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Volumn 1742, Issue 1-3, 2004, Pages 103-112

The Ca 2+/Mn 2+ pumps in the Golgi apparatus

Author keywords

Calcium; Golgi; Hailey Hailey; Manganese; SERCA; SPCA1

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM BINDING PROTEIN; CALCIUM CHANNEL; MANGANESE; CARRIER PROTEIN;

EID: 84862485550     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2004.08.018     Document Type: Conference Paper
Times cited : (111)

References (100)
  • 1
    • 0030982434 scopus 로고    scopus 로고
    • High-resolution calcium mapping of the endoplasmic reticulum-Golgi- exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells
    • R. Pezzati, M. Bossi, P. Podini, J. Meldolesi, and F. Grohovaz High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells Mol. Biol. Cell 8 1997 1501 1512
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1501-1512
    • Pezzati, R.1    Bossi, M.2    Podini, P.3    Meldolesi, J.4    Grohovaz, F.5
  • 2
    • 0026335806 scopus 로고
    • Calcium sequestration in the Golgi apparatus of cultured mammalian cells revealed by laser scanning confocal microscopy and ion microscopy
    • S. Chandra, E.P. Kable, G.H. Morrison, and W.W. Webb Calcium sequestration in the Golgi apparatus of cultured mammalian cells revealed by laser scanning confocal microscopy and ion microscopy J. Cell. Sci. 100 1991 747 752
    • (1991) J. Cell. Sci. , vol.100 , pp. 747-752
    • Chandra, S.1    Kable, E.P.2    Morrison, G.H.3    Webb, W.W.4
  • 3
    • 0028131971 scopus 로고
    • Transport via the regulated secretory pathway in semi-intact PC12 cells: Role of intra-cisternal calcium and pH in the transport and sorting of secretogranin II
    • L. Carnell, and H.P. Moore Transport via the regulated secretory pathway in semi-intact PC12 cells: role of intra-cisternal calcium and pH in the transport and sorting of secretogranin II J. Cell Biol. 127 1994 693 705
    • (1994) J. Cell Biol. , vol.127 , pp. 693-705
    • Carnell, L.1    Moore, H.P.2
  • 5
    • 0026801231 scopus 로고
    • 2+-dependent Golgi endoproteases
    • 2+-dependent Golgi endoproteases J. Biol. Chem. 267 1992 17465 17471
    • (1992) J. Biol. Chem. , vol.267 , pp. 17465-17471
    • Oda, K.1
  • 6
    • 0028791675 scopus 로고
    • The Brefeldin A-induced retrograde transport from the Golgi apparatus to the endoplasmic reticulum depends on calcium sequestered to intracellular stores
    • N.E. Ivessa, C. De Lemos-Chiarini, D. Gravotta, D.D. Sabatini, and G. Kreibich The Brefeldin A-induced retrograde transport from the Golgi apparatus to the endoplasmic reticulum depends on calcium sequestered to intracellular stores J. Biol. Chem. 270 1995 25960 25967
    • (1995) J. Biol. Chem. , vol.270 , pp. 25960-25967
    • Ivessa, N.E.1    De Lemos-Chiarini, C.2    Gravotta, D.3    Sabatini, D.D.4    Kreibich, G.5
  • 7
    • 0034703092 scopus 로고    scopus 로고
    • Regulation of intra-Golgi membrane transport by calcium
    • A. Porat, and Z. Elazar Regulation of intra-Golgi membrane transport by calcium J. Biol. Chem. 275 2000 29233 29237
    • (2000) J. Biol. Chem. , vol.275 , pp. 29233-29237
    • Porat, A.1    Elazar, Z.2
  • 8
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • E. Chanat, and W.B. Huttner Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network J. Cell Biol. 115 1991 1505 1519
    • (1991) J. Cell Biol. , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 9
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • M.J. Berridge Inositol trisphosphate and calcium signalling Nature 361 1993 315 325
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 11
    • 0028318208 scopus 로고
    • Molecular cloning and sequencing of calnexin-t. An abundant male germ cell-specific calcium-binding protein of the endoplasmic reticulum
    • S. Ohsako, Y. Hayashi, and D. Bunick Molecular cloning and sequencing of calnexin-t. An abundant male germ cell-specific calcium-binding protein of the endoplasmic reticulum J. Biol. Chem. 269 1994 14140 14148
    • (1994) J. Biol. Chem. , vol.269 , pp. 14140-14148
    • Ohsako, S.1    Hayashi, Y.2    Bunick, D.3
  • 12
    • 0033978227 scopus 로고    scopus 로고
    • 2+-binding proteins localised to the secretory pathway of mammalian cells
    • 2+-binding proteins localised to the secretory pathway of mammalian cells FEBS Lett. 466 2000 11 18
    • (2000) FEBS Lett. , vol.466 , pp. 11-18
    • Honore, B.1    Vorum, H.2
  • 14
    • 0036176367 scopus 로고    scopus 로고
    • The calcium-binding protein p54/NEFA is a novel luminal resident of medial Golgi cisternae that traffics independently of mannosidase II
    • V.M. Morel-Huaux, M. Pypaert, S. Wouters, A.M. Tartakoff, U. Jurgan, K. Gevaert, and P.J. Courtoy The calcium-binding protein p54/NEFA is a novel luminal resident of medial Golgi cisternae that traffics independently of mannosidase II Eur. J. Cell Biol. 81 2002 87 100
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 87-100
    • Morel-Huaux, V.M.1    Pypaert, M.2    Wouters, S.3    Tartakoff, A.M.4    Jurgan, U.5    Gevaert, K.6    Courtoy, P.J.7
  • 15
    • 0033134009 scopus 로고    scopus 로고
    • Human calumenin localizes to the secretory pathway and is secreted to the medium
    • H. Vorum, H. Hager, B.M. Christensen, S. Nielsen, and B. Honore Human calumenin localizes to the secretory pathway and is secreted to the medium Exp. Cell Res. 248 1999 473 481
    • (1999) Exp. Cell Res. , vol.248 , pp. 473-481
    • Vorum, H.1    Hager, H.2    Christensen, B.M.3    Nielsen, S.4    Honore, B.5
  • 16
    • 0032530396 scopus 로고    scopus 로고
    • 2+ store, with functional properties distinct from those of the endoplasmic reticulum
    • 2+ store, with functional properties distinct from those of the endoplasmic reticulum EMBO J. 17 1998 5298 5308
    • (1998) EMBO J. , vol.17 , pp. 5298-5308
    • Pinton, P.1    Pozzan, T.2    Rizzuto, R.3
  • 17
    • 0035039215 scopus 로고    scopus 로고
    • Mouse mast cell secretory granules can function as intracellular ionic oscillators
    • I. Quesada, W.C. Chin, J. Steed, P. Campos-Bedolla, and P. Verdugo Mouse mast cell secretory granules can function as intracellular ionic oscillators Biophys. J. 80 2001 2133 2139
    • (2001) Biophys. J. , vol.80 , pp. 2133-2139
    • Quesada, I.1    Chin, W.C.2    Steed, J.3    Campos-Bedolla, P.4    Verdugo, P.5
  • 19
    • 0034642182 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of human cytosolic aminopeptidase P: A single manganese(II)-dependent enzyme
    • G.S. Cottrell, N.M. Hooper, and A.J. Turner Cloning, expression, and characterization of human cytosolic aminopeptidase P: a single manganese(II)-dependent enzyme Biochemistry 39 2000 15121 15128
    • (2000) Biochemistry , vol.39 , pp. 15121-15128
    • Cottrell, G.S.1    Hooper, N.M.2    Turner, A.J.3
  • 21
    • 0028877431 scopus 로고
    • Manganese effectively supports yeast cell-cycle progression in place of calcium
    • S. Loukin, and C. Kung Manganese effectively supports yeast cell-cycle progression in place of calcium J. Cell Biol. 131 1995 1025 1037
    • (1995) J. Cell Biol. , vol.131 , pp. 1025-1037
    • Loukin, S.1    Kung, C.2
  • 22
    • 0036715416 scopus 로고    scopus 로고
    • Manganese-induced apoptosis in PC12 cells
    • Y. Hirata Manganese-induced apoptosis in PC12 cells Neurotoxicol. Teratol. 24 2002 639 653
    • (2002) Neurotoxicol. Teratol. , vol.24 , pp. 639-653
    • Hirata, Y.1
  • 24
    • 0034613681 scopus 로고    scopus 로고
    • Natural resistance to intracellular infections: Natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane
    • N. Jabado, A. Jankowski, S. Dougaparsad, V. Picard, S. Grinstein, and P. Gros Natural resistance to intracellular infections: natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane J. Exp. Med. 192 2000 1237 1248
    • (2000) J. Exp. Med. , vol.192 , pp. 1237-1248
    • Jabado, N.1    Jankowski, A.2    Dougaparsad, S.3    Picard, V.4    Grinstein, S.5    Gros, P.6
  • 25
    • 0038240674 scopus 로고    scopus 로고
    • Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria
    • D.G. Kehres, and M.E. Maguire Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria FEMS Microbiol. Rev. 27 2003 263 290
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 263-290
    • Kehres, D.G.1    Maguire, M.E.2
  • 28
    • 0030611178 scopus 로고    scopus 로고
    • 2+-ATPase in yeast Golgi, has properties distinct from sarco/endoplasmic reticulum and plasma membrane calcium pumps
    • 2+-ATPase in yeast Golgi, has properties distinct from sarco/endoplasmic reticulum and plasma membrane calcium pumps J. Biol. Chem. 272 1997 9895 9901
    • (1997) J. Biol. Chem. , vol.272 , pp. 9895-9901
    • Sorin, A.1    Rosas, G.2    Rao, R.3
  • 35
    • 0032580809 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes: X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro
    • K. Ishikawa, T. Nagase, M. Suyama, N. Miyajima, A. Tanaka, H. Kotani, N. Nomura, and O. Ohara Prediction of the coding sequences of unidentified human genes: X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro DNA Res. 5 1998 169 176
    • (1998) DNA Res. , vol.5 , pp. 169-176
    • Ishikawa, K.1    Nagase, T.2    Suyama, M.3    Miyajima, N.4    Tanaka, A.5    Kotani, H.6    Nomura, N.7    Ohara, O.8
  • 36
    • 10044263573 scopus 로고    scopus 로고
    • PhD Thesis
    • R. Fairclough, PhD Thesis (2003).
    • (2003)
    • Fairclough, R.1
  • 37
    • 0027097849 scopus 로고
    • 2+-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • 2+-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution Mol. Biol. Cell 3 1992 633 654
    • (1992) Mol. Biol. Cell , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 38
    • 0035815727 scopus 로고    scopus 로고
    • The Golgi PMR1 P-type ATPase of Caenorhabditis elegans. Identification of the gene and demonstration of calcium and manganese transport
    • K. Van Baelen, J. Vanoevelen, L. Missiaen, L. Raeymaekers, and F. Wuytack The Golgi PMR1 P-type ATPase of Caenorhabditis elegans. Identification of the gene and demonstration of calcium and manganese transport J. Biol. Chem. 276 2001 10683 10691
    • (2001) J. Biol. Chem. , vol.276 , pp. 10683-10691
    • Van Baelen, K.1    Vanoevelen, J.2    Missiaen, L.3    Raeymaekers, L.4    Wuytack, F.5
  • 43
    • 0033199505 scopus 로고    scopus 로고
    • 2+ in the yeast endoplasmic reticulum reaches only 10 μm and is mainly controlled by the secretory pathway pump pmr1
    • 2+ in the yeast endoplasmic reticulum reaches only 10 μM and is mainly controlled by the secretory pathway pump pmr1 EMBO J. 18 1999 4733 4743
    • (1999) EMBO J. , vol.18 , pp. 4733-4743
    • Strayle, J.1    Pozzan, T.2    Rudolph, H.K.3
  • 45
    • 0034604655 scopus 로고    scopus 로고
    • Manganese selectivity of pmr1, the yeast secretory pathway ion pump, is defined by residue Gln783 in transmembrane segment 6. Residue Asp778 is essential for cation transport
    • D. Mandal, T.B. Woolf, and R. Rao Manganese selectivity of pmr1, the yeast secretory pathway ion pump, is defined by residue Gln783 in transmembrane segment 6. Residue Asp778 is essential for cation transport J. Biol. Chem. 275 2000 23933 23938
    • (2000) J. Biol. Chem. , vol.275 , pp. 23933-23938
    • Mandal, D.1    Woolf, T.B.2    Rao, R.3
  • 48
    • 0033111171 scopus 로고    scopus 로고
    • 2+-ATPases and their expression in the mammary gland of pregnant and lactating rats
    • 2+-ATPases and their expression in the mammary gland of pregnant and lactating rats Am. J. Physiol. 276 1999 C796 C802
    • (1999) Am. J. Physiol. , vol.276
    • Reinhardt, T.A.1    Horst, R.L.2
  • 50
    • 0023895049 scopus 로고
    • Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic beta cell via two distinct site-specific endopeptidases
    • H.W. Davidson, C.J. Rhodes, and J.C. Hutton Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic beta cell via two distinct site-specific endopeptidases Nature 333 1988 93 96
    • (1988) Nature , vol.333 , pp. 93-96
    • Davidson, H.W.1    Rhodes, C.J.2    Hutton, J.C.3
  • 51
    • 0028801027 scopus 로고
    • Ionic milieu controls the compartment-specific activation of pro-opiomelanocortin processing in AtT-20 cells
    • W.K. Schmidt, and H.P. Moore Ionic milieu controls the compartment-specific activation of pro-opiomelanocortin processing in AtT-20 cells Mol. Biol. Cell 6 1995 1271 1285
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1271-1285
    • Schmidt, W.K.1    Moore, H.P.2
  • 53
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • F.M. LaFerla Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease Nat. Rev., Neurosci. 3 2002 862 872
    • (2002) Nat. Rev., Neurosci. , vol.3 , pp. 862-872
    • Laferla, F.M.1
  • 58
    • 0028889152 scopus 로고
    • Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase
    • P.J. Lapinskas, K.W. Cunningham, X.F. Liu, G.R. Fink, and V.C. Culotta Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase Mol. Cell. Biol. 15 1995 1382 1388
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1382-1388
    • Lapinskas, P.J.1    Cunningham, K.W.2    Liu, X.F.3    Fink, G.R.4    Culotta, V.C.5
  • 59
    • 0019331870 scopus 로고
    • Adenosine 5′-triphosphate dependent fluxes of manganese and and hydrogen ions in sarcoplasmic reticulum vesicles
    • M. Chiesi, and G. Inesi Adenosine 5′-triphosphate dependent fluxes of manganese and and hydrogen ions in sarcoplasmic reticulum vesicles Biochemistry 19 1980 2912 2918
    • (1980) Biochemistry , vol.19 , pp. 2912-2918
    • Chiesi, M.1    Inesi, G.2
  • 62
    • 0021878793 scopus 로고
    • Heterologous protein secretion from yeast
    • R.A. Smith, M.J. Duncan, and D.T. Moir Heterologous protein secretion from yeast Science 229 1985 1219 1224
    • (1985) Science , vol.229 , pp. 1219-1224
    • Smith, R.A.1    Duncan, M.J.2    Moir, D.T.3
  • 63
    • 0029826047 scopus 로고    scopus 로고
    • Overexpression of binding protein and disruption of the PMR1 gene synergistically stimulate secretion of bovine prochymosin but not plant thaumatin in yeast
    • M.M. Harmsen, M.I. Bruyne, H.A. Raue, and J. Maat Overexpression of binding protein and disruption of the PMR1 gene synergistically stimulate secretion of bovine prochymosin but not plant thaumatin in yeast Appl. Microbiol. Biotechnol. 46 1996 365 370
    • (1996) Appl. Microbiol. Biotechnol. , vol.46 , pp. 365-370
    • Harmsen, M.M.1    Bruyne, M.I.2    Raue, H.A.3    Maat, J.4
  • 64
    • 0022348809 scopus 로고
    • On the fidelity of DNA replication: Manganese mutagenesis in vitro
    • R.A. Beckman, A.S. Mildvan, and L.A. Loeb On the fidelity of DNA replication: manganese mutagenesis in vitro Biochemistry 24 1985 5810 5817
    • (1985) Biochemistry , vol.24 , pp. 5810-5817
    • Beckman, R.A.1    Mildvan, A.S.2    Loeb, L.A.3
  • 66
    • 0035929482 scopus 로고    scopus 로고
    • Manganese mimics the action of 1-methyl-4-phenylpyridinium ion, a dopaminergic neurotoxin, in rat striatal tissue slices
    • Y. Hirata, K. Kiuchi, and T. Nagatsu Manganese mimics the action of 1-methyl-4-phenylpyridinium ion, a dopaminergic neurotoxin, in rat striatal tissue slices Neurosci. Lett. 311 2001 53 56
    • (2001) Neurosci. Lett. , vol.311 , pp. 53-56
    • Hirata, Y.1    Kiuchi, K.2    Nagatsu, T.3
  • 67
    • 0035861588 scopus 로고    scopus 로고
    • Manganese superoxide dismutase in Saccharomyces cerevisiae acquires its metal co-factor through a pathway involving the Nramp metal transporter, Smf2p
    • E.E. Luk, and V.C. Culotta Manganese superoxide dismutase in Saccharomyces cerevisiae acquires its metal co-factor through a pathway involving the Nramp metal transporter, Smf2p J. Biol. Chem. 276 2001 47556 47562
    • (2001) J. Biol. Chem. , vol.276 , pp. 47556-47562
    • Luk, E.E.1    Culotta, V.C.2
  • 68
    • 0036240008 scopus 로고    scopus 로고
    • Inhibition of reverse transcription in vivo by elevated manganese ion concentration
    • E.C. Bolton, A.S. Mildvan, and J.D. Boeke Inhibition of reverse transcription in vivo by elevated manganese ion concentration Mol. Cell 9 2002 879 889
    • (2002) Mol. Cell , vol.9 , pp. 879-889
    • Bolton, E.C.1    Mildvan, A.S.2    Boeke, J.D.3
  • 69
    • 0028040761 scopus 로고
    • Depletion of manganese within the secretory pathway inhibits O-linked glycosylation in mammalian cells
    • R.J. Kaufman, M. Swaroop, and P. Murtha-Riel Depletion of manganese within the secretory pathway inhibits O-linked glycosylation in mammalian cells Biochemistry 33 1994 9813 9819
    • (1994) Biochemistry , vol.33 , pp. 9813-9819
    • Kaufman, R.J.1    Swaroop, M.2    Murtha-Riel, P.3
  • 70
    • 0031976097 scopus 로고    scopus 로고
    • Factors controlling the glycosylation potential of the Golgi apparatus
    • A. Varki Factors controlling the glycosylation potential of the Golgi apparatus Trends Cell Biol. 8 1998 34 40
    • (1998) Trends Cell Biol. , vol.8 , pp. 34-40
    • Varki, A.1
  • 71
    • 0017159511 scopus 로고
    • Metal ion activation of galactosyltransferase
    • J.T. Powell, and K. Brew Metal ion activation of galactosyltransferase J. Biol. Chem. 251 1976 3645 3652
    • (1976) J. Biol. Chem. , vol.251 , pp. 3645-3652
    • Powell, J.T.1    Brew, K.2
  • 72
    • 0021325903 scopus 로고
    • Casein kinase activity in rat mammary gland Golgi vesicles. Demonstration of latency and requirement for a transmembrane ATP carrier
    • D.W. West, and R.A. Clegg Casein kinase activity in rat mammary gland Golgi vesicles. Demonstration of latency and requirement for a transmembrane ATP carrier Biochem. J. 219 1984 181 187
    • (1984) Biochem. J. , vol.219 , pp. 181-187
    • West, D.W.1    Clegg, R.A.2
  • 73
    • 0033757691 scopus 로고    scopus 로고
    • Kinetic characterization of calcium uptake by the rat liver Golgi apparatus
    • P. Rojas, A. Surroca, A. Orellana, and D. Wolff Kinetic characterization of calcium uptake by the rat liver Golgi apparatus Cell Biol. Int. 24 2000 229 233
    • (2000) Cell Biol. Int. , vol.24 , pp. 229-233
    • Rojas, P.1    Surroca, A.2    Orellana, A.3    Wolff, D.4
  • 74
    • 0030822623 scopus 로고    scopus 로고
    • Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities
    • R.S. Taylor, S.M. Jones, R.H. Dahl, M.H. Nordeen, and K.E. Howell Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities Mol. Biol. Cell 8 1997 1911 1931
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1911-1931
    • Taylor, R.S.1    Jones, S.M.2    Dahl, R.H.3    Nordeen, M.H.4    Howell, K.E.5
  • 76
    • 0028069962 scopus 로고
    • Immunohistochemical distribution of CD44 and desmoplakin I and II in Hailey-Hailey's disease and Darier's disease
    • M. Harada, K. Hashimoto, and K. Fujiwara Immunohistochemical distribution of CD44 and desmoplakin I and II in Hailey-Hailey's disease and Darier's disease J. Dermatol. 21 1994 389 393
    • (1994) J. Dermatol. , vol.21 , pp. 389-393
    • Harada, M.1    Hashimoto, K.2    Fujiwara, K.3
  • 77
    • 0028916754 scopus 로고
    • Junctional proteins of keratinocytes in Grover's disease, Hailey-Hailey's disease and Darier's disease
    • K. Hashimoto, K. Fujiwara, M. Harada, M. Setoyama, and H. Eto Junctional proteins of keratinocytes in Grover's disease, Hailey-Hailey's disease and Darier's disease J. Dermatol. 22 1995 159 170
    • (1995) J. Dermatol. , vol.22 , pp. 159-170
    • Hashimoto, K.1    Fujiwara, K.2    Harada, M.3    Setoyama, M.4    Eto, H.5
  • 78
    • 0029905293 scopus 로고    scopus 로고
    • Involvement of the adherens junction-actin filament system in acantholytic dyskeratosis of Hailey-Hailey disease. A histological, ultrastructural, and histochemical study of lesional and non-lesional skin
    • D. Metze, H. Hamm, A. Schorat, and T. Luger Involvement of the adherens junction-actin filament system in acantholytic dyskeratosis of Hailey-Hailey disease. A histological, ultrastructural, and histochemical study of lesional and non-lesional skin J. Cutan. Pathol. 23 1996 211 222
    • (1996) J. Cutan. Pathol. , vol.23 , pp. 211-222
    • Metze, D.1    Hamm, H.2    Schorat, A.3    Luger, T.4
  • 80
    • 0036235818 scopus 로고    scopus 로고
    • Mutation analysis of ATP2C1 gene in Taiwanese patients with Hailey-Hailey disease
    • S.C. Chao, Y.M. Tsai, and M.H. Yang Mutation analysis of ATP2C1 gene in Taiwanese patients with Hailey-Hailey disease Br. J. Dermatol. 146 2002 595 600
    • (2002) Br. J. Dermatol. , vol.146 , pp. 595-600
    • Chao, S.C.1    Tsai, Y.M.2    Yang, M.H.3
  • 81
    • 3042637998 scopus 로고    scopus 로고
    • Hailey-Hailey disease: Identification of novel mutations in ATP2C1 and effect of missense mutation A528P on protein expression levels
    • R.J. Fairclough, L. Lonie, K. Van Baelen, M. Haftek, C.S. Munro, S.M. Burge, and A. Hovnanian Hailey-Hailey disease: identification of novel mutations in ATP2C1 and effect of missense mutation A528P on protein expression levels J. Invest. Dermatol. 123 2004 67 71
    • (2004) J. Invest. Dermatol. , vol.123 , pp. 67-71
    • Fairclough, R.J.1    Lonie, L.2    Van Baelen, K.3    Haftek, M.4    Munro, C.S.5    Burge, S.M.6    Hovnanian, A.7
  • 82
    • 0035679791 scopus 로고    scopus 로고
    • Mutations of ATP2C1 in Japanese patients with Hailey-Hailey disease: Intrafamilial and interfamilial phenotype variations and lack of correlation with mutation patterns
    • S. Ikeda, T. Shigihara, N. Mayuzumi, X. Yu, and H. Ogawa Mutations of ATP2C1 in Japanese patients with Hailey-Hailey disease: intrafamilial and interfamilial phenotype variations and lack of correlation with mutation patterns J. Invest. Dermatol. 117 2001 1654 1656
    • (2001) J. Invest. Dermatol. , vol.117 , pp. 1654-1656
    • Ikeda, S.1    Shigihara, T.2    Mayuzumi, N.3    Yu, X.4    Ogawa, H.5
  • 83
    • 0142088949 scopus 로고    scopus 로고
    • Four novel mutations in ATP2C1 found in Chinese patients with Hailey-Hailey disease
    • H. Li, X.K. Sun, and X.J. Zhu Four novel mutations in ATP2C1 found in Chinese patients with Hailey-Hailey disease Br. J. Dermatol. 149 2003 471 474
    • (2003) Br. J. Dermatol. , vol.149 , pp. 471-474
    • Li, H.1    Sun, X.K.2    Zhu, X.J.3
  • 84
    • 0036125299 scopus 로고    scopus 로고
    • Analysis of ATP2C1 gene mutation in 10 unrelated Japanese families with Hailey-Hailey disease
    • K. Yokota, K. Yasukawa, and H. Shimizu Analysis of ATP2C1 gene mutation in 10 unrelated Japanese families with Hailey-Hailey disease J. Invest. Dermatol. 118 2002 550 551
    • (2002) J. Invest. Dermatol. , vol.118 , pp. 550-551
    • Yokota, K.1    Yasukawa, K.2    Shimizu, H.3
  • 85
    • 0020502456 scopus 로고
    • Factors influencing calcium-induced terminal differentiation in cultured mouse epidermal cells
    • H. Hennings, K.A. Holbrook, and S.H. Yuspa Factors influencing calcium-induced terminal differentiation in cultured mouse epidermal cells J. Cell. Physiol. 116 1983 265 281
    • (1983) J. Cell. Physiol. , vol.116 , pp. 265-281
    • Hennings, H.1    Holbrook, K.A.2    Yuspa, S.H.3
  • 86
    • 0025344640 scopus 로고
    • Calcium regulation of growth and differentiation of normal human keratinocytes: Modulation of differentiation competence by stages of growth and extracellular calcium
    • S. Pillai, D.D. Bikle, M.L. Mancianti, P. Cline, and M. Hincenbergs Calcium regulation of growth and differentiation of normal human keratinocytes: modulation of differentiation competence by stages of growth and extracellular calcium J. Cell. Physiol. 143 1990 294 302
    • (1990) J. Cell. Physiol. , vol.143 , pp. 294-302
    • Pillai, S.1    Bikle, D.D.2    Mancianti, M.L.3    Cline, P.4    Hincenbergs, M.5
  • 87
    • 0034695656 scopus 로고    scopus 로고
    • Directed actin polymerization is the driving force for epithelial cell-cell adhesion
    • V. Vasioukhin, C. Bauer, M. Yin, and E. Fuchs Directed actin polymerization is the driving force for epithelial cell-cell adhesion Cell 100 2000 209 219
    • (2000) Cell , vol.100 , pp. 209-219
    • Vasioukhin, V.1    Bauer, C.2    Yin, M.3    Fuchs, E.4
  • 88
    • 0031793971 scopus 로고    scopus 로고
    • Migration of human keratinocytes in electric fields requires growth factors and extracellular calcium
    • K.S. Fang, B. Farboud, R. Nuccitelli, and R.R. Isseroff Migration of human keratinocytes in electric fields requires growth factors and extracellular calcium J. Invest. Dermatol. 111 1998 751 756
    • (1998) J. Invest. Dermatol. , vol.111 , pp. 751-756
    • Fang, K.S.1    Farboud, B.2    Nuccitelli, R.3    Isseroff, R.R.4
  • 89
    • 0028343412 scopus 로고
    • A role for ions in barrier recovery after acute perturbation
    • S.H. Lee, P.M. Elias, K.R. Feingold, and T. Mauro A role for ions in barrier recovery after acute perturbation J. Invest. Dermatol. 102 1994 976 979
    • (1994) J. Invest. Dermatol. , vol.102 , pp. 976-979
    • Lee, S.H.1    Elias, P.M.2    Feingold, K.R.3    Mauro, T.4
  • 90
    • 0034568948 scopus 로고    scopus 로고
    • Are desmosomes more than tethers for intermediate filaments?
    • K.J. Green, and C.A. Gaudry Are desmosomes more than tethers for intermediate filaments? Nat. Rev., Mol. Cell Biol. 1 2000 208 216
    • (2000) Nat. Rev., Mol. Cell Biol. , vol.1 , pp. 208-216
    • Green, K.J.1    Gaudry, C.A.2
  • 91
    • 0035991944 scopus 로고    scopus 로고
    • Desmosomal adhesion: Structural basis, molecular mechanism and regulation
    • D.R. Garrod, A.J. Merritt, and Z. Nie Desmosomal adhesion: structural basis, molecular mechanism and regulation Mol. Membr. Biol. 19 2002 81 94
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 81-94
    • Garrod, D.R.1    Merritt, A.J.2    Nie, Z.3
  • 94
    • 0025376082 scopus 로고
    • Immunohistochemical localization of desmosomal and cytoskeletal proteins in the epidermis of healthy individuals and patients with Hailey-Hailey's disease
    • S. Inohara, Y. Tatsumi, Y. Tanaka, and S. Sagami Immunohistochemical localization of desmosomal and cytoskeletal proteins in the epidermis of healthy individuals and patients with Hailey-Hailey's disease Acta Derm.-Venereol. 70 1990 239 241
    • (1990) Acta Derm.-Venereol. , vol.70 , pp. 239-241
    • Inohara, S.1    Tatsumi, Y.2    Tanaka, Y.3    Sagami, S.4
  • 95
    • 0034518449 scopus 로고    scopus 로고
    • 2+ in cell physiology and pathophysiology
    • 2+ in cell physiology and pathophysiology Cell Calcium 28 2000 339 348
    • (2000) Cell Calcium , vol.28 , pp. 339-348
    • Duchen, M.R.1
  • 96
    • 0035979490 scopus 로고    scopus 로고
    • Increased calcium vulnerability of senescent cardiac mitochondria: Protective role for a mitochondrial potassium channel opener
    • A. Jahangir, C. Ozcan, E.L. Holmuhamedov, and A. Terzic Increased calcium vulnerability of senescent cardiac mitochondria: protective role for a mitochondrial potassium channel opener Mech. Ageing Dev. 122 2001 1073 1086
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 1073-1086
    • Jahangir, A.1    Ozcan, C.2    Holmuhamedov, E.L.3    Terzic, A.4
  • 98
    • 0348111468 scopus 로고    scopus 로고
    • 2+-ATPase (SERCA) 1 and 2 isoforms and characterization of Darier disease (SERCA2) mutants by steady-state and transient kinetic analyses
    • 2+-ATPase (SERCA) 1 and 2 isoforms and characterization of Darier disease (SERCA2) mutants by steady-state and transient kinetic analyses J. Biol. Chem. 278 2003 47877 47889
    • (2003) J. Biol. Chem. , vol.278 , pp. 47877-47889
    • Dode, L.1    Andersen, J.P.2    Leslie, N.3    Dhitavat, J.4    Vilsen, B.5    Hovnanian, A.6
  • 99
    • 0022678699 scopus 로고
    • An investigation of the molecular components of desmosomes in epithelial cells of five vertebrates
    • A. Suhrbier, and D. Garrod An investigation of the molecular components of desmosomes in epithelial cells of five vertebrates J. Cell. Sci. 81 1986 223 242
    • (1986) J. Cell. Sci. , vol.81 , pp. 223-242
    • Suhrbier, A.1    Garrod, D.2
  • 100
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • T. Schwede, J. Kopp, N. Guex, and M.C. Peitsch SWISS-MODEL: an automated protein homology-modeling server Nucleic Acids Res. 31 2003 3381 3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4


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