메뉴 건너뛰기




Volumn 18, Issue 11, 2008, Pages 552-559

Two-way traffic on the road to plasma membrane repair

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM;

EID: 54049109535     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2008.09.001     Document Type: Review
Times cited : (112)

References (73)
  • 1
    • 0028014529 scopus 로고
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release
    • Steinhardt R.A., et al. Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release. Science 263 (1994) 390-393
    • (1994) Science , vol.263 , pp. 390-393
    • Steinhardt, R.A.1
  • 2
    • 0035958557 scopus 로고    scopus 로고
    • 2+-regulated exocytosis of lysosomes
    • 2+-regulated exocytosis of lysosomes. Cell 106 (2001) 157-169
    • (2001) Cell , vol.106 , pp. 157-169
    • Reddy, A.1
  • 3
    • 0030985763 scopus 로고    scopus 로고
    • Loss, restoration and maintenance of plasma membrane integrity
    • McNeil P.L., and Steinhardt R.A. Loss, restoration and maintenance of plasma membrane integrity. J. Cell Biol. 137 (1997) 1-4
    • (1997) J. Cell Biol. , vol.137 , pp. 1-4
    • McNeil, P.L.1    Steinhardt, R.A.2
  • 4
    • 33644878204 scopus 로고    scopus 로고
    • Membrane resealing: synaptotagmin VII keeps running the show
    • Andrews N.W. Membrane resealing: synaptotagmin VII keeps running the show. Sci. STKE 282 (2005) pe19
    • (2005) Sci. STKE , vol.282
    • Andrews, N.W.1
  • 5
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • Gurcel L., et al. Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell 126 (2006) 1135-1145
    • (2006) Cell , vol.126 , pp. 1135-1145
    • Gurcel, L.1
  • 6
    • 3342901591 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways defend against bacterial pore-forming toxins
    • Huffman D.L., et al. Mitogen-activated protein kinase pathways defend against bacterial pore-forming toxins. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 10995-11000
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10995-11000
    • Huffman, D.L.1
  • 7
    • 0026729383 scopus 로고
    • Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage
    • McNeil P.L., and Khakee R. Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage. Am. J. Pathol. 140 (1992) 1097-1109
    • (1992) Am. J. Pathol. , vol.140 , pp. 1097-1109
    • McNeil, P.L.1    Khakee, R.2
  • 8
    • 0037738510 scopus 로고    scopus 로고
    • Defective membrane repair in dysferlin-deficient muscular dystrophy
    • Bansal D., et al. Defective membrane repair in dysferlin-deficient muscular dystrophy. Nature 423 (2003) 168-172
    • (2003) Nature , vol.423 , pp. 168-172
    • Bansal, D.1
  • 9
    • 0042978564 scopus 로고    scopus 로고
    • Impaired membrane resealing and autoimmune myositis in synaptotagmin VII-deficient mice
    • Chakrabarti S., et al. Impaired membrane resealing and autoimmune myositis in synaptotagmin VII-deficient mice. J. Cell Biol. 162 (2003) 543-549
    • (2003) J. Cell Biol. , vol.162 , pp. 543-549
    • Chakrabarti, S.1
  • 12
    • 0029609143 scopus 로고
    • Calcium-regulated exocytosis is required for cell membrane resealing
    • Bi G.Q., et al. Calcium-regulated exocytosis is required for cell membrane resealing. J. Cell Biol. 131 (1995) 1747-1758
    • (1995) J. Cell Biol. , vol.131 , pp. 1747-1758
    • Bi, G.Q.1
  • 13
    • 0029585288 scopus 로고
    • Vesicle accumulation and exocytosis at sites of plasma membrane disruption
    • Miyake K., and McNeil P.L. Vesicle accumulation and exocytosis at sites of plasma membrane disruption. J. Cell Biol. 131 (1995) 1737-1745
    • (1995) J. Cell Biol. , vol.131 , pp. 1737-1745
    • Miyake, K.1    McNeil, P.L.2
  • 14
    • 0029764204 scopus 로고    scopus 로고
    • 2+ triggers massive exocytosis in Chinese hamster ovary cells
    • 2+ triggers massive exocytosis in Chinese hamster ovary cells. EMBO J. 15 (1996) 3787-3791
    • (1996) EMBO J. , vol.15 , pp. 3787-3791
    • Coorssen, J.R.1
  • 15
    • 0030003892 scopus 로고    scopus 로고
    • A biosynthetic regulated secretory pathway in constitutive secretory cells
    • Chavez R.A., et al. A biosynthetic regulated secretory pathway in constitutive secretory cells. J. Cell Biol. 133 (1996) 1177-1191
    • (1996) J. Cell Biol. , vol.133 , pp. 1177-1191
    • Chavez, R.A.1
  • 16
    • 0027049531 scopus 로고
    • Lysosome recruitment and fusion are early events required for trypanosome invasion of mammalian cells
    • Tardieux I., et al. Lysosome recruitment and fusion are early events required for trypanosome invasion of mammalian cells. Cell 71 (1992) 1117-1130
    • (1992) Cell , vol.71 , pp. 1117-1130
    • Tardieux, I.1
  • 17
    • 0037175388 scopus 로고    scopus 로고
    • Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells
    • Jaiswal J.K., et al. Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells. J. Cell Biol. 159 (2002) 625-635
    • (2002) J. Cell Biol. , vol.159 , pp. 625-635
    • Jaiswal, J.K.1
  • 18
    • 0034256042 scopus 로고    scopus 로고
    • Regulated secretion of conventional lysosomes
    • Andrews N.W. Regulated secretion of conventional lysosomes. Trends Cell Biol. 10 (2000) 316-321
    • (2000) Trends Cell Biol. , vol.10 , pp. 316-321
    • Andrews, N.W.1
  • 19
    • 0036500836 scopus 로고    scopus 로고
    • Repairing a torn cell surface: make way, lysosomes to the rescue
    • McNeil P.L. Repairing a torn cell surface: make way, lysosomes to the rescue. J. Cell Sci. 115 (2002) 873-879
    • (2002) J. Cell Sci. , vol.115 , pp. 873-879
    • McNeil, P.L.1
  • 20
    • 0344824647 scopus 로고    scopus 로고
    • Plasma membrane disruption: repair, prevention, adaptation
    • McNeil P.L., and Steinhardt R.A. Plasma membrane disruption: repair, prevention, adaptation. Annu. Rev. Cell Dev. Biol. 19 (2003) 697-731
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 697-731
    • McNeil, P.L.1    Steinhardt, R.A.2
  • 22
    • 33748940056 scopus 로고    scopus 로고
    • Regulating secretory lysosomes
    • Holt O.J., et al. Regulating secretory lysosomes. J. Biochem. 140 (2006) 7-12
    • (2006) J. Biochem. , vol.140 , pp. 7-12
    • Holt, O.J.1
  • 23
    • 0033923370 scopus 로고    scopus 로고
    • Lysosome-related organelles
    • Dell'Angelica E.C., et al. Lysosome-related organelles. FASEB J. 14 (2000) 1265-1278
    • (2000) FASEB J. , vol.14 , pp. 1265-1278
    • Dell'Angelica, E.C.1
  • 24
    • 0034689023 scopus 로고    scopus 로고
    • 2+-dependent exocytosis of lysosomes in fibroblasts
    • 2+-dependent exocytosis of lysosomes in fibroblasts. J. Cell Biol. 148 (2000) 1141-1149
    • (2000) J. Cell Biol. , vol.148 , pp. 1141-1149
    • Martinez, I.1
  • 25
    • 33846498689 scopus 로고    scopus 로고
    • Expression and function of synaptotagmin VII in CTLs
    • Fowler K.T., et al. Expression and function of synaptotagmin VII in CTLs. J. Immunol. 178 (2007) 1498-1504
    • (2007) J. Immunol. , vol.178 , pp. 1498-1504
    • Fowler, K.T.1
  • 26
    • 44449175502 scopus 로고    scopus 로고
    • Synaptotagmin VII regulates bone remodeling by modulating osteoclast and osteoblast secretion
    • Zhao H., et al. Synaptotagmin VII regulates bone remodeling by modulating osteoclast and osteoblast secretion. Dev. Cell 14 (2008) 914-925
    • (2008) Dev. Cell , vol.14 , pp. 914-925
    • Zhao, H.1
  • 27
    • 0036903036 scopus 로고    scopus 로고
    • Regulated exocytosis: a novel, widely expressed system
    • Borgonovo B., et al. Regulated exocytosis: a novel, widely expressed system. Nat. Cell Biol. 4 (2002) 955-962
    • (2002) Nat. Cell Biol. , vol.4 , pp. 955-962
    • Borgonovo, B.1
  • 28
    • 9444225970 scopus 로고    scopus 로고
    • Enlargeosome, an exocytic vesicle resistant to nonionic detergents, undergoes endocytosis via a nonacidic route
    • Cocucci E., et al. Enlargeosome, an exocytic vesicle resistant to nonionic detergents, undergoes endocytosis via a nonacidic route. Mol. Biol. Cell 15 (2004) 5356-5368
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5356-5368
    • Cocucci, E.1
  • 29
    • 1642488945 scopus 로고    scopus 로고
    • The AHNAKs are a class of giant propeller-like proteins that associate with calcium channel proteins of cardiomyocytes and other cells
    • Komuro A., et al. The AHNAKs are a class of giant propeller-like proteins that associate with calcium channel proteins of cardiomyocytes and other cells. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 4053-4058
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 4053-4058
    • Komuro, A.1
  • 30
    • 37849031432 scopus 로고    scopus 로고
    • A scaffold protein, AHNAK1, is required for calcium signaling during T cell activation
    • Matza D., et al. A scaffold protein, AHNAK1, is required for calcium signaling during T cell activation. Immunity 28 (2008) 64-74
    • (2008) Immunity , vol.28 , pp. 64-74
    • Matza, D.1
  • 31
    • 28744458169 scopus 로고    scopus 로고
    • Ahnak is critical for cardiac Ca(V)1,2 calcium channel function and its β-adrenergic regulation
    • Haase H., et al. Ahnak is critical for cardiac Ca(V)1,2 calcium channel function and its β-adrenergic regulation. FASEB J. 19 (2005) 1969-1977
    • (2005) FASEB J. , vol.19 , pp. 1969-1977
    • Haase, H.1
  • 32
    • 0033637154 scopus 로고    scopus 로고
    • A decrease in membrane tension precedes successful cell-membrane repair
    • Togo T., et al. A decrease in membrane tension precedes successful cell-membrane repair. Mol. Biol. Cell 11 (2000) 4339-4346
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4339-4346
    • Togo, T.1
  • 33
    • 0034130361 scopus 로고    scopus 로고
    • Patching plasma membrane disruptions with cytoplasmic membrane
    • McNeil P.L., et al. Patching plasma membrane disruptions with cytoplasmic membrane. J. Cell Sci. 113 (2000) 1891-1902
    • (2000) J. Cell Sci. , vol.113 , pp. 1891-1902
    • McNeil, P.L.1
  • 34
    • 0030801401 scopus 로고    scopus 로고
    • 2+- dependent vesicle-vesicle fusion events
    • 2+- dependent vesicle-vesicle fusion events. J. Cell Biol. 139 (1997) 63-74
    • (1997) J. Cell Biol. , vol.139 , pp. 63-74
    • Terasaki, M.1
  • 35
    • 0038641718 scopus 로고    scopus 로고
    • Cross-linking of cellular proteins by tissue transglutaminase during necrotic cell death: a mechanism for maintaining tissue integrity
    • Nicholas B., et al. Cross-linking of cellular proteins by tissue transglutaminase during necrotic cell death: a mechanism for maintaining tissue integrity. Biochem. J. 371 (2003) 413-422
    • (2003) Biochem. J. , vol.371 , pp. 413-422
    • Nicholas, B.1
  • 36
    • 0032824155 scopus 로고    scopus 로고
    • Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis
    • Haroon Z.A., et al. Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis. FASEB J. 13 (1999) 1787-1795
    • (1999) FASEB J. , vol.13 , pp. 1787-1795
    • Haroon, Z.A.1
  • 37
    • 0037378609 scopus 로고    scopus 로고
    • Transglutaminase type II plays a protective role in hepatic injury
    • Nardacci R., et al. Transglutaminase type II plays a protective role in hepatic injury. Am. J. Pathol. 162 (2003) 1293-1303
    • (2003) Am. J. Pathol. , vol.162 , pp. 1293-1303
    • Nardacci, R.1
  • 38
    • 0043124302 scopus 로고    scopus 로고
    • Importance of tissue transglutaminase in repair of extracellular matrices and cell death of dermal fibroblasts after exposure to a solarium ultraviolet A source
    • Gross S.R., et al. Importance of tissue transglutaminase in repair of extracellular matrices and cell death of dermal fibroblasts after exposure to a solarium ultraviolet A source. J. Invest. Dermatol. 121 (2003) 412-423
    • (2003) J. Invest. Dermatol. , vol.121 , pp. 412-423
    • Gross, S.R.1
  • 39
    • 47349094892 scopus 로고    scopus 로고
    • Transglutaminase 2 activity promotes membrane resealing after mechanical damage in the lung cancer cell line A549
    • Kawai Y., et al. Transglutaminase 2 activity promotes membrane resealing after mechanical damage in the lung cancer cell line A549. Cell Biol. Int. 32 (2008) 928-934
    • (2008) Cell Biol. Int. , vol.32 , pp. 928-934
    • Kawai, Y.1
  • 40
    • 0035853082 scopus 로고    scopus 로고
    • Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O
    • Walev I., et al. Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 3185-3190
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 3185-3190
    • Walev, I.1
  • 41
    • 40849118150 scopus 로고    scopus 로고
    • 2+-dependent endocytosis
    • 2+-dependent endocytosis. J. Cell Biol. 180 (2008) 905-914
    • (2008) J. Cell Biol. , vol.180 , pp. 905-914
    • Idone, V.1
  • 42
    • 0024425302 scopus 로고
    • Complement membrane attack on nucleated cells: resistance, recovery and non-lethal effects
    • Morgan B.P. Complement membrane attack on nucleated cells: resistance, recovery and non-lethal effects. Biochem. J. 264 (1989) 1-14
    • (1989) Biochem. J. , vol.264 , pp. 1-14
    • Morgan, B.P.1
  • 43
    • 0033067513 scopus 로고    scopus 로고
    • The mechanism of facilitated cell membrane resealing
    • Togo T., et al. The mechanism of facilitated cell membrane resealing. J. Cell Sci. 112 (1999) 719-731
    • (1999) J. Cell Sci. , vol.112 , pp. 719-731
    • Togo, T.1
  • 44
    • 0029148760 scopus 로고
    • Complement membrane attack complex, perforin, and bacterial exotoxins induce in K562 cells calcium-dependent cross-protection from lysis
    • Reiter Y., et al. Complement membrane attack complex, perforin, and bacterial exotoxins induce in K562 cells calcium-dependent cross-protection from lysis. J. Immunol. 155 (1995) 2203-2210
    • (1995) J. Immunol. , vol.155 , pp. 2203-2210
    • Reiter, Y.1
  • 45
    • 0034759113 scopus 로고    scopus 로고
    • An actin barrier to resealing
    • Miyake K., et al. An actin barrier to resealing. J. Cell Sci. 114 (2001) 3487-3494
    • (2001) J. Cell Sci. , vol.114 , pp. 3487-3494
    • Miyake, K.1
  • 46
    • 0027940649 scopus 로고
    • Extent and mechanism of sealing in transected giant axons of squid and earthworms
    • Krause T.L., et al. Extent and mechanism of sealing in transected giant axons of squid and earthworms. J. Neurosci. 14 (1994) 6638-6651
    • (1994) J. Neurosci. , vol.14 , pp. 6638-6651
    • Krause, T.L.1
  • 47
    • 0023695633 scopus 로고
    • Vacuolation of muscle fibers near sarcolemmal breaks represents T-tubule dilatation secondary to enhanced sodium pump activity
    • Casademont J., et al. Vacuolation of muscle fibers near sarcolemmal breaks represents T-tubule dilatation secondary to enhanced sodium pump activity. J. Neuropathol. Exp. Neurol. 47 (1988) 618-628
    • (1988) J. Neuropathol. Exp. Neurol. , vol.47 , pp. 618-628
    • Casademont, J.1
  • 48
    • 17344365600 scopus 로고    scopus 로고
    • Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy
    • Liu J., et al. Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy. Nat. Genet. 20 (1998) 31-36
    • (1998) Nat. Genet. , vol.20 , pp. 31-36
    • Liu, J.1
  • 49
    • 1842556210 scopus 로고    scopus 로고
    • Dysferlin and the plasma membrane repair in muscular dystrophy
    • Bansal D., and Campbell K.P. Dysferlin and the plasma membrane repair in muscular dystrophy. Trends Cell Biol. 14 (2004) 206-213
    • (2004) Trends Cell Biol. , vol.14 , pp. 206-213
    • Bansal, D.1    Campbell, K.P.2
  • 50
    • 26244435478 scopus 로고    scopus 로고
    • 2+ concentration to SNARE-mediated membrane fusion
    • 2+ concentration to SNARE-mediated membrane fusion. Mol. Biol. Cell 16 (2005) 4755-4764
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4755-4764
    • Bhalla, A.1
  • 51
  • 52
    • 1342267006 scopus 로고    scopus 로고
    • Caveolinopathies: mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases
    • Woodman S.E., et al. Caveolinopathies: mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases. Neurology 62 (2004) 538-543
    • (2004) Neurology , vol.62 , pp. 538-543
    • Woodman, S.E.1
  • 53
    • 33749015734 scopus 로고    scopus 로고
    • Molecular mechanisms of muscular dystrophies: old and new players
    • Davies K.E., and Nowak K.J. Molecular mechanisms of muscular dystrophies: old and new players. Nat. Rev. Mol. Cell Biol. 7 (2006) 762-773
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 762-773
    • Davies, K.E.1    Nowak, K.J.2
  • 54
    • 0031030664 scopus 로고    scopus 로고
    • Caveolin-3 associates with developing T-tubules during muscle differentiation
    • Parton R.G., et al. Caveolin-3 associates with developing T-tubules during muscle differentiation. J. Cell Biol. 136 (1997) 137-154
    • (1997) J. Cell Biol. , vol.136 , pp. 137-154
    • Parton, R.G.1
  • 55
    • 0035877753 scopus 로고    scopus 로고
    • Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities
    • Galbiati F., et al. Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities. J. Biol. Chem. 276 (2001) 21425-21433
    • (2001) J. Biol. Chem. , vol.276 , pp. 21425-21433
    • Galbiati, F.1
  • 56
    • 0037124116 scopus 로고    scopus 로고
    • Inhibition of lipid raft-dependent signaling by a dystrophy-associated mutant of caveolin-3
    • Carozzi A.J., et al. Inhibition of lipid raft-dependent signaling by a dystrophy-associated mutant of caveolin-3. J. Biol. Chem. 277 (2002) 17944-17949
    • (2002) J. Biol. Chem. , vol.277 , pp. 17944-17949
    • Carozzi, A.J.1
  • 57
    • 44449121951 scopus 로고    scopus 로고
    • Caveolin regulates endocytosis of the muscle repair protein, dysferlin
    • Hernandez-Deviez D.J., et al. Caveolin regulates endocytosis of the muscle repair protein, dysferlin. J. Biol. Chem. 283 (2008) 6476-6488
    • (2008) J. Biol. Chem. , vol.283 , pp. 6476-6488
    • Hernandez-Deviez, D.J.1
  • 58
    • 0037744845 scopus 로고    scopus 로고
    • Endocytosis of synaptotagmin 1 is mediated by a novel, tryptophan-containing motif
    • Jarousse N., et al. Endocytosis of synaptotagmin 1 is mediated by a novel, tryptophan-containing motif. Traffic 4 (2003) 468-478
    • (2003) Traffic , vol.4 , pp. 468-478
    • Jarousse, N.1
  • 59
    • 0037385218 scopus 로고    scopus 로고
    • Internalization signals in synaptotagmin VII utilizing two independent pathways are masked by intramolecular inhibitions
    • Dasgupta S., and Kelly R.B. Internalization signals in synaptotagmin VII utilizing two independent pathways are masked by intramolecular inhibitions. J. Cell Sci. 116 (2003) 1327-1337
    • (2003) J. Cell Sci. , vol.116 , pp. 1327-1337
    • Dasgupta, S.1    Kelly, R.B.2
  • 60
    • 0035880516 scopus 로고    scopus 로고
    • The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle
    • Matsuda C., et al. The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle. Hum. Mol. Genet. 10 (2001) 1761-1766
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1761-1766
    • Matsuda, C.1
  • 61
    • 34047273570 scopus 로고    scopus 로고
    • Calpain is required for the rapid, calcium-dependent repair of wounded plasma membrane
    • Mellgren R.L., et al. Calpain is required for the rapid, calcium-dependent repair of wounded plasma membrane. J. Biol. Chem. 282 (2007) 2567-2575
    • (2007) J. Biol. Chem. , vol.282 , pp. 2567-2575
    • Mellgren, R.L.1
  • 62
    • 33845951914 scopus 로고    scopus 로고
    • Requirement for annexin A1 in plasma membrane repair
    • McNeil A.K., et al. Requirement for annexin A1 in plasma membrane repair. J. Biol. Chem. 281 (2006) 35202-35207
    • (2006) J. Biol. Chem. , vol.281 , pp. 35202-35207
    • McNeil, A.K.1
  • 63
    • 0034511895 scopus 로고    scopus 로고
    • Beta-granule transport and exocytosis
    • Easom R.A. Beta-granule transport and exocytosis. Semin. Cell Dev. Biol. 11 (2000) 253-266
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 253-266
    • Easom, R.A.1
  • 64
    • 0038050215 scopus 로고    scopus 로고
    • Regulated exocytosis and SNARE function
    • Sollner T.H. Regulated exocytosis and SNARE function. Mol. Membr. Biol. 20 (2003) 209-220
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 209-220
    • Sollner, T.H.1
  • 66
    • 0029666286 scopus 로고    scopus 로고
    • 2+-dependent exocytotic pathways in Chinese hamster ovary fibroblasts revealed by a caged-Ca2+ compound
    • 2+-dependent exocytotic pathways in Chinese hamster ovary fibroblasts revealed by a caged-Ca2+ compound. J. Biol. Chem. 271 (1996) 17751-17754
    • (1996) J. Biol. Chem. , vol.271 , pp. 17751-17754
    • Ninomiya, Y.1
  • 67
    • 0030615262 scopus 로고    scopus 로고
    • 2+-regulated exocytic vesicles in fibroblasts and epithelial cells
    • 2+-regulated exocytic vesicles in fibroblasts and epithelial cells. J. Cell Biol. 137 (1997) 93-104
    • (1997) J. Cell Biol. , vol.137 , pp. 93-104
    • Rodriguez, A.1
  • 68
    • 0030248423 scopus 로고    scopus 로고
    • Secretory lysosomes - a special mechanism of regulated secretion in haemopoietic cells
    • Griffiths G.M. Secretory lysosomes - a special mechanism of regulated secretion in haemopoietic cells. Trends Cell Biol. 6 (1996) 329-332
    • (1996) Trends Cell Biol. , vol.6 , pp. 329-332
    • Griffiths, G.M.1
  • 69
    • 2442584514 scopus 로고    scopus 로고
    • Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis
    • Rao S.K., et al. Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis. J. Biol. Chem. 279 (2004) 20471-20479
    • (2004) J. Biol. Chem. , vol.279 , pp. 20471-20479
    • Rao, S.K.1
  • 70
    • 33745029549 scopus 로고    scopus 로고
    • 2+-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion
    • 2+-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion. Nat. Struct. Mol. Biol. 13 (2006) 323-330
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 323-330
    • Bhalla, A.1
  • 71
    • 0141960930 scopus 로고    scopus 로고
    • 2+ sensor for neurotransmitter release
    • 2+ sensor for neurotransmitter release. Trends Neurosci. 26 (2003) 413-422
    • (2003) Trends Neurosci. , vol.26 , pp. 413-422
    • Koh, T.W.1    Bellen, H.J.2
  • 72
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner S.D., and Schmid S.L. Regulated portals of entry into the cell. Nature 422 (2003) 37-44
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 73
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • Mayor S., and Pagano R.E. Pathways of clathrin-independent endocytosis. Nat. Rev. Mol. Cell Biol. 8 (2007) 603-612
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.