메뉴 건너뛰기




Volumn 3, Issue 1, 2008, Pages

A synaptic nidogen: Developmental regulation and role of nidogen-2 at the neuromuscular junction

Author keywords

[No Author keywords available]

Indexed keywords

ENTACTIN; MEMBRANE PROTEIN; NID2 PROTEIN, MOUSE; UNCLASSIFIED DRUG;

EID: 53949096504     PISSN: None     EISSN: 17498104     Source Type: Journal    
DOI: 10.1186/1749-8104-3-24     Document Type: Article
Times cited : (46)

References (82)
  • 1
    • 33646554798 scopus 로고    scopus 로고
    • Seeking long-term relationship: Axon and target communicate to organize synaptic differentiation
    • 10.1111/j.1471-4159.2006.03834.x. 16638017
    • Seeking long-term relationship: axon and target communicate to organize synaptic differentiation. MA Fox H Umemori, J Neurochem 2006 97 1215 1231 10.1111/j.1471-4159.2006.03834.x 16638017
    • (2006) J Neurochem , vol.97 , pp. 1215-1231
    • Fox, M.A.1    Umemori, H.2
  • 2
    • 30344456451 scopus 로고    scopus 로고
    • How to build a central synapse: Clues from cell culture
    • 10.1016/j.tins.2005.11.002. 16337695
    • How to build a central synapse: clues from cell culture. AM Craig ER Graf MW Linhoff, Trends Neurosci 2006 29 8 20 10.1016/j.tins.2005.11.002 16337695
    • (2006) Trends Neurosci , vol.29 , pp. 8-20
    • Craig, A.M.1    Graf, E.R.2    Linhoff, M.W.3
  • 3
    • 0038071095 scopus 로고    scopus 로고
    • Cell-cell signaling during synapse formation in the CNS
    • 10.1146/annurev.neuro.26.043002.094940. 12626697
    • Cell-cell signaling during synapse formation in the CNS. P Scheiffele, Annu Rev Neurosci 2003 26 485 508 10.1146/annurev.neuro.26.043002.094940 12626697
    • (2003) Annu Rev Neurosci , vol.26 , pp. 485-508
    • Scheiffele, P.1
  • 4
    • 0037832412 scopus 로고    scopus 로고
    • The basement membrane/basal lamina of skeletal muscle
    • 10.1074/jbc.R200027200. 12556454
    • The basement membrane/basal lamina of skeletal muscle. JR Sanes, J Biol Chem 2003 278 12601 12604 10.1074/jbc.R200027200 12556454
    • (2003) J Biol Chem , vol.278 , pp. 12601-12604
    • Sanes, J.R.1
  • 5
    • 3042534412 scopus 로고    scopus 로고
    • Basal lamina and the organization of neuromuscular synapses
    • 10.1023/B:NEUR.0000020630.74955.19. 15034274
    • Basal lamina and the organization of neuromuscular synapses. BL Patton, J Neurocytol 2003 32 883 903 10.1023/B:NEUR.0000020630.74955.19 15034274
    • (2003) J Neurocytol , vol.32 , pp. 883-903
    • Patton, B.L.1
  • 6
    • 0033808066 scopus 로고    scopus 로고
    • Still more complexity in mammalian basement membranes
    • 10990484
    • Still more complexity in mammalian basement membranes. AC Erickson JR Couchman, J Histochem Cytochem 2000 48 1291 1306 10990484
    • (2000) J Histochem Cytochem , vol.48 , pp. 1291-1306
    • Erickson, A.C.1    Couchman, J.R.2
  • 7
    • 0024535958 scopus 로고
    • A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction
    • 10.1038/338229a0. 2922051
    • A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. DD Hunter V Shah JP Merlie JR Sanes, Nature 1989 338 229 234 10.1038/338229a0 2922051
    • (1989) Nature , vol.338 , pp. 229-234
    • Hunter, D.D.1    Shah, V.2    Merlie, J.P.3    Sanes, J.R.4
  • 8
    • 0025010542 scopus 로고
    • Molecular heterogeneity of basal laminae: Isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere
    • 2211832. 10.1083/jcb.111.4.1685
    • Molecular heterogeneity of basal laminae: isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere. JR Sanes E Engvall R Butkowski DD Hunter, J Cell Biol 1990 111 1685 1699 2211832 10.1083/jcb.111.4. 1685
    • (1990) J Cell Biol , vol.111 , pp. 1685-1699
    • Sanes, J.R.1    Engvall, E.2    Butkowski, R.3    Hunter, D.D.4
  • 9
    • 0031456144 scopus 로고    scopus 로고
    • Distribution and function of laminins in the neuromuscular system of developing, adult, and mutant mice
    • 9396756. 10.1083/jcb.139.6.1507
    • Distribution and function of laminins in the neuromuscular system of developing, adult, and mutant mice. BL Patton JH Miner AY Chiu JR Sanes, J Cell Biol 1997 139 1507 1521 9396756 10.1083/jcb.139.6.1507
    • (1997) J Cell Biol , vol.139 , pp. 1507-1521
    • Patton, B.L.1    Miner, J.H.2    Chiu, A.Y.3    Sanes, J.R.4
  • 11
    • 0028171098 scopus 로고
    • Collagen IV alpha 3, alpha 4, and alpha 5 chains in rodent basal laminae: Sequence, distribution, association with laminins, and developmental switches
    • 7962065. 10.1083/jcb.127.3.879
    • Collagen IV alpha 3, alpha 4, and alpha 5 chains in rodent basal laminae: sequence, distribution, association with laminins, and developmental switches. JH Miner JR Sanes, J Cell Biol 1994 127 879 891 7962065 10.1083/jcb.127.3.879
    • (1994) J Cell Biol , vol.127 , pp. 879-891
    • Miner, J.H.1    Sanes, J.R.2
  • 13
    • 0022653671 scopus 로고
    • Basal lamina-associated heparan sulphate proteoglycan in the rat PNS: Characterization and localization using monoclonal antibodies
    • 10.1007/BF02057903. 2940343
    • Basal lamina-associated heparan sulphate proteoglycan in the rat PNS: characterization and localization using monoclonal antibodies. CF Eldridge JR Sanes AY Chiu RP Bunge CJ Cornbrooks, J Neurocytol 1986 15 37 51 10.1007/BF02057903 2940343
    • (1986) J Neurocytol , vol.15 , pp. 37-51
    • Eldridge, C.F.1    Sanes, J.R.2    Chiu, A.Y.3    Bunge, R.P.4    Cornbrooks, C.J.5
  • 14
    • 0022254103 scopus 로고
    • Acetylcholine receptor-aggregating factor is similar to molecules concentrated at neuromuscular junctions
    • 10.1038/315571a0. 3892302
    • Acetylcholine receptor-aggregating factor is similar to molecules concentrated at neuromuscular junctions. JR Fallon RM Nitkin NE Reist BG Wallace UJ McMahan, Nature 1985 315 571 574 10.1038/315571a0 3892302
    • (1985) Nature , vol.315 , pp. 571-574
    • Fallon, J.R.1    Nitkin, R.M.2    Reist, N.E.3    Wallace, B.G.4    McMahan, U.J.5
  • 15
    • 0024522577 scopus 로고
    • Agrin-related molecules are concentrated at acetylcholine receptor clusters in normal and aneural developing muscle
    • 2538482. 10.1083/jcb.108.4.1527
    • Agrin-related molecules are concentrated at acetylcholine receptor clusters in normal and aneural developing muscle. JR Fallon CE Gelfman, J Cell Biol 1989 108 1527 1535 2538482 10.1083/jcb.108.4.1527
    • (1989) J Cell Biol , vol.108 , pp. 1527-1535
    • Fallon, J.R.1    Gelfman, C.E.2
  • 16
    • 0028908326 scopus 로고
    • Aberrant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin beta 2
    • 10.1038/374258a0. 7885444
    • Aberrant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin beta 2. PG Noakes M Gautam J Mudd JR Sanes JP Merlie, Nature 1995 374 258 262 10.1038/374258a0 7885444
    • (1995) Nature , vol.374 , pp. 258-262
    • Noakes, P.G.1    Gautam, M.2    Mudd, J.3    Sanes, J.R.4    Merlie, J.P.5
  • 17
    • 10344221035 scopus 로고    scopus 로고
    • A synaptic laminin-calcium channel interaction organizes active zones in motor nerve terminals
    • 10.1038/nature03112. 15577901
    • A synaptic laminin-calcium channel interaction organizes active zones in motor nerve terminals. H Nishimune JR Sanes SS Carlson, Nature 2004 432 580 587 10.1038/nature03112 15577901
    • (2004) Nature , vol.432 , pp. 580-587
    • Nishimune, H.1    Sanes, J.R.2    Carlson, S.S.3
  • 20
    • 0023461553 scopus 로고
    • Identification of agrin, a synaptic organizing protein from Torpedo electric organ
    • 2826489. 10.1083/jcb.105.6.2471
    • Identification of agrin, a synaptic organizing protein from Torpedo electric organ. RM Nitkin MA Smith C Magill JR Fallon YM Yao BG Wallace UJ McMahan, J Cell Biol 1987 105 2471 2478 2826489 10.1083/jcb.105.6.2471
    • (1987) J Cell Biol , vol.105 , pp. 2471-2478
    • Nitkin, R.M.1    Smith, M.A.2    Magill, C.3    Fallon, J.R.4    Yao, Y.M.5    Wallace, B.G.6    McMahan, U.J.7
  • 21
    • 0029893117 scopus 로고    scopus 로고
    • Defective neuromuscular synaptogenesis in agrin-deficient mutant mice
    • 10.1016/S0092-8674(00)81253-2. 8653788
    • Defective neuromuscular synaptogenesis in agrin-deficient mutant mice. M Gautam PG Noakes L Moscoso F Rupp RH Scheller JP Merlie JR Sanes, Cell 1996 85 525 535 10.1016/S0092-8674(00)81253-2 8653788
    • (1996) Cell , vol.85 , pp. 525-535
    • Gautam, M.1    Noakes, P.G.2    Moscoso, L.3    Rupp, F.4    Scheller, R.H.5    Merlie, J.P.6    Sanes, J.R.7
  • 22
    • 0035953645 scopus 로고    scopus 로고
    • Distinct roles of nerve and muscle in postsynaptic differentiation of the neuromuscular synapse
    • 10.1038/35074025. 11323662
    • Distinct roles of nerve and muscle in postsynaptic differentiation of the neuromuscular synapse. W Lin RW Burgess B Dominguez SL Pfaff JR Sanes KF Lee, Nature 2001 410 1057 1064 10.1038/35074025 11323662
    • (2001) Nature , vol.410 , pp. 1057-1064
    • Lin, W.1    Burgess, R.W.2    Dominguez, B.3    Pfaff, S.L.4    Sanes, J.R.5    Lee, K.F.6
  • 23
    • 20444362083 scopus 로고    scopus 로고
    • Neurotransmitter acetylcholine negatively regulates neuromuscular synapse formation by a Cdk5-dependent mechanism
    • 10.1016/j.neuron.2005.04.002. 15944126
    • Neurotransmitter acetylcholine negatively regulates neuromuscular synapse formation by a Cdk5-dependent mechanism. W Lin B Dominguez J Yang P Aryal EP Brandon FH Gage KF Lee, Neuron 2005 46 569 579 10.1016/j.neuron.2005.04.002 15944126
    • (2005) Neuron , vol.46 , pp. 569-579
    • Lin, W.1    Dominguez, B.2    Yang, J.3    Aryal, P.4    Brandon, E.P.5    Gage, F.H.6    Lee, K.F.7
  • 24
    • 0034983538 scopus 로고    scopus 로고
    • Patterning of muscle acetylcholine receptor gene expression in the absence of motor innervation
    • 10.1016/S0896-6273(01)00287-2. 11395002
    • Patterning of muscle acetylcholine receptor gene expression in the absence of motor innervation. X Yang S Arber C William L Li Y Tanabe TM Jessell C Birchmeier SJ Burden, Neuron 2001 30 399 410 10.1016/S0896-6273(01)00287-2 11395002
    • (2001) Neuron , vol.30 , pp. 399-410
    • Yang, X.1    Arber, S.2    William, C.3    Li, L.4    Tanabe, Y.5    Jessell, T.M.6    Birchmeier, C.7    Burden, S.J.8
  • 25
    • 23344453327 scopus 로고    scopus 로고
    • Agrin promotes synaptic differentiation by counteracting an inhibitory effect of neurotransmitter
    • 16043708. 10.1073/pnas.0504806102
    • Agrin promotes synaptic differentiation by counteracting an inhibitory effect of neurotransmitter. T Misgeld TT Kummer JW Lichtman JR Sanes, Proc Natl Acad Sci USA 2005 102 11088 11093 16043708 10.1073/pnas.0504806102
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11088-11093
    • Misgeld, T.1    Kummer, T.T.2    Lichtman, J.W.3    Sanes, J.R.4
  • 26
    • 0038545348 scopus 로고    scopus 로고
    • The basement membrane components nidogen and type XVIII collagen regulate organization of neuromuscular junctions in Caenorhabditis elegans
    • 12736328
    • The basement membrane components nidogen and type XVIII collagen regulate organization of neuromuscular junctions in Caenorhabditis elegans. BD Ackley SH Kang JR Crew C Suh Y Jin JM Kramer, J Neurosci 2003 23 3577 3587 12736328
    • (2003) J Neurosci , vol.23 , pp. 3577-3587
    • Ackley, B.D.1    Kang, S.H.2    Crew, J.R.3    Suh, C.4    Jin, Y.5    Kramer, J.M.6
  • 27
    • 0019888064 scopus 로고
    • Entactin, a novel basal lamina-associated sulfated glycoprotein
    • 6262321
    • Entactin, a novel basal lamina-associated sulfated glycoprotein. B Carlin R Jaffe B Bender AE Chung, J Biol Chem 1981 256 5209 5214 6262321
    • (1981) J Biol Chem , vol.256 , pp. 5209-5214
    • Carlin, B.1    Jaffe, R.2    Bender, B.3    Chung, A.E.4
  • 28
    • 0021105533 scopus 로고
    • Nidogen: A new, self-aggregating basement membrane protein
    • 10.1111/j.1432-1033.1983.tb07849.x. 6420150
    • Nidogen: a new, self-aggregating basement membrane protein. R Timpl M Dziadek S Fujiwara H Nowack G Wick, Eur J Biochem 1983 137 455 465 10.1111/j.1432-1033.1983.tb07849.x 6420150
    • (1983) Eur J Biochem , vol.137 , pp. 455-465
    • Timpl, R.1    Dziadek, M.2    Fujiwara, S.3    Nowack, H.4    Wick, G.5
  • 29
    • 0031820133 scopus 로고    scopus 로고
    • Entactin-2: A new member of basement membrane protein with high homology to entactin/nidogen
    • 10.1006/excr.1998.4016. 9633511
    • Entactin-2: a new member of basement membrane protein with high homology to entactin/nidogen. N Kimura T Toyoshima T Kojima M Shimane, Exp Cell Res 1998 241 36 45 10.1006/excr.1998.4016 9633511
    • (1998) Exp Cell Res , vol.241 , pp. 36-45
    • Kimura, N.1    Toyoshima, T.2    Kojima, T.3    Shimane, M.4
  • 30
    • 0032508461 scopus 로고    scopus 로고
    • Nidogen-2: A new basement membrane protein with diverse binding properties
    • 10.1006/jmbi.1998.2004. 9733643
    • Nidogen-2: a new basement membrane protein with diverse binding properties. E Kohfeldt T Sasaki W Gohring R Timpl, J Mol Biol 1998 282 99 109 10.1006/jmbi.1998.2004 9733643
    • (1998) J Mol Biol , vol.282 , pp. 99-109
    • Kohfeldt, E.1    Sasaki, T.2    Gohring, W.3    Timpl, R.4
  • 31
    • 0034063444 scopus 로고    scopus 로고
    • Ultrastructural colocalization of nidogen-1 and nidogen-2 with laminin-1 in murine kidney basement membranes
    • 10.1007/s004180050014. 10766264
    • Ultrastructural colocalization of nidogen-1 and nidogen-2 with laminin-1 in murine kidney basement membranes. N Miosge F Kother S Heinemann E Kohfeldt R Herken R Timpl, Histochem Cell Biol 2000 113 115 124 10.1007/s004180050014 10766264
    • (2000) Histochem Cell Biol , vol.113 , pp. 115-124
    • Miosge, N.1    Kother, F.2    Heinemann, S.3    Kohfeldt, E.4    Herken, R.5    Timpl, R.6
  • 32
    • 0033821010 scopus 로고    scopus 로고
    • The absence of nidogen 1 does not affect murine basement membrane formation
    • 10958695. 10.1128/MCB.20.18.7007-7012.2000
    • The absence of nidogen 1 does not affect murine basement membrane formation. M Murshed N Smyth N Miosge J Karolat T Krieg M Paulsson R Nischt, Mol Cell Biol 2000 20 7007 7012 10958695 10.1128/MCB.20.18.7007-7012.2000
    • (2000) Mol Cell Biol , vol.20 , pp. 7007-7012
    • Murshed, M.1    Smyth, N.2    Miosge, N.3    Karolat, J.4    Krieg, T.5    Paulsson, M.6    Nischt, R.7
  • 33
    • 0036785584 scopus 로고    scopus 로고
    • Gene structure and functional analysis of the mouse nidogen-2 gene: Nidogen-2 is not essential for basement membrane formation in mice
    • 12215539. 10.1128/MCB.22.19.6820-6830.2002
    • Gene structure and functional analysis of the mouse nidogen-2 gene: nidogen-2 is not essential for basement membrane formation in mice. J Schymeinsky S Nedbal N Miosge E Poschl C Rao DR Beier WC Skarnes R Timpl BL Bader, Mol Cell Biol 2002 22 6820 6830 12215539 10.1128/MCB.22.19.6820-6830.2002
    • (2002) Mol Cell Biol , vol.22 , pp. 6820-6830
    • Schymeinsky, J.1    Nedbal, S.2    Miosge, N.3    Poschl, E.4    Rao, C.5    Beier, D.R.6    Skarnes, W.C.7    Timpl, R.8    Bader, B.L.9
  • 35
    • 22544456862 scopus 로고    scopus 로고
    • Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice
    • 16024816. 10.1128/MCB.25.15.6846-6856.2005
    • Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice. BL Bader N Smyth S Nedbal N Miosge A Baranowsky S Mokkapati M Murshed R Nischt, Mol Cell Biol 2005 25 6846 6856 16024816 10.1128/MCB.25.15.6846-6856.2005
    • (2005) Mol Cell Biol , vol.25 , pp. 6846-6856
    • Bader, B.L.1    Smyth, N.2    Nedbal, S.3    Miosge, N.4    Baranowsky, A.5    Mokkapati, S.6    Murshed, M.7    Nischt, R.8
  • 36
    • 33845998581 scopus 로고    scopus 로고
    • Loss of nidogen-1 and -2 results in syndactyly and changes in limb development
    • 10.1074/jbc.M607886200. 17023412
    • Loss of nidogen-1 and -2 results in syndactyly and changes in limb development. K Bose R Nischt A Page BL Bader M Paulsson N Smyth, J Biol Chem 2006 281 39620 39629 10.1074/jbc.M607886200 17023412
    • (2006) J Biol Chem , vol.281 , pp. 39620-39629
    • Bose, K.1    Nischt, R.2    Page, A.3    Bader, B.L.4    Paulsson, M.5    Smyth, N.6
  • 37
    • 42949163951 scopus 로고    scopus 로고
    • Nidogens-extracellular matrix linker molecules
    • 10.1002/jemt.20567. 18219668
    • Nidogens-extracellular matrix linker molecules. MS Ho K Bose S Mokkapati R Nischt N Smyth, Microsc Res Tech 2008 71 387 395 10.1002/jemt.20567 18219668
    • (2008) Microsc Res Tech , vol.71 , pp. 387-395
    • Ho, M.S.1    Bose, K.2    Mokkapati, S.3    Nischt, R.4    Smyth, N.5
  • 38
    • 0028288275 scopus 로고
    • A novel epitope of entactin is present at the mammalian neuromuscular junction
    • 7514212
    • A novel epitope of entactin is present at the mammalian neuromuscular junction. AY Chiu J Ko, J Neurosci 1994 14 2809 2817 7514212
    • (1994) J Neurosci , vol.14 , pp. 2809-2817
    • Chiu, A.Y.1    Ko, J.2
  • 39
    • 0032936983 scopus 로고    scopus 로고
    • Development of the vertebrate neuromuscular junction
    • 10.1146/annurev.neuro.22.1.389. 10202544
    • Development of the vertebrate neuromuscular junction. JR Sanes JW Lichtman, Annu Rev Neurosci 1999 22 389 442 10.1146/annurev.neuro.22.1.389 10202544
    • (1999) Annu Rev Neurosci , vol.22 , pp. 389-442
    • Sanes, J.R.1    Lichtman, J.W.2
  • 40
    • 33845528095 scopus 로고    scopus 로고
    • Differential expression of entactin-1/nidogen-1 and entactin-2/nidogen-2 in myogenic differentiation
    • 10.1111/j.1432-0436.2006.00100.x. 17177854
    • Differential expression of entactin-1/nidogen-1 and entactin-2/nidogen-2 in myogenic differentiation. R Neu S Adams B Munz, Differentiation 2006 74 573 582 10.1111/j.1432-0436.2006.00100.x 17177854
    • (2006) Differentiation , vol.74 , pp. 573-582
    • Neu, R.1    Adams, S.2    Munz, B.3
  • 41
    • 34447321556 scopus 로고    scopus 로고
    • Nidogen is a prosurvival and promigratory factor for adult Schwann cells
    • 10.1111/j.1471-4159.2007.04580.x. 17437540
    • Nidogen is a prosurvival and promigratory factor for adult Schwann cells. HK Lee IA Seo HK Park YM Park KJ Ahn YH Yoo HT Park, J Neurochem 2007 102 686 698 10.1111/j.1471-4159.2007.04580.x 17437540
    • (2007) J Neurochem , vol.102 , pp. 686-698
    • Lee, H.K.1    Seo, I.A.2    Park, H.K.3    Park, Y.M.4    Ahn, K.J.5    Yoo, Y.H.6    Park, H.T.7
  • 42
    • 1842613541 scopus 로고    scopus 로고
    • Nerve-independent formation of a topologically complex postsynaptic apparatus
    • 15037598. 10.1083/jcb.200401115
    • Nerve-independent formation of a topologically complex postsynaptic apparatus. TT Kummer T Misgeld JW Lichtman JR Sanes, J Cell Biol 2004 164 1077 1087 15037598 10.1083/jcb.200401115
    • (2004) J Cell Biol , vol.164 , pp. 1077-1087
    • Kummer, T.T.1    Misgeld, T.2    Lichtman, J.W.3    Sanes, J.R.4
  • 43
    • 0025274020 scopus 로고
    • PECAM-1 (CD31) cloning and relation to adhesion molecules of the immunoglobulin gene superfamily
    • 10.1126/science.1690453. 1690453
    • PECAM-1 (CD31) cloning and relation to adhesion molecules of the immunoglobulin gene superfamily. PJ Newman MC Berndt J Gorski GC White 2nd S Lyman C Paddock WA Muller, Science 1990 247 1219 1222 10.1126/science.1690453 1690453
    • (1990) Science , vol.247 , pp. 1219-1222
    • Newman, P.J.1    Berndt, M.C.2    Gorski, J.3    White II, G.C.4    Lyman, S.5    Paddock, C.6    Muller, W.A.7
  • 44
    • 0027369903 scopus 로고
    • Developmental regulation of highly active alternatively spliced forms of agrin
    • 10.1016/0896-6273(93)90152-H. 8398141
    • Developmental regulation of highly active alternatively spliced forms of agrin. W Hoch M Ferns JT Campanelli ZW Hall RH Scheller, Neuron 1993 11 479 490 10.1016/0896-6273(93)90152-H 8398141
    • (1993) Neuron , vol.11 , pp. 479-490
    • Hoch, W.1    Ferns, M.2    Campanelli, J.T.3    Hall, Z.W.4    Scheller, R.H.5
  • 45
    • 0035511932 scopus 로고    scopus 로고
    • Induction, assembly, maturation and maintenance of a postsynaptic apparatus
    • 10.1038/35097557. 11715056
    • Induction, assembly, maturation and maintenance of a postsynaptic apparatus. JR Sanes JW Lichtman, Nat Rev Neurosci 2001 2 791 805 10.1038/35097557 11715056
    • (2001) Nat Rev Neurosci , vol.2 , pp. 791-805
    • Sanes, J.R.1    Lichtman, J.W.2
  • 46
    • 0032066259 scopus 로고    scopus 로고
    • Myotubular myopathy: Morphological, immunohistochemical and clinical variation
    • 10.1016/S0960-8966(98)00010-8. 9631395
    • Myotubular myopathy: morphological, immunohistochemical and clinical variation. TR Helliwell IH Ellis RE Appleton, Neuromuscul Disord 1998 8 152 161 10.1016/S0960-8966(98)00010-8 9631395
    • (1998) Neuromuscul Disord , vol.8 , pp. 152-161
    • Helliwell, T.R.1    Ellis, I.H.2    Appleton, R.E.3
  • 47
    • 23844534710 scopus 로고    scopus 로고
    • The two isoforms of the Caenorhabditis elegans leukocyte-common antigen related receptor tyrosine phosphatase PTP-3 function independently in axon guidance and synapse formation
    • 10.1523/JNEUROSCI.2010-05.2005. 16107639
    • The two isoforms of the Caenorhabditis elegans leukocyte-common antigen related receptor tyrosine phosphatase PTP-3 function independently in axon guidance and synapse formation. BD Ackley RJ Harrington ML Hudson L Williams CJ Kenyon AD Chisholm Y Jin, J Neurosci 2005 25 7517 7528 10.1523/JNEUROSCI.2010- 05.2005 16107639
    • (2005) J Neurosci , vol.25 , pp. 7517-7528
    • Ackley, B.D.1    Harrington, R.J.2    Hudson, M.L.3    Williams, L.4    Kenyon, C.J.5    Chisholm, A.D.6    Jin, Y.7
  • 48
    • 3242661158 scopus 로고    scopus 로고
    • FGF22 and its close relatives are presynaptic organizing molecules in the mammalian brain
    • 10.1016/j.cell.2004.06.025. 15260994
    • FGF22 and its close relatives are presynaptic organizing molecules in the mammalian brain. H Umemori MW Linhoff DM Ornitz JR Sanes, Cell 2004 118 257 270 10.1016/j.cell.2004.06.025 15260994
    • (2004) Cell , vol.118 , pp. 257-270
    • Umemori, H.1    Linhoff, M.W.2    Ornitz, D.M.3    Sanes, J.R.4
  • 49
    • 0032842894 scopus 로고    scopus 로고
    • Induction of presynaptic differentiation in cultured neurons by extracellular matrix components
    • 10.1046/j.1460-9568.1999.00766.x. 10564354
    • Induction of presynaptic differentiation in cultured neurons by extracellular matrix components. YJ Son BL Patton JR Sanes, Eur J Neurosci 1999 11 3457 3467 10.1046/j.1460-9568.1999.00766.x 10564354
    • (1999) Eur J Neurosci , vol.11 , pp. 3457-3467
    • Son, Y.J.1    Patton, B.L.2    Sanes, J.R.3
  • 50
    • 0036860601 scopus 로고    scopus 로고
    • Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice
    • 10.1016/S0945-053X(02)00070-7. 12475645
    • Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice. N Miosge T Sasaki R Timpl, Matrix Biol 2002 21 611 621 10.1016/S0945-053X(02)00070-7 12475645
    • (2002) Matrix Biol , vol.21 , pp. 611-621
    • Miosge, N.1    Sasaki, T.2    Timpl, R.3
  • 51
    • 0032850748 scopus 로고    scopus 로고
    • Angiogenesis inhibitor endostatin is a distinct component of elastic fibers in vessel walls
    • 10506577
    • Angiogenesis inhibitor endostatin is a distinct component of elastic fibers in vessel walls. N Miosge T Sasaki R Timpl, Faseb J 1999 13 1743 1750 10506577
    • (1999) Faseb J , vol.13 , pp. 1743-1750
    • Miosge, N.1    Sasaki, T.2    Timpl, R.3
  • 52
    • 0037151078 scopus 로고    scopus 로고
    • The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin
    • 10.1074/jbc.M107583200. 11956183
    • The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin. H Tu T Sasaki A Snellman W Gohring P Pirila R Timpl T Pihlajaniemi, J Biol Chem 2002 277 23092 23099 10.1074/jbc.M107583200 11956183
    • (2002) J Biol Chem , vol.277 , pp. 23092-23099
    • Tu, H.1    Sasaki, T.2    Snellman, A.3    Gohring, W.4    Pirila, P.5    Timpl, R.6    Pihlajaniemi, T.7
  • 53
    • 0345061697 scopus 로고    scopus 로고
    • Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins
    • 10.1016/S0014-5793(99)01362-9. 10544250
    • Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins. T Sasaki W Gohring N Miosge WR Abrams J Rosenbloom R Timpl, FEBS Lett 1999 460 280 284 10.1016/S0014-5793(99)01362-9 10544250
    • (1999) FEBS Lett , vol.460 , pp. 280-284
    • Sasaki, T.1    Gohring, W.2    Miosge, N.3    Abrams, W.R.4    Rosenbloom, J.5    Timpl, R.6
  • 55
    • 0035911968 scopus 로고    scopus 로고
    • The NC1/endostatin domain of Caenorhabditis elegans type XVIII collagen affects cell migration and axon guidance
    • 11257122. 10.1083/jcb.152.6.1219
    • The NC1/endostatin domain of Caenorhabditis elegans type XVIII collagen affects cell migration and axon guidance. BD Ackley JR Crew H Elamaa T Pihlajaniemi CJ Kuo JM Kramer, J Cell Biol 2001 152 1219 1232 11257122 10.1083/jcb.152.6.1219
    • (2001) J Cell Biol , vol.152 , pp. 1219-1232
    • Ackley, B.D.1    Crew, J.R.2    Elamaa, H.3    Pihlajaniemi, T.4    Kuo, C.J.5    Kramer, J.M.6
  • 56
    • 33646848764 scopus 로고    scopus 로고
    • The myotomal diwanka (lh3) glycosyltransferase and type XVIII collagen are critical for motor growth cone migration
    • 10.1016/j.neuron.2006.04.024. 16731508
    • The myotomal diwanka (lh3) glycosyltransferase and type XVIII collagen are critical for motor growth cone migration. VA Schneider M Granato, Neuron 2006 50 683 695 10.1016/j.neuron.2006.04.024 16731508
    • (2006) Neuron , vol.50 , pp. 683-695
    • Schneider, V.A.1    Granato, M.2
  • 57
    • 0035134403 scopus 로고    scopus 로고
    • Type XIII collagen: A novel cell adhesion component present in a range of cell-matrix adhesions and in the intercalated discs between cardiac muscle cells
    • 10.1016/S0945-053X(00)00119-0. 11223332
    • Type XIII collagen: a novel cell adhesion component present in a range of cell-matrix adhesions and in the intercalated discs between cardiac muscle cells. P Hagg T Vaisanen A Tuomisto M Rehn H Tu P Huhtala S Eskelinen T Pihlajaniemi, Matrix Biol 2001 19 727 742 10.1016/S0945-053X(00)00119-0 11223332
    • (2001) Matrix Biol , vol.19 , pp. 727-742
    • Hagg, P.1    Vaisanen, T.2    Tuomisto, A.3    Rehn, M.4    Tu, H.5    Huhtala, P.6    Eskelinen, S.7    Pihlajaniemi, T.8
  • 58
    • 0037171788 scopus 로고    scopus 로고
    • An intrinsic distinction in neuromuscular junction assembly and maintenance in different skeletal muscles
    • 10.1016/S0896-6273(02)00670-0. 11988168
    • An intrinsic distinction in neuromuscular junction assembly and maintenance in different skeletal muscles. S Pun M Sigrist AF Santos MA Ruegg JR Sanes TM Jessell S Arber P Caroni, Neuron 2002 34 357 370 10.1016/S0896- 6273(02)00670-0 11988168
    • (2002) Neuron , vol.34 , pp. 357-370
    • Pun, S.1    Sigrist, M.2    Santos, A.F.3    Ruegg, M.A.4    Sanes, J.R.5    Jessell, T.M.6    Arber, S.7    Caroni, P.8
  • 60
    • 0027947521 scopus 로고
    • All muscles are not created equal
    • 10.1016/0168-9525(94)90056-6. 7809945
    • All muscles are not created equal. MJ Donoghue JR Sanes, Trends Genet 1994 10 396 401 10.1016/0168-9525(94)90056-6 7809945
    • (1994) Trends Genet , vol.10 , pp. 396-401
    • Donoghue, M.J.1    Sanes, J.R.2
  • 61
    • 3042580699 scopus 로고    scopus 로고
    • Assembly, plasticity and selective vulnerability to disease of mouse neuromuscular junctions
    • 10.1023/B:NEUR.0000020628.36013.88. 15034272
    • Assembly, plasticity and selective vulnerability to disease of mouse neuromuscular junctions. AF Santos P Caroni, J Neurocytol 2003 32 849 862 10.1023/B:NEUR.0000020628.36013.88 15034272
    • (2003) J Neurocytol , vol.32 , pp. 849-862
    • Santos, A.F.1    Caroni, P.2
  • 62
    • 41149113045 scopus 로고    scopus 로고
    • Selective vulnerability of motor neurons and dissociation of pre- and post-synaptic pathology at the neuromuscular junction in mouse models of spinal muscular atrophy
    • 10.1093/hmg/ddm367. 18065780
    • Selective vulnerability of motor neurons and dissociation of pre- and post-synaptic pathology at the neuromuscular junction in mouse models of spinal muscular atrophy. LM Murray LH Comley D Thomson N Parkinson K Talbot TH Gillingwater, Hum Mol Genet 2008 17 949 962 10.1093/hmg/ddm367 18065780
    • (2008) Hum Mol Genet , vol.17 , pp. 949-962
    • Murray, L.M.1    Comley, L.H.2    Thomson, D.3    Parkinson, N.4    Talbot, K.5    Gillingwater, T.H.6
  • 63
    • 0027968231 scopus 로고
    • Basal lamina assembly
    • 10.1016/0955-0674(94)90093-0. 7833047
    • Basal lamina assembly. PD Yurchenco JJ O'Rear, Curr Opin Cell Biol 1994 6 674 681 10.1016/0955-0674(94)90093-0 7833047
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 674-681
    • Yurchenco, P.D.1    O'Rear, J.J.2
  • 64
    • 34547093441 scopus 로고    scopus 로고
    • Role of laminin terminal globular domains in basement membrane assembly
    • 10.1074/jbc.M702963200. 17517882
    • Role of laminin terminal globular domains in basement membrane assembly. KK McKee D Harrison S Capizzi PD Yurchenco, J Biol Chem 2007 282 21437 21447 10.1074/jbc.M702963200 17517882
    • (2007) J Biol Chem , vol.282 , pp. 21437-21447
    • McKee, K.K.1    Harrison, D.2    Capizzi, S.3    Yurchenco, P.D.4
  • 65
    • 0030457613 scopus 로고    scopus 로고
    • Molecular and functional defects in kidneys of mice lacking collagen alpha 3(IV): Implications for Alport syndrome
    • 8947561. 10.1083/jcb.135.5.1403
    • Molecular and functional defects in kidneys of mice lacking collagen alpha 3(IV): implications for Alport syndrome. JH Miner JR Sanes, J Cell Biol 1996 135 1403 1413 8947561 10.1083/jcb.135.5.1403
    • (1996) J Cell Biol , vol.135 , pp. 1403-1413
    • Miner, J.H.1    Sanes, J.R.2
  • 66
    • 8444247525 scopus 로고    scopus 로고
    • Laminin functions in tissue morphogenesis
    • 10.1146/annurev.cellbio.20.010403.094555. 15473841
    • Laminin functions in tissue morphogenesis. JH Miner PD Yurchenco, Annu Rev Cell Dev Biol 2004 20 255 284 10.1146/annurev.cellbio.20.010403.094555 15473841
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 255-284
    • Miner, J.H.1    Yurchenco, P.D.2
  • 67
    • 1442310569 scopus 로고    scopus 로고
    • Basement membrane assembly, stability and activities observed through a developmental lens
    • 10.1016/j.matbio.2003.10.006. 14996432
    • Basement membrane assembly, stability and activities observed through a developmental lens. PD Yurchenco PS Amenta BL Patton, Matrix Biol 2004 22 521 538 10.1016/j.matbio.2003.10.006 14996432
    • (2004) Matrix Biol , vol.22 , pp. 521-538
    • Yurchenco, P.D.1    Amenta, P.S.2    Patton, B.L.3
  • 68
    • 1842482987 scopus 로고    scopus 로고
    • Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development
    • 10.1242/dev.01037. 14998921
    • Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. E Poschl U Schlotzer-Schrehardt B Brachvogel K Saito Y Ninomiya U Mayer, Development 2004 131 1619 1628 10.1242/dev.01037 14998921
    • (2004) Development , vol.131 , pp. 1619-1628
    • Poschl, E.1    Schlotzer-Schrehardt, U.2    Brachvogel, B.3    Saito, K.4    Ninomiya, Y.5    Mayer, U.6
  • 69
    • 0029122801 scopus 로고
    • A synaptic localization domain in the synaptic cleft protein laminin beta 2 (s-laminin)
    • 10.1126/science.7618109. 7618109
    • A synaptic localization domain in the synaptic cleft protein laminin beta 2 (s-laminin). PT Martin AJ Ettinger JR Sanes, Science 1995 269 413 416 10.1126/science.7618109 7618109
    • (1995) Science , vol.269 , pp. 413-416
    • Martin, P.T.1    Ettinger, A.J.2    Sanes, J.R.3
  • 70
    • 0030940161 scopus 로고    scopus 로고
    • Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold
    • 10.1016/S0896-6273(00)80303-7. 9136771
    • Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold. ED Apel DJ Glass LM Moscoso GD Yancopoulos JR Sanes, Neuron 1997 18 623 635 10.1016/S0896-6273(00)80303-7 9136771
    • (1997) Neuron , vol.18 , pp. 623-635
    • Apel, E.D.1    Glass, D.J.2    Moscoso, L.M.3    Yancopoulos, G.D.4    Sanes, J.R.5
  • 73
    • 20344373392 scopus 로고    scopus 로고
    • Epithelial laminin alpha5 is necessary for distal epithelial cell maturation, VEGF production, and alveolization in the developing murine lung
    • 10.1016/j.ydbio.2005.02.031. 15936333
    • Epithelial laminin alpha5 is necessary for distal epithelial cell maturation, VEGF production, and alveolization in the developing murine lung. NM Nguyen DG Kelley JA Schlueter MJ Meyer RM Senior JH Miner, Dev Biol 2005 282 111 125 10.1016/j.ydbio.2005.02.031 15936333
    • (2005) Dev Biol , vol.282 , pp. 111-125
    • Nguyen, N.M.1    Kelley, D.G.2    Schlueter, J.A.3    Meyer, M.J.4    Senior, R.M.5    Miner, J.H.6
  • 74
    • 0038561092 scopus 로고    scopus 로고
    • Beta1 integrins regulate myoblast fusion and sarcomere assembly
    • 10.1016/S1534-5807(03)00118-7. 12737803
    • Beta1 integrins regulate myoblast fusion and sarcomere assembly. M Schwander M Leu M Stumm OM Dorchies UT Ruegg J Schittny U Muller, Dev Cell 2003 4 673 685 10.1016/S1534-5807(03)00118-7 12737803
    • (2003) Dev Cell , vol.4 , pp. 673-685
    • Schwander, M.1    Leu, M.2    Stumm, M.3    Dorchies, O.M.4    Ruegg, U.T.5    Schittny, J.6    Muller, U.7
  • 75
    • 0038692868 scopus 로고    scopus 로고
    • Phosphodiesterase-Ialpha/autotaxin: A counteradhesive protein expressed by oligodendrocytes during onset of myelination
    • 10.1016/S1044-7431(03)00073-3. 12837632
    • Phosphodiesterase-Ialpha/autotaxin: a counteradhesive protein expressed by oligodendrocytes during onset of myelination. MA Fox RJ Colello WB Macklin B Fuss, Mol Cell Neurosci 2003 23 507 519 10.1016/S1044-7431(03)00073-3 12837632
    • (2003) Mol Cell Neurosci , vol.23 , pp. 507-519
    • Fox, M.A.1    Colello, R.J.2    MacKlin, W.B.3    Fuss, B.4
  • 76
    • 34447648009 scopus 로고    scopus 로고
    • Synaptotagmin I and II are present in distinct subsets of central synapses
    • 10.1002/cne.21381. 17492637
    • Synaptotagmin I and II are present in distinct subsets of central synapses. MA Fox JR Sanes, J Comp Neurol 2007 503 280 296 10.1002/cne.21381 17492637
    • (2007) J Comp Neurol , vol.503 , pp. 280-296
    • Fox, M.A.1    Sanes, J.R.2
  • 77
    • 0025288080 scopus 로고
    • Organization of hindbrain segments in the zebrafish embryo
    • 10.1016/0896-6273(90)90194-K. 2344406
    • Organization of hindbrain segments in the zebrafish embryo. B Trevarrow DL Marks CB Kimmel, Neuron 1990 4 669 679 10.1016/0896-6273(90)90194-K 2344406
    • (1990) Neuron , vol.4 , pp. 669-679
    • Trevarrow, B.1    Marks, D.L.2    Kimmel, C.B.3
  • 78
    • 0029098578 scopus 로고
    • Differential expression of two basement membrane collagen genes, COL4A6 and COL4A5, demonstrated by immunofluorescence staining using peptide-specific monoclonal antibodies
    • 7657706. 10.1083/jcb.130.5.1219
    • Differential expression of two basement membrane collagen genes, COL4A6 and COL4A5, demonstrated by immunofluorescence staining using peptide-specific monoclonal antibodies. Y Ninomiya M Kagawa K Iyama I Naito Y Kishiro JM Seyer M Sugimoto T Oohashi Y Sado, J Cell Biol 1995 130 1219 1229 7657706 10.1083/jcb.130.5.1219
    • (1995) J Cell Biol , vol.130 , pp. 1219-1229
    • Ninomiya, Y.1    Kagawa, M.2    Iyama, K.3    Naito, I.4    Kishiro, Y.5    Seyer, J.M.6    Sugimoto, M.7    Oohashi, T.8    Sado, Y.9
  • 79
    • 0036164464 scopus 로고    scopus 로고
    • Domain IV of mouse laminin beta1 and beta2 chains
    • 10.1046/j.0014-2956.2001.02663.x. 11856301
    • Domain IV of mouse laminin beta1 and beta2 chains. T Sasaki K Mann JH Miner N Miosge R Timpl, Eur J Biochem 2002 269 431 442 10.1046/j.0014-2956.2001. 02663.x 11856301
    • (2002) Eur J Biochem , vol.269 , pp. 431-442
    • Sasaki, T.1    Mann, K.2    Miner, J.H.3    Miosge, N.4    Timpl, R.5
  • 80
    • 0034634679 scopus 로고    scopus 로고
    • Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues
    • 10.1074/jbc.M003261200. 10934193
    • Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues. JF Talts T Sasaki N Miosge W Gohring K Mann R Mayne R Timpl, J Biol Chem 2000 275 35192 35199 10.1074/jbc.M003261200 10934193
    • (2000) J Biol Chem , vol.275 , pp. 35192-35199
    • Talts, J.F.1    Sasaki, T.2    Miosge, N.3    Gohring, W.4    Mann, K.5    Mayne, R.6    Timpl, R.7
  • 81
    • 0030919488 scopus 로고    scopus 로고
    • The laminin alpha chains: Expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform
    • 9151674. 10.1083/jcb.137.3.685
    • The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform. JH Miner BL Patton SI Lentz DJ Gilbert WD Snider NA Jenkins NG Copeland JR Sanes, J Cell Biol 1997 137 685 701 9151674 10.1083/jcb.137.3.685
    • (1997) J Cell Biol , vol.137 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.I.3    Gilbert, D.J.4    Snider, W.D.5    Jenkins, N.A.6    Copeland, N.G.7    Sanes, J.R.8
  • 82
    • 0027941192 scopus 로고
    • Dystroglycan binds nerve and muscle agrin
    • 10.1016/0896-6273(94)90462-6. 8043271
    • Dystroglycan binds nerve and muscle agrin. J Sugiyama DC Bowen ZW Hall, Neuron 1994 13 103 115 10.1016/0896-6273(94)90462-6 8043271
    • (1994) Neuron , vol.13 , pp. 103-115
    • Sugiyama, J.1    Bowen, D.C.2    Hall, Z.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.