메뉴 건너뛰기




Volumn 18, Issue 1, 1999, Pages 85-95

In vivo newly translated polypeptides are sequestered in a protected folding environment

Author keywords

Actin; Chaperones; Chaperonin; Protein folding; Translation

Indexed keywords

CHAPERONE; CHAPERONIN; POLYPEPTIDE;

EID: 0033521588     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.1.85     Document Type: Article
Times cited : (278)

References (60)
  • 1
    • 0025303147 scopus 로고
    • Interaction of Hsp70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann, R.P., Mizzen, L.A. and Welch, W.J. (1990). Interaction of Hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science, 248, 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.A.2    Welch, W.J.3
  • 2
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • Blond-Elguindi, S., Cwirla, S.E., Dower, W.J., Lipshutz, R.J., Sprang, S.R., Sambrook, J.F. and Gething, M.J. (1993) Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell, 75, 717-728.
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond-Elguindi, S.1    Cwirla, S.E.2    Dower, W.J.3    Lipshutz, R.J.4    Sprang, S.R.5    Sambrook, J.F.6    Gething, M.J.7
  • 3
    • 0025816663 scopus 로고
    • Folding of influenza hemagglutinin in the endoplasmic-reticulum
    • Braakman, I., Hooverlitty, H., Wagner, K., and Helenius, A. (1991) Folding of influenza hemagglutinin in the endoplasmic-reticulum. J. Cell Biol., 114, 401-411.
    • (1991) J. Cell Biol. , vol.114 , pp. 401-411
    • Braakman, I.1    Hooverlitty, H.2    Wagner, K.3    Helenius, A.4
  • 4
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B. and 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
  • 5
    • 0030560763 scopus 로고    scopus 로고
    • Growing-up in a dangerous environment: A network of multiple targeting and folding pathways for nascent polypeptides in the cytosol
    • Bukau, B., Hesterkamp, T. and Luirink, J. (1996) Growing-up in a dangerous environment: a network of multiple targeting and folding pathways for nascent polypeptides in the cytosol. Trends Cell Biol., 6, 480-486.
    • (1996) Trends Cell Biol. , vol.6 , pp. 480-486
    • Bukau, B.1    Hesterkamp, T.2    Luirink, J.3
  • 6
    • 0032496137 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation-factor EF-Tu
    • Caldas, T.D., Elyaagoubi, A. and Richarme, G. (1998) Chaperone properties of bacterial elongation-factor EF-Tu. J. Biol. Chem., 273, 11478-11482.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11478-11482
    • Caldas, T.D.1    Elyaagoubi, A.2    Richarme, G.3
  • 7
    • 0028586011 scopus 로고
    • Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo
    • Chen, X., Sullivan, D.S. and Huffaker, T.C. (1994) Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo. Proc. Natl Acad. Sci. USA, 91, 9111-9115.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9111-9115
    • Chen, X.1    Sullivan, D.S.2    Huffaker, T.C.3
  • 8
    • 0030584662 scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti, E., Franks, N.P. and Brick, P. (1995) Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure, 4, 287-298.
    • (1995) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 9
    • 0028079904 scopus 로고
    • The folding of the bifunctional Trp3 protein in yeast is influenced by a translational pause which lies in a region of structural divergence with Escherichia coli indoleglycerol-phosphate synthase
    • Crombie, T., Boyle, J., Coggins, J. and Brown, A. (1994) The folding of the bifunctional Trp3 protein in yeast is influenced by a translational pause which lies in a region of structural divergence with Escherichia coli indoleglycerol-phosphate synthase. Eur. J. Biochem., 226, 657-664.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 657-664
    • Crombie, T.1    Boyle, J.2    Coggins, J.3    Brown, A.4
  • 10
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70
    • Cyr, D.M., Langer, T. and Douglas, M.G. (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci., 19, 176-181.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 11
    • 0032478545 scopus 로고    scopus 로고
    • Crystal-structure of the thermosome; the archaeal chaperonin and homolog of CCT
    • Ditzel, L., Lowe, J., Stock, D., Stetter, K.O., Huber, H., Huber, R. and Steinbacher, S. (1998) Crystal-structure of the thermosome; the archaeal chaperonin and homolog of CCT. Cell, 93, 125-138.
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Lowe, J.2    Stock, D.3    Stetter, K.O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 12
    • 0029769797 scopus 로고    scopus 로고
    • Newly-synthesized ß-tubulin demonstrates domain-specific interactions with the cytosolic chaperonin
    • Dobrzynski, J., Sternlicht, M., Farr, G. and Sternlicht, H. (1996) Newly-synthesized ß-tubulin demonstrates domain-specific interactions with the cytosolic chaperonin. Biochemistry, 35, 15870-15882.
    • (1996) Biochemistry , vol.35 , pp. 15870-15882
    • Dobrzynski, J.1    Sternlicht, M.2    Farr, G.3    Sternlicht, H.4
  • 13
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian-cells
    • Eggers, D.K., Welch, W.J. and Hansen, W.J. (1997) Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian-cells. Mol. Biol. Cell, 8, 1559-1573.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1559-1573
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 14
    • 0029937035 scopus 로고    scopus 로고
    • The 'bio' in biochemistry: Protein folding inside and outside the cell
    • Ellis, R.J. (1996) The 'Bio' in biochemistry: protein folding inside and outside the cell. Science, 272, 1448-1449.
    • (1996) Science , vol.272 , pp. 1448-1449
    • Ellis, R.J.1
  • 15
    • 0031239894 scopus 로고    scopus 로고
    • Avoiding the crowd
    • Ellis, R.J. (1997) Avoiding the crowd. Curr. Biol., 7, 531-533.
    • (1997) Curr. Biol. , vol.7 , pp. 531-533
    • Ellis, R.J.1
  • 16
    • 0030042460 scopus 로고    scopus 로고
    • Protein-folding in the cell: Competing models of chaperonin function
    • Ellis, R.J. and Hartl, F.U. (1996) Protein-folding in the cell: competing models of chaperonin function. FASEB J., 10, 20-26.
    • (1996) FASEB J. , vol.10 , pp. 20-26
    • Ellis, R.J.1    Hartl, F.U.2
  • 17
    • 0030750584 scopus 로고    scopus 로고
    • In-vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt, K.L., Hendrick, J.P., Houry, W.A. and Hartl, F.U. (1997) In-vivo observation of polypeptide flux through the bacterial chaperonin system. Cell, 90, 491-500.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.U.4
  • 18
    • 0030730821 scopus 로고    scopus 로고
    • Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and normative forms
    • Farr, G.W., Scharl, E.C. Schumacher, R.J., Sondek, S. and Horwich, A.L. (1997) Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and normative forms. Cell, 89, 927-937.
    • (1997) Cell , vol.89 , pp. 927-937
    • Farr, G.W.1    Scharl, E.C.2    Schumacher, R.J.3    Sondek, S.4    Horwich, A.L.5
  • 19
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn, G.C., Rohl, J., Flocco, M.T. and 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    Rohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 20
    • 0030818720 scopus 로고    scopus 로고
    • Use of tetracycline-controlled gene expression systems to study mammalian cell cycle
    • Freundlieb, S., Baron, U., Bonin, A.L., Gossen, M. and Bujard, H. (1997) Use of tetracycline-controlled gene expression systems to study mammalian cell cycle. Methods Enzymol., 283, 159-173.
    • (1997) Methods Enzymol. , vol.283 , pp. 159-173
    • Freundlieb, S.1    Baron, U.2    Bonin, A.L.3    Gossen, M.4    Bujard, H.5
  • 21
    • 0029980091 scopus 로고    scopus 로고
    • Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
    • Frydman, J. and 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
  • 22
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman, J. and Hohfeld, J. (1997) Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci., 22, 87-92.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Hohfeld, J.2
  • 23
    • 0027077442 scopus 로고
    • Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
    • Frydman, J., Nimmesgern, E., Erdjument, B.H., Wall, J.S., Tempst, P. and Hartl, F.U. (1992) Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J., 11, 4767-4778.
    • (1992) EMBO J. , vol.11 , pp. 4767-4778
    • Frydman, J.1    Nimmesgern, E.2    Erdjument, B.H.3    Wall, J.S.4    Tempst, P.5    Hartl, F.U.6
  • 24
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., Nimmesgern, E., Ohtsuka, K. and Hartl, F.U. (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature, 370, 111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 25
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes ß-actin folding
    • Gao, Y., Thomas, J.O., Chow, R.L., Lee, G.H. and Cowan, N.J. (1992) A cytoplasmic chaperonin that catalyzes ß-actin folding. Cell, 69, 1043-1050.
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 26
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional α-tubulin and γ-tubulin
    • Geissler, S., Siegers, K. and Schiebel, E. (1998) A novel protein complex promoting formation of functional α-tubulin and γ-tubulin. EMBO J., 17, 952-966.
    • (1998) EMBO J. , vol.17 , pp. 952-966
    • Geissler, S.1    Siegers, K.2    Schiebel, E.3
  • 27
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.J. and Sambrook, J. (1992) Protein folding in the cell. Nature, 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 28
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70 and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover, J.R. and Lindquist, S. (1998) Hsp104, Hsp70 and Hsp40: A novel chaperone system that rescues previously aggregated proteins. Cell, 94, 73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 29
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline responsive promoters
    • Gossen, M. and Bujard, H. (1992) Tight control of gene expression in mammalian cells by tetracycline responsive promoters. Proc. Natl Acad. Sci. USA, 89, 5547-5551.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 30
    • 0028125299 scopus 로고
    • Complex environment of nascent polypeptide chains
    • Hansen, W.J., Lingappa, V.R. and Welch, W.J. (1994) Complex environment of nascent polypeptide chains. J. Biol. Chem., 269, 26610-26613.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26610-26613
    • Hansen, W.J.1    Lingappa, V.R.2    Welch, W.J.3
  • 32
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996) Molecular chaperones in cellular protein folding. Nature, 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 33
    • 0028334547 scopus 로고
    • Conformational specificity of the chaperonin GroEL for the compact folding intermediates of α-lactalbumin
    • Hayer-Hartl, M.K., Ewbank, J.J., Creighton, T.E. and Hartl, F.U. (1994) conformational specificity of the chaperonin GroEL for the compact folding intermediates of α-lactalbumin. EMBO J., 13, 3192-3202.
    • (1994) EMBO J. , vol.13 , pp. 3192-3202
    • Hayer-Hartl, M.K.1    Ewbank, J.J.2    Creighton, T.E.3    Hartl, F.U.4
  • 34
    • 0038217763 scopus 로고    scopus 로고
    • Regulation of the heat-shock cognate Hsc70 in the mammalian-cell: The characterization of the anti-apoptotic protein Bag-1 provides novel insights
    • Hohfeld, J. (1998) Regulation of the heat-shock cognate Hsc70 in the mammalian-cell: the characterization of the anti-apoptotic protein Bag-1 provides novel insights. Biol. Chem., 379, 269-274.
    • (1998) Biol. Chem. , vol.379 , pp. 269-274
    • Hohfeld, J.1
  • 35
    • 0028895618 scopus 로고
    • Antibody characterization of 2 distinct conformations of the chaperonin-containing TCP-1 from mouse testis
    • Hynes, G., Kubota, H. and Willison, K.R. (1995) Antibody characterization of 2 distinct conformations of the chaperonin-containing TCP-1 from mouse testis. FEBS Lett., 358, 129-132.
    • (1995) FEBS Lett. , vol.358 , pp. 129-132
    • Hynes, G.1    Kubota, H.2    Willison, K.R.3
  • 36
    • 0030809270 scopus 로고    scopus 로고
    • Protein-folding in-vivo: Unraveling complex pathways
    • Johnson, J.L. and Craig, E.A. (1997) Protein-folding in-vivo: unraveling complex pathways. Cell, 90, 201-204.
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 37
    • 0021647566 scopus 로고
    • Analysis of H-2 and Ia antigens by 2-dimensional polyacrylamide-gel electrophoresis
    • Jones, P.P. (1984) Analysis of H-2 and Ia antigens by 2-dimensional polyacrylamide-gel electrophoresis. Methods Enzymol., 108, 452-466.
    • (1984) Methods Enzymol. , vol.108 , pp. 452-466
    • Jones, P.P.1
  • 38
    • 0022110395 scopus 로고
    • Three-dimensional structure of the complex of actin and Dnase I at 4.5 Å resolution
    • Kabsch, W., Mannherz, H.G. and Suck, D. (1985) Three-dimensional structure of the complex of actin and Dnase I at 4.5 Å resolution. EMBO J., 4, 2113-2118.
    • (1985) EMBO J. , vol.4 , pp. 2113-2118
    • Kabsch, W.1    Mannherz, H.G.2    Suck, D.3
  • 39
    • 0030623528 scopus 로고    scopus 로고
    • Ribosomes and ribosomal-RNA as chaperones for folding of proteins
    • Kudlicki, W., Coffman, A., Kramer, G. and Hardesty, B. (1997) Ribosomes and ribosomal-RNA as chaperones for folding of proteins. Folding Des., 2, 101-108.
    • (1997) Folding Des. , vol.2 , pp. 101-108
    • Kudlicki, W.1    Coffman, A.2    Kramer, G.3    Hardesty, B.4
  • 41
    • 0026683609 scopus 로고
    • T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cystosol
    • Lewis, V.A., Hynes, G.M., Zheng, D., Saibil, H. and Willison, K. (1992) T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cystosol. Nature, 358, 249-252.
    • (1992) Nature , vol.358 , pp. 249-252
    • Lewis, V.A.1    Hynes, G.M.2    Zheng, D.3    Saibil, H.4    Willison, K.5
  • 42
    • 0020130877 scopus 로고
    • Correlation between synthesis of heat-shock proteins and development of thermotolerance in Chinese-hamster fibroblasts
    • Li, G.C. and Werb, Z. (1982) Correlation between synthesis of heat-shock proteins and development of thermotolerance in Chinese-hamster fibroblasts. Proc. Natl Acad. Sci. USA, 79, 3218-3222.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 3218-3222
    • Li, G.C.1    Werb, Z.2
  • 43
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • Nathan, D.F., Vos, M.H. and Lindquist, S. (1997) In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc. Natl Acad. Sci. USA, 94, 12949-12956.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 44
    • 0026649409 scopus 로고
    • The translation machinery and 70 Kd heat shock protein cooperate in protein synthesis
    • Nelson, R.J., Ziegelhoffer, T., Nicolet, C., Werner-Washburne, M. and Craig, E.A. (1993) The translation machinery and 70 Kd heat shock protein cooperate in protein synthesis. Cell, 71, 97-105.
    • (1993) Cell , vol.71 , pp. 97-105
    • Nelson, R.J.1    Ziegelhoffer, T.2    Nicolet, C.3    Werner-Washburne, M.4    Craig, E.A.5
  • 45
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer, W. and Hartl, F.U. (1997) Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature, 388, 343-349.
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.1    Hartl, F.U.2
  • 46
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the α-β-tubulin dimer by electron crystallography
    • Nogales, E., Wolf, S.G. and Downmg, K.H. (1998) Structure of the α-β-tubulin dimer by electron crystallography. Nature, 391, 199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downmg, K.H.3
  • 47
    • 0028305703 scopus 로고
    • Hsp70-protein complexes, complex stability and conformation of bound substrate protein
    • Palleros, D.R., Shi, L., Reid, K.L. and Fink, A.L. (1994) Hsp70-protein complexes, complex stability and conformation of bound substrate protein. J. Biol. Chem., 269, 13107-13114.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13107-13114
    • Palleros, D.R.1    Shi, L.2    Reid, K.L.3    Fink, A.L.4
  • 49
    • 0028908136 scopus 로고
    • Cytoplasmic chaperonin complexes enter neuntes developing in vitro and differ in subunit composition within single cells
    • Roobol, A., Holmes, F.E., Hayes, N.V.L., Baines, A.J. and Carden, M.J. (1995) Cytoplasmic chaperonin complexes enter neuntes developing in vitro and differ in subunit composition within single cells. J. Cell Sci., 108, 1477-1488.
    • (1995) J. Cell Sci. , vol.108 , pp. 1477-1488
    • Roobol, A.1    Holmes, F.E.2    Hayes, N.V.L.3    Baines, A.J.4    Carden, M.J.5
  • 50
    • 0030976048 scopus 로고    scopus 로고
    • Substrate-specificity of the Dnak chaperone determined by screening cellulose-bound peptide libraries
    • Rudiger, S., Germeroth, L., Schneidermergener, J. and Bukau, B. (1997) Substrate-specificity of the Dnak chaperone determined by screening cellulose-bound peptide libraries. EMBO J., 16, 1501-1507.
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rudiger, S.1    Germeroth, L.2    Schneidermergener, J.3    Bukau, B.4
  • 51
    • 0030034646 scopus 로고    scopus 로고
    • Crystal-structure of a G (α) protein β-γ dimer at 2.1 Å resolution
    • Sondek, J., Bohm, A., Lambright, D.G., Hamm, H.E. and Sigler, P.B. (1996) Crystal-structure of a G (α) protein β-γ dimer at 2.1 Å resolution. Nature, 379, 369-374.
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 53
    • 0028587244 scopus 로고
    • A yeast TCP-1 -like protein is required for actin function in vivo
    • Vinh, D.B. and Drubin, D.G. (1994) A yeast TCP-1 -like protein is required for actin function in vivo. Proc. Natl Acad. Sci. USA, 91, 9116-9120.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9116-9120
    • Vinh, D.B.1    Drubin, D.G.2
  • 54
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
    • Weissman, J.S., Kashi, Y., Fenton, W.A. and Horwich, A.L. (1994) GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell, 78, 693-702.
    • (1994) Cell , vol.78 , pp. 693-702
    • Weissman, J.S.1    Kashi, Y.2    Fenton, W.A.3    Horwich, A.L.4
  • 55
    • 0027980239 scopus 로고
    • A protein complex required for signal-sequence sorting and translocation
    • Wiedmann, B., Sakai, H., Davis, T.A. and Wiedmann, M. (1994) A protein complex required for signal-sequence sorting and translocation. Nature, 370, 434-440.
    • (1994) Nature , vol.370 , pp. 434-440
    • Wiedmann, B.1    Sakai, H.2    Davis, T.A.3    Wiedmann, M.4
  • 56
    • 0001314116 scopus 로고    scopus 로고
    • Structure and function of chaperonins in archaebacteria and eukaryotic cytosol
    • Ellis, R.J. (ed.). Academic Press Ltd, London, UK
    • Willison, K.R. and Horwich, A.L. (1996) Structure and function of chaperonins in archaebacteria and eukaryotic cytosol. In Ellis, R.J. (ed.), Cell Biology Series: The Chaperonins. Academic Press Ltd, London, UK, pp. 107-136.
    • (1996) Cell Biology Series: The Chaperonins , pp. 107-136
    • Willison, K.R.1    Horwich, A.L.2
  • 57
    • 0032541489 scopus 로고    scopus 로고
    • Zuotin; a ribosome-associated dnaj molecular chaperone
    • Yan, W., Schilke, B., Pfund, C., Walter, W., Kim, S.W. and Craig, E.A. (1998) Zuotin; a ribosome-associated Dnaj molecular chaperone. EMBO J., 17, 4809-4817.
    • (1998) EMBO J. , vol.17 , pp. 4809-4817
    • Yan, W.1    Schilke, B.2    Pfund, C.3    Walter, W.4    Kim, S.W.5    Craig, E.A.6
  • 58
    • 0019064554 scopus 로고
    • Isolation of polymerization-competent cytoplasmic actin by affinity chromatography on immobilized Dnase I using formamide as eluant
    • Zechel, K. (1980) Isolation of polymerization-competent cytoplasmic actin by affinity chromatography on immobilized Dnase I using formamide as eluant. Eur. J. Biochem., 110, 343-348.
    • (1980) Eur. J. Biochem. , vol.110 , pp. 343-348
    • Zechel, K.1
  • 59
    • 0027256768 scopus 로고
    • The yeast sis1-protein, a dnaj homolog. Is required for the initiation of translation
    • Zhong, T. and Arndt, K. (1993) The yeast Sis1-protein, a DnaJ homolog. is required for the initiation of translation. Cell, 73, 1175-1186.
    • (1993) Cell , vol.73 , pp. 1175-1186
    • Zhong, T.1    Arndt, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.