메뉴 건너뛰기




Volumn 35, Issue 11, 2012, Pages 671-680

Otoferlin: A multi-C 2 domain protein essential for hearing

Author keywords

Calcium; Ferlins; Fusion; Hair cell; Priming; Synaptic vesicle

Indexed keywords

CALCIUM; MEMBRANE PROTEIN; OTOFERLIN; PHOSPHOLIPID; UNCLASSIFIED DRUG; OTOF PROTEIN, HUMAN; OTOFERLIN PROTEIN, MOUSE;

EID: 84867906699     PISSN: 01662236     EISSN: 1878108X     Source Type: Journal    
DOI: 10.1016/j.tins.2012.08.002     Document Type: Review
Times cited : (110)

References (125)
  • 1
    • 0033006442 scopus 로고    scopus 로고
    • SNARE complex at the ribbon synapses of cochlear hair cells: analysis of synaptic vesicle- and synaptic membrane-associated proteins
    • Safieddine S., Wenthold R.J. SNARE complex at the ribbon synapses of cochlear hair cells: analysis of synaptic vesicle- and synaptic membrane-associated proteins. Eur. J. Neurosci. 1999, 11:803-812.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 803-812
    • Safieddine, S.1    Wenthold, R.J.2
  • 2
    • 67649342625 scopus 로고    scopus 로고
    • Complexin-I is required for high-fidelity transmission at the endbulb of held auditory synapse
    • Strenzke N., et al. Complexin-I is required for high-fidelity transmission at the endbulb of held auditory synapse. J. Neurosci. 2009, 29:7991-8004.
    • (2009) J. Neurosci. , vol.29 , pp. 7991-8004
    • Strenzke, N.1
  • 3
    • 77956850256 scopus 로고    scopus 로고
    • Molecular anatomy of the hair cell's ribbon synapse
    • Uthaiah R.C., Hudspeth A.J. Molecular anatomy of the hair cell's ribbon synapse. J. Neurosci. 2010, 30:12387-12399.
    • (2010) J. Neurosci. , vol.30 , pp. 12387-12399
    • Uthaiah, R.C.1    Hudspeth, A.J.2
  • 4
    • 79953219741 scopus 로고    scopus 로고
    • Exocytosis at the hair cell ribbon synapse apparently operates without neuronal SNARE proteins
    • Nouvian R., et al. Exocytosis at the hair cell ribbon synapse apparently operates without neuronal SNARE proteins. Nat. Neurosci. 2011, 14:411-413.
    • (2011) Nat. Neurosci. , vol.14 , pp. 411-413
    • Nouvian, R.1
  • 5
    • 0032947634 scopus 로고    scopus 로고
    • A mutation in OTOF, encoding otoferlin, a FER-1-like protein, causes DFNB9, a nonsyndromic form of deafness
    • Yasunaga S., et al. A mutation in OTOF, encoding otoferlin, a FER-1-like protein, causes DFNB9, a nonsyndromic form of deafness. Nat. Genet. 1999, 21:363-369.
    • (1999) Nat. Genet. , vol.21 , pp. 363-369
    • Yasunaga, S.1
  • 6
    • 48349111572 scopus 로고    scopus 로고
    • Impairment of SLC17A8 encoding vesicular glutamate transporter-3, VGLUT3, underlies nonsyndromic deafness DFNA25 and inner hair cell dysfunction in null mice
    • Ruel J., et al. Impairment of SLC17A8 encoding vesicular glutamate transporter-3, VGLUT3, underlies nonsyndromic deafness DFNA25 and inner hair cell dysfunction in null mice. Am. J. Hum. Genet. 2008, 83:278-292.
    • (2008) Am. J. Hum. Genet. , vol.83 , pp. 278-292
    • Ruel, J.1
  • 7
    • 78650676678 scopus 로고    scopus 로고
    • Loss of Ca(v)1.3 (CACNA1D) function in a human channelopathy with bradycardia and congenital deafness
    • Baig S.M., et al. Loss of Ca(v)1.3 (CACNA1D) function in a human channelopathy with bradycardia and congenital deafness. Nat. Neurosci. 2011, 14:77-84.
    • (2011) Nat. Neurosci. , vol.14 , pp. 77-84
    • Baig, S.M.1
  • 8
    • 33749994043 scopus 로고    scopus 로고
    • Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse
    • Roux I., et al. Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse. Cell 2006, 127:277-289.
    • (2006) Cell , vol.127 , pp. 277-289
    • Roux, I.1
  • 9
    • 77954143206 scopus 로고    scopus 로고
    • Hearing requires otoferlin-dependent efficient replenishment of synaptic vesicles in hair cells
    • PangrŠič T., et al. Hearing requires otoferlin-dependent efficient replenishment of synaptic vesicles in hair cells. Nat. Neurosci. 2010, 13:869-876.
    • (2010) Nat. Neurosci. , vol.13 , pp. 869-876
    • Pangršič, T.1
  • 10
    • 0034616911 scopus 로고    scopus 로고
    • 2+ channels
    • 2+ channels. Cell 2000, 102:89-97.
    • (2000) Cell , vol.102 , pp. 89-97
    • Platzer, J.1
  • 11
    • 0345491881 scopus 로고    scopus 로고
    • Cav1.3 channels are essential for development and presynaptic activity of cochlear inner hair cells
    • Brandt A., et al. Cav1.3 channels are essential for development and presynaptic activity of cochlear inner hair cells. J. Neurosci. 2003, 23:10832-10840.
    • (2003) J. Neurosci. , vol.23 , pp. 10832-10840
    • Brandt, A.1
  • 12
    • 38149120796 scopus 로고    scopus 로고
    • Sensorineural deafness and seizures in mice lacking vesicular glutamate transporter 3
    • Seal R.P., et al. Sensorineural deafness and seizures in mice lacking vesicular glutamate transporter 3. Neuron 2008, 57:263-275.
    • (2008) Neuron , vol.57 , pp. 263-275
    • Seal, R.P.1
  • 13
    • 33845387728 scopus 로고    scopus 로고
    • Diagnostik und Therapie der auditorischen Synaptopathie/Neuropathie
    • Moser T., et al. Diagnostik und Therapie der auditorischen Synaptopathie/Neuropathie. HNO 2006, 54:833-841.
    • (2006) HNO , vol.54 , pp. 833-841
    • Moser, T.1
  • 14
    • 84882541775 scopus 로고    scopus 로고
    • Perspectives on auditory neuropathy: disorders of inner hair cell, auditory nerve, and their synapse
    • Academic Press, Audition
    • Starr A., et al. Perspectives on auditory neuropathy: disorders of inner hair cell, auditory nerve, and their synapse. The Senses: A Comprehensive Reference 2008, Vol. 3, Audition:397-412. Academic Press.
    • (2008) The Senses: A Comprehensive Reference , vol.3 , pp. 397-412
    • Starr, A.1
  • 15
    • 77953275175 scopus 로고    scopus 로고
    • Synaptopathy: dysfunction of synaptic function?
    • Brose N., et al. Synaptopathy: dysfunction of synaptic function?. Biochem. Soc. Trans. 2010, 38:443-444.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 443-444
    • Brose, N.1
  • 17
    • 39749132828 scopus 로고    scopus 로고
    • Calcium- and otoferlin-dependent exocytosis by immature outer hair cells
    • Beurg M., et al. Calcium- and otoferlin-dependent exocytosis by immature outer hair cells. J. Neurosci. 2008, 28:1798-1803.
    • (2008) J. Neurosci. , vol.28 , pp. 1798-1803
    • Beurg, M.1
  • 18
    • 69449092161 scopus 로고    scopus 로고
    • Otoferlin is critical for a highly sensitive and linear calcium-dependent exocytosis at vestibular hair cell ribbon synapses
    • Dulon D., et al. Otoferlin is critical for a highly sensitive and linear calcium-dependent exocytosis at vestibular hair cell ribbon synapses. J. Neurosci. 2009, 29:10474-10487.
    • (2009) J. Neurosci. , vol.29 , pp. 10474-10487
    • Dulon, D.1
  • 19
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • Augustin I., et al. Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles. Nature 1999, 400:457-461.
    • (1999) Nature , vol.400 , pp. 457-461
    • Augustin, I.1
  • 20
    • 0037172972 scopus 로고    scopus 로고
    • Total arrest of spontaneous and evoked synaptic transmission but normal synaptogenesis in the absence of Munc13-mediated vesicle priming
    • Varoqueaux F., et al. Total arrest of spontaneous and evoked synaptic transmission but normal synaptogenesis in the absence of Munc13-mediated vesicle priming. Proc. Natl Acad. Sci. U. S. A. 2002, 99:9037-9042.
    • (2002) Proc. Natl Acad. Sci. U. S. A. , vol.99 , pp. 9037-9042
    • Varoqueaux, F.1
  • 21
    • 0028061861 scopus 로고
    • 2+ sensor for transmitter release at a central synapse
    • 2+ sensor for transmitter release at a central synapse. Cell 1994, 79:717-727.
    • (1994) Cell , vol.79 , pp. 717-727
    • Geppert, M.1
  • 22
    • 0027974130 scopus 로고
    • Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants
    • Littleton J.T., et al. Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants. Proc. Natl. Acad. Sci. U. S. A. 1994, 91:10888-10892.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 10888-10892
    • Littleton, J.T.1
  • 23
    • 3042796387 scopus 로고    scopus 로고
    • Synaptotagmin I synchronizes transmitter release in mouse hippocampal neurons
    • Nishiki T., Augustine G.J. Synaptotagmin I synchronizes transmitter release in mouse hippocampal neurons. J. Neurosci. 2004, 24:6127-6132.
    • (2004) J. Neurosci. , vol.24 , pp. 6127-6132
    • Nishiki, T.1    Augustine, G.J.2
  • 24
    • 67049114053 scopus 로고    scopus 로고
    • Autapses and networks of hippocampal neurons exhibit distinct synaptic transmission phenotypes in the absence of synaptotagmin I
    • Liu H., et al. Autapses and networks of hippocampal neurons exhibit distinct synaptic transmission phenotypes in the absence of synaptotagmin I. J. Neurosci. 2009, 29:7395-7403.
    • (2009) J. Neurosci. , vol.29 , pp. 7395-7403
    • Liu, H.1
  • 25
    • 0037027739 scopus 로고    scopus 로고
    • Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release
    • Yoshihara M., Littleton J.T. Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release. Neuron 2002, 36:897-908.
    • (2002) Neuron , vol.36 , pp. 897-908
    • Yoshihara, M.1    Littleton, J.T.2
  • 26
    • 59449093847 scopus 로고    scopus 로고
    • Direct interaction of otoferlin with syntaxin 1A, SNAP-25, and the L-type voltage-gated calcium channel Cav1. 3
    • Ramakrishnan N.A., et al. Direct interaction of otoferlin with syntaxin 1A, SNAP-25, and the L-type voltage-gated calcium channel Cav1. 3. J. Biol. Chem. 2009, 284:1364-1372.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1364-1372
    • Ramakrishnan, N.A.1
  • 27
    • 77957731333 scopus 로고    scopus 로고
    • Otoferlin is a calcium sensor that directly regulates SNARE-mediated membrane fusion
    • Johnson C.P., Chapman E.R. Otoferlin is a calcium sensor that directly regulates SNARE-mediated membrane fusion. J. Cell Biol. 2010, 191:187-197.
    • (2010) J. Cell Biol. , vol.191 , pp. 187-197
    • Johnson, C.P.1    Chapman, E.R.2
  • 28
    • 79551689695 scopus 로고    scopus 로고
    • 2A domain of otoferlin reveals an unconventional top loop region
    • 2A domain of otoferlin reveals an unconventional top loop region. J. Mol. Biol. 2011, 406:479-490.
    • (2011) J. Mol. Biol. , vol.406 , pp. 479-490
    • Helfmann, S.1
  • 29
    • 79955777937 scopus 로고    scopus 로고
    • Probing the functional equivalence of otoferlin and synaptotagmin 1 in exocytosis
    • Reisinger E., et al. probing the functional equivalence of otoferlin and synaptotagmin 1 in exocytosis. J. Neurosci. 2011, 31:4886.
    • (2011) J. Neurosci. , vol.31 , pp. 4886
    • Reisinger, E.1
  • 30
    • 33847407503 scopus 로고    scopus 로고
    • A forward genetics screen in mice identifies recessive deafness traits and reveals that pejvakin is essential for outer hair cell function
    • Schwander M., et al. A forward genetics screen in mice identifies recessive deafness traits and reveals that pejvakin is essential for outer hair cell function. J. Neurosci. 2007, 27:2163-2175.
    • (2007) J. Neurosci. , vol.27 , pp. 2163-2175
    • Schwander, M.1
  • 31
    • 52049106127 scopus 로고    scopus 로고
    • Multiple roles of calcium ions in the regulation of neurotransmitter release
    • Neher E., Sakaba T. Multiple roles of calcium ions in the regulation of neurotransmitter release. Neuron 2008, 59:861-872.
    • (2008) Neuron , vol.59 , pp. 861-872
    • Neher, E.1    Sakaba, T.2
  • 32
    • 0346874341 scopus 로고    scopus 로고
    • Synaptotagmin I is necessary for compensatory synaptic vesicle endocytosis in vivo
    • Poskanzer K.E., et al. Synaptotagmin I is necessary for compensatory synaptic vesicle endocytosis in vivo. Nature 2003, 426:559-563.
    • (2003) Nature , vol.426 , pp. 559-563
    • Poskanzer, K.E.1
  • 33
    • 9344268267 scopus 로고    scopus 로고
    • Kinetic efficiency of endocytosis at mammalian CNS synapses requires synaptotagmin I
    • Nicholson-Tomishima K., Ryan T.A. Kinetic efficiency of endocytosis at mammalian CNS synapses requires synaptotagmin I. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:16648-16652.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16648-16652
    • Nicholson-Tomishima, K.1    Ryan, T.A.2
  • 34
    • 84856284553 scopus 로고    scopus 로고
    • Uncoupling the roles of synaptotagmin I during endo- and exocytosis of synaptic vesicles
    • Yao J., et al. Uncoupling the roles of synaptotagmin I during endo- and exocytosis of synaptic vesicles. Nat. Neurosci. 2012, 15:243-249.
    • (2012) Nat. Neurosci. , vol.15 , pp. 243-249
    • Yao, J.1
  • 35
    • 0034681118 scopus 로고    scopus 로고
    • Kinetics of exocytosis and endocytosis at the cochlear inner hair cell afferent synapse of the mouse
    • Moser T., Beutner D. Kinetics of exocytosis and endocytosis at the cochlear inner hair cell afferent synapse of the mouse. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:883.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 883
    • Moser, T.1    Beutner, D.2
  • 36
    • 13844252060 scopus 로고    scopus 로고
    • Evidence that rapid vesicle replenishment of the synaptic ribbon mediates recovery from short-term adaptation at the hair cell afferent synapse
    • Spassova M.A., et al. Evidence that rapid vesicle replenishment of the synaptic ribbon mediates recovery from short-term adaptation at the hair cell afferent synapse. J. Assoc. Res. Otolaryngol. 2004, 5:376-390.
    • (2004) J. Assoc. Res. Otolaryngol. , vol.5 , pp. 376-390
    • Spassova, M.A.1
  • 37
    • 79955773909 scopus 로고    scopus 로고
    • 2+ dependent at auditory hair cell synapses
    • 2+ dependent at auditory hair cell synapses. J. Neurosci. 2011, 31:5682-5692.
    • (2011) J. Neurosci. , vol.31 , pp. 5682-5692
    • Cho, S.1
  • 38
    • 81255143007 scopus 로고    scopus 로고
    • 2+ nanodomains beneath the ribbon promote highly synchronous multivesicular release at hair cell synapses
    • 2+ nanodomains beneath the ribbon promote highly synchronous multivesicular release at hair cell synapses. J. Neurosci. 2011, 31:16637-16650.
    • (2011) J. Neurosci. , vol.31 , pp. 16637-16650
    • Graydon, C.W.1
  • 39
    • 80053584605 scopus 로고    scopus 로고
    • Developmental acquisition of a rapid calcium-regulated vesicle supply allows sustained high rates of exocytosis in auditory hair cells
    • Levic S., et al. Developmental acquisition of a rapid calcium-regulated vesicle supply allows sustained high rates of exocytosis in auditory hair cells. PLoS ONE 2011, 6:e25714.
    • (2011) PLoS ONE , vol.6
    • Levic, S.1
  • 40
    • 36049039908 scopus 로고    scopus 로고
    • Time course and calcium dependence of transmitter release at a single ribbon synapse
    • Goutman J.D., Glowatzki E. Time course and calcium dependence of transmitter release at a single ribbon synapse. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:16341-16346.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 16341-16346
    • Goutman, J.D.1    Glowatzki, E.2
  • 41
    • 0019312709 scopus 로고
    • Morphological differences among radial afferent fibers in the cat cochlea: An electron-microscopic study of serial sections
    • Liberman M.C. Morphological differences among radial afferent fibers in the cat cochlea: An electron-microscopic study of serial sections. Hear. Res. 1980, 3:45-63.
    • (1980) Hear. Res. , vol.3 , pp. 45-63
    • Liberman, M.C.1
  • 43
    • 84859318083 scopus 로고    scopus 로고
    • Spike encoding of neurotransmitter release timing by spiral ganglion neurons of the cochlea
    • Rutherford M.A., et al. Spike encoding of neurotransmitter release timing by spiral ganglion neurons of the cochlea. J. Neurosci. 2012, 32:4773-4789.
    • (2012) J. Neurosci. , vol.32 , pp. 4773-4789
    • Rutherford, M.A.1
  • 44
    • 0036159084 scopus 로고    scopus 로고
    • Transmitter release at the hair cell ribbon synapse
    • Glowatzki E., Fuchs P.A. Transmitter release at the hair cell ribbon synapse. Nat. Neurosci. 2002, 5:147-154.
    • (2002) Nat. Neurosci. , vol.5 , pp. 147-154
    • Glowatzki, E.1    Fuchs, P.A.2
  • 45
    • 33646140440 scopus 로고    scopus 로고
    • Vesicle depletion and synaptic depression at a mammalian ribbon synapse
    • Singer J.H., Diamond J.S. Vesicle depletion and synaptic depression at a mammalian ribbon synapse. J. Neurophysiol. 2006, 95:3191-3198.
    • (2006) J. Neurophysiol. , vol.95 , pp. 3191-3198
    • Singer, J.H.1    Diamond, J.S.2
  • 46
    • 70449370992 scopus 로고    scopus 로고
    • Myosin VI is required for the proper maturation and function of inner hair cell ribbon synapses
    • Roux I., et al. Myosin VI is required for the proper maturation and function of inner hair cell ribbon synapses. Hum. Mol. Genet. 2009, 18:4615-4628.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 4615-4628
    • Roux, I.1
  • 47
    • 67650730447 scopus 로고    scopus 로고
    • Otoferlin interacts with myosin VI: implications for maintenance of the basolateral synaptic structure of the inner hair cell
    • Heidrych P., et al. Otoferlin interacts with myosin VI: implications for maintenance of the basolateral synaptic structure of the inner hair cell. Hum. Mol. Genet. 2009, 18:2779-2790.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2779-2790
    • Heidrych, P.1
  • 48
    • 56049124302 scopus 로고    scopus 로고
    • Rab8b GTPase, a protein transport regulator, is an interacting partner of otoferlin, defective in a human autosomal recessive deafness form
    • Heidrych P., et al. Rab8b GTPase, a protein transport regulator, is an interacting partner of otoferlin, defective in a human autosomal recessive deafness form. Hum. Mol. Genet. 2008, 17:3814-3821.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3814-3821
    • Heidrych, P.1
  • 49
    • 84861378565 scopus 로고    scopus 로고
    • Ergic2, a brain specific interacting partner of otoferlin
    • Zak M., et al. Ergic2, a brain specific interacting partner of otoferlin. Cell. Physiol. Biochem. 2012, 29:941-948.
    • (2012) Cell. Physiol. Biochem. , vol.29 , pp. 941-948
    • Zak, M.1
  • 50
    • 78449280421 scopus 로고    scopus 로고
    • 2+ channels and vesicles to add release sites and promote refilling
    • 2+ channels and vesicles to add release sites and promote refilling. Neuron 2010, 68:724-738.
    • (2010) Neuron , vol.68 , pp. 724-738
    • Frank, T.1
  • 51
    • 77949266565 scopus 로고    scopus 로고
    • 2+ regulator of synaptic exocytosis
    • 2+ regulator of synaptic exocytosis. Nat. Struct. Mol. Biol. 2010, 17:280-288.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 280-288
    • Shin, O.-H.1
  • 52
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • Martens S., et al. How synaptotagmin promotes membrane fusion. Science 2007, 316:1205-1208.
    • (2007) Science , vol.316 , pp. 1205-1208
    • Martens, S.1
  • 53
    • 68749083522 scopus 로고    scopus 로고
    • 2+-regulated fusion
    • 2+-regulated fusion. Cell 2009, 138:709-721.
    • (2009) Cell , vol.138 , pp. 709-721
    • Hui, E.1
  • 54
    • 46449093538 scopus 로고    scopus 로고
    • How does synaptotagmin trigger neurotransmitter release?
    • Chapman E.R. How does synaptotagmin trigger neurotransmitter release?. Annu. Rev. Biochem. 2008, 77:615-641.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 615-641
    • Chapman, E.R.1
  • 56
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: disparate players and common principles
    • Martens S., McMahon H.T. Mechanisms of membrane fusion: disparate players and common principles. Nat. Rev. Mol. Cell Biol. 2008, 9:543-556.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 57
    • 70350212639 scopus 로고    scopus 로고
    • Conflicting views on the membrane fusion machinery and the fusion pore
    • Sørensen J.B. Conflicting views on the membrane fusion machinery and the fusion pore. Annu. Rev. Cell Dev. Biol. 2009, 25:513-537.
    • (2009) Annu. Rev. Cell Dev. Biol. , vol.25 , pp. 513-537
    • Sørensen, J.B.1
  • 58
    • 0036071451 scopus 로고    scopus 로고
    • Q829X, a novel mutation in the gene encoding otoferlin (OTOF), is frequently found in Spanish patients with prelingual non-syndromic hearing loss
    • Migliosi V., et al. Q829X, a novel mutation in the gene encoding otoferlin (OTOF), is frequently found in Spanish patients with prelingual non-syndromic hearing loss. J. Med. Genet. 2002, 39:502-506.
    • (2002) J. Med. Genet. , vol.39 , pp. 502-506
    • Migliosi, V.1
  • 59
    • 0036073381 scopus 로고    scopus 로고
    • Substitutions in the conserved C2C domain of otoferlin cause DFNB9, a form of nonsyndromic autosomal recessive deafness
    • Mirghomizadeh F., et al. Substitutions in the conserved C2C domain of otoferlin cause DFNB9, a form of nonsyndromic autosomal recessive deafness. Neurobiol. Dis. 2002, 10:157-164.
    • (2002) Neurobiol. Dis. , vol.10 , pp. 157-164
    • Mirghomizadeh, F.1
  • 60
    • 10744230174 scopus 로고    scopus 로고
    • Auditory neuropathy in patients carrying mutations in the otoferlin gene (OTOF)
    • Rodríguez-Ballesteros M., et al. Auditory neuropathy in patients carrying mutations in the otoferlin gene (OTOF). Hum. Mutat. 2003, 22:451-456.
    • (2003) Hum. Mutat. , vol.22 , pp. 451-456
    • Rodríguez-Ballesteros, M.1
  • 61
    • 0037238597 scopus 로고    scopus 로고
    • Non-syndromic recessive auditory neuropathy is the result of mutations in the otoferlin (OTOF) gene
    • Varga R., et al. Non-syndromic recessive auditory neuropathy is the result of mutations in the otoferlin (OTOF) gene. J. Med. Genet. 2003, 40:45-50.
    • (2003) J. Med. Genet. , vol.40 , pp. 45-50
    • Varga, R.1
  • 62
    • 33745907313 scopus 로고    scopus 로고
    • OTOF mutations revealed by genetic analysis of hearing loss families including a potential temperature sensitive auditory neuropathy allele
    • Varga R., et al. OTOF mutations revealed by genetic analysis of hearing loss families including a potential temperature sensitive auditory neuropathy allele. J. Med. Genet. 2006, 43:576-581.
    • (2006) J. Med. Genet. , vol.43 , pp. 576-581
    • Varga, R.1
  • 63
    • 44849114793 scopus 로고    scopus 로고
    • A multicenter study on the prevalence and spectrum of mutations in the otoferlin gene (OTOF) in subjects with nonsyndromic hearing impairment and auditory neuropathy
    • Rodríguez-Ballesteros M., et al. A multicenter study on the prevalence and spectrum of mutations in the otoferlin gene (OTOF) in subjects with nonsyndromic hearing impairment and auditory neuropathy. Hum. Mutat. 2008, 29:823-831.
    • (2008) Hum. Mutat. , vol.29 , pp. 823-831
    • Rodríguez-Ballesteros, M.1
  • 64
    • 77952643063 scopus 로고    scopus 로고
    • Screening mutations of OTOF gene in Chinese patients with auditory neuropathy, including a familial case of temperature-sensitive auditory neuropathy
    • Wang D.-Y., et al. Screening mutations of OTOF gene in Chinese patients with auditory neuropathy, including a familial case of temperature-sensitive auditory neuropathy. BMC Med. Genet. 2010, 11:79.
    • (2010) BMC Med. Genet. , vol.11 , pp. 79
    • Wang, D.-Y.1
  • 65
    • 77950519874 scopus 로고    scopus 로고
    • Temperature-sensitive auditory neuropathy associated with an otoferlin mutation: deafening fever! Biochem
    • Marlin S., et al. Temperature-sensitive auditory neuropathy associated with an otoferlin mutation: deafening fever! Biochem. Biophys. Res. Commun. 2010, 394:737-742.
    • (2010) Biophys. Res. Commun. , vol.394 , pp. 737-742
    • Marlin, S.1
  • 66
    • 36048993116 scopus 로고    scopus 로고
    • A missense mutation in the conserved C2B domain of otoferlin causes deafness in a new mouse model of DFNB9
    • Longo-Guess C., et al. A missense mutation in the conserved C2B domain of otoferlin causes deafness in a new mouse model of DFNB9. Hear. Res. 2007, 234:21-28.
    • (2007) Hear. Res. , vol.234 , pp. 21-28
    • Longo-Guess, C.1
  • 67
    • 72249092101 scopus 로고    scopus 로고
    • Abnormal cochlear potentials from deaf patients with mutations in the otoferlin gene
    • Santarelli R., et al. Abnormal cochlear potentials from deaf patients with mutations in the otoferlin gene. J. Assoc. Res. Otolaryngol. 2009, 10:545-556.
    • (2009) J. Assoc. Res. Otolaryngol. , vol.10 , pp. 545-556
    • Santarelli, R.1
  • 68
    • 0029886187 scopus 로고    scopus 로고
    • Auditory neuropathy
    • Starr A., et al. Auditory neuropathy. Brain 1996, 119:741-753.
    • (1996) Brain , vol.119 , pp. 741-753
    • Starr, A.1
  • 69
    • 24344458436 scopus 로고    scopus 로고
    • A novel missense mutation in a C2 domain of OTOF results in autosomal recessive auditory neuropathy
    • Tekin M., et al. A novel missense mutation in a C2 domain of OTOF results in autosomal recessive auditory neuropathy. Am. J. Med. Genet. Part A 2005, 138A:6-10.
    • (2005) Am. J. Med. Genet. Part A , vol.138 A , pp. 6-10
    • Tekin, M.1
  • 70
    • 84867658612 scopus 로고    scopus 로고
    • A prevalent founder mutation and genotype-phenotype correlations of OTOF in Japanese patients with auditory neuropathy
    • Matsunaga T., et al. A prevalent founder mutation and genotype-phenotype correlations of OTOF in Japanese patients with auditory neuropathy. Clin. Genet. 2012, 10.1111/j.1399-0004.2012.01897.x.
    • (2012) Clin. Genet.
    • Matsunaga, T.1
  • 71
    • 80051933736 scopus 로고    scopus 로고
    • 2+ sensors in secretion: teammates, competitors or autocrats?
    • 2+ sensors in secretion: teammates, competitors or autocrats?. Trends Neurosci. 2011, 34:487-497.
    • (2011) Trends Neurosci. , vol.34 , pp. 487-497
    • Walter, A.M.1
  • 72
    • 84855912661 scopus 로고    scopus 로고
    • Ferlins: regulators of vesicle fusion for auditory neurotransmission, receptor trafficking and membrane repair
    • Lek A., et al. Ferlins: regulators of vesicle fusion for auditory neurotransmission, receptor trafficking and membrane repair. Traffic 2012, 13:185-194.
    • (2012) Traffic , vol.13 , pp. 185-194
    • Lek, A.1
  • 73
    • 33746054560 scopus 로고    scopus 로고
    • 2+-mediated membrane fusion during C. elegans spermatogenesis
    • 2+-mediated membrane fusion during C. elegans spermatogenesis. J. Cell Sci. 2006, 119:2552-2562.
    • (2006) J. Cell Sci. , vol.119 , pp. 2552-2562
    • Washington, N.L.1    Ward, S.2
  • 74
    • 36349010892 scopus 로고    scopus 로고
    • Probing the mechanism of exocytosis at the hair cell ribbon synapse
    • Neef A., et al. Probing the mechanism of exocytosis at the hair cell ribbon synapse. J. Neurosci. 2007, 27:12933-12944.
    • (2007) J. Neurosci. , vol.27 , pp. 12933-12944
    • Neef, A.1
  • 75
    • 33344472435 scopus 로고    scopus 로고
    • Results of cochlear implantation in two children with mutations in the OTOF gene
    • Rouillon I., et al. Results of cochlear implantation in two children with mutations in the OTOF gene. Int. J. Pediatr. Otorhinolaryngol. 2006, 70:689-696.
    • (2006) Int. J. Pediatr. Otorhinolaryngol. , vol.70 , pp. 689-696
    • Rouillon, I.1
  • 76
    • 60549087171 scopus 로고    scopus 로고
    • Identities and frequencies of mutations of the otoferlin gene (OTOF) causing DFNB9 deafness in Pakistan
    • Choi B.Y., et al. Identities and frequencies of mutations of the otoferlin gene (OTOF) causing DFNB9 deafness in Pakistan. Clin. Genet. 2009, 75:237-243.
    • (2009) Clin. Genet. , vol.75 , pp. 237-243
    • Choi, B.Y.1
  • 77
    • 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
    • Jiménez J.L., Bashir R. 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. J. Neurol. Sci. 2007, 260:114-123.
    • (2007) J. Neurol. Sci. , vol.260 , pp. 114-123
    • Jiménez, J.L.1    Bashir, R.2
  • 78
    • 33748324514 scopus 로고    scopus 로고
    • Membrane binding and subcellular targeting of C2 domains
    • Cho W., Stahelin R.V. Membrane binding and subcellular targeting of C2 domains. Biochim. Biophys. Acta. 2006, 1761:838-849.
    • (2006) Biochim. Biophys. Acta. , vol.1761 , pp. 838-849
    • Cho, W.1    Stahelin, R.V.2
  • 79
    • 8144230701 scopus 로고    scopus 로고
    • The architecture of the active zone in the presynaptic nerve terminal
    • Zhai R.G., Bellen H.J. The architecture of the active zone in the presynaptic nerve terminal. Physiology 2004, 19:262-270.
    • (2004) Physiology , vol.19 , pp. 262-270
    • Zhai, R.G.1    Bellen, H.J.2
  • 80
    • 84863471483 scopus 로고    scopus 로고
    • Molecular organization and plasticity of the cytomatrix at the active zone
    • Gundelfinger E.D., Fejtova A. Molecular organization and plasticity of the cytomatrix at the active zone. Curr. Opin. Neurobiol. 2012, 22:423-430.
    • (2012) Curr. Opin. Neurobiol. , vol.22 , pp. 423-430
    • Gundelfinger, E.D.1    Fejtova, A.2
  • 81
    • 79951948881 scopus 로고    scopus 로고
    • Protein scaffolds in the coupling of synaptic exocytosis and endocytosis
    • Haucke V., et al. Protein scaffolds in the coupling of synaptic exocytosis and endocytosis. Nat. Rev. Neurosci. 2011, 12:127-138.
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 127-138
    • Haucke, V.1
  • 82
    • 0034525302 scopus 로고    scopus 로고
    • RIBEYE, a component of synaptic ribbons: a protein's journey through evolution provides insight into synaptic ribbon function
    • Schmitz F., et al. RIBEYE, a component of synaptic ribbons: a protein's journey through evolution provides insight into synaptic ribbon function. Neuron 2000, 28:857-872.
    • (2000) Neuron , vol.28 , pp. 857-872
    • Schmitz, F.1
  • 83
    • 17244366230 scopus 로고    scopus 로고
    • Hair cell synaptic ribbons are essential for synchronous auditory signalling
    • Khimich D., et al. Hair cell synaptic ribbons are essential for synchronous auditory signalling. Nature 2005, 434:889-894.
    • (2005) Nature , vol.434 , pp. 889-894
    • Khimich, D.1
  • 84
    • 77953204546 scopus 로고    scopus 로고
    • Onset coding is degraded in auditory nerve fibers from mutant mice lacking synaptic ribbons
    • Buran B.N., et al. Onset coding is degraded in auditory nerve fibers from mutant mice lacking synaptic ribbons. J. Neurosci. 2010, 30:7587.
    • (2010) J. Neurosci. , vol.30 , pp. 7587
    • Buran, B.N.1
  • 85
    • 14444271321 scopus 로고    scopus 로고
    • Bassoon, a novel zinc-finger CAG/glutamine-repeat protein selectively localized at the active zone of presynaptic nerve terminals
    • tom Dieck S., et al. Bassoon, a novel zinc-finger CAG/glutamine-repeat protein selectively localized at the active zone of presynaptic nerve terminals. J. Cell Biol. 1998, 142:499-509.
    • (1998) J. Cell Biol. , vol.142 , pp. 499-509
    • tom Dieck, S.1
  • 86
    • 0037421990 scopus 로고    scopus 로고
    • Functional inactivation of a fraction of excitatory synapses in mice deficient for the active zone protein bassoon
    • Altrock W.D., et al. Functional inactivation of a fraction of excitatory synapses in mice deficient for the active zone protein bassoon. Neuron 2003, 37:787-800.
    • (2003) Neuron , vol.37 , pp. 787-800
    • Altrock, W.D.1
  • 87
    • 78449269354 scopus 로고    scopus 로고
    • Bassoon speeds vesicle reloading at a central excitatory synapse
    • Hallermann S., et al. Bassoon speeds vesicle reloading at a central excitatory synapse. Neuron 2010, 68:710-723.
    • (2010) Neuron , vol.68 , pp. 710-723
    • Hallermann, S.1
  • 88
    • 13344284658 scopus 로고    scopus 로고
    • Piccolo, a novel 420 kDa protein associated with the presynaptic cytomatrix
    • Cases-Langhoff C., et al. Piccolo, a novel 420 kDa protein associated with the presynaptic cytomatrix. Eur. J. Cell Biol. 1996, 69:214-223.
    • (1996) Eur. J. Cell Biol. , vol.69 , pp. 214-223
    • Cases-Langhoff, C.1
  • 89
    • 77950869684 scopus 로고    scopus 로고
    • Piccolo and bassoon maintain synaptic vesicle clustering without directly participating in vesicle exocytosis
    • Mukherjee K., et al. Piccolo and bassoon maintain synaptic vesicle clustering without directly participating in vesicle exocytosis. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:6504.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 6504
    • Mukherjee, K.1
  • 90
    • 0036329841 scopus 로고    scopus 로고
    • Cast a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and Munc13-1
    • Ohtsuka T., et al. Cast a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and Munc13-1. J. Cell Biol. 2002, 158:577-590.
    • (2002) J. Cell Biol. , vol.158 , pp. 577-590
    • Ohtsuka, T.1
  • 91
    • 21844479018 scopus 로고    scopus 로고
    • ELKS, a protein structurally related to the active zone-associated protein CAST, is expressed in pancreatic β cells and functions in insulin exocytosis: interaction of ELKS with exocytotic machinery analyzed by total internal reflection fluorescence microscopy
    • Ohara-Imaizumi M., et al. ELKS, a protein structurally related to the active zone-associated protein CAST, is expressed in pancreatic β cells and functions in insulin exocytosis: interaction of ELKS with exocytotic machinery analyzed by total internal reflection fluorescence microscopy. Mol. Biol. Cell 2005, 16:3289-3300.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3289-3300
    • Ohara-Imaizumi, M.1
  • 92
    • 80052262083 scopus 로고    scopus 로고
    • 2+ channels in mouse inner hair cells
    • 2+ channels in mouse inner hair cells. Nat. Neurosci. 2011, 14:1109-1111.
    • (2011) Nat. Neurosci. , vol.14 , pp. 1109-1111
    • Gregory, F.D.1
  • 93
    • 0034637146 scopus 로고    scopus 로고
    • Uptake of glutamate into synaptic vesicles by an inorganic phosphate transporter
    • Bellocchio E.E., et al. Uptake of glutamate into synaptic vesicles by an inorganic phosphate transporter. Science 2000, 289:957-960.
    • (2000) Science , vol.289 , pp. 957-960
    • Bellocchio, E.E.1
  • 94
    • 0013198358 scopus 로고    scopus 로고
    • The expression of vesicular glutamate transporters defines two classes of excitatory synapse
    • Fremeau R.T., et al. The expression of vesicular glutamate transporters defines two classes of excitatory synapse. Neuron 2001, 31:247-260.
    • (2001) Neuron , vol.31 , pp. 247-260
    • Fremeau, R.T.1
  • 95
    • 0035891724 scopus 로고    scopus 로고
    • Identification of differentiation-associated brain-specific phosphate transporter as a second vesicular glutamate transporter (VGLUT2)
    • Takamori S., et al. Identification of differentiation-associated brain-specific phosphate transporter as a second vesicular glutamate transporter (VGLUT2). J. Neurosci. 2001, 21:RC182.
    • (2001) J. Neurosci. , vol.21
    • Takamori, S.1
  • 96
    • 0023788855 scopus 로고
    • Expression of the ras-related ralA, rho12 and rab genes in adult mouse tissues
    • Olofsson B., et al. Expression of the ras-related ralA, rho12 and rab genes in adult mouse tissues. Oncogene 1988, 3:231-234.
    • (1988) Oncogene , vol.3 , pp. 231-234
    • Olofsson, B.1
  • 97
    • 0030980279 scopus 로고    scopus 로고
    • The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion
    • Geppert M., et al. The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion. Nature 1997, 387:810-814.
    • (1997) Nature , vol.387 , pp. 810-814
    • Geppert, M.1
  • 98
    • 80052748802 scopus 로고    scopus 로고
    • How synapsin I may cluster synaptic vesicles
    • Shupliakov O., et al. How synapsin I may cluster synaptic vesicles. Semin. Cell Dev. Biol. 2011, 22:393-399.
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 393-399
    • Shupliakov, O.1
  • 99
    • 77954202334 scopus 로고    scopus 로고
    • The synapsins: Key actors of synapse function and plasticity
    • Cesca F., et al. The synapsins: Key actors of synapse function and plasticity. Prog. Neurobiol. 2010, 91:313-348.
    • (2010) Prog. Neurobiol. , vol.91 , pp. 313-348
    • Cesca, F.1
  • 100
    • 0030877243 scopus 로고    scopus 로고
    • Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion
    • Wang Y., et al. Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion. Nature 1997, 388:593-598.
    • (1997) Nature , vol.388 , pp. 593-598
    • Wang, Y.1
  • 101
    • 0037122458 scopus 로고    scopus 로고
    • RIM1α forms a protein scaffold for regulating neurotransmitter release at the active zone
    • Schoch S., et al. RIM1α forms a protein scaffold for regulating neurotransmitter release at the active zone. Nature 2002, 415:321-326.
    • (2002) Nature , vol.415 , pp. 321-326
    • Schoch, S.1
  • 102
    • 77953231923 scopus 로고    scopus 로고
    • 2+ channel gating by Rab3 interacting molecule
    • 2+ channel gating by Rab3 interacting molecule. Mol. Cell. Neurosci. 2010, 44:246-259.
    • (2010) Mol. Cell. Neurosci. , vol.44 , pp. 246-259
    • Gebhart, M.1
  • 103
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • Hata Y., et al. Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature 1993, 366:347-351.
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1
  • 104
    • 0034603030 scopus 로고    scopus 로고
    • Synaptic assembly of the brain in the absence of neurotransmitter secretion
    • Verhage M., et al. Synaptic assembly of the brain in the absence of neurotransmitter secretion. Science 2000, 287:864-869.
    • (2000) Science , vol.287 , pp. 864-869
    • Verhage, M.1
  • 105
    • 0028791349 scopus 로고
    • Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C-domain proteins
    • Brose N., et al. Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C-domain proteins. J. Biol. Chem. 1995, 270:25273.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25273
    • Brose, N.1
  • 106
    • 0026722645 scopus 로고
    • 2+-regulated secretion in permeable neuroendocrine cells
    • 2+-regulated secretion in permeable neuroendocrine cells. Cell 1992, 70:765-775.
    • (1992) Cell , vol.70 , pp. 765-775
    • Walent, J.H.1
  • 107
    • 36049025863 scopus 로고    scopus 로고
    • CAPS-1 and CAPS-2 are essential synaptic vesicle priming proteins
    • Jockusch W.J., et al. CAPS-1 and CAPS-2 are essential synaptic vesicle priming proteins. Cell 2007, 131:796-808.
    • (2007) Cell , vol.131 , pp. 796-808
    • Jockusch, W.J.1
  • 109
    • 0019851385 scopus 로고
    • Identification of a synaptic vesicle-specific membrane protein with a wide distribution in neuronal and neurosecretory tissue
    • Matthew W.D., et al. Identification of a synaptic vesicle-specific membrane protein with a wide distribution in neuronal and neurosecretory tissue. J. Cell Biol. 1981, 91:257-269.
    • (1981) J. Cell Biol. , vol.91 , pp. 257-269
    • Matthew, W.D.1
  • 110
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin M.S., et al. Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature 1990, 345:260-263.
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1
  • 111
    • 0025879767 scopus 로고
    • Synaptotagmin II. A novel differentially distributed form of synaptotagmin
    • Geppert M., et al. Synaptotagmin II. A novel differentially distributed form of synaptotagmin. J. Biol. Chem. 1991, 266:13548-13552.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13548-13552
    • Geppert, M.1
  • 112
    • 36749078085 scopus 로고    scopus 로고
    • 2+-sensor model for neurotransmitter release in a central synapse
    • 2+-sensor model for neurotransmitter release in a central synapse. Nature 2007, 450:676-682.
    • (2007) Nature , vol.450 , pp. 676-682
    • Sun, J.1
  • 113
    • 73949120302 scopus 로고    scopus 로고
    • 2+ dependence of vesicle fusion at auditory ribbon synapses
    • 2+ dependence of vesicle fusion at auditory ribbon synapses. Nat. Neurosci. 2009, 13:45-52.
    • (2009) Nat. Neurosci. , vol.13 , pp. 45-52
    • Johnson, S.L.1
  • 114
    • 0029117211 scopus 로고
    • Identification of two highly homologous presynaptic proteins distinctly localized at the dendritic and somatic synapses
    • Takahashi S., et al. Identification of two highly homologous presynaptic proteins distinctly localized at the dendritic and somatic synapses. FEBS Lett. 1995, 368:455-460.
    • (1995) FEBS Lett. , vol.368 , pp. 455-460
    • Takahashi, S.1
  • 115
    • 0028880456 scopus 로고
    • Complexins: cytosolic proteins that regulate SNAP receptor function
    • McMahon H.T., et al. Complexins: cytosolic proteins that regulate SNAP receptor function. Cell 1995, 83:111-119.
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.T.1
  • 116
    • 0035846908 scopus 로고    scopus 로고
    • 2+-dependent neurotransmitter release
    • 2+-dependent neurotransmitter release. Cell 2001, 104:71-81.
    • (2001) Cell , vol.104 , pp. 71-81
    • Reim, K.1
  • 117
    • 22344436671 scopus 로고    scopus 로고
    • Structurally and functionally unique complexins at retinal ribbon synapses
    • Reim K., et al. Structurally and functionally unique complexins at retinal ribbon synapses. J. Cell Biol. 2005, 169:669.
    • (2005) J. Cell Biol. , vol.169 , pp. 669
    • Reim, K.1
  • 119
    • 3042543371 scopus 로고    scopus 로고
    • 2+ channel gene results in deafness but no vestibular defect in mice
    • 2+ channel gene results in deafness but no vestibular defect in mice. J. Assoc. Res. Otolaryngol. 2004, 5:215-226.
    • (2004) J. Assoc. Res. Otolaryngol. , vol.5 , pp. 215-226
    • Dou, H.1
  • 120
    • 67049114041 scopus 로고    scopus 로고
    • The unitary event underlying multiquantal EPSCs at a hair cell's ribbon synapse
    • Li G.L., et al. The unitary event underlying multiquantal EPSCs at a hair cell's ribbon synapse. J. Neurosci. 2009, 29:7558.
    • (2009) J. Neurosci. , vol.29 , pp. 7558
    • Li, G.L.1
  • 121
    • 30744434111 scopus 로고    scopus 로고
    • Few Cav1.3 channels regulate the exocytosis of a synaptic vesicle at the hair cell ribbon synapse
    • Brandt A., et al. Few Cav1.3 channels regulate the exocytosis of a synaptic vesicle at the hair cell ribbon synapse. J. Neurosci. 2005, 25:11577.
    • (2005) J. Neurosci. , vol.25 , pp. 11577
    • Brandt, A.1
  • 122
    • 63649100112 scopus 로고    scopus 로고
    • Tuning of synapse number, structure and function in the cochlea
    • Meyer A.C., et al. Tuning of synapse number, structure and function in the cochlea. Nat. Neurosci. 2009, 12:444-453.
    • (2009) Nat. Neurosci. , vol.12 , pp. 444-453
    • Meyer, A.C.1
  • 123
    • 55249110956 scopus 로고    scopus 로고
    • Synaptic ribbon enables temporal precision of hair cell afferent synapse by increasing the number of readily releasable vesicles: a modeling study
    • Wittig J.H., Parsons T.D. Synaptic ribbon enables temporal precision of hair cell afferent synapse by increasing the number of readily releasable vesicles: a modeling study. J. Neurophysiol. 2008, 100:1724-1739.
    • (2008) J. Neurophysiol. , vol.100 , pp. 1724-1739
    • Wittig, J.H.1    Parsons, T.D.2
  • 124
    • 0035047237 scopus 로고    scopus 로고
    • Calcium dependence of exocytosis and endocytosis at the cochlear inner hair cell afferent synapse
    • Beutner D., et al. Calcium dependence of exocytosis and endocytosis at the cochlear inner hair cell afferent synapse. Neuron 2001, 29:681-690.
    • (2001) Neuron , vol.29 , pp. 681-690
    • Beutner, D.1
  • 125
    • 0041878310 scopus 로고    scopus 로고
    • The afferent synapse of cochlear hair cells
    • Fuchs P.A., et al. The afferent synapse of cochlear hair cells. Curr. Opin. Neurobiol. 2003, 13:452-458.
    • (2003) Curr. Opin. Neurobiol. , vol.13 , pp. 452-458
    • Fuchs, P.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.