377:1997;286-297 Shows that a L1-related molecule, the E587 antigen, that is involved in axon fasciculation and outgrowth in the goldfish is upregulated on regenerating retinal ganglion cell axons.
    • (1997) J Comp Neurol , vol.377 , pp. 286-297
    • Giordano, S.1    Laessing, U.2    Ankerhold, R.3    Lottspeich, F.4    Stuermer, C.A.O.5
  • 11
    • 0029852196 scopus 로고    scopus 로고
    • Neurofascin induces neurites by heterophilic interactions with axonal NrCAM while NrCAM requires F11 on the axonal surface to extend neurites
    • of outstanding interest. The authors have characterized the interaction between neurofascin and NrCAM, two members of the L1 subfamily. Neurofascin-induced neurite extension is mediated by axonal NrCAM. Binding between both molecules requires the Ig-like domains of neurofascin.
    • Volkmer H, Leuschner R, Zacharias U, Rathjen FG. Neurofascin induces neurites by heterophilic interactions with axonal NrCAM while NrCAM requires F11 on the axonal surface to extend neurites. of outstanding interest J Cell Biol. 135:1996;1059-1069 The authors have characterized the interaction between neurofascin and NrCAM, two members of the L1 subfamily. Neurofascin-induced neurite extension is mediated by axonal NrCAM. Binding between both molecules requires the Ig-like domains of neurofascin.
    • (1996) J Cell Biol , vol.135 , pp. 1059-1069
    • Volkmer, H.1    Leuschner, R.2    Zacharias, U.3    Rathjen, F.G.4
  • 12
    • 0031548015 scopus 로고    scopus 로고
    • Immunohistochemical localization of neurocan and L1 in the formation of thalamocortical pathway of developing rats
    • Fukuda T, Kawano H, Ohyama K, Li HP, Takeda Y, Oohira A, Kawamura K. Immunohistochemical localization of neurocan and L1 in the formation of thalamocortical pathway of developing rats. J Comp Neurol. 382:1997;141-152.
    • (1997) J Comp Neurol , vol.382 , pp. 141-152
    • Fukuda, T.1    Kawano, H.2    Ohyama, K.3    Li, H.P.4    Takeda, Y.5    Oohira, A.6    Kawamura, K.7
  • 13
    • 0031053137 scopus 로고    scopus 로고
    • The cell adhesion molecule L1: Species and cell type dependent multiple binding mechanisms
    • of special interest. Reviews the distribution and the function of L1 on cells outside the nervous system and its interaction with integrins.
    • Kadmon G, Altevogt P. The cell adhesion molecule L1: species and cell type dependent multiple binding mechanisms. of special interest Differentiation. 61:1997;143-150 Reviews the distribution and the function of L1 on cells outside the nervous system and its interaction with integrins.
    • (1997) Differentiation , vol.61 , pp. 143-150
    • Kadmon, G.1    Altevogt, P.2
  • 14
    • 0031131885 scopus 로고    scopus 로고
    • Expression and regulation of the neural cell adhesion molecule L1 on human cells of myelomonocytic and lymphoid origin
    • Pancook JD, Reisfeld RA, Varki N, Vitiello A, Fox RI, Montgomery AM. Expression and regulation of the neural cell adhesion molecule L1 on human cells of myelomonocytic and lymphoid origin. J Immunol. 158:1997;4413-4421.
    • (1997) J Immunol , vol.158 , pp. 4413-4421
    • Pancook, J.D.1    Reisfeld, R.A.2    Varki, N.3    Vitiello, A.4    Fox, R.I.5    Montgomery, A.M.6
  • 15
    • 0031051846 scopus 로고    scopus 로고
    • Neuroglian is expressed on cells destined to form the prothoracic glands of Manduca embryos as they segregate from surrounding cells and rearrange during morphogenesis
    • Chen CL, Lampe DJ, Robertson HM, Nardi JB. Neuroglian is expressed on cells destined to form the prothoracic glands of Manduca embryos as they segregate from surrounding cells and rearrange during morphogenesis. Dev Biol. 181:1997;1-13.
    • (1997) Dev Biol , vol.181 , pp. 1-13
    • Chen, C.L.1    Lampe, D.J.2    Robertson, H.M.3    Nardi, J.B.4
  • 16
    • 0029845321 scopus 로고    scopus 로고
    • 3 integrin
    • 3 binding site in the sixth Ig-like domain of L1 is defined using RGD-containing peptides and a fusion protein of the sixth Ig-like domain of human L1 and the Fc portion of IgG1. Expression of L1 on CD4+ but not CD8+ T lymphocytes indicates that lymphocytes may use different CAMs to interact with integrins. See also [46,47,48].
    • 3 binding site in the sixth Ig-like domain of L1 is defined using RGD-containing peptides and a fusion protein of the sixth Ig-like domain of human L1 and the Fc portion of IgG1. Expression of L1 on CD4+ but not CD8+ T lymphocytes indicates that lymphocytes may use different CAMs to interact with integrins. See also [46,47,48].
    • (1996) Eur J Immunol , vol.26 , pp. 2508-2516
    • Ebeling, O.1    Duczmal, A.2    Aigner, S.3    Geiger, C.4    Schollhammer, S.5    Kemshead, J.T.6    Moller, P.7    Schwartz Albiez, R.8    Altevogt, P.9
  • 17
    • 0029094783 scopus 로고
    • Silencer elements modulate the expression of the gene for the neuron-glia cell adhesion molecule, Ng-CAM
    • Kallunki P, Jenkinson S, Edelman GM, Jones FS. Silencer elements modulate the expression of the gene for the neuron-glia cell adhesion molecule, Ng-CAM. J Biol Chem. 270:1995;21291-21298.
    • (1995) J Biol Chem , vol.270 , pp. 21291-21298
    • Kallunki, P.1    Jenkinson, S.2    Edelman, G.M.3    Jones, F.S.4
  • 18
    • 0030824576 scopus 로고    scopus 로고
    • Tissue-specific expression of the L1 cell adhesion molecule is modulated by the neural restrictive silencer element
    • of special interest. The authors have characterized a silencer element in the second intron and other sequences of the L1 gene that regulate a neural expression of L1.
    • Kallunki P, Edelman GM, Jones FS. Tissue-specific expression of the L1 cell adhesion molecule is modulated by the neural restrictive silencer element. of special interest J Cell Biol. 138:1997;1343-1354 The authors have characterized a silencer element in the second intron and other sequences of the L1 gene that regulate a neural expression of L1.
    • (1997) J Cell Biol , vol.138 , pp. 1343-1354
    • Kallunki, P.1    Edelman, G.M.2    Jones, F.S.3
  • 20
    • 0029443827 scopus 로고
    • Cell adhesion molecules 1: Immunoglobulin superfamily
    • Brümmendorf T, Rathjen FG. Cell adhesion molecules 1: immunoglobulin superfamily. Protein Profile. 2:1995;963-1108.
    • (1995) Protein Profile , vol.2 , pp. 963-1108
    • Brümmendorf, T.1    Rathjen, F.G.2
  • 21
    • 0030760042 scopus 로고    scopus 로고
    • L1-associated diseases: Clinical geneticists divide, molecular biologists unite
    • of special interest. A recent review on the spectrum of mutations in L1 that give rise to disease in humans.
    • Fransen E, Van Camp G, Vits L, Williams PJ. L1-associated diseases: clinical geneticists divide, molecular biologists unite. of special interest Hum Mol Genet. 6:1997;1625-1632 A recent review on the spectrum of mutations in L1 that give rise to disease in humans.
    • (1997) Hum Mol Genet , vol.6 , pp. 1625-1632
    • Fransen, E.1    Van Camp, G.2    Vits, L.3    Williams, P.J.4
  • 22
    • 0030812083 scopus 로고    scopus 로고
    • Neural cell adhesion molecule L1: Signaling pathways and growth cone motility
    • of special interest. A review of recent advances in the analysis of phosphorylation of L1 and its interaction with the cytoskeleton. These findings are discussed in the context of growth cone motility.
    • Kamiguchi H, Lemmon V. Neural cell adhesion molecule L1: signaling pathways and growth cone motility. of special interest J Neurosci Res. 49:1997;1-8 A review of recent advances in the analysis of phosphorylation of L1 and its interaction with the cytoskeleton. These findings are discussed in the context of growth cone motility.
    • (1997) J Neurosci Res , vol.49 , pp. 1-8
    • Kamiguchi, H.1    Lemmon, V.2
  • 23
    • 0031006110 scopus 로고    scopus 로고
    • Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and increases lateral mobility of neurofascin
    • of outstanding interest. Evidence is provided for modulation of the interaction of the cytoplasmic domain of neurofascin with ankyrin by phosphorylation of a conserved tyrosine residue. Tyrosine phosphorylation of the cytoplasmic segment of neurofascin appears to be regulated developmentally.
    • Garver TD, Ren Q, Tuvia S, Bennett V. Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and increases lateral mobility of neurofascin. of outstanding interest J Cell Biol. 137:1997;703-714 Evidence is provided for modulation of the interaction of the cytoplasmic domain of neurofascin with ankyrin by phosphorylation of a conserved tyrosine residue. Tyrosine phosphorylation of the cytoplasmic segment of neurofascin appears to be regulated developmentally.
    • (1997) J Cell Biol , vol.137 , pp. 703-714
    • Garver, T.D.1    Ren, Q.2    Tuvia, S.3    Bennett, V.4
  • 24
    • 0030029134 scopus 로고    scopus 로고
    • X linked hydrocephalus and MASA syndrome
    • of special interest. A review on L1-associated X-linked hydrocephalus and MASA syndrome, with emphasis on clinical and genetic characteristics and analyses of mutations in the L1 gene.
    • Kenwrick S, Jouet M, Donnai D. X linked hydrocephalus and MASA syndrome. of special interest J Med Genet. 33:1996;59-65 A review on L1-associated X-linked hydrocephalus and MASA syndrome, with emphasis on clinical and genetic characteristics and analyses of mutations in the L1 gene.
    • (1996) J Med Genet , vol.33 , pp. 59-65
    • Kenwrick, S.1    Jouet, M.2    Donnai, D.3
  • 25
    • 0031984128 scopus 로고    scopus 로고
    • Errors in corticospinal axon guidance in mice lacking the neural cell adhesion molecule L1
    • of outstanding interest. L1-deficient mice are smaller than wild-type and show malformations of the corticospinal tract, which connects the sensorimotor cortex with motoneurons, and interneurons in the spinal cord. A substantial portion of axons show guidance errors at the pyramidal decussation at the hindbrain/spinal-cord boundary and fail to cross the midline to the opposite dorsal columns. See also [26].
    • Cohen NR, Taylor JSH, Scott LB, Guillery RW, Soriano P, Furley AJ. Errors in corticospinal axon guidance in mice lacking the neural cell adhesion molecule L1. of outstanding interest Curr Biol. 8:1997;26-33 L1-deficient mice are smaller than wild-type and show malformations of the corticospinal tract, which connects the sensorimotor cortex with motoneurons, and interneurons in the spinal cord. A substantial portion of axons show guidance errors at the pyramidal decussation at the hindbrain/spinal-cord boundary and fail to cross the midline to the opposite dorsal columns. See also [26].
    • (1997) Curr Biol , vol.8 , pp. 26-33
    • Cohen, N.R.1    Taylor, J.S.H.2    Scott, L.B.3    Guillery, R.W.4    Soriano, P.5    Furley, A.J.6
  • 26
    • 0030666794 scopus 로고    scopus 로고
    • Disruption of the mouse L1 gene leads to malformations of the nervous system
    • of outstanding interest. L1-deficient mice are smaller than their wild-type littermates, show delayed motor responses and weakness of their hindlimbs. The size of the corticospinal tract is reduced and many individuals have enlarged lateral ventricies, depending on the genetic background. L1-dependent neurite out-growth as well as interactions of nonmyelinating Schwann cells with axons are impaired. See also [25].
    • Dahme M, Bartsch U, Martini R, Anliker B, Schachner M, Mantei N. Disruption of the mouse L1 gene leads to malformations of the nervous system. of outstanding interest Nat Genet. 17:1997;346-349 L1-deficient mice are smaller than their wild-type littermates, show delayed motor responses and weakness of their hindlimbs. The size of the corticospinal tract is reduced and many individuals have enlarged lateral ventricies, depending on the genetic background. L1-dependent neurite out-growth as well as interactions of nonmyelinating Schwann cells with axons are impaired. See also [25].
    • (1997) Nat Genet , vol.17 , pp. 346-349
    • Dahme, M.1    Bartsch, U.2    Martini, R.3    Anliker, B.4    Schachner, M.5    Mantei, N.6
  • 27
    • 0029042874 scopus 로고
    • Axonin-1, Nr-CAM, and Ng-CAM play different roles in the in vivo guidance of chick commissural neurons
    • Stoeckli ET, Landmesser L. Axonin-1, Nr-CAM, and Ng-CAM play different roles in the in vivo guidance of chick commissural neurons. Neuron. 14:1995;1165-1179.
    • (1995) Neuron , vol.14 , pp. 1165-1179
    • Stoeckli, E.T.1    Landmesser, L.2
  • 28
    • 0031039719 scopus 로고    scopus 로고
    • Interference with axonin-1 and NrCAM interactions unmasks a floor-plate activity inhibitory for commissural axons
    • of outstanding interest. The growth of commissural axons across the ventral midline of the spinal cord was investigated in a co-culture system. It could be demonstrated by antibody perturbation experiments that axon-1 and its binding partner Nr-CAM contribute to the guidance of the axons through the floor plate.
    • Stoeckli ET, Sonderegger P, Pollerberg GE, Landmesser LT. Interference with axonin-1 and NrCAM interactions unmasks a floor-plate activity inhibitory for commissural axons. of outstanding interest Neuron. 18:1997;209-221 The growth of commissural axons across the ventral midline of the spinal cord was investigated in a co-culture system. It could be demonstrated by antibody perturbation experiments that axon-1 and its binding partner Nr-CAM contribute to the guidance of the axons through the floor plate.
    • (1997) Neuron , vol.18 , pp. 209-221
    • Stoeckli, E.T.1    Sonderegger, P.2    Pollerberg, G.E.3    Landmesser, L.T.4
  • 29
    • 0031042085 scopus 로고    scopus 로고
    • Mutations in the Drosophila neuroglian cell adhesion molecule affect motor neuron pathfinding and peripheral nervous system patterning
    • of special interest. The analysis of three lethal mutations that change or abolish the expression of Drosophila neuroglian reveals effects on both motoneuron pathfinding and on the development of the peripheral nervous system.
    • Hall SG, Bieber AJ. Mutations in the Drosophila neuroglian cell adhesion molecule affect motor neuron pathfinding and peripheral nervous system patterning. of special interest J Neurobiol. 32:1997;325-340 The analysis of three lethal mutations that change or abolish the expression of Drosophila neuroglian reveals effects on both motoneuron pathfinding and on the development of the peripheral nervous system.
    • (1997) J Neurobiol , vol.32 , pp. 325-340
    • Hall, S.G.1    Bieber, A.J.2
  • 30
    • 0028670787 scopus 로고
    • Hippocampal long-term potentiation and neural cell adhesion molecules L1 and NCAM
    • Lüthi A, Laurent JP, Figurov A, Müller D, Schachner M. Hippocampal long-term potentiation and neural cell adhesion molecules L1 and NCAM. Nature. 372:1994;777-779.
    • (1994) Nature , vol.372 , pp. 777-779
    • Lüthi, A.1    Laurent, J.P.2    Figurov, A.3    Müller, D.4    Schachner, M.5
  • 31
    • 0029066131 scopus 로고
    • Exon 2 of the gene for neural cell adhesion molecule L1 is alternatively spliced in B cells
    • Jouet M, Rosenthal A, Kenwrick S. Exon 2 of the gene for neural cell adhesion molecule L1 is alternatively spliced in B cells. Mol Brain Res. 30:1995;378-380.
    • (1995) Mol Brain Res , vol.30 , pp. 378-380
    • Jouet, M.1    Rosenthal, A.2    Kenwrick, S.3
  • 32
    • 0030725408 scopus 로고    scopus 로고
    • Organization of the neurofascin gene and analysis of developmentally regulated alternative splicing
    • of special interest. The analysis of the neurofascin gene and a systematic quantification of alternatively spliced forms of neurofascin at different developmental stages in the chicken brain. The study reveals a complex expression pattern of neurofascin isoforms.
    • Hassel B, Rathjen FG, Volkmer H. Organization of the neurofascin gene and analysis of developmentally regulated alternative splicing. of special interest J Biol Chem. 272:1997;28742-28749 The analysis of the neurofascin gene and a systematic quantification of alternatively spliced forms of neurofascin at different developmental stages in the chicken brain. The study reveals a complex expression pattern of neurofascin isoforms.
    • (1997) J Biol Chem , vol.272 , pp. 28742-28749
    • Hassel, B.1    Rathjen, F.G.2    Volkmer, H.3
  • 33
    • 0030219702 scopus 로고    scopus 로고
    • Characterization of a highly conserved human homolog to the chicken neural cell surface protein Bravo/Nr-CAM that maps to chromosome band 7q31
    • Lane RP, Chen XN, Yamakawa K, Vielmetter J, Korenberg JR, Dreyer WJ. Characterization of a highly conserved human homolog to the chicken neural cell surface protein Bravo/Nr-CAM that maps to chromosome band 7q31. Genomics. 35:1996;456-465.
    • (1996) Genomics , vol.35 , pp. 456-465
    • Lane, R.P.1    Chen, X.N.2    Yamakawa, K.3    Vielmetter, J.4    Korenberg, J.R.5    Dreyer, W.J.6
  • 34
    • 0030561313 scopus 로고    scopus 로고
    • Heterophilic interactions of the neural cell adhesion molecules Ng-CAM and Nr-CAM with neural receptors and extracellular matrix proteins
    • Grumet M, Sakurai T. Heterophilic interactions of the neural cell adhesion molecules Ng-CAM and Nr-CAM with neural receptors and extracellular matrix proteins. Semin Neurosci. 8:1996;379-389.
    • (1996) Semin Neurosci , vol.8 , pp. 379-389
    • Grumet, M.1    Sakurai, T.2
  • 35
    • 0026718372 scopus 로고
    • Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily
    • Volkmer H, Hassel B, Wolff JM, Frank R, Rathjen FG. Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily. J Cell Biol. 118:1992;149-161.
    • (1992) J Cell Biol , vol.118 , pp. 149-161
    • Volkmer, H.1    Hassel, B.2    Wolff, J.M.3    Frank, R.4    Rathjen, F.G.5
  • 36
    • 0029125639 scopus 로고
    • Protein tyrosine phosphatases as adhesion receptors
    • Brady-Kalnay SM, Tonks NK. Protein tyrosine phosphatases as adhesion receptors. Curr Opin Cell Biol. 7:1995;650-657.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 650-657
    • Brady-Kalnay, S.M.1    Tonks, N.K.2
  • 37
    • 16044375295 scopus 로고    scopus 로고
    • Continuous renewal of the axonal pathway sensor apparatus by insertion of new sensor molecules into the growth cone membrane
    • of special interest. The authors demonstrate, by using an adenoviral gene transfer vector, that newly synthesized chick NgCAM or axonin-1 are exclusively inserted at the growth cone of extending DRG axons and not at the axon shaft.
    • Vogt L, Giger RJ, Ziegler U, Kunz B, Buchstaller A, Hermens WTJMC, Kaplitt MG, Rosenfeld MR, Pfaff DW, Verhaagen J, Sonderegger P. Continuous renewal of the axonal pathway sensor apparatus by insertion of new sensor molecules into the growth cone membrane. of special interest Curr Biol. 6:1996;1153-1158 The authors demonstrate, by using an adenoviral gene transfer vector, that newly synthesized chick NgCAM or axonin-1 are exclusively inserted at the growth cone of extending DRG axons and not at the axon shaft.
    • (1996) Curr Biol , vol.6 , pp. 1153-1158
    • Vogt, L.1    Giger, R.J.2    Ziegler, U.3    Kunz, B.4    Buchstaller, A.5    Hermens, W.T.J.M.C.6    Kaplitt, M.G.7    Rosenfeld, M.R.8    Pfaff, D.W.9    Verhaagen, J.10    Sonderegger, P.11
  • 38
    • 0029957549 scopus 로고    scopus 로고
    • Outline structure of the human L1 cell adhesion molecule and the sites where mutations cause neurological disorders
    • of outstanding interest. The authors derived structural models for the Ig- and FNIII-like domains of human L1 by comparing the L1 sequence with those of resolved domains of telokin and neuroglian. They then used the 'outline structures' to divide pathological missense mutations of the extracellular domain into those that would alter domain conformation and those that would affect surface properties.
    • Bateman A, Jouet M, MacFarlane J, Du JS, Kenwrick S, Chothia C. Outline structure of the human L1 cell adhesion molecule and the sites where mutations cause neurological disorders. of outstanding interest EMBO J. 15:1996;6050-6059 The authors derived structural models for the Ig- and FNIII-like domains of human L1 by comparing the L1 sequence with those of resolved domains of telokin and neuroglian. They then used the 'outline structures' to divide pathological missense mutations of the extracellular domain into those that would alter domain conformation and those that would affect surface properties.
    • (1996) EMBO J , vol.15 , pp. 6050-6059
    • Bateman, A.1    Jouet, M.2    MacFarlane, J.3    Du, J.S.4    Kenwrick, S.5    Chothia, C.6
  • 39
    • 0030449701 scopus 로고    scopus 로고
    • Structural analysis of the murine cell adhesion molecule L1 by electron microscopy and computer assisted modelling
    • Drescher B, Spiess E, Schachner M, Probstmeier R. Structural analysis of the murine cell adhesion molecule L1 by electron microscopy and computer assisted modelling. Eur J Neurosci. 8:1996;2467-2478.
    • (1996) Eur J Neurosci , vol.8 , pp. 2467-2478
    • Drescher, B.1    Spiess, E.2    Schachner, M.3    Probstmeier, R.4
  • 40
    • 0030330152 scopus 로고    scopus 로고
    • A locus-specific mutation database for the neural cell adhesion molecule L1CAM (Xq28)
    • of special interest. An up-to-date reference to mutations in the L1 gene (http://dnalab-www.uia.ac.be/dnalab/l1), which are also collected in the Human Gene Mutation Database at the Institute of Medical Genetics in Cardiff, UK (http://www.uwcm.ac.uk/uwcm/mg).
    • Van Camp G, Fransen E, Vits L, Raes G, Willems PJ. A locus-specific mutation database for the neural cell adhesion molecule L1CAM (Xq28). of special interest Hum Mutat. 8:1996;391 An up-to-date reference to mutations in the L1 gene (http://dnalab-www.uia.ac.be/dnalab/l1), which are also collected in the Human Gene Mutation Database at the Institute of Medical Genetics in Cardiff, UK (http://www.uwcm.ac.uk/uwcm/mg).
    • (1996) Hum Mutat , vol.8 , pp. 391
    • Van Camp, G.1    Fransen, E.2    Vits, L.3    Raes, G.4    Willems, P.J.5
  • 41
    • 0030858735 scopus 로고    scopus 로고
    • CRASH syndrome: Mutations in L1CAM correlate with severity of the disease
    • of special interest. Assessment of the literature on 129 patients with 34 L1 mutations in relation to morbidity, the development of hydrocephalus, mental retardation and adducted thumbs.
    • Yamasaki M, Thompson P, Lemmon V. CRASH syndrome: mutations in L1CAM correlate with severity of the disease. of special interest Neuropediatrics. 28:1997;175-178 Assessment of the literature on 129 patients with 34 L1 mutations in relation to morbidity, the development of hydrocephalus, mental retardation and adducted thumbs.
    • (1997) Neuropediatrics , vol.28 , pp. 175-178
    • Yamasaki, M.1    Thompson, P.2    Lemmon, V.3
  • 42
    • 0028841097 scopus 로고
    • The cytoplasmic domain of the cell adhesion molecule L1 is not required for homophilic adhesion
    • Wong EV, Cheng GH, Payne HR, Lemmon V. The cytoplasmic domain of the cell adhesion molecule L1 is not required for homophilic adhesion. Neurosci Lett. 200:1995;155-158.
    • (1995) Neurosci Lett , vol.200 , pp. 155-158
    • Wong, E.V.1    Cheng, G.H.2    Payne, H.R.3    Lemmon, V.4
  • 43
    • 0029161504 scopus 로고
    • The cytoplasmic domain of the Drosophila cell adhesion molecule neuroglian is not essential for its homophilic adhesive properties in S2 cells
    • Hortsch M, Wang YM, Marikar Y, Bieber AJ. The cytoplasmic domain of the Drosophila cell adhesion molecule neuroglian is not essential for its homophilic adhesive properties in S2 cells. J Biol Chem. 270:1995;18809-18817.
    • (1995) J Biol Chem , vol.270 , pp. 18809-18817
    • Hortsch, M.1    Wang, Y.M.2    Marikar, Y.3    Bieber, A.J.4
  • 44
    • 0029923451 scopus 로고    scopus 로고
    • Differential effects of two hydrocephalus/MASA syndrome-related mutations on the homophilic binding and neuritogenic activities of the cell adhesion molecule L1
    • of special interest. Microspheres coated with E. coli-expressed Ig-like domain 2 containing mutations Arg184→Gln and His210→Gln are included in binding assays. Both are shown to have reduced binding activity, with Arg184→Gln being most deleterious. Neurite outgrowth studies show a similar difference in the ability of mutant domains to promote neurite growth compared to wild-type.
    • Zhao X, Siu CH. Differential effects of two hydrocephalus/MASA syndrome-related mutations on the homophilic binding and neuritogenic activities of the cell adhesion molecule L1. of special interest J Biol Chem. 271:1996;6563-6566 Microspheres coated with E. coli-expressed Ig-like domain 2 containing mutations Arg184→Gln and His210→Gln are included in binding assays. Both are shown to have reduced binding activity, with Arg184→Gln being most deleterious. Neurite outgrowth studies show a similar difference in the ability of mutant domains to promote neurite growth compared to wild-type.
    • (1996) J Biol Chem , vol.271 , pp. 6563-6566
    • Zhao, X.1    Siu, C.H.2
  • 45
    • 0028891952 scopus 로고
    • Colocalization of the homophilic binding site and the neuritogenic activity of the cell adhesion molecule L1 to its second Ig-like domain
    • Zhao X, Siu CH. Colocalization of the homophilic binding site and the neuritogenic activity of the cell adhesion molecule L1 to its second Ig-like domain. J Biol Chem. 270:1995;29413-29421.
    • (1995) J Biol Chem , vol.270 , pp. 29413-29421
    • Zhao, X.1    Siu, C.H.2
  • 49
    • 0029666274 scopus 로고    scopus 로고
    • rsk in neurite outgrowth mediated by the cell adhesion molecule L1
    • rsk phosphorylates L1 at serine residue 1152. The region including this serine seems to be important for DRG neurite outgrowth, as shown by in vitro experiments using specific synthetic peptides.
    • rsk phosphorylates L1 at serine residue 1152. The region including this serine seems to be important for DRG neurite outgrowth, as shown by in vitro experiments using specific synthetic peptides.
    • (1996) J Biol Chem , vol.271 , pp. 18217-18223
    • Wong, E.V.1    Schaefer, A.W.2    Landreth, G.3    Lemmon, V.4
  • 50
    • 0030066569 scopus 로고    scopus 로고
    • Casein kinase II phosphorylates the neural cell adhesion molecule L1
    • of special interest. The authors demonstrate that the serine/threonine kinase casein kinase II (CK II) is associated in immunoprecipitations with L1. The use of synthetic peptides identifies the serine residue at position 1181 as a phosphorylation site of CK II. This site was also found to be phosphorylated in vivo.
    • Wong EV, Schaefer AW, Landreth G, Lemmon V. Casein kinase II phosphorylates the neural cell adhesion molecule L1. of special interest J Neurochem. 66:1996;779-786 The authors demonstrate that the serine/threonine kinase casein kinase II (CK II) is associated in immunoprecipitations with L1. The use of synthetic peptides identifies the serine residue at position 1181 as a phosphorylation site of CK II. This site was also found to be phosphorylated in vivo.
    • (1996) J Neurochem , vol.66 , pp. 779-786
    • Wong, E.V.1    Schaefer, A.W.2    Landreth, G.3    Lemmon, V.4
  • 51
    • 0024675417 scopus 로고
    • Li-mediated axon outgrowth occurs via a homophilic binding mechanism
    • Lemmon V, Farr KL, Lagenaur C. Li-mediated axon outgrowth occurs via a homophilic binding mechanism. Neuron. 2:1989;1597-1603.
    • (1989) Neuron , vol.2 , pp. 1597-1603
    • Lemmon, V.1    Farr, K.L.2    Lagenaur, C.3
  • 52
    • 0030578448 scopus 로고    scopus 로고
    • Clustering and functional cooperation of Ng-CAM and axonin-1 in the substratum-contact area of growth cones
    • Stoeckli ET, Ziegler U, Bleiker AJ, Groscurth P, Sonderegger P. Clustering and functional cooperation of Ng-CAM and axonin-1 in the substratum-contact area of growth cones. Dev Biol. 177:1996;15-29.
    • (1996) Dev Biol , vol.177 , pp. 15-29
    • Stoeckli, E.T.1    Ziegler, U.2    Bleiker, A.J.3    Groscurth, P.4    Sonderegger, P.5
  • 53
    • 0030455845 scopus 로고    scopus 로고
    • Cell adhesion molecules NgCAM and axonin-1 form heterodimers in the neuronal membrane and cooperate in neurite outgrowth promotion
    • of special interest. of outstanding interest. Co-capping and chemical crosslinking experiments show that NgCAM forms a cis-complex with axonin-1 in DRG cells. This cis-interaction as well as a NgCAM-NgCAM trans-interaction are essential for neurite outgrowth on immobilized NgCAM. See also [52,54,74].
    • of special interest Buchstaller A, Kunz S, Berger P, Kunz B, Ziegler U, Rader C, Sonderegger P. Cell adhesion molecules NgCAM and axonin-1 form heterodimers in the neuronal membrane and cooperate in neurite outgrowth promotion. of outstanding interest J Cell Biol. 135:1996;1593-1607 Co-capping and chemical crosslinking experiments show that NgCAM forms a cis-complex with axonin-1 in DRG cells. This cis-interaction as well as a NgCAM-NgCAM trans-interaction are essential for neurite outgrowth on immobilized NgCAM. See also [52,54,74].
    • (1996) J Cell Biol , vol.135 , pp. 1593-1607
    • Buchstaller, A.1    Kunz, S.2    Berger, P.3    Kunz, B.4    Ziegler, U.5    Rader, C.6    Sonderegger, P.7
  • 54
    • 0031034895 scopus 로고    scopus 로고
    • Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase β
    • of outstanding interest. Shows that the L1-like molecule NrCAM may form cis-complexes with the GPI-linked molecule F11/contactin and that a complex of both proteins is involved in neurite outgrowth induced by glial receptor protein tyrosine phosphatase β/ζ. See also [53].
    • Sakurai T, Lustig M, Nativ M, Hemperly JJ, Schlessinger J, Peles E, Grumet M. Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase β of outstanding interest J Cell Biol. 136:1997;907-918 Shows that the L1-like molecule NrCAM may form cis-complexes with the GPI-linked molecule F11/contactin and that a complex of both proteins is involved in neurite outgrowth induced by glial receptor protein tyrosine phosphatase β/ζ. See also [53].
    • (1997) J Cell Biol , vol.136 , pp. 907-918
    • Sakurai, T.1    Lustig, M.2    Nativ, M.3    Hemperly, J.J.4    Schlessinger, J.5    Peles, E.6    Grumet, M.7
  • 56
    • 0343416810 scopus 로고    scopus 로고
    • The gene of the neural cell recognition molecule F11: Conserved exon-intron arrangement in genes of neural members of the immunoglobulin superfamily
    • Plagge A, Brümmendorf T. The gene of the neural cell recognition molecule F11: conserved exon-intron arrangement in genes of neural members of the immunoglobulin superfamily. Gene. 192:1997;215-225.
    • (1997) Gene , vol.192 , pp. 215-225
    • Plagge, A.1    Brümmendorf, T.2
  • 57
    • 0029093081 scopus 로고
    • Overlapping and differential expression of BIG-2, BIG-1, TAG-1, and F3 - Four members of an axon-associated cell adhesion molecule subgroup of the immunoglobulin superfamily
    • Yoshihara Y, Kawasaki M, Tamada A, Nagata S, Kagamiyama H, Mori K. Overlapping and differential expression of BIG-2, BIG-1, TAG-1, and F3 - four members of an axon-associated cell adhesion molecule subgroup of the immunoglobulin superfamily. J Neurobiol. 28:1995;51-69.
    • (1995) J Neurobiol , vol.28 , pp. 51-69
    • Yoshihara, Y.1    Kawasaki, M.2    Tamada, A.3    Nagata, S.4    Kagamiyama, H.5    Mori, K.6
  • 58
    • 0024566580 scopus 로고
    • Distribution and possible interactions of actin-associated proteins and cell adhesion molecules of nerve growth cones
    • Letourneau PC, Shattuck TA. Distribution and possible interactions of actin-associated proteins and cell adhesion molecules of nerve growth cones. Development. 105:1989;505-519.
    • (1989) Development , vol.105 , pp. 505-519
    • Letourneau, P.C.1    Shattuck, T.A.2
  • 59
    • 0027999616 scopus 로고
    • Ankyrin binding activity shared by the neurofascin/L1/NrCAM family of nervous system cell adhesion molecules
    • David JQ, Bennett V. Ankyrin binding activity shared by the neurofascin/L1/NrCAM family of nervous system cell adhesion molecules. J Biol Chem. 269:1994;27163-27166.
    • (1994) J Biol Chem , vol.269 , pp. 27163-27166
    • David, J.Q.1    Bennett, V.2
  • 60
    • 0029899939 scopus 로고    scopus 로고
    • Neuroglian-mediated cell adhesion induces assembly of the membrane skeleton at cell contact sites
    • Dubreuil RR, Macvicar G, Dissanayake S, Liu CH, Homer D, Hortsch M. Neuroglian-mediated cell adhesion induces assembly of the membrane skeleton at cell contact sites. J Cell Biol. 133:1996;647-655.
    • (1996) J Cell Biol , vol.133 , pp. 647-655
    • Dubreuil, R.R.1    MacVicar, G.2    Dissanayake, S.3    Liu, C.H.4    Homer, D.5    Hortsch, M.6
  • 61
    • 0028985712 scopus 로고
    • G: A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier
    • G: a new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier. J Biol Chem. 270:1995;2352-2359.
    • (1995) J Biol Chem , vol.270 , pp. 2352-2359
    • Kordeli, E.1    Lambert, S.2    Bennett, V.3
  • 62
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
    • Bennett V, Gilligan DM. The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu Rev Cell Biol. 9:1993;27-66.
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 27-66
    • Bennett, V.1    Gilligan, D.M.2
  • 63
    • 0026607234 scopus 로고
    • The ANK repeat: A ubiquituous motif involved in macromolecular recognition
    • Michaely P, Bennett V. The ANK repeat: a ubiquituous motif involved in macromolecular recognition. Trends Cell Biol. 2:1992;127-129.
    • (1992) Trends Cell Biol , vol.2 , pp. 127-129
    • Michaely, P.1    Bennett, V.2
  • 66
    • 0030443956 scopus 로고    scopus 로고
    • -) and NrCAM at nodal axon segments
    • G and voltage-gated sodium channels. An isoform containing the third FNIII-like domain and lacking the fifth FNIII-like domain was found to be present in unmyelinated axons. NrCAM was also found to be co-localized at the node of Ranvier.
    • G and voltage-gated sodium channels. An isoform containing the third FNIII-like domain and lacking the fifth FNIII-like domain was found to be present in unmyelinated axons. NrCAM was also found to be co-localized at the node of Ranvier.
    • (1996) J Cell Biol , vol.135 , pp. 1355-1367
    • Davis, J.Q.1    Lambert, S.2    Bennett, V.3
  • 67
    • 0030824001 scopus 로고    scopus 로고
    • Morphogenesis of the node of Ranvier: Co-clusters of ankyrin and ankyrin-binding integral proteins define early developmental intermediates
    • G and the voltage-gated sodium channel.
    • G and the voltage-gated sodium channel.
    • (1997) J Neurosci , vol.17 , pp. 7025-7036
    • Lambert, S.1    Davis, J.Q.2    Bennett, V.3
  • 68
    • 0030957351 scopus 로고    scopus 로고
    • Clustering sodium channels at the node of Ranvier: Close encounters of the axon-glia kind
    • G. As ankyrin is known to bind sodium channels and L1-like proteins, it is proposed that this may provide a link between extracellular cues and the clustering of sodium channels. One putative cue may be tenascin-R, which is secreted by oligodendrocytes and which binds to F11, one of the L1-binding molecules.
    • G. As ankyrin is known to bind sodium channels and L1-like proteins, it is proposed that this may provide a link between extracellular cues and the clustering of sodium channels. One putative cue may be tenascin-R, which is secreted by oligodendrocytes and which binds to F11, one of the L1-binding molecules.
    • (1997) Neuron , vol.18 , pp. 843-846
    • Salzer, J.L.1
  • 69
    • 0030747306 scopus 로고    scopus 로고
    • Mutational analysis of the L1 neuronal cell adhesion molecule identifies membrane-proximal amino acids of the cytoplasmic domain that are required for cytoskeletal anchorage
    • of special interest. L1 was shown to co-localize with actin- and myosin-containing stress fibers in rat B28 glioma cells. This array of L1 seems to require a membrane-proximal motif of the cytoplasmic segment and is therefore independent of the ankyrin-binding motif near the carboxyl terminus of L1.
    • Dahlin Huppe K, Berglund EO, Ranscht B, Stallcup WB. Mutational analysis of the L1 neuronal cell adhesion molecule identifies membrane-proximal amino acids of the cytoplasmic domain that are required for cytoskeletal anchorage. of special interest Mol Cell Neurosci. 9:1997;144-156 L1 was shown to co-localize with actin- and myosin-containing stress fibers in rat B28 glioma cells. This array of L1 seems to require a membrane-proximal motif of the cytoplasmic segment and is therefore independent of the ankyrin-binding motif near the carboxyl terminus of L1.
    • (1997) Mol Cell Neurosci , vol.9 , pp. 144-156
    • Dahlin Huppe, K.1    Berglund, E.O.2    Ranscht, B.3    Stallcup, W.B.4
  • 70
    • 0029906430 scopus 로고    scopus 로고
    • Review: A role for the FGF receptor in the axonal growth response stimulated by cell adhesion molecules?
    • Hall H, Walsh FS, Doherty P. Review: a role for the FGF receptor in the axonal growth response stimulated by cell adhesion molecules? Cell Adhes Commun. 3:1996;441-450.
    • (1996) Cell Adhes Commun , vol.3 , pp. 441-450
    • Hall, H.1    Walsh, F.S.2    Doherty, P.3
  • 71
    • 0031039771 scopus 로고    scopus 로고
    • Expression of a dominant negative FGF receptor inhibits axonal growth and FGF receptor phosphorylation stimulated by CAMs
    • of outstanding interest. Demonstration that the activation of L1 or NCAM can lead to a phosphorylation of the FGF receptor 1 in PC12 cells. Stimulation of neurite extension by CAMs including L1 is lost when a dominant-negative form of FGF receptor 1 that lacks the kinase activity is expressed in PC12 cells or in neurons using the neuron-specific enolase promoter. A peptide inhibitor of the phospholipase Cγ was also found to inhibit neurite extension induced by CAMs. These studies support the view that the activation of the FGF receptor 1 is important for CAM-mediated axonal growth.
    • Saffell JL, Williams EJ, Mason IJ, Walsh FS, Doherty P. Expression of a dominant negative FGF receptor inhibits axonal growth and FGF receptor phosphorylation stimulated by CAMs. of outstanding interest Neuron. 18:1997;231-242 Demonstration that the activation of L1 or NCAM can lead to a phosphorylation of the FGF receptor 1 in PC12 cells. Stimulation of neurite extension by CAMs including L1 is lost when a dominant-negative form of FGF receptor 1 that lacks the kinase activity is expressed in PC12 cells or in neurons using the neuron-specific enolase promoter. A peptide inhibitor of the phospholipase Cγ was also found to inhibit neurite extension induced by CAMs. These studies support the view that the activation of the FGF receptor 1 is important for CAM-mediated axonal growth.
    • (1997) Neuron , vol.18 , pp. 231-242
    • Saffell, J.L.1    Williams, E.J.2    Mason, I.J.3    Walsh, F.S.4    Doherty, P.5
  • 73
    • 0024457480 scopus 로고
    • A protein kinase activity is associated with and specifically phosphorylates the neural cell adhesion molecule L1
    • Sadoul R, Kirchhoff F, Schachner M. A protein kinase activity is associated with and specifically phosphorylates the neural cell adhesion molecule L1. J Neurochem. 53:1989;1471-1478.
    • (1989) J Neurochem , vol.53 , pp. 1471-1478
    • Sadoul, R.1    Kirchhoff, F.2    Schachner, M.3
  • 74
    • 0029662193 scopus 로고    scopus 로고
    • Intracellular signaling is changed after clustering of the neural cell adhesion molecules axonin-1 and NgCAM during neurite fasciculation
    • of outstanding interest. of special interest. Co-immunoprecipitation experiments suggest that L1/NgCAM is associated with a serine/threonine kinase related to S6 kinase and that L1/NgCAM phosphorylation is correlated with binding to axonin-1. Furthermore, evidence is presented that two NgCAM - axonin-1 cis complexes may form a tetramer in trans in fasciculated DRG cultures. See also [53].
    • of outstanding interest Kunz S, Ziegler U, Kunz B, Sonderegger P. Intracellular signaling is changed after clustering of the neural cell adhesion molecules axonin-1 and NgCAM during neurite fasciculation. of special interest J Cell Biol. 135:1996;253-267 Co-immunoprecipitation experiments suggest that L1/NgCAM is associated with a serine/threonine kinase related to S6 kinase and that L1/NgCAM phosphorylation is correlated with binding to axonin-1. Furthermore, evidence is presented that two NgCAM - axonin-1 cis complexes may form a tetramer in trans in fasciculated DRG cultures. See also [53].
    • (1996) J Cell Biol , vol.135 , pp. 253-267
    • Kunz, S.1    Ziegler, U.2    Kunz, B.3    Sonderegger, P.4
  • 75
    • 0028152333 scopus 로고
    • MAP kinase kinase kinase, MAP kinase kinase and MAP kinase
    • Marshall CJ. MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr Opin Genet Dev. 4:1994;82-89.
    • (1994) Curr Opin Genet Dev , vol.4 , pp. 82-89
    • Marshall, C.J.1
  • 76
    • 0031589004 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro
    • Nagase TM, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O. Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 4:1997;141-150.
    • (1997) DNA Res , vol.4 , pp. 141-150
    • Nagase, T.M.1    Ishikawa, K.2    Nakajima, D.3    Ohira, M.4    Seki, N.5    Miyajima, N.6    Tanaka, A.7    Kotani, H.8    Nomura, N.9    Ohara, O.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.