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Volumn 52, Issue 6, 2007, Pages 987-1000

In vivo analysis of the lumenal binding protein (BiP) reveals multiple functions of its ATPase domain

Author keywords

ATPase; BiP; Chaperone; Endoplasmic reticulum; Hsp70; Protein folding

Indexed keywords

ATPASE; CHAPERONES; ENDOPLASMIC RETICULUM; HYDROPHOBIC REGIONS; SECRETORY PROTEIN SYNTHESIS;

EID: 36849074225     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2007.03296.x     Document Type: Article
Times cited : (11)

References (56)
  • 1
    • 13444271726 scopus 로고    scopus 로고
    • The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum
    • Alder, N.N., Shen, Y., Brodsky, J.L., Hendershot, L.M. Johnson, A.E. (2005) The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum. J. Cell Biol. 168, 389 399.
    • (2005) J. Cell Biol. , vol.168 , pp. 389-399
    • Alder, N.N.1    Shen, Y.2    Brodsky, J.L.3    Hendershot, L.M.4    Johnson, A.E.5
  • 2
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. (1973) Principles that govern the folding of protein chains. Science, 181, 223 230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 3
    • 4444288866 scopus 로고    scopus 로고
    • Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones
    • Ben-Zvi, A., De Los Rios, P., Dietler, G. Goloubinoff, P. (2004) Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones. J. Biol. Chem. 279, 37298 37303.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37298-37303
    • Ben-Zvi, A.1    De Los Rios, P.2    Dietler, G.3    Goloubinoff, P.4
  • 4
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti, A., Zhang, Y., Hendershot, L.M., Harding, H.P. Ron, D. (2000) Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol. 2, 326 332.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 5
    • 0027164203 scopus 로고
    • Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers
    • Blond-Elguindi, S., Fourie, A.M., Sambrook, J.F. Gething, M.J. (1993) Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers. J. Biol. Chem. 268, 12730 12735.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12730-12735
    • Blond-Elguindi, S.1    Fourie, A.M.2    Sambrook, J.F.3    Gething, M.J.4
  • 6
    • 0038029881 scopus 로고    scopus 로고
    • ER quality control can lead to retrograde transport from the ER lumen to the cytosol and nucleoplasm in plants
    • Brandizzi, F., Hanton, S.L., daSilva, L.L.P., Boevink, P., Evans, D., Oparka, K., Denecke, J. Hawes, C. (2003) ER quality control can lead to retrograde transport from the ER lumen to the cytosol and nucleoplasm in plants. Plant J. 34, 269 281.
    • (2003) Plant J. , vol.34 , pp. 269-281
    • Brandizzi, F.1    Hanton, S.L.2    Dasilva, L.L.P.3    Boevink, P.4    Evans, D.5    Oparka, K.6    Denecke, J.7    Hawes, C.8
  • 7
    • 0027759380 scopus 로고
    • A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome
    • Brodsky, J.L. Schekman, R. (1993) A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J. Cell Biol. 123, 1355 1363.
    • (1993) J. Cell Biol. , vol.123 , pp. 1355-1363
    • Brodsky, J.L.1    Schekman, R.2
  • 8
    • 0033525198 scopus 로고    scopus 로고
    • The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
    • Brodsky, J.L., Werner, E.D., Dubas, M.E., Goeckeler, J.L., Kruse, K.B. McCracken, A.A. (1999) The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J. Biol. Chem. 274, 3453 3460.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3453-3460
    • Brodsky, J.L.1    Werner, E.D.2    Dubas, M.E.3    Goeckeler, J.L.4    Kruse, K.B.5    McCracken, A.A.6
  • 9
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B. Horwich, A.L. (1998) The Hsp70 and Hsp60 chaperone machines. Cell, 92, 351 366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 10
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban, M.J. Cohen, S.N. (1980) Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138, 179 207.
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 11
    • 0032500673 scopus 로고    scopus 로고
    • Substrate binding induces depolymerization of the C-terminal peptide binding domain of murine GRP78/BiP
    • Chevalier, M., King, L., Wang, C., Gething, M.J., Elguindi, E. Blond, S.Y. (1998) Substrate binding induces depolymerization of the C-terminal peptide binding domain of murine GRP78/BiP. J. Biol. Chem. 273, 26827 26835.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26827-26835
    • Chevalier, M.1    King, L.2    Wang, C.3    Gething, M.J.4    Elguindi, E.5    Blond, S.Y.6
  • 12
    • 0347033285 scopus 로고    scopus 로고
    • BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP
    • Chung, K.T., Shen, Y. Hendershot, L.M. (2002) BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP. J. Biol. Chem. 277, 47557 47563.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47557-47563
    • Chung, K.T.1    Shen, Y.2    Hendershot, L.M.3
  • 13
    • 0031774263 scopus 로고    scopus 로고
    • BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress
    • Crofts, A.J., Leborgne-Castel, N., Pesca, M., Vitale, A. Denecke, J. (1998) BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress. Plant Cell, 10, 813 824.
    • (1998) Plant Cell , vol.10 , pp. 813-824
    • Crofts, A.J.1    Leborgne-Castel, N.2    Pesca, M.3    Vitale, A.4    Denecke, J.5
  • 15
    • 0036626120 scopus 로고    scopus 로고
    • The 78 kDa glucose-regulated protein (GRP78/BIP) is expressed on the cell membrane, is released into cell culture medium and is also present in human peripheral circulation
    • Delpino, A. Castelli, M. (2002) The 78 kDa glucose-regulated protein (GRP78/BIP) is expressed on the cell membrane, is released into cell culture medium and is also present in human peripheral circulation. Biosci. Rep. 22, 407 420.
    • (2002) Biosci. Rep. , vol.22 , pp. 407-420
    • Delpino, A.1    Castelli, M.2
  • 17
    • 0026523624 scopus 로고
    • Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope
    • Denecke, J., De Rycke, R. Botterman, J. (1992) Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope. EMBO J. 11, 2345 2355.
    • (1992) EMBO J. , vol.11 , pp. 2345-2355
    • Denecke, J.1    De Rycke, R.2    Botterman, J.3
  • 18
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L. Helenius, A. (2003) Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4, 181 191.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 19
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty, K.M., DeLuca-Flaherty, C. McKay, D.B. (1990) Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature, 346, 623 628.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    Deluca-Flaherty, C.2    McKay, D.B.3
  • 20
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn, G.C., Pohl, J., Flocco, M.T. Rothman, J.E. (1991) Peptide-binding specificity of the molecular chaperone BiP. Nature, 353, 726 730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 21
    • 0142092348 scopus 로고    scopus 로고
    • A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP
    • Foresti, O., Frigerio, L., Holkeri, H., De Virgilio, M., Vavassori, S. Vitale, A. (2003) A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP. Plant Cell, 15, 2464 2475.
    • (2003) Plant Cell , vol.15 , pp. 2464-2475
    • Foresti, O.1    Frigerio, L.2    Holkeri, H.3    De Virgilio, M.4    Vavassori, S.5    Vitale, A.6
  • 22
    • 0029980091 scopus 로고    scopus 로고
    • Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
    • Frydman, J. Hartl, F.U. (1996) Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. Science, 272, 1497 1502.
    • (1996) Science , vol.272 , pp. 1497-1502
    • Frydman, J.1    Hartl, F.U.2
  • 23
    • 0027528476 scopus 로고
    • Mutations within the nucleotide binding-site of immunoglobulin-binding protein inhibit atpase activity and interfere with release of immunoglobulin heavy-chain
    • Gaut, J.R. Hendershot, L.M. (1993) Mutations within the nucleotide binding-site of immunoglobulin-binding protein inhibit atpase activity and interfere with release of immunoglobulin heavy-chain. J. Biol. Chem. 268, 7248 7255.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7248-7255
    • Gaut, J.R.1    Hendershot, L.M.2
  • 24
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • Gething, M.J. (1999) Role and regulation of the ER chaperone BiP. Semin. Cell Dev. Biol. 10, 465 472.
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 465-472
    • Gething, M.J.1
  • 25
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff, P., Mogk, A., Zvi, A.P.B., Tomoyasu, T. Bukau, B. (1999) Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl Acad. Sci. USA 96, 13732 13737.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.B.3    Tomoyasu, T.4    Bukau, B.5
  • 26
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman, B.D., Hendershot, L.M. Johnson, A.E. (1998) BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell, 92, 747 758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 27
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996) Molecular chaperones in cellular protein folding. Nature, 381, 571 580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 28
    • 0028965528 scopus 로고
    • In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum
    • Hendershot, L.M., Wei, J.Y., Gaut, J.R., Lawson, B., Freiden, P.J. Murti, K.G. (1995) In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum. Mol. Biol. Cell, 6, 283 296.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 283-296
    • Hendershot, L.M.1    Wei, J.Y.2    Gaut, J.R.3    Lawson, B.4    Freiden, P.J.5    Murti, K.G.6
  • 29
    • 0029890917 scopus 로고    scopus 로고
    • Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants
    • Hendershot, L., Wei, J., Gaut, J., Melnick, J., Aviel, S. Argon, Y. (1996) Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants. Proc. Natl Acad. Sci. USA, 93, 5269 5274.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5269-5274
    • Hendershot, L.1    Wei, J.2    Gaut, J.3    Melnick, J.4    Aviel, S.5    Argon, Y.6
  • 30
    • 0024400060 scopus 로고
    • Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
    • Hurtley, S.M., Bole, D.G., Hoover-Litty, H., Helenius, A. Copeland, C.S. (1989) Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J. Cell Biol. 108, 2117 2126.
    • (1989) J. Cell Biol. , vol.108 , pp. 2117-2126
    • Hurtley, S.M.1    Bole, D.G.2    Hoover-Litty, H.3    Helenius, A.4    Copeland, C.S.5
  • 32
    • 0028809495 scopus 로고
    • Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae
    • Lyman, S.K. Schekman, R. (1995) Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae. J. Cell Biol. 131, 1163 1171.
    • (1995) J. Cell Biol. , vol.131 , pp. 1163-1171
    • Lyman, S.K.1    Schekman, R.2
  • 33
    • 0030970268 scopus 로고    scopus 로고
    • Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP
    • Lyman, S.K. Schekman, R. (1997) Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell, 88, 85 96.
    • (1997) Cell , vol.88 , pp. 85-96
    • Lyman, S.K.1    Schekman, R.2
  • 35
    • 0015914077 scopus 로고
    • Streptomycin resistant plants from callus culture of haploid tobacco
    • Maliga, P., Breznowitz, A. Marton, L. (1973) Streptomycin resistant plants from callus culture of haploid tobacco. Nature, 244, 29 30.
    • (1973) Nature , vol.244 , pp. 29-30
    • Maliga, P.1    Breznowitz, A.2    Marton, L.3
  • 36
    • 0030764015 scopus 로고    scopus 로고
    • Protein transport by purified yeast sec complex and Kar2p without membranes
    • Matlack, K.E.S., Plath, K., Misselwitz, B. Rapoport, T.A. (1997) Protein transport by purified yeast sec complex and Kar2p without membranes. Science, 277, 938 941.
    • (1997) Science , vol.277 , pp. 938-941
    • Matlack, K.E.S.1    Plath, K.2    Misselwitz, B.3    Rapoport, T.A.4
  • 37
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane
    • Matlack, K.E., Misselwitz, B., Plath, K. Rapoport, T.A. (1999) BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell, 97, 553 564.
    • (1999) Cell , vol.97 , pp. 553-564
    • Matlack, K.E.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 38
    • 0033575256 scopus 로고    scopus 로고
    • Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex
    • Misselwitz, B., Staeck, O., Matlack, K.E. Rapoport, T.A. (1999) Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex. J. Biol. Chem. 274, 20110 20115.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20110-20115
    • Misselwitz, B.1    Staeck, O.2    Matlack, K.E.3    Rapoport, T.A.4
  • 39
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with the 78-kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro, S. Pelham, H.R.B. (1986) An Hsp70-like protein in the ER: identity with the 78-kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell, 46, 291 300.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 40
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue culture
    • Murashige, T. Skoog, F. (1962) A revised medium for rapid growth and bioassays with tobacco tissue culture. Physiol. Plant. 15, 473 497.
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 41
    • 18744378812 scopus 로고    scopus 로고
    • ER-resident chaperone interactions with recombinant antibodies in transgenic plants
    • Nuttall, J., Vine, N., Hadlington, J.L., Drake, P., Frigerio, L. Ma, J.K. (2002) ER-resident chaperone interactions with recombinant antibodies in transgenic plants. Eur. J. Biochem. 269, 6042 6051.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 6042-6051
    • Nuttall, J.1    Vine, N.2    Hadlington, J.L.3    Drake, P.4    Frigerio, L.5    Ma, J.K.6
  • 45
    • 33645737420 scopus 로고    scopus 로고
    • Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway
    • Pimpl, P., Taylor, J.P., Snowden, C., Hillmer, S., Robinson, D.G. Denecke, J. (2006) Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway. Plant Cell, 18, 198 211.
    • (2006) Plant Cell , vol.18 , pp. 198-211
    • Pimpl, P.1    Taylor, J.P.2    Snowden, C.3    Hillmer, S.4    Robinson, D.G.5    Denecke, J.6
  • 46
    • 12844257546 scopus 로고    scopus 로고
    • Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response
    • Shen, J., Snapp, E.L., Lippincott-Schwartz, J. Prywes, R. (2005) Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response. Mol. Cell. Biol. 25, 921 932.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 921-932
    • Shen, J.1    Snapp, E.L.2    Lippincott-Schwartz, J.3    Prywes, R.4
  • 48
    • 0036049850 scopus 로고    scopus 로고
    • The unfolding story of the Escherichia coli Hsp70 DnaK: Is DnaK a holdase or an unfoldase?
    • Slepenkov, S.V. Witt, S.N. (2002) The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase? Mol. Microbiol. 45, 1197 1206.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1197-1206
    • Slepenkov, S.V.1    Witt, S.N.2
  • 50
    • 33847324367 scopus 로고    scopus 로고
    • Lobe IB of the ATPase domain of Kar2p/BiP interacts with Ire1p to negatively regulate the unfolded protein response in Saccharomyces cerevisiae
    • Todd-Corlett, A., Jones, E., Seghers, C. Gething, M.J. (2007) Lobe IB of the ATPase domain of Kar2p/BiP interacts with Ire1p to negatively regulate the unfolded protein response in Saccharomyces cerevisiae. J. Mol. Biol. 367, 770 787.
    • (2007) J. Mol. Biol. , vol.367 , pp. 770-787
    • Todd-Corlett, A.1    Jones, E.2    Seghers, C.3    Gething, M.J.4
  • 51
    • 0029167492 scopus 로고
    • The binding protein associates with monomeric phaseolin
    • Vitale, A., Bielli, A. Ceriotti, A. (1995) The binding protein associates with monomeric phaseolin. Plant Physiol. 107, 1411 1418.
    • (1995) Plant Physiol. , vol.107 , pp. 1411-1418
    • Vitale, A.1    Bielli, A.2    Ceriotti, A.3
  • 52
    • 0025339295 scopus 로고
    • Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast
    • Vogel, J.P., Misra, L.M. Rose, M.D. (1990) Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J. Cell Biol. 110, 1885 1895.
    • (1990) J. Cell Biol. , vol.110 , pp. 1885-1895
    • Vogel, J.P.1    Misra, L.M.2    Rose, M.D.3
  • 53
    • 0028853568 scopus 로고
    • In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis
    • Wei, J., Gaut, J.R. Hendershot, L.M. (1995) In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis. J. Biol. Chem. 270, 26677 26682.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26677-26682
    • Wei, J.1    Gaut, J.R.2    Hendershot, L.M.3
  • 54
    • 0035862963 scopus 로고    scopus 로고
    • Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo
    • Young, B.P., Craven, R.A., Reid, P.J., Willer, M. Stirling, C.J. (2001) Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J. 20, 262 271.
    • (2001) EMBO J. , vol.20 , pp. 262-271
    • Young, B.P.1    Craven, R.A.2    Reid, P.J.3    Willer, M.4    Stirling, C.J.5
  • 55
    • 25144520251 scopus 로고    scopus 로고
    • Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP
    • Zhao, L., Longo-Guess, C., Harris, B.S., Lee, J.W. Ackerman, S.L. (2005) Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat. Genet. 37, 974 979.
    • (2005) Nat. Genet. , vol.37 , pp. 974-979
    • Zhao, L.1    Longo-Guess, C.2    Harris, B.S.3    Lee, J.W.4    Ackerman, S.L.5


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