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1
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0029085733
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Cell adhesion molecules as morphoregulators
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of outstanding interest. The author reviews recent work on cell adhesion molecule (CAM) structure and binding, and on the regulation of CAM gene expression by homeodomain proteins.
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of outstanding interest Cunningham BA. Cell adhesion molecules as morphoregulators. Curr Opin Cell Biol. 7:1995;628-633 The author reviews recent work on cell adhesion molecule (CAM) structure and binding, and on the regulation of CAM gene expression by homeodomain proteins.
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(1995)
Curr Opin Cell Biol
, vol.7
, pp. 628-633
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Cunningham, B.A.1
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2
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0029443827
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Cell adhesion molecules 1: Immunoglobulin superfamily
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of outstanding interest. A comprehensive review that highlights common aspects of nervous system and immune system IgSF cell adhesion receptors.
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of outstanding interest Brümmendorf T, Rathjen FG. Cell adhesion molecules 1: immunoglobulin superfamily. Protein Profile. 2:1995;963-1108 A comprehensive review that highlights common aspects of nervous system and immune system IgSF cell adhesion receptors.
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(1995)
Protein Profile
, vol.2
, pp. 963-1108
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Brümmendorf, T.1
Rathjen, F.G.2
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3
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0029093081
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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
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of special interest. Reports the cloning of rat brain-derived Ig molecule 2 (BIG-2) and a detailed comparison of the expression patterns of BIG-1, BIG-2, F3/F11 and TAG-1/axonin-1 in the developing and adult rat brain.
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of special interest 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 Reports the cloning of rat brain-derived Ig molecule 2 (BIG-2) and a detailed comparison of the expression patterns of BIG-1, BIG-2, F3/F11 and TAG-1/axonin-1 in the developing and adult rat brain.
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(1995)
J Neurobiol
, vol.28
, pp. 51-69
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-
Yoshihara, Y.1
Kawasaki, M.2
Tamada, A.3
Nagata, S.4
Kagamiyama, H.5
Mori, K.6
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4
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0029117624
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Fish E587 glycoprotein, a member of the L1 family of cell adhesion molecules, participates in axonal fasciculation and the age-related order of ganglion cell axons in the goldfish retina
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of special interest. Shows that an L1-related molecule in goldfish is involved in age-related fasciculation in the retina.
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of special interest Bastmeyer M, Ott H, Leppert CA, Stuermer CA. Fish E587 glycoprotein, a member of the L1 family of cell adhesion molecules, participates in axonal fasciculation and the age-related order of ganglion cell axons in the goldfish retina. J Cell Biol. 130:1995;969-976 Shows that an L1-related molecule in goldfish is involved in age-related fasciculation in the retina.
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(1995)
J Cell Biol
, vol.130
, pp. 969-976
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Bastmeyer, M.1
Ott, H.2
Leppert, C.A.3
Stuermer, C.A.4
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5
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0028789329
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Zebrafish neurons express two L1-related molecules during early axonogenesis
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Tongiorgi E, Bernhardt RR, Schachner M. Zebrafish neurons express two L1-related molecules during early axonogenesis. J Neurosci Res. 42:1995;547-561.
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(1995)
J Neurosci Res
, vol.42
, pp. 547-561
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Tongiorgi, E.1
Bernhardt, R.R.2
Schachner, M.3
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6
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0028959978
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DCC: Linking tumor suppressor genes and altered cell surface interactions in cancer
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Cho KR, Fearon ER. DCC: linking tumor suppressor genes and altered cell surface interactions in cancer. Curr Opin Genet Dev. 5:1995;72-78.
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(1995)
Curr Opin Genet Dev
, vol.5
, pp. 72-78
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Cho, K.R.1
Fearon, E.R.2
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7
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0028606322
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Neogenin, an avian cell surface protein expressed during terminal neuronal differentiation, is closely related to the human tumor suppressor molecule deleted in colorectal cancer
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Vielmetter J, Kayyem JF, Roman J, Dreyer WJ. Neogenin, an avian cell surface protein expressed during terminal neuronal differentiation, is closely related to the human tumor suppressor molecule deleted in colorectal cancer. J Cell Biol. 127:1994;2009-2020.
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(1994)
J Cell Biol
, vol.127
, pp. 2009-2020
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Vielmetter, J.1
Kayyem, J.F.2
Roman, J.3
Dreyer, W.J.4
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8
-
-
0028324194
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An ICAM-related neuronal glycoprotein, telencephalin, with brain segment-specific expression
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Yoshihara Y, Oka S, Nemoto Y, Watanabe Y, Nagata S, Kagamiyama H, Mori K. An ICAM-related neuronal glycoprotein, telencephalin, with brain segment-specific expression. Neuron. 12:1994;541-553.
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(1994)
Neuron
, vol.12
, pp. 541-553
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-
Yoshihara, Y.1
Oka, S.2
Nemoto, Y.3
Watanabe, Y.4
Nagata, S.5
Kagamiyama, H.6
Mori, K.7
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9
-
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0028905174
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Cloning of neurotrimin defines a new subfamily of differentially expressed neural cell adhesion molecules
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Struyk AF, Canoll PD, Wolfgang MJ, Rosen CL, Deustachio P, Salzer JL. Cloning of neurotrimin defines a new subfamily of differentially expressed neural cell adhesion molecules. J Neurosci. 15:1995;2141-2156.
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(1995)
J Neurosci
, vol.15
, pp. 2141-2156
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Struyk, A.F.1
Canoll, P.D.2
Wolfgang, M.J.3
Rosen, C.L.4
Deustachio, P.5
Salzer, J.L.6
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10
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0029082199
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The limbic system-associated membrane protein is an Ig superfamily member that mediates selective neuronal growth and axon targeting
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of outstanding interest. Reports the cloning of limbic system associated membrane protein (LAMP) and extends previous functional in vitro studies [68]. LAMP selectively enhances neurite outgrowth of limbic neurons and plays a role in the invasion of the hippocampus by septal afferents and in the formation of the intrahippocampal mossy fibre projection.
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of outstanding interest Pimenta AF, Zhukareva V, Barbe MF, Reinoso BS, Grimley C, Henzel W, Fischer I, Levitt P. The limbic system-associated membrane protein is an Ig superfamily member that mediates selective neuronal growth and axon targeting. Neuron. 15:1995;287-297 Reports the cloning of limbic system associated membrane protein (LAMP) and extends previous functional in vitro studies [68]. LAMP selectively enhances neurite outgrowth of limbic neurons and plays a role in the invasion of the hippocampus by septal afferents and in the formation of the intrahippocampal mossy fibre projection.
-
(1995)
Neuron
, vol.15
, pp. 287-297
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-
Pimenta, A.F.1
Zhukareva, V.2
Barbe, M.F.3
Reinoso, B.S.4
Grimley, C.5
Henzel, W.6
Fischer, I.7
Levitt, P.8
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11
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0029865781
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CEPU-1, a novel immunoglobulin superfamily molecule is expressed by developing cerebellar Purkinje cells
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of special interest. Cloning of a neural IgSF member on the basis of sequence characteristics of Ig-like domains. This molecule is found in dendrites, the soma and the axon of Purkinje cells.
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of special interest Spaltmann F, Brümmendorf T. CEPU-1, a novel immunoglobulin superfamily molecule is expressed by developing cerebellar Purkinje cells. J Neurosci. 16:1996;1770-1779 Cloning of a neural IgSF member on the basis of sequence characteristics of Ig-like domains. This molecule is found in dendrites, the soma and the axon of Purkinje cells.
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(1996)
J Neurosci
, vol.16
, pp. 1770-1779
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Spaltmann, F.1
Brümmendorf, T.2
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12
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0028361540
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Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains
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Harpaz Y, Chothia C. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J Mol Biol. 238:1994;528-539.
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(1994)
J Mol Biol
, vol.238
, pp. 528-539
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Harpaz, Y.1
Chothia, C.2
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13
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0028965141
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Glycans and the modulation of neural-recognition molecule function
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Schachner M, Martini R. Glycans and the modulation of neural-recognition molecule function. Trends Neurosci. 18:1995;183-191.
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(1995)
Trends Neurosci
, vol.18
, pp. 183-191
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Schachner, M.1
Martini, R.2
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14
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0029042874
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Axonin-1, Nr-CAM, and Ng-CAM play different roles in the in vivo guidance of chick commissural neurons
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of outstanding interest. The guidance of commissural axons across the floor plate was investigated by antibody application in the central canal of the spinal cord in ovo. Axonin-1 on commissural growth cones and NrCAM on floor plate cells were found to be required for accurate pathfinding.
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of outstanding interest 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 The guidance of commissural axons across the floor plate was investigated by antibody application in the central canal of the spinal cord in ovo. Axonin-1 on commissural growth cones and NrCAM on floor plate cells were found to be required for accurate pathfinding.
-
(1995)
Neuron
, vol.14
, pp. 1165-1179
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-
Stoeckli, E.T.1
Landmesser, L.2
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15
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0029889132
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CRASH syndrome: The clinical spectrum of mutations in L1, a neuronal cell adhesion molecule
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of special interest. A recent review on 34 mutations in the L1 gene of patients suffering from human hereditary disorders affecting brain development. The authors proposed to refer to these disorders with the acronym CRASH, for corpus callosum agenesis, mental retardation, adducted thumbs, spastic paraplegia and hydrocephalus. (See also http://dnalab-www.uia.ac.be/dnalab/l1.html for an updated collection of at least 52 mutations in the L1 gene.)
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of special interest Fransen E, Vits L, Van Camp G, Willems PJ. CRASH syndrome: the clinical spectrum of mutations in L1, a neuronal cell adhesion molecule. Am J Med Genet. 64:1996;73-77 A recent review on 34 mutations in the L1 gene of patients suffering from human hereditary disorders affecting brain development. The authors proposed to refer to these disorders with the acronym CRASH, for corpus callosum agenesis, mental retardation, adducted thumbs, spastic paraplegia and hydrocephalus. (See also http://dnalab-www.uia.ac.be/dnalab/l1.html for an updated collection of at least 52 mutations in the L1 gene.).
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(1996)
Am J Med Genet
, vol.64
, pp. 73-77
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Fransen, E.1
Vits, L.2
Van Camp, G.3
Willems, P.J.4
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16
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0030029134
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X linked hydrocephalus and MASA syndrome
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of special interest. A recent review of L1-associated X-linked hydrocephalus and MASA syndrome, with emphasis on clinical and genetic characteristics. The authors also discuss mutations in the L1 gene.
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of special interest Kenwrick S, Jouet M, Donnai D. X linked hydrocephalus and MASA syndrome. J Med Genet. 33:1996;59-65 A recent review of L1-associated X-linked hydrocephalus and MASA syndrome, with emphasis on clinical and genetic characteristics. The authors also discuss mutations in the L1 gene.
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(1996)
J Med Genet
, vol.33
, pp. 59-65
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Kenwrick, S.1
Jouet, M.2
Donnai, D.3
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17
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0030048089
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Myelin protein zero (mpz) gene mutations in nonduplication type 1 Charcot - Marie - Tooth disease
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Roa BB, Warner LE, Garcia CA, Russo D, Lovelace R, Chance PF, Lupski JR. Myelin protein zero (mpz) gene mutations in nonduplication type 1 Charcot - Marie - Tooth disease. Hum Mutat. 7:1996;36-45.
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(1996)
Hum Mutat
, vol.7
, pp. 36-45
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-
Roa, B.B.1
Warner, L.E.2
Garcia, C.A.3
Russo, D.4
Lovelace, R.5
Chance, P.F.6
Lupski, J.R.7
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18
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0029096048
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The carbonic anhydrase domain of receptor tyrosine phosphatase β is a functional ligand for the axonal cell recognition molecule contactin
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of outstanding interest. The carbonic anhydrase domain of RPTPβ binds specifically to the F11 protein, also termed contactin, and induces neurite extension mediated by neuronal F11
-
of outstanding interest Peles E, Nativ M, Campbell PL, Sakurai T, Martinez R, Lev S, Clary DO, Schilling J, Barnea G, Plowman GD, et al. The carbonic anhydrase domain of receptor tyrosine phosphatase β is a functional ligand for the axonal cell recognition molecule contactin. Cell. 82:1995;251-260 The carbonic anhydrase domain of RPTPβ binds specifically to the F11 protein, also termed contactin, and induces neurite extension mediated by neuronal F11.
-
(1995)
Cell
, vol.82
, pp. 251-260
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-
Peles, E.1
Nativ, M.2
Campbell, P.L.3
Sakurai, T.4
Martinez, R.5
Lev, S.6
Clary, D.O.7
Schilling, J.8
Barnea, G.9
Plowman, G.D.10
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19
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0029953598
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Heterophilic interactions of DM-GRASP - GRASP-NgCAM interactions involved in neurite extension
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of special interest. Antibodies to DM-GRASP were found to inhibit neurite extension on immobilized NgCAM, suggesting that DM-GRASP on the axonal surface interacts with NgCAM. NgCAM also binds to DM-GRASP columns.
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of special interest DeBernardo AP, Chang S. Heterophilic interactions of DM-GRASP - GRASP-NgCAM interactions involved in neurite extension. J Cell Biol. 133:1996;657-666 Antibodies to DM-GRASP were found to inhibit neurite extension on immobilized NgCAM, suggesting that DM-GRASP on the axonal surface interacts with NgCAM. NgCAM also binds to DM-GRASP columns.
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(1996)
J Cell Biol
, vol.133
, pp. 657-666
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-
DeBernardo, A.P.1
Chang, S.2
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20
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0029612178
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NCAM requires a cytoplasmic domain to function as a neurite outgrowth-promoting neuronal receptor
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Saffell JL, Doherty P, Tiveron MC, Morris RJ, Walsh FS. NCAM requires a cytoplasmic domain to function as a neurite outgrowth-promoting neuronal receptor. Mol Cell Neurosci. 6:1995;521-531.
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(1995)
Mol Cell Neurosci
, vol.6
, pp. 521-531
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-
Saffell, J.L.1
Doherty, P.2
Tiveron, M.C.3
Morris, R.J.4
Walsh, F.S.5
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21
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0026319551
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Neurite outgrowth on immobilized axonin-1 is mediated by a heterophilic interaction with L1(G4)
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Kuhn TB, Stoeckli ET, Condrau MA, Rathjen FG, Sonderegger P. Neurite outgrowth on immobilized axonin-1 is mediated by a heterophilic interaction with L1(G4). J Cell Biol. 115:1991;1113-1126.
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(1991)
J Cell Biol
, vol.115
, pp. 1113-1126
-
-
Kuhn, T.B.1
Stoeckli, E.T.2
Condrau, M.A.3
Rathjen, F.G.4
Sonderegger, P.5
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22
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0030578448
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Clustering and functional cooperation of Ng-CAM and axonin-1 in the substratum-contact area of growth cones
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of special interest. The authors examine the distribution of axonin-1 and NgCAM in the growth cone membrane of DRG neurites. They show that neurite outgrowth depends on a cooperation of axonin-1 with NgCAM in the growth cone membrane.
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of special interest 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 The authors examine the distribution of axonin-1 and NgCAM in the growth cone membrane of DRG neurites. They show that neurite outgrowth depends on a cooperation of axonin-1 with NgCAM in the growth cone membrane.
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(1996)
Dev Biol
, vol.177
, pp. 15-29
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-
Stoeckli, E.T.1
Ziegler, U.2
Bleiker, A.J.3
Groscurth, P.4
Sonderegger, P.5
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23
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0027723273
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Induction of axonal growth by heterophilic interactions between the cell surface recognition proteins F11 and NrCAM/Bravo
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Morales G, Hubert M, Brümmendorf T, Treubert U, Tarnok A, Schwarz U, Rathjen FG. Induction of axonal growth by heterophilic interactions between the cell surface recognition proteins F11 and NrCAM/Bravo. Neuron. 11:1993;1113-1122.
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(1993)
Neuron
, vol.11
, pp. 1113-1122
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Morales, G.1
Hubert, M.2
Brümmendorf, T.3
Treubert, U.4
Tarnok, A.5
Schwarz, U.6
Rathjen, F.G.7
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24
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0027526588
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The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180
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Pesheva P, Gennarini G, Goridis C, Schachner M. The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180. Neuron. 10:1993;69-82.
-
(1993)
Neuron
, vol.10
, pp. 69-82
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-
Pesheva, P.1
Gennarini, G.2
Goridis, C.3
Schachner, M.4
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25
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0029114404
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Characterization of functional domains of the tenascin-R (restrictin) polypeptide - Cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R
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of outstanding interest. The authors analyze the interaction between F11 and TN-R. The amino-terminal Ig domains of F11 were found to bind to FNIII-like domains 2 to 3 within TN-R. F11-mediated neurite extension of tectal cells is enhanced by TN-R, sugesting that the combined action of F11 and TNR-R regulates axon extension.
-
of outstanding interest Nörenberg U, Hubert M, Brümmendorf T, Tarnok A, Rathjen FG. Characterization of functional domains of the tenascin-R (restrictin) polypeptide - cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R. J Cell Biol. 130:1995;473-484 The authors analyze the interaction between F11 and TN-R. The amino-terminal Ig domains of F11 were found to bind to FNIII-like domains 2 to 3 within TN-R. F11-mediated neurite extension of tectal cells is enhanced by TN-R, sugesting that the combined action of F11 and TNR-R regulates axon extension.
-
(1995)
J Cell Biol
, vol.130
, pp. 473-484
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-
Nörenberg, U.1
Hubert, M.2
Brümmendorf, T.3
Tarnok, A.4
Rathjen, F.G.5
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26
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0030065691
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3
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3 plays an important role in many developmental processes. Its binding to L1 may provide insights into functions of L1 outside the nervous system. See also annotation [27].
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3 plays an important role in many developmental processes. Its binding to L1 may provide insights into functions of L1 outside the nervous system. See also annotation [27].
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(1996)
J Cell Biol
, vol.132
, pp. 475-485
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-
Montgomery, A.M.P.1
Becker, J.C.2
Siu, C.H.3
Lemmon, V.P.4
Cheresh, D.A.5
Pancook, J.D.6
Zhao, X.N.7
Reisfeld, R.A.8
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27
-
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0029565212
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The L1 adhesion molecule is a cellular ligand for VLA-5
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1. By contrast to human L1, mouse L1 contains two RGD sites in its sixth Ig-like domain. The study shows that L1, as well as a synthetic peptide comprising both RGD sites, can bind the integrin. See also annotation [26].
-
1. By contrast to human L1, mouse L1 contains two RGD sites in its sixth Ig-like domain. The study shows that L1, as well as a synthetic peptide comprising both RGD sites, can bind the integrin. See also annotation [26].
-
(1995)
J Cell Biol
, vol.131
, pp. 1881-1891
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-
Ruppert, M.1
Aigner, S.2
Hubbe, M.3
Yagita, H.4
Altevogt, P.5
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28
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0029879354
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Implications for the domain arrangement of axonin-1 derived from the mapping of its NgCAM binding site
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of outstanding interest. A systematic analysis of domain deletions within axonin-1 that affect NgCAM binding. The authors propose that axonin-1 has a horseshoe-shaped domain arrangement. Looking at DRG neurons, they found that axonin-1's neurite-outgrowth-promoting site is distinct from its NgCAM-binding site.
-
of outstanding interest Rader C, Kunz B, Lierheimer R, Giger RJ, Berger P, Tittmann P, Gross H, Sonderegger P. Implications for the domain arrangement of axonin-1 derived from the mapping of its NgCAM binding site. EMBO J. 15:1996;2056-2068 A systematic analysis of domain deletions within axonin-1 that affect NgCAM binding. The authors propose that axonin-1 has a horseshoe-shaped domain arrangement. Looking at DRG neurons, they found that axonin-1's neurite-outgrowth-promoting site is distinct from its NgCAM-binding site.
-
(1996)
EMBO J
, vol.15
, pp. 2056-2068
-
-
Rader, C.1
Kunz, B.2
Lierheimer, R.3
Giger, R.J.4
Berger, P.5
Tittmann, P.6
Gross, H.7
Sonderegger, P.8
-
29
-
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0027158056
-
The axonal recognition molecule F11 is a multifunctional protein: Specific domains mediate interactions with Ng-CAM and restrictin
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Brümmendorf T, Hubert M, Treubert U, Leuschner R, Tarnok A, Rathjen FG. The axonal recognition molecule F11 is a multifunctional protein: specific domains mediate interactions with Ng-CAM and restrictin. Neuron. 10:1993;711-727.
-
(1993)
Neuron
, vol.10
, pp. 711-727
-
-
Brümmendorf, T.1
Hubert, M.2
Treubert, U.3
Leuschner, R.4
Tarnok, A.5
Rathjen, F.G.6
-
30
-
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0026688638
-
Neuronal cell adhesion molecule contactin/F11 binds to tenascin via its immunoglobulin-like domains
-
Zisch AH, D'Alessandri L, Ranscht B, Falchetto R, Winterhalter KH, Vaughan L. Neuronal cell adhesion molecule contactin/F11 binds to tenascin via its immunoglobulin-like domains. J Cell Biol. 119:1992;203-213.
-
(1992)
J Cell Biol
, vol.119
, pp. 203-213
-
-
Zisch, A.H.1
D'Alessandri, L.2
Ranscht, B.3
Falchetto, R.4
Winterhalter, K.H.5
Vaughan, L.6
-
31
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0029978087
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Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11
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of special interest. Identification of the segments in TN-R that mediate its interaction with F11. The authors found that the epidermal growth factor (EGF)-like repeats, in conjunction with the amino-terminal cysteine-rich segment, of TN-R might bind to F11. This interaction appears to mediate an avoidance response in cerebellar neurons.
-
of special interest Xiao ZC, Taylor J, Montag D, Rougon G, Schachner M. Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11. Eur J Neurosci. 1996; Identification of the segments in TN-R that mediate its interaction with F11. The authors found that the epidermal growth factor (EGF)-like repeats, in conjunction with the amino-terminal cysteine-rich segment, of TN-R might bind to F11. This interaction appears to mediate an avoidance response in cerebellar neurons.
-
(1996)
Eur J Neurosci
-
-
Xiao, Z.C.1
Taylor, J.2
Montag, D.3
Rougon, G.4
Schachner, M.5
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32
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0028273033
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TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and β1 integrins
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Felsenfeld DP, Hynes MA, Skoler KM, Furley AJ, Jessell TM. TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and β1 integrins. Neuron. 12:1994;675-690.
-
(1994)
Neuron
, vol.12
, pp. 675-690
-
-
Felsenfeld, D.P.1
Hynes, M.A.2
Skoler, K.M.3
Furley, A.J.4
Jessell, T.M.5
-
33
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0028783746
-
Binding between the neural cell adhesion molecules axonin-1 and Nr-CAM/Bravo is involved in neuronglia interaction
-
of special interest. In this study, the authors identified NrCAM as a glial receptor for neuronal axonin-1 in DRGs. This interactions is involved in the formation of contacts between neurons and glia.
-
of special interest Suter DM, Pollerberg GE, Buchstaller A, Giger RJ, Dreyer WJ, Sonderegger P. Binding between the neural cell adhesion molecules axonin-1 and Nr-CAM/Bravo is involved in neuronglia interaction. J Cell Biol. 131:1995;1067-1081 In this study, the authors identified NrCAM as a glial receptor for neuronal axonin-1 in DRGs. This interactions is involved in the formation of contacts between neurons and glia.
-
(1995)
J Cell Biol
, vol.131
, pp. 1067-1081
-
-
Suter, D.M.1
Pollerberg, G.E.2
Buchstaller, A.3
Giger, R.J.4
Dreyer, W.J.5
Sonderegger, P.6
-
34
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0029148550
-
Functional analysis of postranslational cleavage product of the neuron-glia cell adhesion molecule, Ng-CAM
-
of outstanding interest. A detailed analysis of the binding activites of the proteolytic cleavage products of NgCAM. The homophilic and heterophilic binding sites reside in the 135 kDa fragment that contains six Ig-like domains and two and a half FNIII-related repeats. The FNIII-like domains 4 to 5 were demonstrated to be sufficient to promote neurite extension of DRG neurons.
-
of outstanding interest Burgoon MP, Hazan RB, Phillips GR, Crossin KL, Edelman GM, Cunningham BA. Functional analysis of postranslational cleavage product of the neuron-glia cell adhesion molecule, Ng-CAM. J Cell Biol. 130:1995;733-744 A detailed analysis of the binding activites of the proteolytic cleavage products of NgCAM. The homophilic and heterophilic binding sites reside in the 135 kDa fragment that contains six Ig-like domains and two and a half FNIII-related repeats. The FNIII-like domains 4 to 5 were demonstrated to be sufficient to promote neurite extension of DRG neurons.
-
(1995)
J Cell Biol
, vol.130
, pp. 733-744
-
-
Burgoon, M.P.1
Hazan, R.B.2
Phillips, G.R.3
Crossin, K.L.4
Edelman, G.M.5
Cunningham, B.A.6
-
35
-
-
0028891952
-
Colocalization of the homophilic binding site and the neuritogenic activity of the cell adhesion molecule L1 to its second Ig-like domain
-
of special interest. Recombinant proteins of human L1 were generated in bacteria and analyzed in binding and neurite outgrowth assays. The second Ig domain was found to be important for homophilic binding of L1 and for promoting neurite outgrowth.
-
of special interest 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 Recombinant proteins of human L1 were generated in bacteria and analyzed in binding and neurite outgrowth assays. The second Ig domain was found to be important for homophilic binding of L1 and for promoting neurite outgrowth.
-
(1995)
J Biol Chem
, vol.270
, pp. 29413-29421
-
-
Zhao, X.1
Siu, C.H.2
-
36
-
-
0029124955
-
Several extracellular domains of the neural cell adhesion molecule L1 are involved in homophilic interactions
-
of special interest. Protein fragments of mouse L1 composed of Ig domains 1 to 2 generated in prokaryotic cells were found to bind to each other, suggesting that they are important for the homophilic binding activity of L1.
-
of special interest Holm J, Appel F, Schachner M. Several extracellular domains of the neural cell adhesion molecule L1 are involved in homophilic interactions. J Neurosci Res. 42:1995;9-20 Protein fragments of mouse L1 composed of Ig domains 1 to 2 generated in prokaryotic cells were found to bind to each other, suggesting that they are important for the homophilic binding activity of L1.
-
(1995)
J Neurosci Res
, vol.42
, pp. 9-20
-
-
Holm, J.1
Appel, F.2
Schachner, M.3
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37
-
-
0029923451
-
Differential effects of two hydro-cephalus/MASA syndrome-related mutations on the homophilic binding and neuritogenic activites of the cell adhesion molecule L1
-
of special interest. Two mutations within the second Ig-like domain of human L1 that might be responsible for X-linked hydrocephalus and MASA were found to affect the homophilic binding activity of the second Ig-like domain.
-
of special interest Zhao X, Siu CH. Differential effects of two hydro-cephalus/MASA syndrome-related mutations on the homophilic binding and neuritogenic activites of the cell adhesion molecule L1. J Biol Chem. 271:1996;6563-6566 Two mutations within the second Ig-like domain of human L1 that might be responsible for X-linked hydrocephalus and MASA were found to affect the homophilic binding activity of the second Ig-like domain.
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(1996)
J Biol Chem
, vol.271
, pp. 6563-6566
-
-
Zhao, X.1
Siu, C.H.2
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38
-
-
0028786572
-
Identification of the border between fibronectin type III homologous repeats 2 and 3 of the neural cell adhesion molecule L1 as a neurite outgrowth promoting and signal transducing domain
-
of special interest. Characterization of a peptide region within mouse L1 using a mAb important for neurite extension of cerebellar cells.
-
of special interest Appel F, Holm J, Conscience JF, Von Bohlen, Halbach F, Faissner A, James P, Schachner M. Identification of the border between fibronectin type III homologous repeats 2 and 3 of the neural cell adhesion molecule L1 as a neurite outgrowth promoting and signal transducing domain. J Neurobiol. 28:1995;297-312 Characterization of a peptide region within mouse L1 using a mAb important for neurite extension of cerebellar cells.
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(1995)
J Neurobiol
, vol.28
, pp. 297-312
-
-
Appel, F.1
Holm, J.2
Conscience, J.F.3
Von Bohlen4
Halbach, F.5
Faissner, A.6
James, P.7
Schachner, M.8
-
39
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-
0028236467
-
The homophilic binding site of the neural cell adhesion molecule NCAM is directly involved in promoting neurite outgrowth from cultured neural retinal cells
-
Sandig M, Rao Y, Siu CH. The homophilic binding site of the neural cell adhesion molecule NCAM is directly involved in promoting neurite outgrowth from cultured neural retinal cells. J Biol Chem. 269:1994;14841-14848.
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(1994)
J Biol Chem
, vol.269
, pp. 14841-14848
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Sandig, M.1
Rao, Y.2
Siu, C.H.3
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40
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0027185021
-
Structural characterization of a homophilic binding site in the neural cell adhesion molecule
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Rao Y, Wu XF, Yip P, Gariepy J, Siu CH. Structural characterization of a homophilic binding site in the neural cell adhesion molecule. J Biol Chem. 268:1993;20630-20638.
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(1993)
J Biol Chem
, vol.268
, pp. 20630-20638
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Rao, Y.1
Wu, X.F.2
Yip, P.3
Gariepy, J.4
Siu, C.H.5
-
41
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0027184253
-
Homophilic adhesion between Ig superfamily carcinoembryonic antigen molecules involves double reciprocal bonds
-
Zhou H, Fuks A, Alcaraz G, Bolling TJ, Stanners CP. Homophilic adhesion between Ig superfamily carcinoembryonic antigen molecules involves double reciprocal bonds. J Cell Biol. 122:1993;951-960.
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(1993)
J Cell Biol
, vol.122
, pp. 951-960
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Zhou, H.1
Fuks, A.2
Alcaraz, G.3
Bolling, T.J.4
Stanners, C.P.5
-
42
-
-
0027243414
-
The fourth immunoglobulin-like domain of NCAM contains a carbohydrate recognition domain for oligomannosidic glycans implicated in association with L1 and neurite outgrowth
-
Horstkorte R, Schachner M, Magyar JP, Vorherr T, Schmitz B. The fourth immunoglobulin-like domain of NCAM contains a carbohydrate recognition domain for oligomannosidic glycans implicated in association with L1 and neurite outgrowth. J Cell Biol. 121:1993;1409-1421.
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(1993)
J Cell Biol
, vol.121
, pp. 1409-1421
-
-
Horstkorte, R.1
Schachner, M.2
Magyar, J.P.3
Vorherr, T.4
Schmitz, B.5
-
43
-
-
0029914878
-
The role of polysialic acid in migration of olfactory bulb interneuron precursors in the subventricular zone
-
of outstanding interest. Transplantation and in vitro studies indicate that PSA on NCAM is important in the regulation of cell - cell interactions during tangential migration of olfactory bulb interneuron precursors. Radial migration of cell within the olfactory bulb do not require PSA.
-
of outstanding interest Hu HY, Tomasiewicz H, Magnuson T, Rutishauser U. The role of polysialic acid in migration of olfactory bulb interneuron precursors in the subventricular zone. Neuron. 16:1996;735-743 Transplantation and in vitro studies indicate that PSA on NCAM is important in the regulation of cell - cell interactions during tangential migration of olfactory bulb interneuron precursors. Radial migration of cell within the olfactory bulb do not require PSA.
-
(1996)
Neuron
, vol.16
, pp. 735-743
-
-
Hu, H.Y.1
Tomasiewicz, H.2
Magnuson, T.3
Rutishauser, U.4
-
44
-
-
0028927456
-
Molecular characterization of eukaryotic polysialyltransferase-1
-
of outstanding interest. CHO cells are capable of producing polysialylated NCAM (PSA - NCAM). In this study, a PSA-negative mutant line of CHO cells, isolated by negative selection panning using a PSA-specific mAb, was used for expression cloning.The PSA-negative line was transfected with a cDNA plasmid library from wild-type CHO cells, and PSA-positive cells were enriched by panning on a PSA-specific mAb. A plasmid encoding PSA transferase could be isolated using a modification of the Seed and Aruffo procedure [69]. See also annotation [45].
-
of outstanding interest Eckhardt M, Muhlenhoff M, Bethe A, Koopman J, Frosch M, Gerardy-Schahn R. Molecular characterization of eukaryotic polysialyltransferase-1. Nature. 373:1995;715-718 CHO cells are capable of producing polysialylated NCAM (PSA - NCAM). In this study, a PSA-negative mutant line of CHO cells, isolated by negative selection panning using a PSA-specific mAb, was used for expression cloning.The PSA-negative line was transfected with a cDNA plasmid library from wild-type CHO cells, and PSA-positive cells were enriched by panning on a PSA-specific mAb. A plasmid encoding PSA transferase could be isolated using a modification of the Seed and Aruffo procedure [69]. See also annotation [45].
-
(1995)
Nature
, vol.373
, pp. 715-718
-
-
Eckhardt, M.1
Muhlenhoff, M.2
Bethe, A.3
Koopman, J.4
Frosch, M.5
Gerardy-Schahn, R.6
-
45
-
-
0029119976
-
Expression cloning of a human polysialyltransferase that forms the polysialylated neural cell adhesion molecule present in embryonic brain
-
of outstanding interest. In this study, COS cells, which do not normally synthesize PSA or NCAM, were co-transfected with a NCAM expression plasmid and with a human fetal brain plasmid cDNA expression library. PSA-positive COS cells were then enriched by fluorescence-activated cell sorting using a PSA-specific mAb, and clones encoding PSA transferase could be isolated using a modification of the Seed and Aruffo procedure [69]. See also annotation [44].
-
of outstanding interest Nakayama J, Fukuda MN, Fredette B, Ranscht B, Fukuda M. Expression cloning of a human polysialyltransferase that forms the polysialylated neural cell adhesion molecule present in embryonic brain. Proc Natl Acad Sci USA. 92:1995;7031-7035 In this study, COS cells, which do not normally synthesize PSA or NCAM, were co-transfected with a NCAM expression plasmid and with a human fetal brain plasmid cDNA expression library. PSA-positive COS cells were then enriched by fluorescence-activated cell sorting using a PSA-specific mAb, and clones encoding PSA transferase could be isolated using a modification of the Seed and Aruffo procedure [69]. See also annotation [44].
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 7031-7035
-
-
Nakayama, J.1
Fukuda, M.N.2
Fredette, B.3
Ranscht, B.4
Fukuda, M.5
-
46
-
-
0029081145
-
A human stx cDNA confers polysialic acid expression in mammalian cells
-
of outstanding interest. Reports the cloning of a second human polysialyltransferase with 59% sequence identity with PSA transferase [45].
-
of outstanding interest Scheidegger EP, Sternberg LR, Roth J, Lowe JB. A human stx cDNA confers polysialic acid expression in mammalian cells. J Biol Chem. 270:1995;22685-22688 Reports the cloning of a second human polysialyltransferase with 59% sequence identity with PSA transferase [45].
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(1995)
J Biol Chem
, vol.270
, pp. 22685-22688
-
-
Scheidegger, E.P.1
Sternberg, L.R.2
Roth, J.3
Lowe, J.B.4
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47
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-
0029125212
-
Protein determinants for specific polysialylation of the neural cell adhesion molecule
-
of special interest. In this study, rodent cells that synthesize polysialylated NCAM were transfected with modified plasmid constructs encoding variants of chicken NCAM. The latter could be distinguished from endogenous rodent NCAM by a chicken-specific antibody. Transfection of deletion mutants showed that the minimal PSA acceptor structure contains Ig-like domains 4 and 5, as well as the first FNIII-like domain. Point mutations of the amino-terminal-linked carbohydrate-acceptor sites within the fifth Ig-like domain demonstrated that PSA is mainly attached to Asn459 and Asn430, where Asn404 receives little or no PSA.
-
of special interest Nelson RW, Bates PA, Rutishauser U. Protein determinants for specific polysialylation of the neural cell adhesion molecule. J Biol Chem. 270:1995;17171-17179 In this study, rodent cells that synthesize polysialylated NCAM were transfected with modified plasmid constructs encoding variants of chicken NCAM. The latter could be distinguished from endogenous rodent NCAM by a chicken-specific antibody. Transfection of deletion mutants showed that the minimal PSA acceptor structure contains Ig-like domains 4 and 5, as well as the first FNIII-like domain. Point mutations of the amino-terminal-linked carbohydrate-acceptor sites within the fifth Ig-like domain demonstrated that PSA is mainly attached to Asn459 and Asn430, where Asn404 receives little or no PSA.
-
(1995)
J Biol Chem
, vol.270
, pp. 17171-17179
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Nelson, R.W.1
Bates, P.A.2
Rutishauser, U.3
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48
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0029125639
-
Protein tyrosine phosphatases as adhesion receptors
-
of outstanding interest. A detailed review on recent advances on RPTPs with Ig/FNIII-like domains in their extracellular regions.
-
of outstanding interest Brady-Kalnay SM, Tonks NK. Protein tyrosine phosphatases as adhesion receptors. Curr Opin Cell Biol. 7:1995;650-657 A detailed review on recent advances on RPTPs with Ig/FNIII-like domains in their extracellular regions.
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(1995)
Curr Opin Cell Biol
, vol.7
, pp. 650-657
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-
Brady-Kalnay, S.M.1
Tonks, N.K.2
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49
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0029005270
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Homophilic interactions mediated by receptor tyrosine phosphatases μ and κ. A critical role for the novel extracellular MAM domain
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Zondag GC, Koningstein GM, Jiang YP, Sap J, Moolenaar WH, Gebbink MF. Homophilic interactions mediated by receptor tyrosine phosphatases μ and κ. A critical role for the novel extracellular MAM domain. J Biol Chem. 270:1995;14247-14250.
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(1995)
J Biol Chem
, vol.270
, pp. 14247-14250
-
-
Zondag, G.C.1
Koningstein, G.M.2
Jiang, Y.P.3
Sap, J.4
Moolenaar, W.H.5
Gebbink, M.F.6
-
50
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-
0029149746
-
Receptor protein tyrosine phosphatase PTPμ associates with cadherins and catenins in vivo
-
of outstanding interest
-
of outstanding interest Brady-Kalnay SM, Rimm DL, Tonks NK. Receptor protein tyrosine phosphatase PTPμ associates with cadherins and catenins in vivo. J Cell Biol. 130:1995;977-986.
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(1995)
J Cell Biol
, vol.130
, pp. 977-986
-
-
Brady-Kalnay, S.M.1
Rimm, D.L.2
Tonks, N.K.3
-
51
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0030030320
-
The transmembrane tyrosine phosphatase DLAR control motor axon guidance in Drosophila
-
of outstanding interest. DLAR, a Drosophila RPTP, is implicated in the navigation of specific motor axons. Like DPTP69D, DLAR is expressed on axons and contains multiple Ig/FNIII-like domains. See also annotation [52].
-
of outstanding interest Krueger NX, Vanvactor D, Wan HI, Gelbart WM, Goodman CS, Saito H. The transmembrane tyrosine phosphatase DLAR control motor axon guidance in Drosophila. Cell. 84:1996;611-622 DLAR, a Drosophila RPTP, is implicated in the navigation of specific motor axons. Like DPTP69D, DLAR is expressed on axons and contains multiple Ig/FNIII-like domains. See also annotation [52].
-
(1996)
Cell
, vol.84
, pp. 611-622
-
-
Krueger, N.X.1
Vanvactor, D.2
Wan, H.I.3
Gelbart, W.M.4
Goodman, C.S.5
Saito, H.6
-
52
-
-
0030026858
-
Receptor tyrosine phosphatases are required for motor axon guidance in the Drosophila embryo
-
of outstanding interest. The receptor tyrosine phosphatase DPTP69D, which contains Ig/FNIII-like domains, is expressed on Drosophila CNS axons and is essential for guidance of specific motor axons. See also annotation [51].
-
of outstanding interest Desai CJ, Gindhart JG Jr, Goldstein LS, Zinn K. Receptor tyrosine phosphatases are required for motor axon guidance in the Drosophila embryo. Cell. 84:1996;599-609 The receptor tyrosine phosphatase DPTP69D, which contains Ig/FNIII-like domains, is expressed on Drosophila CNS axons and is essential for guidance of specific motor axons. See also annotation [51].
-
(1996)
Cell
, vol.84
, pp. 599-609
-
-
Desai, C.J.1
Gindhart J.G., Jr.2
Goldstein, L.S.3
Zinn, K.4
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53
-
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0028029162
-
Activation of the FGF receptor underlies neurite outgrowth stimulated by L1, N-CAM, and N-cadherin
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Williams EJ, Furness J, Walsh FS, Doherty P. Activation of the FGF receptor underlies neurite outgrowth stimulated by L1, N-CAM, and N-cadherin. Neuron. 13:1994;583-594.
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(1994)
Neuron
, vol.13
, pp. 583-594
-
-
Williams, E.J.1
Furness, J.2
Walsh, F.S.3
Doherty, P.4
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54
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0028817332
-
A soluble chimeric form of the L1 glycoprotein stimulates neurite outgrowth
-
of outstanding interest. Shows that soluble recombinant L1 induces neurite outgrowth as effectively as L1 expressed on the surface of transfected cells. Outgrowth induction most likely occurs via homophilic binding to neuronal L1 and involves the direct or indirect activation of neuronal FGF receptor(s).
-
of outstanding interest Doherty P, Williams E, Walsh FS. A soluble chimeric form of the L1 glycoprotein stimulates neurite outgrowth. Neuron. 14:1995;57-66 Shows that soluble recombinant L1 induces neurite outgrowth as effectively as L1 expressed on the surface of transfected cells. Outgrowth induction most likely occurs via homophilic binding to neuronal L1 and involves the direct or indirect activation of neuronal FGF receptor(s).
-
(1995)
Neuron
, vol.14
, pp. 57-66
-
-
Doherty, P.1
Williams, E.2
Walsh, F.S.3
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55
-
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0028805468
-
The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum
-
of special interest. This study provides evidence that F3/F11 is associated with the src-family tyrosine kinase fyn in Triton X-100-insoluble membrane microdomains.
-
of special interest Olive S, Dubois C, Schachner M, Rougon G. The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum. J Neurochem. 65:1995;2307-2317 This study provides evidence that F3/F11 is associated with the src-family tyrosine kinase fyn in Triton X-100-insoluble membrane microdomains.
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(1995)
J Neurochem
, vol.65
, pp. 2307-2317
-
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Olive, S.1
Dubois, C.2
Schachner, M.3
Rougon, G.4
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56
-
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0029165973
-
The glypiated neuronal cell adhesion molecule contactin/F11 complexes with src-family protein tyrosine kinase fyn
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Zisch AH, D'Alessandri L, Amrein K, Ranscht B, Winterhalter KH, Vaughan L. The glypiated neuronal cell adhesion molecule contactin/F11 complexes with src-family protein tyrosine kinase fyn. Mol Cell Neurosci. 6:1995;263-279.
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(1995)
Mol Cell Neurosci
, vol.6
, pp. 263-279
-
-
Zisch, A.H.1
D'Alessandri, L.2
Amrein, K.3
Ranscht, B.4
Winterhalter, K.H.5
Vaughan, L.6
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57
-
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0027971705
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NCAM-dependent neurite outgrowth is inhibited in neurons from Fyn-minus mice
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Beggs HE, Soriano P, Maness PF. NCAM-dependent neurite outgrowth is inhibited in neurons from Fyn-minus mice. J Cell Biol. 127:1994;825-833.
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(1994)
J Cell Biol
, vol.127
, pp. 825-833
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-
Beggs, H.E.1
Soriano, P.2
Maness, P.F.3
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58
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0028878702
-
The receptor tyrosine kinase ARK mediates cell aggregation by homophilic binding
-
of special interest. ARK, a recpetor tyrosine kinase with Ig/FNIII-like domains in its extracellular region, is highly expressed in the brain and mediates homotypic binding of transfected cells. Binding of ligand to ARK results in receptor autophosphorylation.
-
of special interest Bellosta P, Costa M, Lin DA, Basilico C. The receptor tyrosine kinase ARK mediates cell aggregation by homophilic binding. Mol Cell Biol. 15:1995;614-625 ARK, a recpetor tyrosine kinase with Ig/FNIII-like domains in its extracellular region, is highly expressed in the brain and mediates homotypic binding of transfected cells. Binding of ligand to ARK results in receptor autophosphorylation.
-
(1995)
Mol Cell Biol
, vol.15
, pp. 614-625
-
-
Bellosta, P.1
Costa, M.2
Lin, D.A.3
Basilico, C.4
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59
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0028841097
-
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
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-
Wong, E.V.1
Cheng, G.H.2
Payne, H.R.3
Lemmon, V.4
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60
-
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0029161504
-
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.
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(1995)
J Biol Chem
, vol.270
, pp. 18809-18817
-
-
Hortsch, M.1
Wang, Y.M.2
Marikar, Y.3
Bieber, A.J.4
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61
-
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0029567019
-
anion exchanger
-
of outstanding interest. Different combinations of ank repeats of ankyrin were found to form two distinct high affinity binding sites for neurofascin. Furthermore, the results obtained suggested that ankyrin may simultaneously associate with multiple types of membrane proteins that may be important for the assembly of membrane proteins into specialized regions.
-
anion exchanger. J Biol Chem. 270:1995;31298-31302 Different combinations of ank repeats of ankyrin were found to form two distinct high affinity binding sites for neurofascin. Furthermore, the results obtained suggested that ankyrin may simultaneously associate with multiple types of membrane proteins that may be important for the assembly of membrane proteins into specialized regions.
-
(1995)
J Biol Chem
, vol.270
, pp. 31298-31302
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-
Michaely, P.1
Bennett, V.2
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62
-
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0029899939
-
Neuroglian-mediated cell adhesion induces assembly of the membrane skeleton at cell contact sites
-
of outstanding interest. Accumulation of ankyrin at cell - cell contact sites was induced by expression of neuroglian Drosophila S2 tissue culture cells. A direct interaction between ankyrin and the cytoplasmic segment of neuroglian was shown by the yeast two-hybrid system.
-
of outstanding interest 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 Accumulation of ankyrin at cell - cell contact sites was induced by expression of neuroglian Drosophila S2 tissue culture cells. A direct interaction between ankyrin and the cytoplasmic segment of neuroglian was shown by the yeast two-hybrid system.
-
(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
-
63
-
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0029074731
-
An ankyrin-related gene (unc-44) is necessary for proper axonal guidance in Caenorhabditis elegans
-
of outstanding interest. Mutations in the unc-44 gene, which encodes ankyrin-related proteins, result in aberrant axon guidance and fasciculation in C. elegans. Ankyrin, which links transmembrane proteins to the spectrin-based membrane skeleton, has been shown by other investigations to interact with the cytoplasmic segments of the L1-related proteins. See also annotations [61,62].
-
of outstanding interest Otsuka AJ, Franco R, Yang B, Shim KH, Tang LZ, Zhang YY, Boontrakulpoontawee P, Jeyaprakash A, Hedgecock E, Wheaton VI. An ankyrin-related gene (unc-44) is necessary for proper axonal guidance in Caenorhabditis elegans. J Cell Biol. 129:1995;1081-1092 Mutations in the unc-44 gene, which encodes ankyrin-related proteins, result in aberrant axon guidance and fasciculation in C. elegans. Ankyrin, which links transmembrane proteins to the spectrin-based membrane skeleton, has been shown by other investigations to interact with the cytoplasmic segments of the L1-related proteins. See also annotations [61,62].
-
(1995)
J Cell Biol
, vol.129
, pp. 1081-1092
-
-
Otsuka, A.J.1
Franco, R.2
Yang, B.3
Shim, K.H.4
Tang, L.Z.5
Zhang, Y.Y.6
Boontrakulpoontawee, P.7
Jeyaprakash, A.8
Hedgecock, E.9
Wheaton, V.I.10
-
64
-
-
0028058827
-
The cytoplasmic domain of the myelin Po protein influences the adhesive interactions of its extracellular domain
-
of special interest
-
of special interest Wong MH, Filbin MT. The cytoplasmic domain of the myelin Po protein influences the adhesive interactions of its extracellular domain. J Cell Biol. 126:1994;1089-1097.
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(1994)
J Cell Biol
, vol.126
, pp. 1089-1097
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Wong, M.H.1
Filbin, M.T.2
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65
-
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0029089750
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Identification of residues in the V domain of CD80 (B7-1) implicated in functional interactions with CD28 and CTLA4
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Fargeas CA, Truneh A, Reddy M, Hurle M, Sweet R, Sekaly RP. Identification of residues in the V domain of CD80 (B7-1) implicated in functional interactions with CD28 and CTLA4. J Exp Med. 182:1995;667-675.
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(1995)
J Exp Med
, vol.182
, pp. 667-675
-
-
Fargeas, C.A.1
Truneh, A.2
Reddy, M.3
Hurle, M.4
Sweet, R.5
Sekaly, R.P.6
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66
-
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0028925551
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Mutational analysis and an alternatively spliced product of B7 defines its CD28/CTLA4-binding site on immunoglobulin C-like domain
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Guo Y, Wu Y, Zhao M, Kong XP, Liu Y. Mutational analysis and an alternatively spliced product of B7 defines its CD28/CTLA4-binding site on immunoglobulin C-like domain. J Exp Med. 181:1995;1345-1355.
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(1995)
J Exp Med
, vol.181
, pp. 1345-1355
-
-
Guo, Y.1
Wu, Y.2
Zhao, M.3
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CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the α-6/β-1 integrin and the neural adhesion molecule L1
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Evidence for cis interaction and cooperative signalling by the heat-stable antigen nectadrin (murine cd24) and the cell adhesion molecule L1 in neurons
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Yang LJ, Zeller CB, Shaper NL, Kiso M, Hasegawa A, Shapiro RE, Schnaar RL. Gangliosides are neuronal ligands for myelin-associated glycoprotein. Proc Natl Acad Sci USA. 93:1996;814-818.
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Restricted expression of the irrect-rst protein is required for normal axonal projections of columnar visual neurons
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of outstanding interest. The irreC-rst molecule functions as a homophilic cell adhesion molecule in transfected Drosophila Schneider cells. In mutants (loss of function and global overexpression), severe defects of axonal projections have been observed.
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of outstanding interest Schneider T, Reiter C, Eule E, Bader B, Lichte B, Nie Z, Schimansky T, Ramos RG, Fischback K. Restricted expression of the irrect-rst protein is required for normal axonal projections of columnar visual neurons. Neuron. 15:1995;259-271 The irreC-rst molecule functions as a homophilic cell adhesion molecule in transfected Drosophila Schneider cells. In mutants (loss of function and global overexpression), severe defects of axonal projections have been observed.
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Schneider, T.1
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Schimansky, T.7
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Fischback, K.9
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76
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77
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Functional topography of myelin-associated glycoprotein. II. Mapping of domains on molecular fragments
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Meyer-Franke A, Tropak MB, Roder JC, Fischer P, Beyreuther K, Probstmeier R, Schachner M. Functional topography of myelin-associated glycoprotein. II. Mapping of domains on molecular fragments. J Neurosci Res. 41:1995;311-323.
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Meyer-Franke, A.1
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78
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0029896991
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TAG-1/axonin-1 is a high-affinity ligand of neurocan phosphacan/protein-tyrosine phosphatase-zeta/beta, and N-CAM
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of special interest. The affinity of the binding of TAG-1/axonin-1 to distinct ligands has been measured using solid phase binding assays and radiolabeled purified proteins. It could be demonstrated that this molecule binds to the proteoglycans neurocan and phosphocan, as well as to TN-C and NCAM.
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of special interest Milev P, Maurel P, Haring M, Margolis RK, Margolis RU. TAG-1/axonin-1 is a high-affinity ligand of neurocan phosphacan/protein-tyrosine phosphatase-zeta/beta, and N-CAM. J Biol Chem. 271:1996;15716-15723 The affinity of the binding of TAG-1/axonin-1 to distinct ligands has been measured using solid phase binding assays and radiolabeled purified proteins. It could be demonstrated that this molecule binds to the proteoglycans neurocan and phosphocan, as well as to TN-C and NCAM.
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J Biol Chem
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Milev, P.1
Maurel, P.2
Haring, M.3
Margolis, R.K.4
Margolis, R.U.5
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79
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0029867737
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Homophilic adhesion mediated by the neural cell adhesion molecule involves multiple immunoglobulin domains
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of special interest. A detailed molecular analysis of the homophilic NCAM interaction using soluble recombinant single Ig-like domains expressed in E. coli. The third Ig-like domain was found to be more important for this interaction; however, binding involves all five Ig-like domains of NCAM and probably occurs in an antiparallel orientation.
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of special interest Ranheim TS, Edelman GM, Cunningham BA. Homophilic adhesion mediated by the neural cell adhesion molecule involves multiple immunoglobulin domains. Proc Natl Acad Sci USA. 93:1996;4071-4075 A detailed molecular analysis of the homophilic NCAM interaction using soluble recombinant single Ig-like domains expressed in E. coli. The third Ig-like domain was found to be more important for this interaction; however, binding involves all five Ig-like domains of NCAM and probably occurs in an antiparallel orientation.
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(1996)
Proc Natl Acad Sci USA
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Ranheim, T.S.1
Edelman, G.M.2
Cunningham, B.A.3
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80
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0029852196
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Neurofascin induces neurites by heterophilic interactions with axonal NrCAM while NrCAM requires F1 on the axonal surface to extend neurites
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of special interest. A molecular interaction of neurofascin with NrCAM could be demonstrated and the NrCAM-binding site of neurofascin could be mapped to its Ig-like region. This interaction, which can be modulated by alternative splicing of neurofascin, was shown to be involved in the neurofascin-mediated outgrowth response of tectal neurons.
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of special interest Volkmer H, Leuscher R, Zacharias U, Rathjen FG. Neurofascin induces neurites by heterophilic interactions with axonal NrCAM while NrCAM requires F1 on the axonal surface to extend neurites. J Cell Biol. 135:1996; A molecular interaction of neurofascin with NrCAM could be demonstrated and the NrCAM-binding site of neurofascin could be mapped to its Ig-like region. This interaction, which can be modulated by alternative splicing of neurofascin, was shown to be involved in the neurofascin-mediated outgrowth response of tectal neurons.
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(1996)
J Cell Biol
, vol.135
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Volkmer, H.1
Leuscher, R.2
Zacharias, U.3
Rathjen, F.G.4
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