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Volumn 315, Issue 2, 2009, Pages 190-205

70-kDa peroxisomal membrane protein related protein (P70R/ABCD4) localizes to endoplasmic reticulum not peroxisomes, and NH2-terminal hydrophobic property determines the subcellular localization of ABC subfamily D proteins

Author keywords

ABC protein; Endoplasmic reticulum; Membrane protein targeting; Peroxisome

Indexed keywords

ATP BINDING CASSETTE PROTEIN D4; MEMBRANE PROTEIN; PEROXISOMAL MEMBRANE PROTEIN 70 RELATED PROTEIN; UNCLASSIFIED DRUG;

EID: 57749175975     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.10.031     Document Type: Article
Times cited : (50)

References (53)
  • 1
    • 0141690650 scopus 로고    scopus 로고
    • Human and Drosophila ABC proteins
    • Holland I.B., Cole S.P.C., Kuchler K., and Higgins C.F. (Eds), Academic Press, Amsterdam
    • Dean M., Rzhetsky A., and Allikmets R. Human and Drosophila ABC proteins. In: Holland I.B., Cole S.P.C., Kuchler K., and Higgins C.F. (Eds). ABC PROTEINS From Bacteria to Man (2003), Academic Press, Amsterdam 47-61
    • (2003) ABC PROTEINS From Bacteria to Man , pp. 47-61
    • Dean, M.1    Rzhetsky, A.2    Allikmets, R.3
  • 2
    • 0025255475 scopus 로고
    • The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily
    • Kamijo K., Taketani S., Yokota S., Osumi T., and Hashimoto T. The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily. J. Biol. Chem. 265 (1990) 4534-4540
    • (1990) J. Biol. Chem. , vol.265 , pp. 4534-4540
    • Kamijo, K.1    Taketani, S.2    Yokota, S.3    Osumi, T.4    Hashimoto, T.5
  • 3
    • 0026500670 scopus 로고
    • Nucleotide sequence of the human 70 kDa peroxisomal membrane protein: a member of ATP-binding cassette transporters
    • Kamijo K., Kamijo T., Ueno I., Osumi T., and Hashimoto T. Nucleotide sequence of the human 70 kDa peroxisomal membrane protein: a member of ATP-binding cassette transporters. Biochim. Biophys. Acta 1129 (1992) 323-327
    • (1992) Biochim. Biophys. Acta , vol.1129 , pp. 323-327
    • Kamijo, K.1    Kamijo, T.2    Ueno, I.3    Osumi, T.4    Hashimoto, T.5
  • 4
    • 0026849933 scopus 로고
    • Mutations in the 70 K peroxisomal membrane protein gene in Zellweger syndrome
    • Gärtner J., Moser H., and Valle D. Mutations in the 70 K peroxisomal membrane protein gene in Zellweger syndrome. Nat. Genet. 1 (1992) 16-23
    • (1992) Nat. Genet. , vol.1 , pp. 16-23
    • Gärtner, J.1    Moser, H.2    Valle, D.3
  • 6
    • 0030034602 scopus 로고    scopus 로고
    • A close relative of the adrenoleukodystrophy (ALD) gene codes for a peroxisomal protein with a specific expression pattern
    • Lombard-Platet G., Savary S., Sarde C.O., Mander G.L., and Chimini G. A close relative of the adrenoleukodystrophy (ALD) gene codes for a peroxisomal protein with a specific expression pattern. Proc. Natl. Acad. Sci. USA 93 (1996) 1265-1269
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1265-1269
    • Lombard-Platet, G.1    Savary, S.2    Sarde, C.O.3    Mander, G.L.4    Chimini, G.5
  • 7
    • 0031561433 scopus 로고    scopus 로고
    • cDNA cloning and mRNA expression of the human adrenoleukodystrophy related protein (ALDRP), a peroxisomal ABC transporter
    • Holzinger A., Kammerer S., Berger J., and Roscher A.A. cDNA cloning and mRNA expression of the human adrenoleukodystrophy related protein (ALDRP), a peroxisomal ABC transporter. Biochem. Biophys. Res. Commun. 239 (1997) 261-264
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 261-264
    • Holzinger, A.1    Kammerer, S.2    Berger, J.3    Roscher, A.A.4
  • 8
    • 0030776037 scopus 로고    scopus 로고
    • Identification of a fourth half ABC transporter in the human peroxisomal membrane
    • Shani N., Jimenz-sanchez G., Steel G., Dean M., and Valle D. Identification of a fourth half ABC transporter in the human peroxisomal membrane. Hum. Mol. Genet. 6 (1997) 1925-1931
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1925-1931
    • Shani, N.1    Jimenz-sanchez, G.2    Steel, G.3    Dean, M.4    Valle, D.5
  • 9
    • 0031559581 scopus 로고    scopus 로고
    • Primary structure of human PMP69, a putative peroxisomal ABC-transporter
    • Holzinger A., Kammerer S., and Roscher A.A. Primary structure of human PMP69, a putative peroxisomal ABC-transporter. Biochem. Biophys. Res. Commun. 237 (1997) 152-157
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 152-157
    • Holzinger, A.1    Kammerer, S.2    Roscher, A.A.3
  • 10
    • 0022761273 scopus 로고    scopus 로고
    • Purification of membrane polypeptides of rat liver peroxisomes
    • Hashimoto T., Kuwabara T., Usuda N., and Nagata T. Purification of membrane polypeptides of rat liver peroxisomes. J. Biochem. (Tokyo) 100 (1996) 301-310
    • (1996) J. Biochem. (Tokyo) , vol.100 , pp. 301-310
    • Hashimoto, T.1    Kuwabara, T.2    Usuda, N.3    Nagata, T.4
  • 11
    • 0023654944 scopus 로고
    • Integral membrane polypeptides of rat liver peroxisomes: topology and response to different metabolic states
    • Hartl F.-U., and Just W.W. Integral membrane polypeptides of rat liver peroxisomes: topology and response to different metabolic states. Arch. Biochem. Biophys. 255 (1987) 109-119
    • (1987) Arch. Biochem. Biophys. , vol.255 , pp. 109-119
    • Hartl, F.-U.1    Just, W.W.2
  • 12
    • 0033597211 scopus 로고    scopus 로고
    • Characterization of the 70-kDa peroxisomal membrane protein, an ATP binding cassette transporter
    • Imanaka T., Aihara K., Takano T., Yamashita A., Sato R., Suzuki Y., Yokota S., and Osumi T. Characterization of the 70-kDa peroxisomal membrane protein, an ATP binding cassette transporter. J. Biol. Chem. 274 (1999) 11968-11976
    • (1999) J. Biol. Chem. , vol.274 , pp. 11968-11976
    • Imanaka, T.1    Aihara, K.2    Takano, T.3    Yamashita, A.4    Sato, R.5    Suzuki, Y.6    Yokota, S.7    Osumi, T.8
  • 15
    • 0032924991 scopus 로고    scopus 로고
    • Adrenoleukodystrophy-related protein can compensate functionally for adrenoleukodystrophy protein deficiency (X-ALD): implications for therapy
    • Netik A., Forss-Petter S., Holzinger A., Molzer B., Unterrainer G., and Berger J. Adrenoleukodystrophy-related protein can compensate functionally for adrenoleukodystrophy protein deficiency (X-ALD): implications for therapy. Hum. Mol. Genet. 8 (1999) 907-913
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 907-913
    • Netik, A.1    Forss-Petter, S.2    Holzinger, A.3    Molzer, B.4    Unterrainer, G.5    Berger, J.6
  • 18
    • 0019877801 scopus 로고
    • Affinity purification of antibodies from diazotized paper blots of heterogeneous protein samples
    • Olmsted J.B. Affinity purification of antibodies from diazotized paper blots of heterogeneous protein samples. J. Biol. Chem. 256 (1981) 11955-11957
    • (1981) J. Biol. Chem. , vol.256 , pp. 11955-11957
    • Olmsted, J.B.1
  • 19
    • 16344387139 scopus 로고    scopus 로고
    • Switching the sorting mode of membrane proteins from cotranslational endoplasmic reticulum targeting to posttranslational mitochondrial import
    • Miyazaki E., Kida Y., Mihara K., and Sakaguchi M. Switching the sorting mode of membrane proteins from cotranslational endoplasmic reticulum targeting to posttranslational mitochondrial import. Mol. Biol. Cell 16 (2005) 1788-1799
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1788-1799
    • Miyazaki, E.1    Kida, Y.2    Mihara, K.3    Sakaguchi, M.4
  • 22
    • 77049229661 scopus 로고
    • Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
    • de Duve C., Pressman B.C., Gianetto R., Wattiaux R., and Appelmans F. Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem. J. 60 (1955) 604-617
    • (1955) Biochem. J. , vol.60 , pp. 604-617
    • de Duve, C.1    Pressman, B.C.2    Gianetto, R.3    Wattiaux, R.4    Appelmans, F.5
  • 23
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum
    • Fujiki Y., Hubbard A.L., Fowler S., and Lazarow P.B. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93 (1982) 97-102
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 24
    • 0025973236 scopus 로고
    • Suramin prevents import of acyl-CoA oxidase into rat liver peroxisomes
    • Imanaka T., Lazarow P.B., and Takano T. Suramin prevents import of acyl-CoA oxidase into rat liver peroxisomes. Biochim. Biophys. Acta 1062 (1991) 264-270
    • (1991) Biochim. Biophys. Acta , vol.1062 , pp. 264-270
    • Imanaka, T.1    Lazarow, P.B.2    Takano, T.3
  • 25
    • 0036291180 scopus 로고    scopus 로고
    • Nucleotide-induced conformational changes of PMP70, an ATP binding cassette transporter on rat liver peroxisomal membranes
    • Kashiwayama Y., Morita M., Kamijo K., and Imanaka T. Nucleotide-induced conformational changes of PMP70, an ATP binding cassette transporter on rat liver peroxisomal membranes. Biochim. Biophys. Res. Commun. 291 (2002) 1245-1251
    • (2002) Biochim. Biophys. Res. Commun. , vol.291 , pp. 1245-1251
    • Kashiwayama, Y.1    Morita, M.2    Kamijo, K.3    Imanaka, T.4
  • 26
    • 0032185234 scopus 로고    scopus 로고
    • Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins
    • Ota K., Sakaguchi M., von Heijne G., Hamasaki N., and Mihara K. Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins. Mol. Cell 2 (1998) 495-503
    • (1998) Mol. Cell , vol.2 , pp. 495-503
    • Ota, K.1    Sakaguchi, M.2    von Heijne, G.3    Hamasaki, N.4    Mihara, K.5
  • 27
    • 0242575404 scopus 로고    scopus 로고
    • Peroxisomal ABC transporters
    • Holland I.B., Cole S.P.C., Kuchler K., and Higgins C.F. (Eds), Academic Press, Amsterdam
    • Almashanu S., and Valle D. Peroxisomal ABC transporters. In: Holland I.B., Cole S.P.C., Kuchler K., and Higgins C.F. (Eds). ABC PROTEINS From Bacteria to Man (2003), Academic Press, Amsterdam 497-513
    • (2003) ABC PROTEINS From Bacteria to Man , pp. 497-513
    • Almashanu, S.1    Valle, D.2
  • 28
    • 36348963175 scopus 로고    scopus 로고
    • Hydrophobic regions adjacent to transmembrane domains 1 and 5 are important for the targeting of the 70-kDa peroxisomal membrane protein
    • Kashiwayama Y., Asahina K., Morita M., and Imanaka T. Hydrophobic regions adjacent to transmembrane domains 1 and 5 are important for the targeting of the 70-kDa peroxisomal membrane protein. J. Biol. Chem. 282 (2007) 33831-33844
    • (2007) J. Biol. Chem. , vol.282 , pp. 33831-33844
    • Kashiwayama, Y.1    Asahina, K.2    Morita, M.3    Imanaka, T.4
  • 30
    • 0345861756 scopus 로고    scopus 로고
    • PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins
    • Jones J.M., Morrell J.C., and Gould S.J. PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins. J. Cell Biol. 164 (2004) 57-67
    • (2004) J. Cell Biol. , vol.164 , pp. 57-67
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.J.3
  • 31
    • 0034611003 scopus 로고    scopus 로고
    • PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis
    • Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., and Gould S.J. PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis. J. Cell Biol. 148 (2000) 931-944
    • (2000) J. Cell Biol. , vol.148 , pp. 931-944
    • Sacksteder, K.A.1    Jones, J.M.2    South, S.T.3    Li, X.4    Liu, Y.5    Gould, S.J.6
  • 32
    • 0034641098 scopus 로고    scopus 로고
    • The peroxin Pex19p interacts with multiple, integral membrane proteins at the peroxisomal membrane
    • Snyder W.B., Koller A., Choy A.J., and Subramani S. The peroxin Pex19p interacts with multiple, integral membrane proteins at the peroxisomal membrane. J. Cell Biol. 149 (2000) 1171-1178
    • (2000) J. Cell Biol. , vol.149 , pp. 1171-1178
    • Snyder, W.B.1    Koller, A.2    Choy, A.J.3    Subramani, S.4
  • 33
    • 0034972812 scopus 로고    scopus 로고
    • Human pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences
    • Fransen M., Wylin T., Brees C., Mannaerts G.P., and Van Veldhoven P.P. Human pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences. Mol. Cell Biol. 21 (2001) 4413-4424
    • (2001) Mol. Cell Biol. , vol.21 , pp. 4413-4424
    • Fransen, M.1    Wylin, T.2    Brees, C.3    Mannaerts, G.P.4    Van Veldhoven, P.P.5
  • 35
    • 4644250692 scopus 로고    scopus 로고
    • Domain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteins
    • Shibata H., Kashiwayama Y., Imanaka T., and Kato H. Domain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteins. J. Biol. Chem. 279 (2004) 38486-38494
    • (2004) J. Biol. Chem. , vol.279 , pp. 38486-38494
    • Shibata, H.1    Kashiwayama, Y.2    Imanaka, T.3    Kato, H.4
  • 36
    • 3042724871 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals
    • Rottensteiner H., Kramer A., Lorenzen S., Stein K., Landgraf C., Volkmer-Engert R., and Erdmann R. Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals. Mol. Biol. Cell 15 (2004) 3406-3417
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3406-3417
    • Rottensteiner, H.1    Kramer, A.2    Lorenzen, S.3    Stein, K.4    Landgraf, C.5    Volkmer-Engert, R.6    Erdmann, R.7
  • 37
    • 20444400829 scopus 로고    scopus 로고
    • Function of the PEX19-binding site of human adrenoleukodystrophy protein as targeting motif in man and yeast. PMP targeting is evolutionarily conserved
    • Halbach A., Lorenzen S., Landgraf C., Volkmer-Engert R., Erdmann R., and Rottensteiner H. Function of the PEX19-binding site of human adrenoleukodystrophy protein as targeting motif in man and yeast. PMP targeting is evolutionarily conserved. J. Biol. Chem. 280 (2005) 21176-21182
    • (2005) J. Biol. Chem. , vol.280 , pp. 21176-21182
    • Halbach, A.1    Lorenzen, S.2    Landgraf, C.3    Volkmer-Engert, R.4    Erdmann, R.5    Rottensteiner, H.6
  • 38
    • 33744949079 scopus 로고    scopus 로고
    • Pex19p binds Pex30p and Pex32p at regions required for their peroxisomal localization but separate from their peroxisomal targeting signals
    • Vizeacoumar F.J., Vreden W.N., Aitchison J.D., and Rachubinski R.A. Pex19p binds Pex30p and Pex32p at regions required for their peroxisomal localization but separate from their peroxisomal targeting signals. J. Biol. Chem. 281 (2006) 14805-14812
    • (2006) J. Biol. Chem. , vol.281 , pp. 14805-14812
    • Vizeacoumar, F.J.1    Vreden, W.N.2    Aitchison, J.D.3    Rachubinski, R.A.4
  • 39
    • 0345791524 scopus 로고    scopus 로고
    • Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease
    • Kikuchi M., Hatano N., Yokota S., Shimozawa N., Imanaka T., and Taniguchi H. Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease. J. Biol. Chem. 279 (2004) 421-428
    • (2004) J. Biol. Chem. , vol.279 , pp. 421-428
    • Kikuchi, M.1    Hatano, N.2    Yokota, S.3    Shimozawa, N.4    Imanaka, T.5    Taniguchi, H.6
  • 40
    • 34548166529 scopus 로고    scopus 로고
    • Rat liver peroxisomes after fibrate treatment. A survey using quantitative mass spectrometry
    • Islinger M., Lüers G.H., Li K.W., Loos M., and Völkl A. Rat liver peroxisomes after fibrate treatment. A survey using quantitative mass spectrometry. J. Biol. Chem. 282 (2007) 23055-23069
    • (2007) J. Biol. Chem. , vol.282 , pp. 23055-23069
    • Islinger, M.1    Lüers, G.H.2    Li, K.W.3    Loos, M.4    Völkl, A.5
  • 42
    • 0031812285 scopus 로고    scopus 로고
    • The mouse gene encoding the peroxisomal membrane protein 1-like protein (PXMP1-L): cDNA cloning, genomic organization and comparative expression studies
    • Holzinger A., Muntau A., Mayerhofer P., Kammerer S., Albet S., Bugaut M., and Roscher A.A. The mouse gene encoding the peroxisomal membrane protein 1-like protein (PXMP1-L): cDNA cloning, genomic organization and comparative expression studies. FEBS Lett. 433 (1998) 179-183
    • (1998) FEBS Lett. , vol.433 , pp. 179-183
    • Holzinger, A.1    Muntau, A.2    Mayerhofer, P.3    Kammerer, S.4    Albet, S.5    Bugaut, M.6    Roscher, A.A.7
  • 44
    • 0030021833 scopus 로고    scopus 로고
    • Insertion of the 70-kDa peroxisomal membrane protein into peroxisomal membranes in vivo and in vitro
    • Imanaka T., Shiina Y., Takano T., Hashimoto T., and Osumi T. Insertion of the 70-kDa peroxisomal membrane protein into peroxisomal membranes in vivo and in vitro. J. Biol. Chem. 271 (1996) 3706-3713
    • (1996) J. Biol. Chem. , vol.271 , pp. 3706-3713
    • Imanaka, T.1    Shiina, Y.2    Takano, T.3    Hashimoto, T.4    Osumi, T.5
  • 45
    • 0141605433 scopus 로고    scopus 로고
    • Targeting of the human adrenoleukodystrophy protein to the peroxisomal membrane by an internal region containing a highly conserved motif
    • Landgraf P., Mayerhofer P.U., Polanetz R., Roscher A.A., and Holzinger A. Targeting of the human adrenoleukodystrophy protein to the peroxisomal membrane by an internal region containing a highly conserved motif. Eur. J. Cell Biol. 82 (2003) 401-410
    • (2003) Eur. J. Cell Biol. , vol.82 , pp. 401-410
    • Landgraf, P.1    Mayerhofer, P.U.2    Polanetz, R.3    Roscher, A.A.4    Holzinger, A.5
  • 46
    • 0032189258 scopus 로고    scopus 로고
    • Signal sequences: more than just greasy peptides
    • Martoglio B., and Dobberstein B. Signal sequences: more than just greasy peptides. Trends Cell Biol. 8 (1998) 410-415
    • (1998) Trends Cell Biol. , vol.8 , pp. 410-415
    • Martoglio, B.1    Dobberstein, B.2
  • 47
    • 0023390030 scopus 로고
    • A short amino-terminal segment of microsomal cytochrome P-450 functions both as an insertion signal and as a stop-transfer sequence
    • Sakaguchi M., Mihara K., and Sato R. A short amino-terminal segment of microsomal cytochrome P-450 functions both as an insertion signal and as a stop-transfer sequence. EMBO J. 6 (1987) 2425-2431
    • (1987) EMBO J. , vol.6 , pp. 2425-2431
    • Sakaguchi, M.1    Mihara, K.2    Sato, R.3
  • 48
    • 0028834958 scopus 로고
    • Properties of N-terminal tails in G-protein coupled receptors: a statistical study
    • Wallin E., and von Heijne G. Properties of N-terminal tails in G-protein coupled receptors: a statistical study. Protein Eng. 8 (1995) 693-698
    • (1995) Protein Eng. , vol.8 , pp. 693-698
    • Wallin, E.1    von Heijne, G.2
  • 49
    • 19244384687 scopus 로고    scopus 로고
    • Membrane topology of NADPH-cytochrome P450 reductase on the endoplasmic reticulum
    • Kida Y., Ohgiya S., Mihara K., and Sakaguchi M. Membrane topology of NADPH-cytochrome P450 reductase on the endoplasmic reticulum. Arch. Biochem. Biophys. 351 (1998) 175-179
    • (1998) Arch. Biochem. Biophys. , vol.351 , pp. 175-179
    • Kida, Y.1    Ohgiya, S.2    Mihara, K.3    Sakaguchi, M.4
  • 50
    • 0034698758 scopus 로고    scopus 로고
    • Membrane topogenesis of a type I signal-anchor protein, mouse synaptotagmin II, on the endoplasmic reticulum
    • Kida Y., Sakaguchi M., Fukuda M., Mikoshiba K., and Mihara K. Membrane topogenesis of a type I signal-anchor protein, mouse synaptotagmin II, on the endoplasmic reticulum. J. Cell Biol. 150 (2000) 719-730
    • (2000) J. Cell Biol. , vol.150 , pp. 719-730
    • Kida, Y.1    Sakaguchi, M.2    Fukuda, M.3    Mikoshiba, K.4    Mihara, K.5
  • 51
    • 2542464145 scopus 로고    scopus 로고
    • Targeting of inositol 1, 4, 5-trisphosphate receptors to the endoplasmic reticulum by multiple signals within their transmembrane domains
    • Parker A.K., Gergely F.V., and Taylor C.W. Targeting of inositol 1, 4, 5-trisphosphate receptors to the endoplasmic reticulum by multiple signals within their transmembrane domains. J. Biol. Chem. 279 (2004) 23797-23805
    • (2004) J. Biol. Chem. , vol.279 , pp. 23797-23805
    • Parker, A.K.1    Gergely, F.V.2    Taylor, C.W.3
  • 52
    • 34548188753 scopus 로고    scopus 로고
    • Targeting and retention of type 1 ryanodine receptors to the endoplasmic reticulum
    • Meur G., Parker A.K., Gergely F.V., and Taylor C.W. Targeting and retention of type 1 ryanodine receptors to the endoplasmic reticulum. J. Biol. Chem. 282 (2007) 23096-23103
    • (2007) J. Biol. Chem. , vol.282 , pp. 23096-23103
    • Meur, G.1    Parker, A.K.2    Gergely, F.V.3    Taylor, C.W.4
  • 53
    • 0034675885 scopus 로고    scopus 로고
    • Characterization of the signal that directs Tom20 to the mitochondrial outer membrane
    • Kanaji S., Iwahashi J., Kida Y., Sakaguchi M., and Mihara K. Characterization of the signal that directs Tom20 to the mitochondrial outer membrane. J. Cell Biol. 151 (2000) 277-288
    • (2000) J. Cell Biol. , vol.151 , pp. 277-288
    • Kanaji, S.1    Iwahashi, J.2    Kida, Y.3    Sakaguchi, M.4    Mihara, K.5


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