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Volumn 2, Issue 2, 2014, Pages 243-257

The proteome of the murine presynaptic active zone

Author keywords

Presynaptic active zone; Proteome

Indexed keywords


EID: 84984607139     PISSN: None     EISSN: 22277382     Source Type: Journal    
DOI: 10.3390/proteomes2020243     Document Type: Review
Times cited : (6)

References (95)
  • 1
    • 29144493185 scopus 로고    scopus 로고
    • Immunoisolation of two synaptic vesicle pools from synaptosomes: A proteomics analysis
    • Morciano, M.; Burre, J.; Corvey, C.; Karas, M.; Zimmermann, H.; Volknandt, W. Immunoisolation of two synaptic vesicle pools from synaptosomes: A proteomics analysis. J. Neurochem. 2005, 95, 1732-1745
    • (2005) J. Neurochem , vol.95 , pp. 1732-1745
    • Morciano, M.1    Burre, J.2    Corvey, C.3    Karas, M.4    Zimmermann, H.5    Volknandt, W.6
  • 2
    • 58149352395 scopus 로고    scopus 로고
    • The proteome of the presynaptic active zone: From docked synaptic vesicles to adhesion molecules and maxi-channels
    • Morciano, M.; Beckhaus, T.; Karas, M.; Zimmermann, H.; Volknandt, W. The proteome of the presynaptic active zone: From docked synaptic vesicles to adhesion molecules and maxi-channels. J. Neurochem. 2009, 108, 662-675
    • (2009) J. Neurochem , vol.108 , pp. 662-675
    • Morciano, M.1    Beckhaus, T.2    Karas, M.3    Zimmermann, H.4    Volknandt, W.5
  • 3
    • 84876809468 scopus 로고    scopus 로고
    • Molecular profiling of synaptic vesicle docking sites reveals novel proteins but few differences between glutamatergic and gabaergic synapses
    • Boyken, J.; Gronborg, M.; Riedel, D.; Urlaub, H.; Jahn, R.; Chua, J.J. Molecular profiling of synaptic vesicle docking sites reveals novel proteins but few differences between glutamatergic and gabaergic synapses. Neuron 2013, 78, 285-297
    • (2013) Neuron , vol.78 , pp. 285-297
    • Boyken, J.1    Gronborg, M.2    Riedel, D.3    Urlaub, H.4    Jahn, R.5    Chua, J.J.6
  • 5
    • 0002358665 scopus 로고
    • The separation of synaptic vesicles from nerve-ending particles (synaptosomes)
    • Whittaker, V.P.; Michaelson, I.A.; Kirkland, R.J. The separation of synaptic vesicles from nerve-ending particles (synaptosomes). Biochem. J. 1964, 90, 293-303
    • (1964) Biochem. J , vol.90 , pp. 293-303
    • Whittaker, V.P.1    Michaelson, I.A.2    Kirkland, R.J.3
  • 7
    • 73049155988 scopus 로고
    • The isolation of nerve endings from brain: An electron-microscopic study of cell fragments derived by homogenization and centrifugation
    • Gray, E.G.; Whittaker, V.P. The isolation of nerve endings from brain: An electron-microscopic study of cell fragments derived by homogenization and centrifugation. J. Anat. 1962, 96, 79-88
    • (1962) J. Anat , vol.96 , pp. 79-88
    • Gray, E.G.1    Whittaker, V.P.2
  • 8
    • 84863040103 scopus 로고    scopus 로고
    • Presynaptic active zone density during development and synaptic plasticity
    • Clarke, G.L.; Chen, J.; Nishimune, H. Presynaptic active zone density during development and synaptic plasticity. Front. Mol. Neurosci. 2012, 5, e12
    • (2012) Front. Mol. Neurosci , vol.5
    • Clarke, G.L.1    Chen, J.2    Nishimune, H.3
  • 10
    • 84865765275 scopus 로고    scopus 로고
    • The presynaptic active zone protein rim1alpha controls epileptogenesis following status epilepticus
    • Pitsch, J.; Opitz, T.; Borm, V.; Woitecki, A.; Staniek, M.; Beck, H.; Becker, A.J.; Schoch, S. The presynaptic active zone protein rim1alpha controls epileptogenesis following status epilepticus. J. Neurosci. 2012, 32, 12384-12395
    • (2012) J. Neurosci , vol.32 , pp. 12384-12395
    • Pitsch, J.1    Opitz, T.2    Borm, V.3    Woitecki, A.4    Staniek, M.5    Beck, H.6    Becker, A.J.7    Schoch, S.8
  • 11
    • 84863826404 scopus 로고    scopus 로고
    • The presynaptic active zone
    • Sudhof, T.C. The presynaptic active zone. Neuron 2012, 75, 11-25
    • (2012) Neuron , vol.75 , pp. 11-25
    • Sudhof, T.C.1
  • 12
    • 84862864468 scopus 로고    scopus 로고
    • Proteomic analysis of the presynaptic active zone
    • Volknandt, W.; Karas, M. Proteomic analysis of the presynaptic active zone. Exp. Brain Res. 2012, 217, 449-461
    • (2012) Exp. Brain Res , vol.217 , pp. 449-461
    • Volknandt, W.1    Karas, M.2
  • 13
    • 84884702582 scopus 로고    scopus 로고
    • Cast: Functional scaffold for the integrity of the presynaptic active zone
    • Ohtsuka, T. Cast: Functional scaffold for the integrity of the presynaptic active zone. Neurosci. Res. 2013, 76, 10-15
    • (2013) Neurosci. Res , vol.76 , pp. 10-15
    • Ohtsuka, T.1
  • 14
    • 38449113394 scopus 로고    scopus 로고
    • Synaptosome proteomics. Sub-Cell
    • Bai, F.; Witzmann, F.A. Synaptosome proteomics. Sub-Cell. Biochem.2007, 43, 77-98
    • (2007) Biochem , vol.43 , pp. 77-98
    • Bai, F.1    Witzmann, F.A.2
  • 17
    • 0020955120 scopus 로고
    • Synapsin I (protein I), a nerve terminal-specific phosphoprotein III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation
    • Huttner, W.B.; Schiebler, W.; Greengard, P.; de Camilli, P. Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation. J. Cell Biol. 1983, 96, 1374-1388
    • (1983) J. Cell Biol , vol.96 , pp. 1374-1388
    • Huttner, W.B.1    Schiebler, W.2    Greengard, P.3    de Camilli, P.4
  • 18
    • 34249808797 scopus 로고    scopus 로고
    • The synaptic vesicle proteome
    • Burre, J.; Volknandt, W. The synaptic vesicle proteome. J. Neurochem. 2007, 101, 1448-1462
    • (2007) J. Neurochem , vol.101 , pp. 1448-1462
    • Burre, J.1    Volknandt, W.2
  • 20
    • 58749107499 scopus 로고    scopus 로고
    • A rapid percoll gradient procedure for preparation of synaptosomes
    • Dunkley, P.R.; Jarvie, P.E.; Robinson, P.J. A rapid percoll gradient procedure for preparation of synaptosomes. Nat. Protoc. 2008, 3, 1718-1728
    • (2008) Nat. Protoc , vol.3 , pp. 1718-1728
    • Dunkley, P.R.1    Jarvie, P.E.2    Robinson, P.J.3
  • 21
    • 0018070988 scopus 로고
    • A rapid method for the preparation of relatively pure metabolically competent synaptosomes from rat brain
    • Booth, R.F.; Clark, J.B. A rapid method for the preparation of relatively pure metabolically competent synaptosomes from rat brain. Biochem. J. 1978, 176, 365-370
    • (1978) Biochem. J , vol.176 , pp. 365-370
    • Booth, R.F.1    Clark, J.B.2
  • 25
    • 74849093404 scopus 로고    scopus 로고
    • Quantitative comparison of glutamatergic and gabaergic synaptic vesicles unveils selectivity for few proteins including mal2, a novel synaptic vesicle protein
    • Gronborg, M.; Pavlos, N.J.; Brunk, I.; Chua, J.J.; Munster-Wandowski, A.; Riedel, D.; Ahnert-Hilger, G.; Urlaub, H.; Jahn, R. Quantitative comparison of glutamatergic and gabaergic synaptic vesicles unveils selectivity for few proteins including mal2, a novel synaptic vesicle protein. J. Neurosci. 2010, 30, 2-12
    • (2010) J. Neurosci , vol.30 , pp. 2-12
    • Gronborg, M.1    Pavlos, N.J.2    Brunk, I.3    Chua, J.J.4    Munster-Wandowski, A.5    Riedel, D.6    Ahnert-Hilger, G.7    Urlaub, H.8    Jahn, R.9
  • 28
    • 0017744449 scopus 로고
    • Adenosine 3':5'-monophosphate-regulated phosphoprotein system of neuronal membranes I. Solubilization, purification, and some properties of an endogenous phosphoprotein
    • Ueda, T.; Greengard, P. Adenosine 3':5'-monophosphate-regulated phosphoprotein system of neuronal membranes. I. Solubilization, purification, and some properties of an endogenous phosphoprotein. J. Biol. Chem. 1977, 252, 5155-5163
    • (1977) J. Biol. Chem , vol.252 , pp. 5155-5163
    • Ueda, T.1    Greengard, P.2
  • 29
    • 0021922503 scopus 로고
    • Identification of a transmembrane glycoprotein specific for secretory vesicles of neural and endocrine cells
    • Buckley, K.; Kelly, R.B. Identification of a transmembrane glycoprotein specific for secretory vesicles of neural and endocrine cells. J. Cell Biol. 1985, 100, 1284-1294
    • (1985) J. Cell Biol , vol.100 , pp. 1284-1294
    • Buckley, K.1    Kelly, R.B.2
  • 30
    • 0344237032 scopus 로고
    • A 38, 000-dalton membrane protein (p38) present in synaptic vesicles
    • Jahn, R.; Schiebler, W.; Ouimet, C.; Greengard, P. A 38, 000-dalton membrane protein (p38) present in synaptic vesicles. Proc. Natl. Acad. Sci. USA 1985, 82, 4137-4141
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4137-4141
    • Jahn, R.1    Schiebler, W.2    Ouimet, C.3    Greengard, P.4
  • 32
    • 33748929314 scopus 로고    scopus 로고
    • Synaptic vesicle proteins under conditions of rest and activation: Analysis by 2-D difference gel electrophoresis
    • Burre, J.; Beckhaus, T.; Corvey, C.; Karas, M.; Zimmermann, H.; Volknandt, W. Synaptic vesicle proteins under conditions of rest and activation: Analysis by 2-D difference gel electrophoresis. Electrophoresis 2006, 27, 3488-3496
    • (2006) Electrophoresis , vol.27 , pp. 3488-3496
    • Burre, J.1    Beckhaus, T.2    Corvey, C.3    Karas, M.4    Zimmermann, H.5    Volknandt, W.6
  • 33
    • 79955066072 scopus 로고    scopus 로고
    • Proteomic investigations of the synaptic vesicle interactome
    • Barth, J.; Volknandt, W. Proteomic investigations of the synaptic vesicle interactome. Expert Rev. Proteomics 2011, 8, 211-220
    • (2011) Expert Rev. Proteomics , vol.8 , pp. 211-220
    • Barth, J.1    Volknandt, W.2
  • 35
    • 34247627759 scopus 로고    scopus 로고
    • Two-dimensional fluorescence difference gel electrophoresis for comparative proteomics profiling
    • Tannu, N.S.; Hemby, S.E. Two-dimensional fluorescence difference gel electrophoresis for comparative proteomics profiling. Nat. Protoc. 2006, 1, 1732-1742
    • (2006) Nat. Protoc , vol.1 , pp. 1732-1742
    • Tannu, N.S.1    Hemby, S.E.2
  • 36
    • 0036127937 scopus 로고    scopus 로고
    • Improved in-gel approaches to generate peptide maps of integral membrane proteins with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Van Montfort, B.A.; Canas, B.; Duurkens, R.; Godovac-Zimmermann, J.; Robillard, G.T. Improved in-gel approaches to generate peptide maps of integral membrane proteins with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Mass Spectrom. 2002, 37, 322-330
    • (2002) J. Mass Spectrom , vol.37 , pp. 322-330
    • Van Montfort, B.A.1    Canas, B.2    Duurkens, R.3    Godovac-Zimmermann, J.4    Robillard, G.T.5
  • 39
    • 33748940272 scopus 로고    scopus 로고
    • Molecular organization of the presynaptic active zone
    • Schoch, S.; Gundelfinger, E.D. Molecular organization of the presynaptic active zone. Cell Tissue Res. 2006, 326, 379-391
    • (2006) Cell Tissue Res , vol.326 , pp. 379-391
    • Schoch, S.1    Gundelfinger, E.D.2
  • 40
    • 42349091996 scopus 로고    scopus 로고
    • Actin in action: The interplay between the actin cytoskeleton and synaptic efficacy
    • Cingolani, L.A.; Goda, Y. Actin in action: The interplay between the actin cytoskeleton and synaptic efficacy. Nat. Rev. Neurosci. 2008, 9, 344-356
    • (2008) Nat. Rev. Neurosci , vol.9 , pp. 344-356
    • Cingolani, L.A.1    Goda, Y.2
  • 41
    • 0035894852 scopus 로고    scopus 로고
    • Axon branching requires interactions between dynamic microtubules and actin filaments
    • Dent, E.W.; Kalil, K. Axon branching requires interactions between dynamic microtubules and actin filaments. J. Neurosci. 2001, 21, 9757-9769
    • (2001) J. Neurosci , vol.21 , pp. 9757-9769
    • Dent, E.W.1    Kalil, K.2
  • 44
    • 84855947003 scopus 로고    scopus 로고
    • Activation of ezrin/radixin/moesin mediates attractive growth cone guidance through regulation of growth cone actin and adhesion receptors
    • Marsick, B.M.; San Miguel-Ruiz, J.E.; Letourneau, P.C. Activation of ezrin/radixin/moesin mediates attractive growth cone guidance through regulation of growth cone actin and adhesion receptors. J. Neurosci. 2012, 32, 282-296
    • (2012) J. Neurosci , vol.32 , pp. 282-296
    • Marsick, B.M.1    San Miguel-Ruiz, J.E.2    Letourneau, P.C.3
  • 45
    • 0033953888 scopus 로고    scopus 로고
    • Functional cooperation between the microtubule and actin cytoskeletons
    • Goode, B.L.; Drubin, D.G.; Barnes, G. Functional cooperation between the microtubule and actin cytoskeletons. Curr. Opin. Cell Biol. 2000, 12, 63-71
    • (2000) Curr. Opin. Cell Biol , vol.12 , pp. 63-71
    • Goode, B.L.1    Drubin, D.G.2    Barnes, G.3
  • 46
    • 0032891376 scopus 로고    scopus 로고
    • Identification of baiap2 (bai-associated protein 2), a novel human homologue of hamster irsp53, whose sh3 domain interacts with the cytoplasmic domain of bai1
    • Oda, K.; Shiratsuchi, T.; Nishimori, H.; Inazawa, J.; Yoshikawa, H.; Taketani, Y.; Nakamura, Y.; Tokino, T. Identification of baiap2 (bai-associated protein 2), a novel human homologue of hamster irsp53, whose sh3 domain interacts with the cytoplasmic domain of bai1. Cytogenetics Cell Genet. 1999, 84, 75-82
    • (1999) Cytogenetics Cell Genet , vol.84 , pp. 75-82
    • Oda, K.1    Shiratsuchi, T.2    Nishimori, H.3    Inazawa, J.4    Yoshikawa, H.5    Taketani, Y.6    Nakamura, Y.7    Tokino, T.8
  • 47
    • 80052758995 scopus 로고    scopus 로고
    • Characterization of presynaptic septin complexes in mammalian hippocampal neurons
    • Tsang, C.W.; Estey, M.P.; DiCiccio, J.E.; Xie, H.; Patterson, D.; Trimble, W.S. Characterization of presynaptic septin complexes in mammalian hippocampal neurons. Biol. Chem. 2011, 392, 739-749
    • (2011) Biol. Chem , vol.392 , pp. 739-749
    • Tsang, C.W.1    Estey, M.P.2    DiCiccio, J.E.3    Xie, H.4    Patterson, D.5    Trimble, W.S.6
  • 48
    • 0142244521 scopus 로고    scopus 로고
    • Dihydropyrimidinase related protein-2 as a biomarker for temperature and time dependent post mortem changes in the mouse brain proteome
    • Franzen, B.; Yang, Y.; Sunnemark, D.; Wickman, M.; Ottervald, J.; Oppermann, M.; Sandberg, K. Dihydropyrimidinase related protein-2 as a biomarker for temperature and time dependent post mortem changes in the mouse brain proteome. Proteomics 2003, 3, 1920-1929
    • (2003) Proteomics , vol.3 , pp. 1920-1929
    • Franzen, B.1    Yang, Y.2    Sunnemark, D.3    Wickman, M.4    Ottervald, J.5    Oppermann, M.6    Sandberg, K.7
  • 49
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in alzheimer's disease bra Part II: Dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71
    • Castegna, A.; Aksenov, M.; Thongboonkerd, V.; Klein, J.B.; Pierce, W.M.; Booze, R.; Markesbery, W.R.; Butterfield, D.A. Proteomic identification of oxidatively modified proteins in alzheimer's disease brain. Part II: Dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71. J. Neurochem. 2002, 82, 1524-1532
    • (2002) J. Neurochem , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6    Markesbery, W.R.7    Butterfield, D.A.8
  • 51
    • 70350348378 scopus 로고    scopus 로고
    • F-bar proteins of the syndapin family shape the plasma membrane and are crucial for neuromorphogenesis
    • Dharmalingam, E.; Haeckel, A.; Pinyol, R.; Schwintzer, L.; Koch, D.; Kessels, M.M.; Qualmann, B. F-bar proteins of the syndapin family shape the plasma membrane and are crucial for neuromorphogenesis. J. Neurosci. 2009, 29, 13315-13327
    • (2009) J. Neurosci , vol.29 , pp. 13315-13327
    • Dharmalingam, E.1    Haeckel, A.2    Pinyol, R.3    Schwintzer, L.4    Koch, D.5    Kessels, M.M.6    Qualmann, B.7
  • 55
    • 78649317246 scopus 로고    scopus 로고
    • How are ion pumps and agrin signaling integrated?
    • Tidow, H.; Aperia, A.; Nissen, P. How are ion pumps and agrin signaling integrated? Trends Biochem. Sci. 2010, 35, 653-659
    • (2010) Trends Biochem. Sci , vol.35 , pp. 653-659
    • Tidow, H.1    Aperia, A.2    Nissen, P.3
  • 56
    • 0036098774 scopus 로고    scopus 로고
    • +-ATPase as a signal transducer
    • +-ATPase as a signal transducer. Eur. J. Biochem. 2002, 269, 2434-2439
    • (2002) Eur. J. Biochem , vol.269 , pp. 2434-2439
    • Xie, Z.1    Askari, A.2
  • 59
    • 57649130788 scopus 로고    scopus 로고
    • Ankyrin-B is required for coordinated expression of beta-2-spectrin, the Na/K-ATPase and the Na/Ca exchanger in the inner segment of rod photoreceptors
    • Kizhatil, K.; Sandhu, N.K.; Peachey, N.S.; Bennett, V. Ankyrin-B is required for coordinated expression of beta-2-spectrin, the Na/K-ATPase and the Na/Ca exchanger in the inner segment of rod photoreceptors. Exp. Eye Res. 2009, 88, 57-64
    • (2009) Exp. Eye Res , vol.88 , pp. 57-64
    • Kizhatil, K.1    Sandhu, N.K.2    Peachey, N.S.3    Bennett, V.4
  • 60
    • 23644447071 scopus 로고    scopus 로고
    • Cell adhesion and neurite outgrowth are promoted by neurofascin NF155 and inhibited by NF186
    • Koticha, D.; Babiarz, J.; Kane-Goldsmith, N.; Jacob, J.; Raju, K.; Grumet, M. Cell adhesion and neurite outgrowth are promoted by neurofascin NF155 and inhibited by NF186. Mol. Cell. Neurosci. 2005, 30, 137-148
    • (2005) Mol. Cell. Neurosci , vol.30 , pp. 137-148
    • Koticha, D.1    Babiarz, J.2    Kane-Goldsmith, N.3    Jacob, J.4    Raju, K.5    Grumet, M.6
  • 61
    • 0037199663 scopus 로고    scopus 로고
    • Establishment of a novel enzyme-linked immunosorbent assay for thy-1; quantitative assessment of neuronal degeneration
    • Seki, M.; Nawa, H.; Morioka, T.; Fukuchi, T.; Oite, T.; Abe, H.; Takei, N. Establishment of a novel enzyme-linked immunosorbent assay for thy-1; quantitative assessment of neuronal degeneration. Neurosci. Lett. 2002, 329, 185-188
    • (2002) Neurosci. Lett , vol.329 , pp. 185-188
    • Seki, M.1    Nawa, H.2    Morioka, T.3    Fukuchi, T.4    Oite, T.5    Abe, H.6    Takei, N.7
  • 63
    • 0022621284 scopus 로고
    • Regional and subcellular distribution of thy-1 in human brain assayed by a solid-phase radioimmunoassay
    • Almqvist, P.; Carlsson, S.R.; Hardy, J.A.; Winblad, B. Regional and subcellular distribution of thy-1 in human brain assayed by a solid-phase radioimmunoassay. J. Neurochem. 1986, 46, 681-685
    • (1986) J. Neurochem , vol.46 , pp. 681-685
    • Almqvist, P.1    Carlsson, S.R.2    Hardy, J.A.3    Winblad, B.4
  • 64
    • 0031193390 scopus 로고    scopus 로고
    • Cloning of a novel human neural cell adhesion molecule gene (ncam2) that maps to chromosome region 21q21 and is potentially involved in down syndrome
    • Paoloni-Giacobino, A.; Chen, H.; Antonarakis, S.E. Cloning of a novel human neural cell adhesion molecule gene (ncam2) that maps to chromosome region 21q21 and is potentially involved in down syndrome. Genomics 1997, 43, 43-51
    • (1997) Genomics , vol.43 , pp. 43-51
    • Paoloni-Giacobino, A.1    Chen, H.2    Antonarakis, S.E.3
  • 66
    • 0034717512 scopus 로고    scopus 로고
    • Shared and unique roles of cap23 and gap43 in actin regulation, neurite outgrowth, and anatomical plasticity
    • Frey, D.; Laux, T.; Xu, L.; Schneider, C.; Caroni, P. Shared and unique roles of cap23 and gap43 in actin regulation, neurite outgrowth, and anatomical plasticity. J. Cell Biol. 2000, 149, 1443-1454
    • (2000) J. Cell Biol , vol.149 , pp. 1443-1454
    • Frey, D.1    Laux, T.2    Xu, L.3    Schneider, C.4    Caroni, P.5
  • 67
    • 0036814534 scopus 로고    scopus 로고
    • F3/contactin, a neuronal cell adhesion molecule implicated in axogenesis and myelination
    • Falk, J.; Bonnon, C.; Girault, J.A.; Faivre-Sarrailh, C. F3/contactin, a neuronal cell adhesion molecule implicated in axogenesis and myelination. Biol. Cell 2002, 94, 327-334
    • (2002) Biol. Cell , vol.94 , pp. 327-334
    • Falk, J.1    Bonnon, C.2    Girault, J.A.3    Faivre-Sarrailh, C.4
  • 69
    • 84863219195 scopus 로고    scopus 로고
    • Igsf8: A developmentally and functionally regulated cell adhesion molecule in olfactory sensory neuron axons and synapses
    • Ray, A.; Treloar, H.B. Igsf8: A developmentally and functionally regulated cell adhesion molecule in olfactory sensory neuron axons and synapses. Mol. Cell. Neurosci. 2012, 50, 238-249
    • (2012) Mol. Cell. Neurosci , vol.50 , pp. 238-249
    • Ray, A.1    Treloar, H.B.2
  • 70
    • 0034066303 scopus 로고    scopus 로고
    • Expression of T-cadherin (CDH13, h-cadherin) in human brain and its characteristics as a negative growth regulator of epidermal growth factor in neuroblastoma cells
    • Takeuchi, T.; Misaki, A.; Liang, S.B.; Tachibana, A.; Hayashi, N.; Sonobe, H.; Ohtsuki, Y. Expression of T-cadherin (CDH13, h-cadherin) in human brain and its characteristics as a negative growth regulator of epidermal growth factor in neuroblastoma cells. J. Neurochem. 2000, 74, 1489-1497
    • (2000) J. Neurochem , vol.74 , pp. 1489-1497
    • Takeuchi, T.1    Misaki, A.2    Liang, S.B.3    Tachibana, A.4    Hayashi, N.5    Sonobe, H.6    Ohtsuki, Y.7
  • 72
    • 0032533331 scopus 로고    scopus 로고
    • Neurotrimin mediates bifunctional effects on neurite outgrowth via homophilic and heterophilic interactions
    • Gil, O.D.; Zanazzi, G.; Struyk, A.F.; Salzer, J.L. Neurotrimin mediates bifunctional effects on neurite outgrowth via homophilic and heterophilic interactions. J. Neurosci. 1998, 18, 9312-9325
    • (1998) J. Neurosci , vol.18 , pp. 9312-9325
    • Gil, O.D.1    Zanazzi, G.2    Struyk, A.F.3    Salzer, J.L.4
  • 76
    • 33746704413 scopus 로고    scopus 로고
    • Identification of members of the annexin family in the detergent-insoluble fraction of rat morris hepatoma plasma membranes
    • Clifton, J.G.; Brown, M.K.; Huang, F.; Li, X.; Reutter, W.; Hofmann, W.; Hixson, D.C.; Josic, D. Identification of members of the annexin family in the detergent-insoluble fraction of rat morris hepatoma plasma membranes. J. Chromatogr. A 2006, 1123, 205-211
    • (2006) J. Chromatogr. A , vol.1123 , pp. 205-211
    • Clifton, J.G.1    Brown, M.K.2    Huang, F.3    Li, X.4    Reutter, W.5    Hofmann, W.6    Hixson, D.C.7    Josic, D.8
  • 77
    • 0026708526 scopus 로고
    • Ca(2+)-regulated actin and phospholipid binding protein (68 kD-protein) from bovine liver: Identification as a homologue for annexin VI and intracellular localization
    • Hosoya, H.; Kobayashi, R.; Tsukita, S.; Matsumura, F. Ca(2+)-regulated actin and phospholipid binding protein (68 kD-protein) from bovine liver: Identification as a homologue for annexin VI and intracellular localization. Cell Motil. Cytoskeleton 1992, 22, 200-210
    • (1992) Cell Motil. Cytoskeleton , vol.22 , pp. 200-210
    • Hosoya, H.1    Kobayashi, R.2    Tsukita, S.3    Matsumura, F.4
  • 78
    • 0025924751 scopus 로고
    • Ca2+-dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1
    • Tanaka, T.; Kadowaki, K.; Lazarides, E.; Sobue, K. Ca2+-dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1. J. Biol. Chem. 1991, 266, 1134-1140
    • (1991) J. Biol. Chem , vol.266 , pp. 1134-1140
    • Tanaka, T.1    Kadowaki, K.2    Lazarides, E.3    Sobue, K.4
  • 79
    • 3242875557 scopus 로고    scopus 로고
    • Axonal mitochondrial transport and potential are correlated
    • Miller, K.E.; Sheetz, M.P. Axonal mitochondrial transport and potential are correlated. J. Cell Sci. 2004, 117, 2791-2804
    • (2004) J. Cell Sci , vol.117 , pp. 2791-2804
    • Miller, K.E.1    Sheetz, M.P.2
  • 80
    • 33745921507 scopus 로고    scopus 로고
    • Mitochondria at the synapse
    • Ly, C.V.; Verstreken, P. Mitochondria at the synapse. Neuroscientist 2006, 12, 291-299
    • (2006) Neuroscientist , vol.12 , pp. 291-299
    • Ly, C.V.1    Verstreken, P.2
  • 81
    • 0028137817 scopus 로고
    • Mitochondria buffer physiological calcium loads in cultured rat dorsal root ganglion neurons
    • Werth, J.L.; Thayer, S.A. Mitochondria buffer physiological calcium loads in cultured rat dorsal root ganglion neurons. J. Neurosci. 1994, 14, 348-356
    • (1994) J. Neurosci , vol.14 , pp. 348-356
    • Werth, J.L.1    Thayer, S.A.2
  • 82
    • 0037101606 scopus 로고    scopus 로고
    • Presynaptic mitochondrial calcium sequestration influences transmission at mammalian central synapses
    • Billups, B.; Forsythe, I.D. Presynaptic mitochondrial calcium sequestration influences transmission at mammalian central synapses. J. Neurosci. 2002, 22, 5840-5847
    • (2002) J. Neurosci , vol.22 , pp. 5840-5847
    • Billups, B.1    Forsythe, I.D.2
  • 83
    • 0038381516 scopus 로고    scopus 로고
    • Mitochondrial regulation of synaptic plasticity in the hippocampus
    • Levy, M.; Faas, G.C.; Saggau, P.; Craigen, W.J.; Sweatt, J.D. Mitochondrial regulation of synaptic plasticity in the hippocampus. J. Biol. Chem. 2003, 278, 17727-17734
    • (2003) J. Biol. Chem , vol.278 , pp. 17727-17734
    • Levy, M.1    Faas, G.C.2    Saggau, P.3    Craigen, W.J.4    Sweatt, J.D.5
  • 84
    • 0030891028 scopus 로고    scopus 로고
    • Mitochondrial involvement in post-tetanic potentiation of synaptic transmission
    • Tang, Y.; Zucker, R.S. Mitochondrial involvement in post-tetanic potentiation of synaptic transmission. Neuron 1997, 18, 483-491
    • (1997) Neuron , vol.18 , pp. 483-491
    • Tang, Y.1    Zucker, R.S.2
  • 86
    • 0034671350 scopus 로고    scopus 로고
    • Specialized synapse-associated structures within the calyx of held
    • Rowland, K.C.; Irby, N.K.; Spirou, G.A. Specialized synapse-associated structures within the calyx of held. J. Neurosci. 2000, 20, 9135-9144
    • (2000) J. Neurosci , vol.20 , pp. 9135-9144
    • Rowland, K.C.1    Irby, N.K.2    Spirou, G.A.3
  • 87
    • 75749098116 scopus 로고    scopus 로고
    • The micro-architecture of mitochondria at active zones: Electron tomography reveals novel anchoring scaffolds and cristae structured for high-rate metabolism
    • Perkins, G.A.; Tjong, J.; Brown, J.M.; Poquiz, P.H.; Scott, R.T.; Kolson, D.R.; Ellisman, M.H.; Spirou, G.A. The micro-architecture of mitochondria at active zones: Electron tomography reveals novel anchoring scaffolds and cristae structured for high-rate metabolism. J. Neurosci. 2010, 30, 1015-1026
    • (2010) J. Neurosci , vol.30 , pp. 1015-1026
    • Perkins, G.A.1    Tjong, J.2    Brown, J.M.3    Poquiz, P.H.4    Scott, R.T.5    Kolson, D.R.6    Ellisman, M.H.7    Spirou, G.A.8
  • 89
    • 23044492524 scopus 로고    scopus 로고
    • Opening of plasma membrane voltage-dependent anion channels (VDAC) precedes caspase activation in neuronal apoptosis induced by toxic stimuli
    • Elinder, F.; Akanda, N.; Tofighi, R.; Shimizu, S.; Tsujimoto, Y.; Orrenius, S.; Ceccatelli, S. Opening of plasma membrane voltage-dependent anion channels (VDAC) precedes caspase activation in neuronal apoptosis induced by toxic stimuli. Cell Death Differ. 2005, 12, 1134-1140
    • (2005) Cell Death Differ , vol.12 , pp. 1134-1140
    • Elinder, F.1    Akanda, N.2    Tofighi, R.3    Shimizu, S.4    Tsujimoto, Y.5    Orrenius, S.6    Ceccatelli, S.7
  • 90
    • 2942703809 scopus 로고    scopus 로고
    • Reversal of obesity by targeted ablation of adipose tissue
    • Kolonin, M.G.; Saha, P.K.; Chan, L.; Pasqualini, R.; Arap, W. Reversal of obesity by targeted ablation of adipose tissue. Nat. Med. 2004, 10, 625-632
    • (2004) Nat. Med , vol.10 , pp. 625-632
    • Kolonin, M.G.1    Saha, P.K.2    Chan, L.3    Pasqualini, R.4    Arap, W.5
  • 91
    • 34247402973 scopus 로고    scopus 로고
    • Voltage-dependent anion channel (VDAC) participates in amyloid beta-induced toxicity and interacts with plasma membrane estrogen receptor alpha in septal and hippocampal neurons
    • Marin, R.; Ramirez, C.M.; Gonzalez, M.; Gonzalez-Munoz, E.; Zorzano, A.; Camps, M.; Alonso, R.; Diaz, M. Voltage-dependent anion channel (VDAC) participates in amyloid beta-induced toxicity and interacts with plasma membrane estrogen receptor alpha in septal and hippocampal neurons. Mol. Membr. Biol. 2007, 24, 148-160
    • (2007) Mol. Membr. Biol , vol.24 , pp. 148-160
    • Marin, R.1    Ramirez, C.M.2    Gonzalez, M.3    Gonzalez-Munoz, E.4    Zorzano, A.5    Camps, M.6    Alonso, R.7    Diaz, M.8
  • 93
    • 0033133729 scopus 로고    scopus 로고
    • Mitochondrial-matrix proteins at unexpected locations: Are they exported?
    • Soltys, B.J.; Gupta, R.S. Mitochondrial-matrix proteins at unexpected locations: Are they exported? Trends Biochem. Sci. 1999, 24, 174-177
    • (1999) Trends Biochem. Sci , vol.24 , pp. 174-177
    • Soltys, B.J.1    Gupta, R.S.2
  • 94
    • 33745136102 scopus 로고    scopus 로고
    • The voltage-dependent anion channel (VDAC): Function in intracellular signalling, cell life and cell death
    • Shoshan-Barmatz, V.; Israelson, A.; Brdiczka, D.; Sheu, S.S. The voltage-dependent anion channel (VDAC): Function in intracellular signalling, cell life and cell death. Curr. Pharm. Des. 2006, 12, 2249-2270
    • (2006) Curr. Pharm. Des , vol.12 , pp. 2249-2270
    • Shoshan-Barmatz, V.1    Israelson, A.2    Brdiczka, D.3    Sheu, S.S.4


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