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Volumn 10, Issue 1, 2010, Pages

Phylogenetic analysis of ferlin genes reveals ancient eukaryotic origins

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTE; EVOLUTIONARY BIOLOGY; GENETIC ANALYSIS; GENOME; MEMBRANE; PHYLOGENETICS; PHYTOPLANKTON; PROTEIN; SPECIALIZATION; VERTEBRATE;

EID: 77955001359     PISSN: None     EISSN: 14712148     Source Type: Journal    
DOI: 10.1186/1471-2148-10-231     Document Type: Article
Times cited : (47)

References (49)
  • 1
    • 33750502406 scopus 로고    scopus 로고
    • Mutation impact on dysferlin inferred from database analysis and computer-based structural predictions
    • 10.1016/j.jns.2006.07.004. 16996541
    • Mutation impact on dysferlin inferred from database analysis and computer-based structural predictions. C Therrien D Dodig G Karpati M Sinnreich, J Neurol Sci 2006 250 71 78 10.1016/j.jns.2006.07.004 16996541
    • (2006) J Neurol Sci , vol.250 , pp. 71-78
    • Therrien, C.1    Dodig, D.2    Karpati, G.3    Sinnreich, M.4
  • 2
    • 17344363640 scopus 로고    scopus 로고
    • A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B
    • 10.1038/1689. 9731527
    • A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B. R Bashir S Britton T Strachan S Keers E Vafiadaki M Lako I Richard S Marchand N Bourg Z Argov, et al. Nat Genet 1998 20 37 42 10.1038/1689 9731527
    • (1998) Nat Genet , vol.20 , pp. 37-42
    • Bashir, R.1    Britton, S.2    Strachan, T.3    Keers, S.4    Vafiadaki, E.5    Lako, M.6    Richard, I.7    Marchand, S.8    Bourg, N.9    Argov, Z.10
  • 3
    • 33746054560 scopus 로고    scopus 로고
    • FER-1 regulates Ca2+ -mediated membrane fusion during C. elegans spermatogenesis
    • 10.1242/jcs.02980. 16735442
    • FER-1 regulates Ca2+ -mediated membrane fusion during C. elegans spermatogenesis. NL Washington S Ward, J Cell Sci 2006 119 2552 2562 10.1242/jcs.02980 16735442
    • (2006) J Cell Sci , vol.119 , pp. 2552-2562
    • Washington, N.L.1    Ward, S.2
  • 7
    • 0028014529 scopus 로고
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release
    • 10.1126/science.7904084. 7904084
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release. RA Steinhardt G Bi JM Alderton, Science 1994 263 390 393 10.1126/science.7904084 7904084
    • (1994) Science , vol.263 , pp. 390-393
    • Steinhardt, R.A.1    Bi, G.2    Alderton, J.M.3
  • 8
    • 0030801401 scopus 로고    scopus 로고
    • Large plasma membrane disruptions are rapidly resealed by Ca2+-dependent vesicle-vesicle fusion events
    • 10.1083/jcb.139.1.63. 9314529
    • Large plasma membrane disruptions are rapidly resealed by Ca2+-dependent vesicle-vesicle fusion events. M Terasaki K Miyake PL McNeil, J Cell Biol 1997 139 63 74 10.1083/jcb.139.1.63 9314529
    • (1997) J Cell Biol , vol.139 , pp. 63-74
    • Terasaki, M.1    Miyake, K.2    McNeil, P.L.3
  • 9
    • 40849118150 scopus 로고    scopus 로고
    • Repair of injured plasma membrane by rapid Ca2+-dependent endocytosis
    • 10.1083/jcb.200708010. 18316410
    • Repair of injured plasma membrane by rapid Ca2+-dependent endocytosis. V Idone C Tam JW Goss D Toomre M Pypaert NW Andrews, J Cell Biol 2008 180 905 914 10.1083/jcb.200708010 18316410
    • (2008) J Cell Biol , vol.180 , pp. 905-914
    • Idone, V.1    Tam, C.2    Goss, J.W.3    Toomre, D.4    Pypaert, M.5    Andrews, N.W.6
  • 10
    • 33749994043 scopus 로고    scopus 로고
    • Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse
    • 10.1016/j.cell.2006.08.040. 17055430
    • Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse. I Roux S Safieddine R Nouvian M Grati MC Simmler A Bahloul I Perfettini M Le Gall P Rostaing G Hamard, et al. Cell 2006 127 277 289 10.1016/j.cell.2006.08.040 17055430
    • (2006) Cell , vol.127 , pp. 277-289
    • Roux, I.1    Safieddine, S.2    Nouvian, R.3    Grati, M.4    Simmler, M.C.5    Bahloul, A.6    Perfettini, I.7    Le Gall, M.8    Rostaing, P.9    Hamard, G.10
  • 12
    • 12544256900 scopus 로고    scopus 로고
    • Evolutionarily conserved multiple C2 domain proteins with two transmembrane regions (MCTPs) and unusual Ca2+ binding properties
    • 10.1074/jbc.M407305200. 15528213
    • Evolutionarily conserved multiple C2 domain proteins with two transmembrane regions (MCTPs) and unusual Ca2+ binding properties. OH Shin W Han Y Wang TC Sudhof, J Biol Chem 2005 280 1641 1651 10.1074/jbc.M407305200 15528213
    • (2005) J Biol Chem , vol.280 , pp. 1641-1651
    • Shin, O.H.1    Han, W.2    Wang, Y.3    Sudhof, T.C.4
  • 13
    • 34247280982 scopus 로고    scopus 로고
    • E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 domains
    • 10.1073/pnas.0611725104. 17360437
    • E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 domains. SW Min WP Chang TC Sudhof, Proc Natl Acad Sci USA 2007 104 3823 3828 10.1073/pnas.0611725104 17360437
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 3823-3828
    • Min, S.W.1    Chang, W.P.2    Sudhof, T.C.3
  • 14
    • 0027332736 scopus 로고
    • A single C2 domain from synaptotagmin i is sufficient for high affinity Ca2+/phospholipid binding
    • 8253763
    • A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding. BA Davletov TC Sudhof, J Biol Chem 1993 268 26386 26390 8253763
    • (1993) J Biol Chem , vol.268 , pp. 26386-26390
    • Davletov, B.A.1    Sudhof, T.C.2
  • 15
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • 10.1002/pro.5560051201. 8976547
    • The C2 domain calcium-binding motif: structural and functional diversity. EA Nalefski JJ Falke, Protein Sci 1996 5 2375 2390 10.1002/pro.5560051201 8976547
    • (1996) Protein Sci , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 16
    • 0032568662 scopus 로고    scopus 로고
    • C2-domains, structure and function of a universal Ca2+-binding domain
    • 10.1074/jbc.273.26.15879. 9632630
    • C2-domains, structure and function of a universal Ca2+-binding domain. J Rizo TC Sudhof, J Biol Chem 1998 273 15879 15882 10.1074/jbc.273.26.15879 9632630
    • (1998) J Biol Chem , vol.273 , pp. 15879-15882
    • Rizo, J.1    Sudhof, T.C.2
  • 17
    • 0031019191 scopus 로고    scopus 로고
    • Synaptotagmin-syntaxin interaction: The C2 domain as a Ca2+-dependent electrostatic switch
    • 10.1016/S0896-6273(01)80052-0. 9010211
    • Synaptotagmin-syntaxin interaction: the C2 domain as a Ca2+-dependent electrostatic switch. X Shao C Li I Fernandez X Zhang TC Sudhof J Rizo, Neuron 1997 18 133 142 10.1016/S0896-6273(01)80052-0 9010211
    • (1997) Neuron , vol.18 , pp. 133-142
    • Shao, X.1    Li, C.2    Fernandez, I.3    Zhang, X.4    Sudhof, T.C.5    Rizo, J.6
  • 18
    • 33748324514 scopus 로고    scopus 로고
    • Membrane binding and subcellular targeting of C2 domains
    • 16945584
    • Membrane binding and subcellular targeting of C2 domains. W Cho RV Stahelin, Biochim Biophys Acta 2006 1761 838 849 16945584
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 838-849
    • Cho, W.1    Stahelin, R.V.2
  • 19
    • 34548009359 scopus 로고    scopus 로고
    • Dysferlin and muscle membrane repair
    • 10.1016/j.ceb.2007.07.001. 17662592
    • Dysferlin and muscle membrane repair. R Han KP Campbell, Curr Opin Cell Biol 2007 19 409 416 10.1016/j.ceb.2007.07.001 17662592
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 409-416
    • Han, R.1    Campbell, K.P.2
  • 20
    • 41649109400 scopus 로고    scopus 로고
    • Dysferlin domain-containing proteins, Pex30p and Pex31p, localized to two compartments, control the number and size of oleate-induced peroxisomes in Pichia pastoris
    • 10.1091/mbc.E07-10-1042. 18094040
    • Dysferlin domain-containing proteins, Pex30p and Pex31p, localized to two compartments, control the number and size of oleate-induced peroxisomes in Pichia pastoris. M Yan DA Rachubinski S Joshi RA Rachubinski S Subramani, Mol Biol Cell 2008 19 885 898 10.1091/mbc.E07-10-1042 18094040
    • (2008) Mol Biol Cell , vol.19 , pp. 885-898
    • Yan, M.1    Rachubinski, D.A.2    Joshi, S.3    Rachubinski, R.A.4    Subramani, S.5
  • 21
    • 44549087843 scopus 로고    scopus 로고
    • Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b
    • 10.1016/j.jmb.2008.04.046. 18495154
    • Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b. P Patel R Harris SM Geddes EM Strehle JD Watson R Bashir K Bushby PC Driscoll NH Keep, J Mol Biol 2008 379 981 990 10.1016/j.jmb.2008.04.046 18495154
    • (2008) J Mol Biol , vol.379 , pp. 981-990
    • Patel, P.1    Harris, R.2    Geddes, S.M.3    Strehle, E.M.4    Watson, J.D.5    Bashir, R.6    Bushby, K.7    Driscoll, P.C.8    Keep, N.H.9
  • 22
    • 34547792309 scopus 로고    scopus 로고
    • In silico functional and structural characterisation of ferlin proteins by mapping disease-causing mutations and evolutionary information onto three-dimensional models of their C2 domains
    • 10.1016/j.jns.2007.04.016. 17512949
    • In silico functional and structural characterisation of ferlin proteins by mapping disease-causing mutations and evolutionary information onto three-dimensional models of their C2 domains. JL Jimenez R Bashir, J Neurol Sci 2007 260 114 123 10.1016/j.jns.2007.04.016 17512949
    • (2007) J Neurol Sci , vol.260 , pp. 114-123
    • Jimenez, J.L.1    Bashir, R.2
  • 23
    • 0024988375 scopus 로고
    • Protein database searches for multiple alignments
    • 10.1073/pnas.87.14.5509. 2196570
    • Protein database searches for multiple alignments. SF Altschul DJ Lipman, Proc Natl Acad Sci USA 1990 87 5509 5513 10.1073/pnas.87.14.5509 2196570
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5509-5513
    • Altschul, S.F.1    Lipman, D.J.2
  • 24
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • 10.1073/pnas.95.11.5857. 9600884
    • SMART, a simple modular architecture research tool: identification of signaling domains. J Schultz F Milpetz P Bork CP Ponting, Proc Natl Acad Sci USA 1998 95 5857 5864 10.1073/pnas.95.11.5857 9600884
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 26
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier transform
    • 10.1093/nar/gkf436. 12136088
    • MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. K Katoh K Misawa K Kuma T Miyata, Nucleic Acids Res 2002 30 3059 3066 10.1093/nar/gkf436 12136088
    • (2002) Nucleic Acids Res , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 27
    • 0034791613 scopus 로고    scopus 로고
    • CHROMA: Consensus-based colouring of multiple alignments for publication
    • 10.1093/bioinformatics/17.9.845. 11590103
    • CHROMA: consensus-based colouring of multiple alignments for publication. L Goodstadt CP Ponting, Bioinformatics 2001 17 845 846 10.1093/bioinformatics/ 17.9.845 11590103
    • (2001) Bioinformatics , vol.17 , pp. 845-846
    • Goodstadt, L.1    Ponting, C.P.2
  • 28
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • 10.1093/nar/gkn238. 18463136
    • The Jpred 3 secondary structure prediction server. C Cole JD Barber GJ Barton, Nucleic Acids Res 2008 36 197 201 10.1093/nar/gkn238 18463136
    • (2008) Nucleic Acids Res , vol.36 , pp. 23197-201
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 29
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European Molecular Biology Open Software Suite
    • 10.1016/S0168-9525(00)02024-2. 10827456
    • EMBOSS: the European Molecular Biology Open Software Suite. P Rice I Longden A Bleasby, Trends Genet 2000 16 276 277 10.1016/S0168-9525(00)02024-2 10827456
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 30
    • 0028986240 scopus 로고
    • Structure of the first C2 domain of synaptotagmin I: A novel Ca2+/phospholipid-binding fold
    • 10.1016/0092-8674(95)90296-1. 7697723
    • Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold. RB Sutton BA Davletov AM Berghuis TC Sudhof SR Sprang, Cell 1995 80 929 938 10.1016/0092-8674(95)90296-1 7697723
    • (1995) Cell , vol.80 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3    Sudhof, T.C.4    Sprang, S.R.5
  • 32
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • 10.1080/10635150390235520. 14530136
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. S Guindon O Gascuel, Syst Biol 2003 52 696 704 10.1080/10635150390235520 14530136
    • (2003) Syst Biol , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 34
    • 0030473920 scopus 로고    scopus 로고
    • Gen(om)e duplications in the evolution of early vertebrates
    • 10.1016/S0959-437X(96)80026-8. 8994842
    • Gen(om)e duplications in the evolution of early vertebrates. A Sidow, Curr Opin Genet Dev 1996 6 715 722 10.1016/S0959-437X(96)80026-8 8994842
    • (1996) Curr Opin Genet Dev , vol.6 , pp. 715-722
    • Sidow, A.1
  • 35
    • 34247388474 scopus 로고    scopus 로고
    • Complex regulation and multiple developmental functions of misfire, the Drosophila melanogaster ferlin gene
    • 10.1186/1471-213X-7-21. 17386097
    • Complex regulation and multiple developmental functions of misfire, the Drosophila melanogaster ferlin gene. MK Smith BT Wakimoto, BMC Dev Biol 2007 7 21 10.1186/1471-213X-7-21 17386097
    • (2007) BMC Dev Biol , vol.7 , pp. 21
    • Smith, M.K.1    Wakimoto, B.T.2
  • 36
    • 0030952081 scopus 로고    scopus 로고
    • The evolutionary pressure to inactivate. A subclass of synaptotagmins with an amino acid substitution that abolishes Ca2+ binding
    • 10.1074/jbc.272.22.14314. 9162066
    • The evolutionary pressure to inactivate. A subclass of synaptotagmins with an amino acid substitution that abolishes Ca2+ binding. C von Poser K Ichtchenko X Shao J Rizo TC Sudhof, J Biol Chem 1997 272 14314 14319 10.1074/jbc.272.22.14314 9162066
    • (1997) J Biol Chem , vol.272 , pp. 14314-14319
    • Von Poser, C.1    Ichtchenko, K.2    Shao, X.3    Rizo, J.4    Sudhof, T.C.5
  • 37
    • 67649415132 scopus 로고    scopus 로고
    • Role of the parasite and host cytoskeleton in apicomplexa parasitism
    • 10.1016/j.chom.2009.05.013. 19527887
    • Role of the parasite and host cytoskeleton in apicomplexa parasitism. K Frenal D Soldati-Favre, Cell Host Microbe 2009 5 602 611 10.1016/j.chom.2009.05. 013 19527887
    • (2009) Cell Host Microbe , vol.5 , pp. 602-611
    • Frenal, K.1    Soldati-Favre, D.2
  • 38
    • 0031808982 scopus 로고    scopus 로고
    • The parasitophorous vacuole membrane surrounding Plasmodium and Toxoplasma: An unusual compartment in infected cells
    • 9580555
    • The parasitophorous vacuole membrane surrounding Plasmodium and Toxoplasma: an unusual compartment in infected cells. K Lingelbach KA Joiner, J Cell Sci 1998 111 Pt 11 1467 1475 9580555
    • (1998) J Cell Sci , vol.111 , Issue.PART 11 , pp. 1467-1475
    • Lingelbach, K.1    Joiner, K.A.2
  • 39
    • 34548221348 scopus 로고    scopus 로고
    • Dysferlin is expressed in human placenta but does not associate with caveolin
    • 10.1095/biolreprod.107.062190. 17554076
    • Dysferlin is expressed in human placenta but does not associate with caveolin. DD Vandre WEt Ackerman DA Kniss AK Tewari M Mori T Takizawa JM Robinson, Biol Reprod 2007 77 533 542 10.1095/biolreprod.107.062190 17554076
    • (2007) Biol Reprod , vol.77 , pp. 533-542
    • Vandre, D.D.1    Wet, A.2    Kniss, D.A.3    Tewari, A.K.4    Mori, M.5    Takizawa, T.6    Robinson, J.M.7
  • 40
    • 33846148653 scopus 로고    scopus 로고
    • Sperm plasma membrane breakdown during Drosophila fertilization requires sneaky, an acrosomal membrane protein
    • 10.1242/dev.02671. 17092953
    • Sperm plasma membrane breakdown during Drosophila fertilization requires sneaky, an acrosomal membrane protein. KL Wilson KR Fitch BT Bafus BT Wakimoto, Development 2006 133 4871 4879 10.1242/dev.02671 17092953
    • (2006) Development , vol.133 , pp. 4871-4879
    • Wilson, K.L.1    Fitch, K.R.2    Bafus, B.T.3    Wakimoto, B.T.4
  • 42
    • 33748742531 scopus 로고    scopus 로고
    • Identification and characterization of a novel human dysferlin transcript: Dysferlin-v1
    • 10.1007/s00439-006-0230-1. 16896923
    • Identification and characterization of a novel human dysferlin transcript: dysferlin-v1. ZA Pramono PS Lai CL Tan S Takeda WC Yee, Hum Genet 2006 120 410 419 10.1007/s00439-006-0230-1 16896923
    • (2006) Hum Genet , vol.120 , pp. 410-419
    • Pramono, Z.A.1    Lai, P.S.2    Tan, C.L.3    Takeda, S.4    Yee, W.C.5
  • 43
    • 33847406320 scopus 로고    scopus 로고
    • AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration
    • 10.1096/fj.06-6628com. 17185750
    • AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration. Y Huang SH Laval A van Remoortere J Baudier C Benaud LV Anderson V Straub A Deelder RR Frants JT den Dunnen, et al. FASEB J 2007 21 732 742 10.1096/fj.06-6628com 17185750
    • (2007) FASEB J , vol.21 , pp. 732-742
    • Huang, Y.1    Laval, S.H.2    Van Remoortere, A.3    Baudier, J.4    Benaud, C.5    Anderson, L.V.6    Straub, V.7    Deelder, A.8    Frants, R.R.9    Den Dunnen, J.T.10
  • 44
    • 64849112183 scopus 로고    scopus 로고
    • Characterization of Lipid Binding Specificities of Dysferlin C2 Domains Reveals Novel Interactions with Phosphoinositides (dagger)
    • 10.1021/bi802242r. 19253956
    • Characterization of Lipid Binding Specificities of Dysferlin C2 Domains Reveals Novel Interactions with Phosphoinositides (dagger). C Therrien S Di Fulvio S Pickles M Sinnreich, Biochemistry 2009 48 2377 2384 10.1021/bi802242r 19253956
    • (2009) Biochemistry , vol.48 , pp. 2377-2384
    • Therrien, C.1    Di Fulvio, S.2    Pickles, S.3    Sinnreich, M.4
  • 45
    • 0037458711 scopus 로고    scopus 로고
    • Mechanism of calcium-independent synaptotagmin binding to target SNAREs
    • 10.1074/jbc.C200692200. 12496268
    • Mechanism of calcium-independent synaptotagmin binding to target SNAREs. C Rickman B Davletov, J Biol Chem 2003 278 5501 5504 10.1074/jbc.C200692200 12496268
    • (2003) J Biol Chem , vol.278 , pp. 5501-5504
    • Rickman, C.1    Davletov, B.2
  • 46
    • 59449093847 scopus 로고    scopus 로고
    • Direct interaction of otoferlin with syntaxin 1A, SNAP-25, and the L-type voltage-gated calcium channel Cav1.3
    • 10.1074/jbc.M803605200. 19004828
    • Direct interaction of otoferlin with syntaxin 1A, SNAP-25, and the L-type voltage-gated calcium channel Cav1.3. NA Ramakrishnan MJ Drescher DG Drescher, J Biol Chem 2009 284 1364 1372 10.1074/jbc.M803605200 19004828
    • (2009) J Biol Chem , vol.284 , pp. 1364-1372
    • Ramakrishnan, N.A.1    Drescher, M.J.2    Drescher, D.G.3
  • 47
    • 67649884533 scopus 로고    scopus 로고
    • Solution and membrane-bound conformations of the tandem C2A and C2B domains of synaptotagmin 1: Evidence for bilayer bridging
    • 10.1016/j.jmb.2009.06.007. 19501597
    • Solution and membrane-bound conformations of the tandem C2A and C2B domains of synaptotagmin 1: Evidence for bilayer bridging. DZ Herrick W Kuo H Huang CD Schwieters JF Ellena DS Cafiso, J Mol Biol 2009 390 913 923 10.1016/j.jmb.2009.06.007 19501597
    • (2009) J Mol Biol , vol.390 , pp. 913-923
    • Herrick, D.Z.1    Kuo, W.2    Huang, H.3    Schwieters, C.D.4    Ellena, J.F.5    Cafiso, D.S.6
  • 48
    • 0035904238 scopus 로고    scopus 로고
    • The tandem C2 domains of synaptotagmin contain redundant Ca2+ binding sites that cooperate to engage t-SNAREs and trigger exocytosis
    • 10.1083/jcb.200105020. 11551981
    • The tandem C2 domains of synaptotagmin contain redundant Ca2+ binding sites that cooperate to engage t-SNAREs and trigger exocytosis. CA Earles J Bai P Wang ER Chapman, J Cell Biol 2001 154 1117 1123 10.1083/jcb.200105020 11551981
    • (2001) J Cell Biol , vol.154 , pp. 1117-1123
    • Earles, C.A.1    Bai, J.2    Wang, P.3    Chapman, E.R.4
  • 49
    • 0036385643 scopus 로고    scopus 로고
    • Adeno-associated virus vector-mediated minidystrophin gene therapy improves dystrophic muscle contractile function in mdx mice
    • 10.1089/10430340260185085. 12215266
    • Adeno-associated virus vector-mediated minidystrophin gene therapy improves dystrophic muscle contractile function in mdx mice. J Watchko T O'Day B Wang L Zhou Y Tang J Li X Xiao, Hum Gene Ther 2002 13 1451 1460 10.1089/10430340260185085 12215266
    • (2002) Hum Gene Ther , vol.13 , pp. 1451-1460
    • Watchko, J.1    O'Day, T.2    Wang, B.3    Zhou, L.4    Tang, Y.5    Li, J.6    Xiao, X.7


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