메뉴 건너뛰기




Volumn 8, Issue 12, 2007, Pages

The reticulons: A family of proteins with diverse functions

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; PROTEIN; RETICULON; UNCLASSIFIED DRUG; MEMBRANE PROTEIN; NERVE PROTEIN;

EID: 40449124075     PISSN: 14747596     EISSN: 1474760X     Source Type: Journal    
DOI: 10.1186/gb-2007-8-12-234     Document Type: Review
Times cited : (175)

References (100)
  • 1
    • 0038799728 scopus 로고    scopus 로고
    • A reticular rhapsody: Phylogenic evolution and nomenclature of the RTN/ Nogo gene family
    • 10.1096/fj.02-1166hyp 12832288
    • Oertle T Klinger M Stuermer CA Schwab ME A reticular rhapsody: phylogenic evolution and nomenclature of the RTN/Nogo gene family. FASEB J 2003, 17:1238-1247. 10.1096/fj.02-1166hyp 12832288
    • (2003) FASEB J , vol.17 , pp. 1238-1247
    • Oertle, T.1    Klinger, M.2    Stuermer, C.A.3    Schwab, M.E.4
  • 2
    • 34447269976 scopus 로고    scopus 로고
    • Reticulon-like proteins in Arabidopsis thaliana: Structural organization and ER localization
    • 10.1016/j.febslet.2007.06.032 17604024
    • Nziengui H Bouhidel K Pillon D Der C Marty F Schoefs B Reticulon-like proteins in Arabidopsis thaliana: Structural organization and ER localization. FEBS Lett 2007, 581:3356-3362. 10.1016/ j.febslet.2007.06.032 17604024
    • (2007) FEBS Lett , vol.581 , pp. 3356-3362
    • Nziengui, H.1    Bouhidel, K.2    Pillon, D.3    Der, C.4    Marty, F.5    Schoefs, B.6
  • 3
    • 33748509747 scopus 로고    scopus 로고
    • The Drosophila reticulon, Rtnl-1, has multiple differentially expressed isoforms that are associated with a sub-compartment of the endoplasmic reticulum
    • 10.1007/s00018-006-6142-3 16847576
    • Wakefield S Tear G The Drosophila reticulon, Rtnl-1, has multiple differentially expressed isoforms that are associated with a sub-compartment of the endoplasmic reticulum. Cell Mol Life Sci 2006, 63:2027-2038. 10.1007/s00018-006-6142-3 16847576
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2027-2038
    • Wakefield, S.1    Tear, G.2
  • 4
    • 25444450572 scopus 로고    scopus 로고
    • Analysis of the reticulon gene family demonstrates the absence of the neurite growth inhibitor Nogo-A in fish
    • 10.1093/molbev/msi158 15858203
    • Diekmann H Klinger M Oertle T Heinz D Pogoda HM Schwab ME Stuermer CA Analysis of the reticulon gene family demonstrates the absence of the neurite growth inhibitor Nogo-A in fish. Mol Biol Evol 2005, 22:1635-1648. 10.1093/molbev/msi158 15858203
    • (2005) Mol Biol Evol , vol.22 , pp. 1635-1648
    • Diekmann, H.1    Klinger, M.2    Oertle, T.3    Heinz, D.4    Pogoda, H.M.5    Schwab, M.E.6    Stuermer, C.A.7
  • 5
    • 0033562960 scopus 로고    scopus 로고
    • Cloning of a novel member of the reticulon gene family (RTN3): Gene structure and chromosomal localization to 11q13
    • 10.1006/geno.1999.5807 10331947
    • Moreira EF Jaworski CJ Rodriguez IR Cloning of a novel member of the reticulon gene family (RTN3): Gene structure and chromosomal localization to 11q13. Genomics 1999, 58:73-81. 10.1006/geno.1999.5807 10331947
    • (1999) Genomics , vol.58 , pp. 73-81
    • Moreira, E.F.1    Jaworski, C.J.2    Rodriguez, I.R.3
  • 6
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • 10.1016/j.cell.2005.11.047 16469703
    • Voeltz GK Prinz WA Shibata Y Rist JM Rapoport TA A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 2006, 124:573-586. 10.1016/j.cell.2005.11.047 16469703
    • (2006) Cell , vol.124 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 7
    • 33646577429 scopus 로고    scopus 로고
    • Reticulon proteins: Emerging players in neurodegenerative diseases
    • 10.1007/s00018-005-5338-2 16505974
    • Yan R Shi Q Hu X Zhou X Reticulon proteins: Emerging players in neurodegenerative diseases. Cell Mol Life Sci 2006, 63:877-889. 10.1007/ s00018-005-5338-2 16505974
    • (2006) Cell Mol Life Sci , vol.63 , pp. 877-889
    • Yan, R.1    Shi, Q.2    Hu, X.3    Zhou, X.4
  • 8
    • 0034719371 scopus 로고    scopus 로고
    • Identification of the Nogo inhibitor of axon regeneration as a reticulon protein
    • 10.1038/35000226 10667797
    • GrandPré T Nakamura F Vartanian T Strittmatter SM Identification of the Nogo inhibitor of axon regeneration as a reticulon protein. Nature 2000, 403:439-444. 10.1038/35000226 10667797
    • (2000) Nature , vol.403 , pp. 439-444
    • GrandPré, T.1    Nakamura, F.2    Vartanian, T.3    Strittmatter, S.M.4
  • 9
    • 0036582979 scopus 로고    scopus 로고
    • Patterns of Nogo mRNA and protein expression in the developing and adult rat and after CNS lesions
    • 11978832
    • Huber AB Weinmann O Brosamle C Oertle T Schwab ME Patterns of Nogo mRNA and protein expression in the developing and adult rat and after CNS lesions. J Neurosci 2002, 22:3553-3567. 11978832
    • (2002) J Neurosci , vol.22 , pp. 3553-3567
    • Huber, A.B.1    Weinmann, O.2    Brosamle, C.3    Oertle, T.4    Schwab, M.E.5
  • 10
    • 0036663013 scopus 로고    scopus 로고
    • Localization of Nogo-A and Nogo-66 receptor proteins at sites of axon-myelin and synaptic contact
    • 12097502
    • Wang X Chun SJ Treloar H Vartanian T Greer CA Strittmatter SM Localization of Nogo-A and Nogo-66 receptor proteins at sites of axon-myelin and synaptic contact. J Neurosci 2002, 22:5505-5515. 12097502
    • (2002) J Neurosci , vol.22 , pp. 5505-5515
    • Wang, X.1    Chun, S.J.2    Treloar, H.3    Vartanian, T.4    Greer, C.A.5    Strittmatter, S.M.6
  • 11
    • 0345863397 scopus 로고    scopus 로고
    • Nogo-A expression in the intact and injured nervous system
    • 10.1016/j.mcn.2003.09.002 14697671
    • Hunt D Coffin RS Prinjha RK Campbell G Anderson PN Nogo-A expression in the intact and injured nervous system. Mol Cell Neurosci 2003, 24:1083-1102. 10.1016/j.mcn.2003.09.002 14697671
    • (2003) Mol Cell Neurosci , vol.24 , pp. 1083-1102
    • Hunt, D.1    Coffin, R.S.2    Prinjha, R.K.3    Campbell, G.4    Anderson, P.N.5
  • 13
    • 0034719513 scopus 로고    scopus 로고
    • Nogo-A is a myelin-associated neurite outgrowth inhibitor and an antigen for monoclonal antibody IN-1
    • 10.1038/35000601 10667796
    • Chen MS Huber AB van der Haar ME Frank M Schnell L Spillmann AA Christ F Schwab ME Nogo-A is a myelin-associated neurite outgrowth inhibitor and an antigen for monoclonal antibody IN-1. Nature 2000, 403:434-439. 10.1038/35000601 10667796
    • (2000) Nature , vol.403 , pp. 434-439
    • Chen, M.S.1    Huber, A.B.2    van der Haar, M.E.3    Frank, M.4    Schnell, L.5    Spillmann, A.A.6    Christ, F.7    Schwab, M.E.8
  • 15
    • 20044379411 scopus 로고    scopus 로고
    • Nogo-A interacts with the Nogo-66 receptor through multiple sites to create an isoform-selective subnanomolar agonist
    • 10.1523/JNEUROSCI.5235-04.2005 15930377
    • Hu F Liu BP Budel S Liao J Chin J Fournier A Strittmatter SM Nogo-A interacts with the Nogo-66 receptor through multiple sites to create an isoform-selective subnanomolar agonist. J Neurosci 2005, 25:5298-5304. 10.1523/JNEUROSCI.5235-04.2005 15930377
    • (2005) J Neurosci , vol.25 , pp. 5298-5304
    • Hu, F.1    Liu, B.P.2    Budel, S.3    Liao, J.4    Chin, J.5    Fournier, A.6    Strittmatter, S.M.7
  • 17
    • 33845285911 scopus 로고    scopus 로고
    • Delayed Nogo receptor therapy improves recovery from spinal cord contusion
    • 10.1002/ana.20953 16958113
    • Wang X Baughman KW Basso DM Strittmatter SM Delayed Nogo receptor therapy improves recovery from spinal cord contusion. Ann Neurol 2006, 60:540-549. 10.1002/ana.20953 16958113
    • (2006) Ann Neurol , vol.60 , pp. 540-549
    • Wang, X.1    Baughman, K.W.2    Basso, D.M.3    Strittmatter, S.M.4
  • 18
    • 18144393017 scopus 로고    scopus 로고
    • Transgenic inhibition of Nogo-66 receptor function allows axonal sprouting and improved locomotion after spinal injury
    • 10.1016/j.mcn.2004.12.008 15866044
    • Li S Kim JE Budel S Hampton TG Strittmatter SM Transgenic inhibition of Nogo-66 receptor function allows axonal sprouting and improved locomotion after spinal injury. Mol Cell Neurosci 2005, 29:26-39. 10.1016/j.mcn.2004.12.008 15866044
    • (2005) Mol Cell Neurosci , vol.29 , pp. 26-39
    • Li, S.1    Kim, J.E.2    Budel, S.3    Hampton, T.G.4    Strittmatter, S.M.5
  • 20
    • 16344384722 scopus 로고    scopus 로고
    • Neurodegenerative illness in transgenic mice expressing a transmembrane form of the prion protein
    • 10.1523/JNEUROSCI.0105-05.2005 15800202
    • Stewart RS Piccardo P Ghetti B Harris DA Neurodegenerative illness in transgenic mice expressing a transmembrane form of the prion protein. J Neurosci 2005, 25:3469-3477. 10.1523/JNEUROSCI.0105-05.2005 15800202
    • (2005) J Neurosci , vol.25 , pp. 3469-3477
    • Stewart, R.S.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 21
    • 33746528014 scopus 로고    scopus 로고
    • Nogo goes in the pure water: Solution structure of Nogo-60 and design of the structured and buffer-soluble Nogo-54 for enhancing CNS regeneration
    • 10.1110/ps.062306906 16877707
    • Li M Liu J Song J Nogo goes in the pure water: Solution structure of Nogo-60 and design of the structured and buffer-soluble Nogo-54 for enhancing CNS regeneration. Protein Sci 2006, 15:1835-1841. 10.1110/ ps.062306906 16877707
    • (2006) Protein Sci , vol.15 , pp. 1835-1841
    • Li, M.1    Liu, J.2    Song, J.3
  • 22
    • 34247567960 scopus 로고    scopus 로고
    • Biochemical characterization of the recombinant human Nogo-A ectodomain
    • 10.1111/j.1742-4658.2007.05796.x 17437522
    • Zander H Hettich E Greiff K Chatwell L Skerra A Biochemical characterization of the recombinant human Nogo-A ectodomain. FEBS J 2007, 274:2603-2613. 10.1111/j.1742-4658.2007.05796.x 17437522
    • (2007) FEBS J , vol.274 , pp. 2603-2613
    • Zander, H.1    Hettich, E.2    Greiff, K.3    Chatwell, L.4    Skerra, A.5
  • 23
    • 0035905799 scopus 로고    scopus 로고
    • Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration
    • 10.1038/35053072 11201742
    • Fournier AE GrandPre T Strittmatter SM Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration. Nature 2001, 409:341-346. 10.1038/35053072 11201742
    • (2001) Nature , vol.409 , pp. 341-346
    • Fournier, A.E.1    GrandPre, T.2    Strittmatter, S.M.3
  • 24
    • 0242389835 scopus 로고    scopus 로고
    • Nogo-A at CNS paranodes is a ligand of Caspr: Possible regulation of K(+) channel localization
    • 275427 14592966 10.1093/emboj/cdg570
    • Nie DY Zhou ZH Ang BT Teng FY Xu G Xiang T Wang CY Zeng L Takeda Y Xu TL et al. Nogo-A at CNS paranodes is a ligand of Caspr: Possible regulation of K(+) channel localization. EMBO J 2003, 22:5666-5678. 275427 14592966 10.1093/emboj/cdg570
    • (2003) EMBO J , vol.22 , pp. 5666-5678
    • Nie, D.Y.1    Zhou, Z.H.2    Ang, B.T.3    Teng, F.Y.4    Xu, G.5    Xiang, T.6    Wang, C.Y.7    Zeng, L.8    Takeda, Y.9    Xu, T.L.10
  • 25
    • 34249876378 scopus 로고    scopus 로고
    • The N- and C-termini of the human Nogo molecules are intrinsically unstructured: Bioinformatics, CD, NMR characterization, and functional implications
    • 10.1002/prot.21385 17397058
    • Li M Song J The N- and C-termini of the human Nogo molecules are intrinsically unstructured: Bioinformatics, CD, NMR characterization, and functional implications. Proteins 2007, 68:100-108. 10.1002/ prot.21385 17397058
    • (2007) Proteins , vol.68 , pp. 100-108
    • Li, M.1    Song, J.2
  • 26
    • 34547943482 scopus 로고    scopus 로고
    • Molecular principles of the interactions of disordered proteins
    • 10.1016/j.jmb.2007.07.004 17681540
    • Meszaros B Tompa P Simon I Dosztanyi Z Molecular principles of the interactions of disordered proteins. J Mol Biol 2007, 372:549-561. 10.1016/j.jmb.2007.07.004 17681540
    • (2007) J Mol Biol , vol.372 , pp. 549-561
    • Meszaros, B.1    Tompa, P.2    Simon, I.3    Dosztanyi, Z.4
  • 27
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • 10.1038/nrm1589 15738986
    • Dyson HJ Wright PE Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005, 6:197-208. 10.1038/nrm1589 15738986
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 28
    • 0025973421 scopus 로고
    • Developmentally regulated cDNA expressed exclusively in neural tissue
    • 10.1016/0169-328X(91)90053-Z
    • Wieczorek DF Hughes SR Developmentally regulated cDNA expressed exclusively in neural tissue. Brain Res 1991, 10:33-41. 10.1016/ 0169-328X(91)90053-Z
    • (1991) Brain Res , vol.10 , pp. 33-41
    • Wieczorek, D.F.1    Hughes, S.R.2
  • 29
    • 0027497328 scopus 로고
    • Cloning and expression of alternative transcripts of a novel neuroendocrine-specific gene and identification of its 135-kDa translational product
    • 7685762
    • Roebroek AJ van de Velde HJ Van Bokhoven A Broers JL Ramaekers FC Van de Ven WJ Cloning and expression of alternative transcripts of a novel neuroendocrine-specific gene and identification of its 135-kDa translational product. J Biol Chem 1993, 268:13439-13447. 7685762
    • (1993) J Biol Chem , vol.268 , pp. 13439-13447
    • Roebroek, A.J.1    van de Velde, H.J.2    Van Bokhoven, A.3    Broers, J.L.4    Ramaekers, F.C.5    Van de Ven, W.J.6
  • 30
    • 0027963419 scopus 로고
    • NSP-encoded reticulons, neuroendocrine proteins of a novel gene family associated with membranes of the endoplasmic reticulum
    • 7844160
    • van de Velde HJ Roebroek AJ Senden NH Ramaekers FC Van de Ven WJ NSP-encoded reticulons, neuroendocrine proteins of a novel gene family associated with membranes of the endoplasmic reticulum. J Cell Sci 1994, 107:2403-2416. 7844160
    • (1994) J Cell Sci , vol.107 , pp. 2403-2416
    • van de Velde, H.J.1    Roebroek, A.J.2    Senden, N.H.3    Ramaekers, F.C.4    Van de Ven, W.J.5
  • 31
    • 33847164931 scopus 로고    scopus 로고
    • Two hydrophobic segments of the RTN1 family determine the ER localization and retention
    • 10.1016/j.bbrc.2007.02.001 17303085
    • Iwahashi J Hamada N Watanabe H Two hydrophobic segments of the RTN1 family determine the ER localization and retention. Biochem Biophys Res Commun 2007, 355:508-512. 10.1016/j.bbrc.2007.02.001 17303085
    • (2007) Biochem Biophys Res Commun , vol.355 , pp. 508-512
    • Iwahashi, J.1    Hamada, N.2    Watanabe, H.3
  • 33
    • 34347385833 scopus 로고    scopus 로고
    • A role for Rab5 in structuring the endoplasmic reticulum
    • 10.1083/jcb.200701139 17591921
    • Audhya A Desai A Oegema K A role for Rab5 in structuring the endoplasmic reticulum. J Cell Biol 2007, 178 43-56. 10.1083/jcb.200701139 17591921
    • (2007) J Cell Biol , vol.178 , pp. 43-56
    • Audhya, A.1    Desai, A.2    Oegema, K.3
  • 34
    • 17444397767 scopus 로고    scopus 로고
    • Identification and expression of XRTN2 and XRTN3 during Xenopus development
    • 10.1002/dvdy.20327 15765506
    • Park EC Shim S Han JK Identification and expression of XRTN2 and XRTN3 during Xenopus development. Dev Dyn 2005, 233:240-247. 10.1002/ dvdy.20327 15765506
    • (2005) Dev Dyn , vol.233 , pp. 240-247
    • Park, E.C.1    Shim, S.2    Han, J.K.3
  • 35
    • 35148885295 scopus 로고    scopus 로고
    • Reticulon 4a/NogoA locates to regions of high membrane curvature and may have a role in nuclear envelope growth
    • 2048824 17889556 10.1016/j.jsb.2007.08.005
    • Kiseleva E Morozova KN Voeltz GK Allen TD Goldberg MW Reticulon 4a/NogoA locates to regions of high membrane curvature and may have a role in nuclear envelope growth. J Struct Biol 2007, 160:224-235. 2048824 17889556 10.1016/j.jsb.2007.08.005
    • (2007) J Struct Biol , vol.160 , pp. 224-235
    • Kiseleva, E.1    Morozova, K.N.2    Voeltz, G.K.3    Allen, T.D.4    Goldberg, M.W.5
  • 37
    • 0034965057 scopus 로고    scopus 로고
    • Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells
    • 10.1038/35078543 11389441
    • Lin SX Grant B Hirsh D Maxfield FR Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells. Nat Cell Biol 2001, 3:567-572. 10.1038/35078543 11389441
    • (2001) Nat Cell Biol , vol.3 , pp. 567-572
    • Lin, S.X.1    Grant, B.2    Hirsh, D.3    Maxfield, F.R.4
  • 38
    • 0034965059 scopus 로고    scopus 로고
    • Evidence that RME-1, a conserved C. elegans EH-domain protein, functions in endocytic recycling
    • 10.1038/35078549 11389442
    • Grant B Zhang Y Paupard MC Lin SX Hall DH Hirsh D Evidence that RME-1, a conserved C. elegans EH-domain protein, functions in endocytic recycling. Nat Cell Biol 2001, 3:573-579. 10.1038/35078549 11389442
    • (2001) Nat Cell Biol , vol.3 , pp. 573-579
    • Grant, B.1    Zhang, Y.2    Paupard, M.C.3    Lin, S.X.4    Hall, D.H.5    Hirsh, D.6
  • 39
    • 2042465892 scopus 로고    scopus 로고
    • Reticulon 1-C/neuroendocrine-specific protein-C interacts with SNARE proteins
    • 10.1111/j.1471-4159.2004.02345.x 15086514
    • Steiner P Kulangara K Sarria JC Glauser L Regazzi R Hirling H Reticulon 1-C/neuroendocrine-specific protein-C interacts with SNARE proteins. J Neurochem 2004, 89:569-580. 10.1111/j.1471-4159.2004.02345.x 15086514
    • (2004) J Neurochem , vol.89 , pp. 569-580
    • Steiner, P.1    Kulangara, K.2    Sarria, J.C.3    Glauser, L.4    Regazzi, R.5    Hirling, H.6
  • 40
    • 33750496816 scopus 로고    scopus 로고
    • Novel putative targets of N-ethylmaleimide sensitive fusion protein (NSF) and alpha/beta soluble NSF attachment proteins (SNAPs) include the Pak-binding nucleotide exchange factor betaPIX
    • 10.1002/jcb.20998 16795052
    • Martin HG Henley JM Meyer G Novel putative targets of N-ethylmaleimide sensitive fusion protein (NSF) and alpha/beta soluble NSF attachment proteins (SNAPs) include the Pak-binding nucleotide exchange factor betaPIX. J Cell Biochem 2006, 99:1203-1215. 10.1002/jcb.20998 16795052
    • (2006) J Cell Biochem , vol.99 , pp. 1203-1215
    • Martin, H.G.1    Henley, J.M.2    Meyer, G.3
  • 42
    • 22444450305 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Rab-GDI displacement factor ortholog Yip3p forms distinct complexes with the Ypt1 Rab GTPase and the reticulon Rtn1p
    • 10.1128/EC.4.7.1166-1174.2005
    • Geng J Shin ME Gilbert PM Collins RN Burd CG Saccharomyces cerevisiae Rab-GDI displacement factor ortholog Yip3p forms distinct complexes with the Ypt1 Rab GTPase and the reticulon Rtn1p. Eukaryotic Cell 2005, 4:1166-1174. 1168965 16002643 10.1128/EC.4.7.1166-1174.2005
    • (2005) Eukaryotic Cell , vol.4 , pp. 1166-1174
    • Geng, J.1    Shin, M.E.2    Gilbert, P.M.3    Collins, R.N.4    Burd, C.G.5
  • 43
    • 34948874261 scopus 로고    scopus 로고
    • Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells
    • 10.1242/jcs.014225 17684057
    • Haas AK Yoshimura S Stephens DJ Preisinger C Fuchs E Barr FA Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells. J Cell Sci 2007, 120:2997-3010. 10.1242/jcs.014225 17684057
    • (2007) J Cell Sci , vol.120 , pp. 2997-3010
    • Haas, A.K.1    Yoshimura, S.2    Stephens, D.J.3    Preisinger, C.4    Fuchs, E.5    Barr, F.A.6
  • 44
    • 0034706918 scopus 로고    scopus 로고
    • A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity
    • 10.1038/sj.onc.1203948 11126360
    • Tagami S Eguchi Y Kinoshita M Takeda M Tsujimoto Y A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity. Oncogene 2000, 19:5736-5746. 10.1038/sj.onc.1203948 11126360
    • (2000) Oncogene , vol.19 , pp. 5736-5746
    • Tagami, S.1    Eguchi, Y.2    Kinoshita, M.3    Takeda, M.4    Tsujimoto, Y.5
  • 45
    • 34347230960 scopus 로고    scopus 로고
    • Reticulon-1C acts as a molecular switch between endoplasmic reticulum stress and genotoxic cell death pathway in human neuroblastoma cells
    • 10.1111/j.1471-4159.2007.04479.x 17596210
    • Di Sano F Fazi B Tufi R Nardacci R Piacentini M Reticulon-1C acts as a molecular switch between endoplasmic reticulum stress and genotoxic cell death pathway in human neuroblastoma cells. J Neurochem 2007, 102:345-353. 10.1111/j.1471-4159.2007.04479.x 17596210
    • (2007) J Neurochem , vol.102 , pp. 345-353
    • Di Sano, F.1    Fazi, B.2    Tufi, R.3    Nardacci, R.4    Piacentini, M.5
  • 46
    • 34248576323 scopus 로고    scopus 로고
    • Anti-apoptotic activity of Bcl-2 is enhanced by its interaction with RTN3
    • 10.1016/j.cellbi.2007.01.032 17379544
    • Zhu L Xiang R Dong W Liu Y Qi Y Anti-apoptotic activity of Bcl-2 is enhanced by its interaction with RTN3. Cell Biol Int 2007, 31:825-830. 10.1016/j.cellbi.2007.01.032 17379544
    • (2007) Cell Biol Int , vol.31 , pp. 825-830
    • Zhu, L.1    Xiang, R.2    Dong, W.3    Liu, Y.4    Qi, Y.5
  • 47
    • 33846492356 scopus 로고    scopus 로고
    • Reticulon 3 mediates Bcl-2 accumulation in mitochondria in response to endoplasmic reticulum stress
    • 10.1007/s10495-006-0574-y 17191123
    • Wan Q Kuang E Dong W Zhou S Xu H Qi Y Liu Y Reticulon 3 mediates Bcl-2 accumulation in mitochondria in response to endoplasmic reticulum stress. Apoptosis 2007, 12:319-328. 10.1007/s10495-006-0574-y 17191123
    • (2007) Apoptosis , vol.12 , pp. 319-328
    • Wan, Q.1    Kuang, E.2    Dong, W.3    Zhou, S.4    Xu, H.5    Qi, Y.6    Liu, Y.7
  • 48
    • 21644448744 scopus 로고    scopus 로고
    • 2+ depletion triggers apoptotic signals for endoplasmic reticulum (ER) overload response induced by overexpressed reticulon 3 (RTN3/HAP)
    • 10.1002/jcp.20340 15799019
    • 2+ depletion triggers apoptotic signals for endoplasmic reticulum (ER) overload response induced by overexpressed reticulon 3 (RTN3/HAP). J Cell Physiol 2005, 204:549-559. 10.1002/jcp.20340 15799019
    • (2005) J Cell Physiol , vol.204 , pp. 549-559
    • Kuang, E.1    Wan, Q.2    Li, X.3    Xu, H.4    Liu, Q.5    Qi, Y.6
  • 49
    • 0037422190 scopus 로고    scopus 로고
    • Do cancer cells die because of Nogo-B?
    • 10.1038/sj.onc.1206278 12618765
    • Oertle T Merkler D Schwab ME Do cancer cells die because of Nogo-B? Oncogene 2003, 22:1390-1399. 10.1038/sj.onc.1206278 12618765
    • (2003) Oncogene , vol.22 , pp. 1390-1399
    • Oertle, T.1    Merkler, D.2    Schwab, M.E.3
  • 50
    • 33749028999 scopus 로고    scopus 로고
    • Extracellular regulators of axonal growth in the adult central nervous system
    • 10.1098/rstb.2006.1891
    • Liu BP Cafferty WB Budel SO Strittmatter SM Extracellular regulators of axonal growth in the adult central nervous system. Philos Trans R Soc Lond 2006, 361:1593-1610. 10.1098/rstb.2006.1891
    • (2006) Philos Trans R Soc Lond , vol.361 , pp. 1593-1610
    • Liu, B.P.1    Cafferty, W.B.2    Budel, S.O.3    Strittmatter, S.M.4
  • 51
    • 0019856865 scopus 로고
    • Axonal elongation into peripheral nervous system "bridges" after central nervous system injury in adult rats
    • 10.1126/science.6171034 6171034
    • David S Aguayo AJ Axonal elongation into peripheral nervous system "bridges" after central nervous system injury in adult rats. Science 1981, 214:931-933. 10.1126/science.6171034 6171034
    • (1981) Science , vol.214 , pp. 931-933
    • David, S.1    Aguayo, A.J.2
  • 52
    • 0023896592 scopus 로고
    • Two membrane protein fractions from rat central myelin with inhibitory properties for neurite growth and fibroblast spreading
    • 10.1083/jcb.106.4.1281 3360853
    • Caroni P Schwab ME Two membrane protein fractions from rat central myelin with inhibitory properties for neurite growth and fibroblast spreading. J Cell Biol 1988, 106:1281-1288. 10.1083/jcb.106.4.1281 3360853
    • (1988) J Cell Biol , vol.106 , pp. 1281-1288
    • Caroni, P.1    Schwab, M.E.2
  • 53
    • 0037198689 scopus 로고    scopus 로고
    • Nogo-66 receptor antagonist peptide promotes axonal regeneration
    • 10.1038/417547a 12037567
    • GrandPre T Li S Strittmatter SM Nogo-66 receptor antagonist peptide promotes axonal regeneration. Nature 2002, 417:547-551. 10.1038/417547a 12037567
    • (2002) Nature , vol.417 , pp. 547-551
    • GrandPre, T.1    Li, S.2    Strittmatter, S.M.3
  • 54
    • 20844439022 scopus 로고    scopus 로고
    • Blockade of Nogo-66, myelin-associated glycoprotein, and oligodendrocyte myelin glycoprotein by soluble Nogo-66 receptor promotes axonal sprouting and recovery after spinal injury
    • 10.1523/JNEUROSCI.2828-04.2004 15548666
    • Li S Liu BP Budel S Li M Ji B Walus L Li W Jirik A Rabacchi S Choi E et al. Blockade of Nogo-66, myelin-associated glycoprotein, and oligodendrocyte myelin glycoprotein by soluble Nogo-66 receptor promotes axonal sprouting and recovery after spinal injury. J Neurosci 2004, 24:10511-10520. 10.1523/JNEUROSCI.2828-04.2004 15548666
    • (2004) J Neurosci , vol.24 , pp. 10511-10520
    • Li, S.1    Liu, B.P.2    Budel, S.3    Li, M.4    Ji, B.5    Walus, L.6    Li, W.7    Jirik, A.8    Rabacchi, S.9    Choi, E.10
  • 55
    • 7044246002 scopus 로고    scopus 로고
    • Nogo-66 receptor prevents raphespinal and rubrospinal axon regeneration and limits functional recovery from spinal cord injury
    • 10.1016/j.neuron.2004.10.015 15504325
    • Kim JE Liu BP Park JH Strittmatter SM Nogo-66 receptor prevents raphespinal and rubrospinal axon regeneration and limits functional recovery from spinal cord injury. Neuron 2004, 44:439-451. 10.1016/ j.neuron.2004.10.015 15504325
    • (2004) Neuron , vol.44 , pp. 439-451
    • Kim, J.E.1    Liu, B.P.2    Park, J.H.3    Strittmatter, S.M.4
  • 56
    • 0038692887 scopus 로고    scopus 로고
    • Nogo-C is sufficient to delay nerve regeneration
    • 10.1016/S1044-7431(03)00076-9 12837628
    • Kim JE Bonilla IE Qiu D Strittmatter SM Nogo-C is sufficient to delay nerve regeneration. Mol Cell Neurosci 2003, 23:451-459. 10.1016/ S1044-7431(03)00076-9 12837628
    • (2003) Mol Cell Neurosci , vol.23 , pp. 451-459
    • Kim, J.E.1    Bonilla, I.E.2    Qiu, D.3    Strittmatter, S.M.4
  • 57
    • 0028867947 scopus 로고
    • Recovery from spinal cord injury mediated by antibodies to neurite growth inhibitors
    • 10.1038/378498a0 7477407
    • Bregman BS Kunkel-Bagden E Schnell L Dai HN Gao D Schwab ME Recovery from spinal cord injury mediated by antibodies to neurite growth inhibitors. Nature 1995, 378:498-501. 10.1038/378498a0 7477407
    • (1995) Nature , vol.378 , pp. 498-501
    • Bregman, B.S.1    Kunkel-Bagden, E.2    Schnell, L.3    Dai, H.N.4    Gao, D.5    Schwab, M.E.6
  • 58
    • 8144228423 scopus 로고    scopus 로고
    • Regenerating corticospinal fibers in the marmoset (Callitrix jacchus) after spinal cord lesion and treatment with the anti-Nogo-A antibody IN-1
    • 10.1111/j.1460-9568.2004.03716.x 15525289
    • Fouad K Klusman I Schwab ME Regenerating corticospinal fibers in the marmoset (Callitrix jacchus) after spinal cord lesion and treatment with the anti-Nogo-A antibody IN-1. Eur J Neurosci 2004, 20:2479-2482. 10.1111/j.1460-9568.2004.03716.x 15525289
    • (2004) Eur J Neurosci , vol.20 , pp. 2479-2482
    • Fouad, K.1    Klusman, I.2    Schwab, M.E.3
  • 59
    • 0037109760 scopus 로고    scopus 로고
    • Truncated soluble Nogo receptor binds Nogo-66 and blocks inhibition of axon growth by myelin
    • 12388594
    • Fournier AE Gould GC Liu BP Strittmatter SM Truncated soluble Nogo receptor binds Nogo-66 and blocks inhibition of axon growth by myelin. J Neurosci 2002, 22:8876-8883. 12388594
    • (2002) J Neurosci , vol.22 , pp. 8876-8883
    • Fournier, A.E.1    Gould, G.C.2    Liu, B.P.3    Strittmatter, S.M.4
  • 60
    • 0038076000 scopus 로고    scopus 로고
    • Systemic deletion of the myelin-associated outgrowth inhibitor Nogo-A improves regenerative and plastic responses after spinal cord injury
    • 10.1016/S0896-6273(03)00226-5 12718855
    • Simonen M Pedersen V Weinmann O Schnell L Buss A Ledermann B Christ F Sansig G van der Putten H Schwab ME Systemic deletion of the myelin-associated outgrowth inhibitor Nogo-A improves regenerative and plastic responses after spinal cord injury. Neuron 2003, 38:201-211. 10.1016/S0896-6273(03)00226-5 12718855
    • (2003) Neuron , vol.38 , pp. 201-211
    • Simonen, M.1    Pedersen, V.2    Weinmann, O.3    Schnell, L.4    Buss, A.5    Ledermann, B.6    Christ, F.7    Sansig, G.8    van der Putten, H.9    Schwab, M.E.10
  • 61
    • 33751326329 scopus 로고    scopus 로고
    • The Nogo-Nogo receptor pathway limits a spectrum of adult CNS axonal growth
    • 10.1523/JNEUROSCI.3827-06.2006 17122049
    • Cafferty WB Strittmatter SM The Nogo-Nogo receptor pathway limits a spectrum of adult CNS axonal growth. J Neurosci 2006, 26:12242-12250. 10.1523/JNEUROSCI.3827-06.2006 17122049
    • (2006) J Neurosci , vol.26 , pp. 12242-12250
    • Cafferty, W.B.1    Strittmatter, S.M.2
  • 62
    • 0038042274 scopus 로고    scopus 로고
    • Delayed systemic Nogo-66 receptor antagonist promotes recovery from spinal cord injury
    • 12764110
    • Li S Strittmatter SM Delayed systemic Nogo-66 receptor antagonist promotes recovery from spinal cord injury. J Neurosci 2003, 23:4219-4227. 12764110
    • (2003) J Neurosci , vol.23 , pp. 4219-4227
    • Li, S.1    Strittmatter, S.M.2
  • 63
    • 3042838912 scopus 로고    scopus 로고
    • Nogo receptor antagonism promotes stroke recovery by enhancing axonal plasticity
    • 10.1523/JNEUROSCI.1643-04.2004 15240813
    • Lee JK Kim JE Sivula M Strittmatter SM Nogo receptor antagonism promotes stroke recovery by enhancing axonal plasticity. J Neurosci 2004, 24:6209-6217. 10.1523/JNEUROSCI.1643-04.2004 15240813
    • (2004) J Neurosci , vol.24 , pp. 6209-6217
    • Lee, J.K.1    Kim, J.E.2    Sivula, M.3    Strittmatter, S.M.4
  • 64
    • 33644902962 scopus 로고    scopus 로고
    • Dendritic plasticity in the adult rat following middle cerebral artery occlusion and Nogo-a neutralization
    • 10.1093/cercor/bhi132 16033928
    • Papadopoulos CM Tsai SY Cheatwood JL Bollnow MR Kolb BE Schwab ME Kartje GL Dendritic plasticity in the adult rat following middle cerebral artery occlusion and Nogo-a neutralization. Cereb Cortex 2006, 16:529-536. 10.1093/cercor/bhi132 16033928
    • (2006) Cereb Cortex , vol.16 , pp. 529-536
    • Papadopoulos, C.M.1    Tsai, S.Y.2    Cheatwood, J.L.3    Bollnow, M.R.4    Kolb, B.E.5    Schwab, M.E.6    Kartje, G.L.7
  • 65
    • 0036196245 scopus 로고    scopus 로고
    • Functional recovery and neuroanatomical plasticity following middle cerebral artery occlusion and IN-1 antibody treatment in the adult rat
    • 10.1002/ana.10144 11921049
    • Papadopoulos CM Tsai SY Alsbiei T O'Brien TE Schwab ME Kartje GL Functional recovery and neuroanatomical plasticity following middle cerebral artery occlusion and IN-1 antibody treatment in the adult rat. Ann Neurol 2002, 51:433-441. 10.1002/ana.10144 11921049
    • (2002) Ann Neurol , vol.51 , pp. 433-441
    • Papadopoulos, C.M.1    Tsai, S.Y.2    Alsbiei, T.3    O'Brien, T.E.4    Schwab, M.E.5    Kartje, G.L.6
  • 66
    • 34147121483 scopus 로고    scopus 로고
    • Response to: Kim et al., "Axon regeneration in young adult mice lacking Nogo-A/B." Neuron 38, 187-199
    • 10.1016/j.neuron.2007.04.004 17442241
    • Steward O Zheng B Banos K Yee KM Response to: Kim et al., "Axon regeneration in young adult mice lacking Nogo-A/B." Neuron 38, 187-199. Neuron 2007, 54:191-195. 10.1016/j.neuron.2007.04.004 17442241
    • (2007) Neuron , vol.54 , pp. 191-195
    • Steward, O.1    Zheng, B.2    Banos, K.3    Yee, K.M.4
  • 67
    • 34147151105 scopus 로고    scopus 로고
    • Response to correspondence: Kim et al., "axon regeneration in young adult mice lacking Nogo-A/B." Neuron 38, 187-199
    • 10.1016/j.neuron.2007.04.005 17442242
    • Cafferty WB Kim JE Lee JK Strittmatter SM et al. Response to correspondence: Kim et al., "axon regeneration in young adult mice lacking Nogo-A/B." Neuron 38, 187-199. Neuron 2007, 54:195-199. 10.1016/j.neuron.2007.04.005 17442242
    • (2007) Neuron , vol.54 , pp. 195-199
    • Cafferty, W.B.1    Kim, J.E.2    Lee, J.K.3    Strittmatter, S.M.4
  • 69
    • 0038414519 scopus 로고    scopus 로고
    • Lack of enhanced spinal regeneration in Nogo-deficient mice
    • 10.1016/S0896-6273(03)00225-3 12718856
    • Zheng B Ho C Li S Keirstead H Steward O Tessier-Lavigne M Lack of enhanced spinal regeneration in Nogo-deficient mice. Neuron 2003, 38:213-224. 10.1016/S0896-6273(03)00225-3 12718856
    • (2003) Neuron , vol.38 , pp. 213-224
    • Zheng, B.1    Ho, C.2    Li, S.3    Keirstead, H.4    Steward, O.5    Tessier-Lavigne, M.6
  • 70
    • 0038702465 scopus 로고    scopus 로고
    • No Nogo: Now where to go?
    • 10.1016/S0896-6273(03)00233-2 12718850
    • Woolf CJ No Nogo: Now where to go? Neuron 2003, 38:153-156. 10.1016/ S0896-6273(03)00233-2 12718850
    • (2003) Neuron , vol.38 , pp. 153-156
    • Woolf, C.J.1
  • 71
    • 12844272145 scopus 로고    scopus 로고
    • Genetic deletion of the Nogo receptor does not reduce neurite inhibition in vitro or promote corticospinal tract regeneration in vivo
    • 544342 15647357 10.1073/pnas.0409026102
    • Zheng B Atwal J Ho C Case L He XL Garcia KC Steward O Tessier-Lavigne M Genetic deletion of the Nogo receptor does not reduce neurite inhibition in vitro or promote corticospinal tract regeneration in vivo. Proc Natl Acad Sci USA 2005, 102:1205-1210. 544342 15647357 10.1073/pnas.0409026102
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1205-1210
    • Zheng, B.1    Atwal, J.2    Ho, C.3    Case, L.4    He, X.L.5    Garcia, K.C.6    Steward, O.7    Tessier-Lavigne, M.8
  • 72
    • 0037038435 scopus 로고    scopus 로고
    • P75 interacts with the Nogo receptor as a co-receptor for Nogo, MAG and OMgp
    • 10.1038/nature01176 12422217
    • Wang KC Kim JA Sivasankaran R Segal R He Z P75 interacts with the Nogo receptor as a co-receptor for Nogo, MAG and OMgp. Nature 2002, 420:74-78. 10.1038/nature01176 12422217
    • (2002) Nature , vol.420 , pp. 74-78
    • Wang, K.C.1    Kim, J.A.2    Sivasankaran, R.3    Segal, R.4    He, Z.5
  • 73
    • 20444365447 scopus 로고    scopus 로고
    • MAG induces regulated intramembrane proteolysis of the p75 neurotrophin receptor to inhibit neurite outgrowth
    • 10.1016/j.neuron.2005.05.029 15953414
    • Domeniconi M Zampieri N Spencer T Hilaire M Mellado W Chao MV Filbin MT MAG induces regulated intramembrane proteolysis of the p75 neurotrophin receptor to inhibit neurite outgrowth. Neuron 2005, 46:849-855. 10.1016/ j.neuron.2005.05.029 15953414
    • (2005) Neuron , vol.46 , pp. 849-855
    • Domeniconi, M.1    Zampieri, N.2    Spencer, T.3    Hilaire, M.4    Mellado, W.5    Chao, M.V.6    Filbin, M.T.7
  • 76
    • 13244255374 scopus 로고    scopus 로고
    • A TNF receptor family member, TROY, is a coreceptor with Nogo receptor in mediating the inhibitory activity of myelin inhibitors
    • 10.1016/j.neuron.2004.12.040 15694321
    • Park JB Yiu G Kaneko S Wang J Chang J He XL Garcia KC He Z A TNF receptor family member, TROY, is a coreceptor with Nogo receptor in mediating the inhibitory activity of myelin inhibitors. Neuron 2005, 45:345-351. 10.1016/j.neuron.2004.12.040 15694321
    • (2005) Neuron , vol.45 , pp. 345-351
    • Park, J.B.1    Yiu, G.2    Kaneko, S.3    Wang, J.4    Chang, J.5    He, X.L.6    Garcia, K.C.7    He, Z.8
  • 77
    • 19944432743 scopus 로고    scopus 로고
    • TAJ/TROY, an orphan TNF receptor family member, binds Nogo-66 receptor 1 and regulates axonal regeneration
    • 10.1016/j.neuron.2004.12.050 15694322
    • Shao Z Browning JL Lee X Scott ML Shulga-Morskaya S Allaire N Thill G Levesque M Sah D McCoy JM et al. TAJ/TROY, an orphan TNF receptor family member, binds Nogo-66 receptor 1 and regulates axonal regeneration. Neuron 2005, 45:353-359. 10.1016/j.neuron.2004.12.050 15694322
    • (2005) Neuron , vol.45 , pp. 353-359
    • Shao, Z.1    Browning, J.L.2    Lee, X.3    Scott, M.L.4    Shulga-Morskaya, S.5    Allaire, N.6    Thill, G.7    Levesque, M.8    Sah, D.9    McCoy, J.M.10
  • 78
    • 26444459836 scopus 로고    scopus 로고
    • EGFR activation mediates inhibition of axon regeneration by myelin and chondroitin sulfate proteoglycans
    • 10.1126/science.1115462 16210539
    • Koprivica V Cho KS Park JB Yiu G Atwal J Gore B Kim JA Lin E Tessier-Lavigne M Chen DF et al. EGFR activation mediates inhibition of axon regeneration by myelin and chondroitin sulfate proteoglycans. Science 2005, 310:106-110. 10.1126/science.1115462 16210539
    • (2005) Science , vol.310 , pp. 106-110
    • Koprivica, V.1    Cho, K.S.2    Park, J.B.3    Yiu, G.4    Atwal, J.5    Gore, B.6    Kim, J.A.7    Lin, E.8    Tessier-Lavigne, M.9    Chen, D.F.10
  • 80
    • 0038325765 scopus 로고    scopus 로고
    • Structure of the Nogo receptor ectodomain: A recognition module implicated in myelin inhibition
    • 10.1016/S0896-6273(03)00232-0 12718853
    • He XL Bazan JF G. M Park JB Wang K Tessier-Lavigne M He Z Garcia KC Structure of the Nogo receptor ectodomain: A recognition module implicated in myelin inhibition. Neuron 2003, 38:177-185. 10.1016/ S0896-6273(03)00232-0 12718853
    • (2003) Neuron , vol.38 , pp. 177-185
    • He, X.L.1    Bazan, J.F.G.M.2    Park, J.B.3    Wang, K.4    Tessier-Lavigne, M.5    He, Z.6    Garcia, K.C.7
  • 82
    • 0037443069 scopus 로고    scopus 로고
    • Rho kinase inhibition enhances axonal regeneration in the injured CNS
    • 12598630
    • Fournier AE Takizawa BT Strittmatter SM Rho kinase inhibition enhances axonal regeneration in the injured CNS. J Neurosci 2003, 23:1416-1423. 12598630
    • (2003) J Neurosci , vol.23 , pp. 1416-1423
    • Fournier, A.E.1    Takizawa, B.T.2    Strittmatter, S.M.3
  • 86
    • 4644357534 scopus 로고    scopus 로고
    • Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation
    • 10.1038/nm1088 15286784
    • He W Lu Y Qahwash I Hu XY Chang A Yan R Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation. Nat Med 2004, 10:959-965. 10.1038/nm1088 15286784
    • (2004) Nat Med , vol.10 , pp. 959-965
    • He, W.1    Lu, Y.2    Qahwash, I.3    Hu, X.Y.4    Chang, A.5    Yan, R.6
  • 87
    • 33748755837 scopus 로고    scopus 로고
    • Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid beta-protein
    • 10.1111/j.1460-9568.2006.05005.x 16965550
    • Murayama KS Kametani F Saito S Kume H Akiyama H Araki W Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid beta-protein. Eur J Neurosci 2006, 24:1237-1244. 10.1111/ j.1460-9568.2006.05005.x 16965550
    • (2006) Eur J Neurosci , vol.24 , pp. 1237-1244
    • Murayama, K.S.1    Kametani, F.2    Saito, S.3    Kume, H.4    Akiyama, H.5    Araki, W.6
  • 92
    • 34147208586 scopus 로고    scopus 로고
    • Increased expression of Noga-A in ALS muscle biopsies is not unique for this disease
    • 17626519
    • Wojcik S Engel WK Askanas V Increased expression of Noga-A in ALS muscle biopsies is not unique for this disease. Acta Myol 2006, 25:116-118. 17626519
    • (2006) Acta Myol , vol.25 , pp. 116-118
    • Wojcik, S.1    Engel, W.K.2    Askanas, V.3
  • 93
    • 33750527780 scopus 로고    scopus 로고
    • The neurite outgrowth inhibitor Nogo-A promotes denervation in an amyotrophic lateral sclerosis model
    • 1679784 17039253 10.1038/sj.embor.7400826
    • Jokic N Gonzalez de Aguilar JL Dimou L Lin S Fergani A Ruegg MA Schwab ME Dupuis L Loeffler JP The neurite outgrowth inhibitor Nogo-A promotes denervation in an amyotrophic lateral sclerosis model. EMBO Rep 2006, 7:1162-1167. 1679784 17039253 10.1038/sj.embor.7400826
    • (2006) EMBO Rep , vol.7 , pp. 1162-1167
    • Jokic, N.1    Gonzalez de Aguilar, J.L.2    Dimou, L.3    Lin, S.4    Fergani, A.5    Ruegg, M.A.6    Schwab, M.E.7    Dupuis, L.8    Loeffler, J.P.9
  • 94
    • 0344838573 scopus 로고    scopus 로고
    • Nogo (Reticulon 4) expression in innervated and denervated mouse skeletal muscle
    • 10.1016/S1044-7431(02)00036-2 12691732
    • Magnusson C Libelius R Tagerud S Nogo (Reticulon 4) expression in innervated and denervated mouse skeletal muscle. Mol Cell Neurosci 2003, 22:298-307. 10.1016/S1044-7431(02)00036-2 12691732
    • (2003) Mol Cell Neurosci , vol.22 , pp. 298-307
    • Magnusson, C.1    Libelius, R.2    Tagerud, S.3
  • 97
    • 33746536549 scopus 로고    scopus 로고
    • ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia
    • 1559503 16826525 10.1086/504927
    • Mannan AU Krawen P Sauter SM Boehm J Chronowska A Paulus W Neesen J Engel W ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia. Am J Hum Genet 2006, 79:351-357. 1559503 16826525 10.1086/504927
    • (2006) Am J Hum Genet , vol.79 , pp. 351-357
    • Mannan, A.U.1    Krawen, P.2    Sauter, S.M.3    Boehm, J.4    Chronowska, A.5    Paulus, W.6    Neesen, J.7    Engel, W.8
  • 98
    • 33646419824 scopus 로고    scopus 로고
    • Spastin, the most commonly mutated protein in hereditary spastic paraplegia interacts with Reticulon 1 an endoplasmic reticulum protein
    • 10.1007/s10048-006-0034-4 16602018
    • Mannan AU Boehm J Sauter SM Rauber A Byrne PC Neesen J Engel W Spastin, the most commonly mutated protein in hereditary spastic paraplegia interacts with Reticulon 1 an endoplasmic reticulum protein. Neurogenetics 2006, 7:93-103. 10.1007/s10048-006-0034-4 16602018
    • (2006) Neurogenetics , vol.7 , pp. 93-103
    • Mannan, A.U.1    Boehm, J.2    Sauter, S.M.3    Rauber, A.4    Byrne, P.C.5    Neesen, J.6    Engel, W.7
  • 99
    • 58149313410 scopus 로고    scopus 로고
    • ClustalW2 http://www.ebi.ac.uk/Tools/clustalw2
    • ClustalW2
  • 100
    • 58149309740 scopus 로고    scopus 로고
    • Phylo_win http://pbil.univ-lyon1.fr/software/phylowin.html
    • Phylo_win


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.