메뉴 건너뛰기




Volumn 112, Issue 10, 1999, Pages 1477-1486

The Sec61 complex is located in both the ER and the ER-Golgi intermediate compartment

Author keywords

Endoplasmic reticulum; ER retrieval; ERGIC; GFP; Translocation

Indexed keywords

CARRIER PROTEIN; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; OLIGOMER;

EID: 0032977841     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (102)

References (52)
  • 1
    • 0030222342 scopus 로고    scopus 로고
    • Principles of selective transport - Coat complexes hold the key
    • Aridor, M. and Balch, W. E. (1996). Principles of selective transport - coat complexes hold the key. Trends Cell Biol. 6, 315-320.
    • (1996) Trends Cell Biol. , vol.6 , pp. 315-320
    • Aridor, M.1    Balch, W.E.2
  • 3
    • 0031052040 scopus 로고    scopus 로고
    • TGN38 and its orthologues: Roles in post-TGN vesicle formation and maintenance of TGN morphology
    • Banting, G. and Ponnambalam, S. (1997). TGN38 and its orthologues: roles in post-TGN vesicle formation and maintenance of TGN morphology. Biochim. Biophys. Acta 1355, 209-217.
    • (1997) Biochim. Biophys. Acta , vol.1355 , pp. 209-217
    • Banting, G.1    Ponnambalam, S.2
  • 5
    • 0031473345 scopus 로고    scopus 로고
    • Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex
    • Beckmann, R., Bubeck, D., Grassucci, R., Penczek, P., Verschoor, A., Blobel, G. and Frank, J. (1997). Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex. Science 278, 2123-2126.
    • (1997) Science , vol.278 , pp. 2123-2126
    • Beckmann, R.1    Bubeck, D.2    Grassucci, R.3    Penczek, P.4    Verschoor, A.5    Blobel, G.6    Frank, J.7
  • 7
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson, P. and Letourneur, F. (1994). Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 263, 1629-1631.
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 9
    • 0030960372 scopus 로고    scopus 로고
    • The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins
    • Elliott, J. G., Oliver, J. D. and High, S. (1997). The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. J. Biol. Chem. 272, 13849-13855.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13849-13855
    • Elliott, J.G.1    Oliver, J.D.2    High, S.3
  • 10
    • 0028233139 scopus 로고
    • A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins
    • Fiedler, K. and Simons, K. (1994). A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins. Cell 77, 625-626.
    • (1994) Cell , vol.77 , pp. 625-626
    • Fiedler, K.1    Simons, K.2
  • 11
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Gorlich, D. and Rapoport, T. A. (1993). Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75, 615-630.
    • (1993) Cell , vol.75 , pp. 615-630
    • Gorlich, D.1    Rapoport, T.A.2
  • 12
    • 0028091981 scopus 로고
    • Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells
    • Griffiths, G., Ericsson, M., Krijnse-Locker, J., Nilsson, T., Goud, B., Soling, H. D., Tang, B. L., Wong, S. H. and Hong, W. (1994). Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells. J. Cell Biol. 127, 1557-1574.
    • (1994) J. Cell Biol. , vol.127 , pp. 1557-1574
    • Griffiths, G.1    Ericsson, M.2    Krijnse-Locker, J.3    Nilsson, T.4    Goud, B.5    Soling, H.D.6    Tang, B.L.7    Wong, S.H.8    Hong, W.9
  • 13
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond, C. and Helenius, A. (1994). Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J. Cell Biol. 126, 41-52.
    • (1994) J. Cell Biol. , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 15
    • 0029941141 scopus 로고    scopus 로고
    • The secretory pathway: Mechanisms of protein sorting and transport
    • Harter, C. and Wieland, F. (1996). The secretory pathway: mechanisms of protein sorting and transport. Biochim. Biophys. Acta 1286, 75-93.
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 75-93
    • Harter, C.1    Wieland, F.2
  • 17
    • 0029139091 scopus 로고
    • Protein translocation at the membrane of the endoplasmic reticulum
    • High, S. (1995). Protein translocation at the membrane of the endoplasmic reticulum. Prog. Biophys. Mol. Biol. 63, 233-250.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 233-250
    • High, S.1
  • 18
    • 0030878575 scopus 로고    scopus 로고
    • Membrane protein biosynthesis - All sewn up?
    • High, S. and Laird, V. (1997). Membrane protein biosynthesis - All sewn up? Trends Cell Biol. 7, 206-210.
    • (1997) Trends Cell Biol. , vol.7 , pp. 206-210
    • High, S.1    Laird, V.2
  • 19
    • 0029097932 scopus 로고
    • Recycling of the endoplasmic reticulum/Golgi intermediate compartment protein ERGIC-53 in the secretory pathway
    • Itin, C., Foguet, M., Kappeler, F., Klumperman, J. and Hauri, H. P. (1995). Recycling of the endoplasmic reticulum/Golgi intermediate compartment protein ERGIC-53 in the secretory pathway. Biochem. Soc. Trans. 23, 541-544.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 541-544
    • Itin, C.1    Foguet, M.2    Kappeler, F.3    Klumperman, J.4    Hauri, H.P.5
  • 20
    • 0029876344 scopus 로고    scopus 로고
    • ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins
    • Itin, C., Roche, A. C., Monsigny, M. and Hauri, H. P. (1996). ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins. Mol. Biol. Cell 7, 483-493.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 483-493
    • Itin, C.1    Roche, A.C.2    Monsigny, M.3    Hauri, H.P.4
  • 21
    • 0026754116 scopus 로고
    • O-glycosylation of intact and truncated ribophorins in brefeldin A-treated cells: Newly synthesized intact ribophorins are only transiently accessible to the relocated glycosyltransferases
    • Ivessa, N. E., De Lemos-Chiarandini, C., Tsao, Y. S., Takatsuki, A., Adesnik, M., Sabatini, D. D. and Kreibich, G. (1992). O-glycosylation of intact and truncated ribophorins in brefeldin A-treated cells: newly synthesized intact ribophorins are only transiently accessible to the relocated glycosyltransferases. J. Cell Biol. 117, 949-958.
    • (1992) J. Cell Biol. , vol.117 , pp. 949-958
    • Ivessa, N.E.1    De Lemos-Chiarandini, C.2    Tsao, Y.S.3    Takatsuki, A.4    Adesnik, M.5    Sabatini, D.D.6    Kreibich, G.7
  • 22
    • 0027538121 scopus 로고
    • Retrieval of transmembrane proteins to the endoplasmic reticulum
    • Jackson, M. R., Nilsson, T. and Peterson, P. A. (1993). Retrieval of transmembrane proteins to the endoplasmic reticulum. J. Cell Biol. 121, 317-333.
    • (1993) J. Cell Biol. , vol.121 , pp. 317-333
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 23
    • 0027953913 scopus 로고
    • Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex
    • Kalies, K. U., Gorlich, D. and Rapoport, T. A. (1994). Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex. J. Cell Biol. 126, 925-934.
    • (1994) J. Cell Biol. , vol.126 , pp. 925-934
    • Kalies, K.U.1    Gorlich, D.2    Rapoport, T.A.3
  • 24
    • 0031030059 scopus 로고    scopus 로고
    • Discrete cross-linking products identified during membrane protein biosynthesis
    • Laird, V. and High, S. (1997). Discrete cross-linking products identified during membrane protein biosynthesis. J. Biol. Chem. 272, 1983-1989.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1983-1989
    • Laird, V.1    High, S.2
  • 25
    • 0025187298 scopus 로고
    • A human homologue of the yeast HDEL receptor
    • Lewis, M. J. and Pelham, H. R. (1990). A human homologue of the yeast HDEL receptor. Nature 348, 162-163.
    • (1990) Nature , vol.348 , pp. 162-163
    • Lewis, M.J.1    Pelham, H.R.2
  • 26
    • 0026604647 scopus 로고
    • Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum
    • Lewis, M. J. and Pelham, H. R. (1992a). Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum. Cell 68, 353-364.
    • (1992) Cell , vol.68 , pp. 353-364
    • Lewis, M.J.1    Pelham, H.R.2
  • 27
    • 0026489626 scopus 로고
    • Sequence of a second human KDEL receptor
    • Lewis, M. J. and Pelham, H. R. (1992b). Sequence of a second human KDEL receptor. J. Mol. Biol. 226, 913-916.
    • (1992) J. Mol. Biol. , vol.226 , pp. 913-916
    • Lewis, M.J.1    Pelham, H.R.2
  • 28
    • 0029975529 scopus 로고    scopus 로고
    • Membrane topology and retention of microsomal aldehyde dehydrogenase in the endoplasmic reticulum
    • Masaki, R., Yamamoto, A. and Tashiro, Y. (1996). Membrane topology and retention of microsomal aldehyde dehydrogenase in the endoplasmic reticulum. J. Biol. Chem. 271, 16939-16944.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16939-16944
    • Masaki, R.1    Yamamoto, A.2    Tashiro, Y.3
  • 30
    • 0029941071 scopus 로고    scopus 로고
    • The glut 1 glucose transporter interacts with calnexin and calreticulin
    • Oliver, J. D., Hresko, R. C., Mueckler, M. and High, S. (1996). The glut 1 glucose transporter interacts with calnexin and calreticulin. J. Biol. Chem. 271, 13691-13696.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13691-13696
    • Oliver, J.D.1    Hresko, R.C.2    Mueckler, M.3    High, S.4
  • 31
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver, J. D., van der Wal, F. J., Bulleid, N. J. and High, S. (1997). Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275, 86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    Van Der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 32
    • 0025225456 scopus 로고
    • The retention signal for soluble proteins of the endoplasmic reticulum
    • Pelham, H. R. (1990). The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem. Sci. 15, 483-486.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 483-486
    • Pelham, H.R.1
  • 33
    • 0030889062 scopus 로고    scopus 로고
    • Distinct compartmentalization of TGN46 and beta 1,4-galactosyltransferase in HeLa cells
    • Prescott, A. R., Lucocq, J. M., James, J., Lister, J. M. and Ponnambalam, S. (1997). Distinct compartmentalization of TGN46 and beta 1,4-galactosyltransferase in HeLa cells. Eur. J. Cell Biol. 72, 238-246.
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 238-246
    • Prescott, A.R.1    Lucocq, J.M.2    James, J.3    Lister, J.M.4    Ponnambalam, S.5
  • 34
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport, T. A., Jungnickel, B. and Kutay, U. (1996). Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65, 271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 35
    • 0029564918 scopus 로고
    • Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment
    • Raposo, G., van Santen, H. M., Leijendekker, R., Geuze, H. J. and Ploegh, H. L. (1995). Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment. J. Cell Biol. 131, 1403-1419.
    • (1995) J. Cell Biol. , vol.131 , pp. 1403-1419
    • Raposo, G.1    Van Santen, H.M.2    Leijendekker, R.3    Geuze, H.J.4    Ploegh, H.L.5
  • 36
    • 0029836930 scopus 로고    scopus 로고
    • COPII vesicles derived from mammalian endoplasmic reticulum microsomes recruit COPI
    • Rowe, T., Aridor, M., McCaffery, J. M., Plutner, H., Nuoffer, C. and Balch, W. E. (1996). COPII vesicles derived from mammalian endoplasmic reticulum microsomes recruit COPI. J. Cell Biol. 135, 895-911.
    • (1996) J. Cell Biol. , vol.135 , pp. 895-911
    • Rowe, T.1    Aridor, M.2    McCaffery, J.M.3    Plutner, H.4    Nuoffer, C.5    Balch, W.E.6
  • 37
    • 0021148465 scopus 로고
    • Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface
    • Saraste, J. and Kuismanen, E. (1984). Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell 38, 535-549.
    • (1984) Cell , vol.38 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2
  • 38
    • 0026052099 scopus 로고
    • Distribution of the intermediate elements operating in ER to Golgi transport
    • Saraste, J. and Svensson, K. (1991). Distribution of the intermediate elements operating in ER to Golgi transport. J. Cell Sci. 100, 415-430.
    • (1991) J. Cell Sci. , vol.100 , pp. 415-430
    • Saraste, J.1    Svensson, K.2
  • 39
    • 0029953563 scopus 로고    scopus 로고
    • Endoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rerlp-dependent retrieval that requires the transmembrane domain and Rerlp-independent retention that involves the cytoplasmic domain
    • Sato, M., Sato, K. and Nakano, A. (1996). Endoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rerlp-dependent retrieval that requires the transmembrane domain and Rerlp-independent retention that involves the cytoplasmic domain. J. Cell Biol. 134, 279-293.
    • (1996) J. Cell Biol. , vol.134 , pp. 279-293
    • Sato, M.1    Sato, K.2    Nakano, A.3
  • 40
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
    • Schweizer, A., Fransen, J. A., Bachi, T., Ginsel, L. and Hauri, H. P. (1988). Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J. Cell Biol. 107, 1643-1653.
    • (1988) J. Cell Biol. , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.2    Bachi, T.3    Ginsel, L.4    Hauri, H.P.5
  • 41
    • 0030943027 scopus 로고    scopus 로고
    • Partitioning of the Golgi apparatus during mitosis in living HeLa cells
    • Shima, D. T., Haldar, K., Pepperkok, R., Watson, R. and Warren, G. (1997). Partitioning of the Golgi apparatus during mitosis in living HeLa cells. J. Cell Biol. 137, 1211-1228.
    • (1997) J. Cell Biol. , vol.137 , pp. 1211-1228
    • Shima, D.T.1    Haldar, K.2    Pepperkok, R.3    Watson, R.4    Warren, G.5
  • 42
    • 0027526896 scopus 로고
    • An N-terminal glycosylation signal on cytochrome P450 is restricted to the endoplasmic reticulum in a luminal orientation
    • Szczesna-Skorupa, E. and Kemper, B. (1993). An N-terminal glycosylation signal on cytochrome P450 is restricted to the endoplasmic reticulum in a luminal orientation. J. Biol. Chem. 268, 1757-1762.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1757-1762
    • Szczesna-Skorupa, E.1    Kemper, B.2
  • 43
    • 0028885696 scopus 로고
    • The cytoplasmic and N-terminal transmembrane domains of cytochrome P450 contain independent signals for retention in the endoplasmic reticulum
    • Szczesna-Skorupa, E., Ahn, K., Chen, C. D., Doray, B. and Kemper, B. (1995). The cytoplasmic and N-terminal transmembrane domains of cytochrome P450 contain independent signals for retention in the endoplasmic reticulum. J. Biol. Chem. 270, 24327-24333.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24327-24333
    • Szczesna-Skorupa, E.1    Ahn, K.2    Chen, C.D.3    Doray, B.4    Kemper, B.5
  • 44
    • 0027439583 scopus 로고
    • Molecular cloning, characterization, subcellular localization and dynamics of p23, the mammalian KDEL receptor
    • Tang, B. L., Wong, S. H., Qi, X. L., Low, S. H. and Hong, W. (1993). Molecular cloning, characterization, subcellular localization and dynamics of p23, the mammalian KDEL receptor. J. Cell Biol. 120, 325-328.
    • (1993) J. Cell Biol. , vol.120 , pp. 325-328
    • Tang, B.L.1    Wong, S.H.2    Qi, X.L.3    Low, S.H.4    Hong, W.5
  • 45
    • 0030970343 scopus 로고    scopus 로고
    • Endoplasmic reticulum retention mediated by the transmembrane domain of type II membrane proteins Sec12p and glucosidase 1
    • Tang, B. L., Low, S. H. and Hong, W. (1997). Endoplasmic reticulum retention mediated by the transmembrane domain of type II membrane proteins Sec12p and glucosidase 1. Eur. J. Cell Biol. 73, 98-104.
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 98-104
    • Tang, B.L.1    Low, S.H.2    Hong, W.3
  • 46
    • 0029778556 scopus 로고    scopus 로고
    • Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus
    • Teasdale, R. D. and Jackson, M. R. (1996). Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus. Annu. Rev. Cell Dev. Biol. 12, 27-54.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 27-54
    • Teasdale, R.D.1    Jackson, M.R.2
  • 47
    • 0025282543 scopus 로고
    • Identification by anti-idiotype antibodies of an intracellular membrane protein that recognizes a mammalian endoplasmic reticulum retention signal
    • Vaux, D., Tooze, J. and Fuller, S. (1990). Identification by anti-idiotype antibodies of an intracellular membrane protein that recognizes a mammalian endoplasmic reticulum retention signal. Nature 345, 495-502.
    • (1990) Nature , vol.345 , pp. 495-502
    • Vaux, D.1    Tooze, J.2    Fuller, S.3
  • 48
    • 0032572579 scopus 로고    scopus 로고
    • Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme
    • Vollenweider, F., Kappeler, F., Itin, C., Hauri, H. P. (1998). Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme. J. Cell Biol. 142, 377-389.
    • (1998) J. Cell Biol. , vol.142 , pp. 377-389
    • Vollenweider, F.1    Kappeler, F.2    Itin, C.3    Hauri, H.P.4
  • 49
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz, E. J., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T. R., Rapoport, T. A. and Ploegh, H. L. (1996). Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384, 432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6    Rapoport, T.A.7    Ploegh, H.L.8
  • 50
    • 0029024163 scopus 로고
    • The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells
    • Wilson, R., Alien, A. J., Oliver, J., Brookman, J. L., High, S. and Bulleid, N. J. (1995). The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells. Biochem. J. 307, 679-687.
    • (1995) Biochem. J. , vol.307 , pp. 679-687
    • Wilson, R.1    Alien, A.J.2    Oliver, J.3    Brookman, J.L.4    High, S.5    Bulleid, N.J.6
  • 51
    • 0031910288 scopus 로고    scopus 로고
    • Scattered Golgi elements during microtubule disruption are initially enriched in trans-Golgi proteins
    • Yang, W. and Storrie, B. (1998). Scattered Golgi elements during microtubule disruption are initially enriched in trans-Golgi proteins. Mol. Biol. Cell 9, 191-207.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 191-207
    • Yang, W.1    Storrie, B.2
  • 52
    • 0028977992 scopus 로고
    • The beta-glucuronidase propeptide contains a serpin-related octamer necessary for complex formation with egasyn esterase and for retention within the endoplasmic reticulum
    • Zhen, L., Rusiniak, M. E. and Swank, R. T. (1995). The beta-glucuronidase propeptide contains a serpin-related octamer necessary for complex formation with egasyn esterase and for retention within the endoplasmic reticulum. J. Biol Chem. 270, 11912-11920.
    • (1995) J. Biol Chem. , vol.270 , pp. 11912-11920
    • Zhen, L.1    Rusiniak, M.E.2    Swank, R.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.