REFERENCES
- Agashe V. R., Guha S., Chang H. C., Genevaux P., Hayer-Hartl M., Stemp M., Georgopoulos C., Hartl F. U., Barral J. M.. 2004. Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed. Cell. 117(2)199, [PUBMED], [INFOTRIEVE]
- Anfinsen C. B.. 1973. Principles that govern the folding of protein chains. Science. 181: 223, [PUBMED], [INFOTRIEVE]
- Ban N., Nissen P., Hansen J., Capel M., Moore P. B., Steitz T. A.. 1999. Placement of protein and RNA structures into a 5 Å-resolution map of the 50S ribosomal subunit. Nature. 400: 841, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Ban N., Nissen P., Hansen J., Moore P. B., Steitz T. A.. 2000. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science. 289: 905, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Beatrix B., Sakai H., Wiedmann M.. 2000. The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functions. J Biol Chem. 275(48)37838, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Behrens S., Maier R., de, Cock H., Schmid F. X., Gross C. A.. 2001. The SurA periplasmic PPlase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 20(1)285, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Buchberger A., Schröder H., Hesterkamp T., Schönfeld H.-J., Bukau B.. 1996. Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J Mol Biol. 261: 328, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Buchner J.. 1996. Supervising the fold: functional principles of molecular chaperones. FASEB J. 10: 10, [PUBMED], [INFOTRIEVE], [CSA]
- Bukau B., Deuerling E., Pfund C., Craig E. A.. 2000. Getting newly synthesized proteins into shape. Cell. 101: 119, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Bukau B., Horwich A. L.. 1998. The Hsp70 and Hsp60 chaperone machines. Cell. 92: 351, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Bukau B., Walker G. C.. 1989. Cellular Defects caused by deletion of the Escherichia coli dnaK gene indicates roles for heat shock protein in normal metabolism. J Bact. 171(5)2337, [PUBMED], [INFOTRIEVE]
- Chaudhuri T. K., Farr G. W., Fenton W. A., Rospert S., Horwich A. L.. 2001. GroEL/GroES-mediated folding of a protein too large to be encapsulated. Cell. 107(2)235, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Chen J., Walter S., Horwich A. L., Smith D. L.. 2001. Folding of malate dehydrogenase inside the GroEL-GroES cavity. Nat Struct Biol. 8(8)721, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Cheng M. Y., Hartl F. U., Martin J., Pollock R. A., Kalousek F., Neupert W., Hallberg E. M., Hallberg R. L., Horwich A. L.. 1989. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature. 337(6208)620, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Coyle J. E., Texter F. L., Ashcroft A. E., Masselos D., Robinson C. V., Radford S. E.. 1999. GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism. Nature Struct Biol. 6: 683, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Craig E., Yan W., James P.. 1999. Genetic dissection of the Hsp70 chaperone system of yeast. Molecular Chaperones and Folding Catalysts. Regulation, Cellular Function and Mechanisms, Bukau B. Ed., Amsterdam, Harwood Academic Publishers. 139
- Deng J. M., Behringer R. R.. 1995. An insertional mutation in the BTF3 transcription factor gene leads to an early postimplantation lethality in mice. Transgenic Res. 4(4)264, [PUBMED], [INFOTRIEVE], [CSA]
- Deuerling E., Patzelt H., Vorderwülbecke S., Rauch T., Kramer G., Schaffitzel E., Mogk A., Schulze-Specking A., Langen H., Bukau B.. 2003. Trigger Factor and DnaK possess overlapping substrate pools and binding specificities. Mol Microbiol. 47(5)1317, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Deuerling E., Schulze-Specking A., Tomoyasu T., Mogk A., Bukau B.. 1999. Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature. 400: 693, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Dill K. A., Chan H. S.. 1997. From Levinthal to pathways to funnels. Nature Struct Biol. 4: 10, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Dinner A. R., Sali A., Smith L. J., Dobson C. M., Karplus M.. 2000. Understanding protein folding via free-energy surfaces from theory and experiment. Trends Biochem Sci. 25(7)331, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Driessen A. J., Manting E. H., van der, Does C.. 2001. The structural basis of protein targeting and translocation in bacteria. Nat Struct Biol. 8(6)492, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Ellis J.. 1987. Proteins as molecular chaperones. Nature (London). 328: 378, [CROSSREF]
- Ellis R. J., Hartl F. U.. 1999. Principles of protein folding in the cellular environment. Curr Opin Struct Biol. 9: 102, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Elowitz M. B., Surette M. G., Wolf P.-E., Stock J. B., Leibler S.. 1999. Protein mobility in the cytoplasm of Escherichia coli. J Bacteriol. 181: 197, [PUBMED], [INFOTRIEVE]
- Ewalt K. L., Hendrick J. P., Houry W. A., Hartl F. U.. 1997. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 90: 491, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Farr G. W., Fenton W. A., Chaudhuri T. K., Clare D. K., Saibil H. R., Horwich A. L.. 2003. Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes. Embo J. 22(13)3220, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Fayet O., Ziegelhoffer T., Georgopoulos C.. 1989. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J Bacteriol. 171(3)1379, [PUBMED], [INFOTRIEVE]
- Fedorov A. N., Baldwin T. O.. 1997. Cotranslational protein folding. J Biol Chem. 272: 32175, [CROSSREF]
- Fenton W. A.a.H., Arthur L.. 1997. GroEL-mediated protein folding. Protein Sci. 6: 743, [PUBMED], [INFOTRIEVE], [CSA]
- Ferbitz L., Maier T., Patzelt H., Bukau B., Deuerling E., Ban N.. 2004. Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature. 431: 590, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Fersht A. R., Daggett V.. 2002. Protein folding and unfolding at atomic resolution. Cell. 108(4)573, [PUBMED], [INFOTRIEVE], [CROSSREF]
- 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, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Friguet B., Djavadi-Ohaniance L., King J., Goldberg M. E.. 1994. In vitro and ribosome-bound folding intermediates of P22 tailspike protein detected with monoclonal antibodies. J Biol Chem. 269(22)15945, [PUBMED], [INFOTRIEVE]
- Frydman J.. 2001. Folding of newly translated proteins in vivo: The role of molecular chaperones. Annu Rev Biochem. 70: 603, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Frydman J., Nimmesgern E., Erdjument-Bromage H., Wall J. S., Tempst P., 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, [PUBMED], [INFOTRIEVE], [CSA]
- Frydman J., Nimmesgern E., Ohtsuka K., Hartl F. U.. 1994. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature. 370: 111, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Fünfschilling U., Rospert S.. 1999. Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria. Mol Biol Cell. 10: 3289, [CSA]
- Gao Y., Thomas J. O., Chow R. L., Lee G.-H., Cowan N. J.. 1992. A cytoplasmic chaperonin that catalyzes β-actin folding. Cell. 69: 1043, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Gautschi M., Lilie H., Fünfschilling U., Mun A., Ross S., Lithgow T., Rucknagel P., Rospert S.. 2001. RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin. Proc Natl Acad Sci USA. 98: 3762, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Gautschi M., Mun A., Ross S., Rospert S.. 2002. A functional chaperone triad on the yeast ribosome. Proc Natl Acad Sci USA. 99(7)4209, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Genevaux P., Keppel F., Schwager F., Langendijk-Genevaux P. S., Hartl F. U., Georgopoulos C.. 2004. In vivo analysis of the overlapping functions of DnaK and trigger factor. EMBO Rep. 5(2)195, [PUBMED], [INFOTRIEVE], [CROSSREF]
- George R., Beddoe T., Landl K., Lithgow T.. 1998. The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo. Proc Natl Acad Sci USA. 95: 2296, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Gething M. J.. 1999. Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol. 10(5)465, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Gilbert R. J., Fucini P., Connell S., Fuller S. D., Nierhaus K. H., Robinson C. V., Dobson C. M., Stuart D. I.. 2004. Three-dimensional structures of translating ribosomes by Cryo-EM. Mol Cell. 14(1)57, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Göthel S. F., Scholz C., Schmid F. X., Marahiel M. A.. 1998. Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions. Biochemistry. 37: 13392, [CROSSREF]
- Hardesty B., Kramer G.. 2001. Folding of a nascent peptide on the ribosome. Prog Nucleic Acid Res Mol Biol. 66: 41, [PUBMED], [INFOTRIEVE], [CSA]
- Hartl F. U., Hayer-Hartl M.. 2002. Molecular chaperones in the cytosol: From nascent chain to folded protein. Science. 295(5561)1852, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Hartl F. U., Lecker S., Schiebel E., Hendrick J. P., Wickner W.. 1990. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell. 63: 269, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Hennecke J., Sebbel P., Glockshuber R.. 1999. Random Circular Permutation of DsbA Reveals Segments that are Essential for Protein Folding and Stability. J Mol Biol. 286: 1197, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Hesterkamp T., Deuerling E., Bukau B.. 1997. The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes. J Biol Chem. 272: 21865, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Hesterkamp T., Hauser S., Lütcke H., Bukau B.. 1996. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc Natl Acad Sci USA. 93: 4437, [PUBMED], [INFOTRIEVE], [CSA]
- Horwich A. L., Brooks Low K., Fenton W. A., Hirshfield I. N., Furtak K.. 1993. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell. 74: 909, [PUBMED], [INFOTRIEVE]
- Horwich A. L., Weber-Ban E. U., Finley D.. 1999. Chaperone rings in protein folding and degradation. Proc Natl Acad Sci USA, 1. 96: 11033, [CROSSREF]
- Houry W. A., Frishman D., Eckerskorn C., Lottspeich F., Hartl F. U.. 1999. Identification of in vivo substrates of the chaperonin GroEL. Nature. 402: 147, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Hundley H., Eisenman H., Walter W., Evans T., Hotokezaka Y., Wiedmann M., Craig E.. 2002. The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain. Proc Natl Acad Sci USA. 99(7)4203, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Ito K.. 1996. The major pathways of protein translocation across membranes. Genes Cells. 1: 337, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Jacob M., Schindler T., Balbach J., Schmid F. X.. 1997. Diffusion control in an elementary protein folding reaction. Proc Natl Acad Sci USA. 94: 5622, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Kandror O., Busconi L., Sherman M., Goldberg A. L.. 1994. Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES. J Biol Chem. 269: 23575, [PUBMED], [INFOTRIEVE]
- Kramer G., Rauch T., Rist W., Vorderwülbecke S., Patzelt H., Schulze-Specking A., Ban N., Deuerling E., Bukau B.. 2002. L23 protein functions as a chaperone docking site on the ribosome. Nature. 419: 171, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Kramer G., Rutkowska A., Wegrzyn R. D., Patzelt H., Kurz T. A., Merz F., Rauch T., Vorderwülbecke S., Deuerling E., Bukau B.. 2004. Functional dissection of Escherichia coli Trigger Factor: Unraveling the function of individual domains. J Bacteriol. 186(12)3777, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Kusukawa N., Yura T., Ueguchi C., Akiyama Y., Ito K.. 1989. Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli. EMBO J. 8(11)3517, [PUBMED], [INFOTRIEVE], [CSA]
- Laminet A. A., Ziegelhoffer T., Georgopoulos C., Pluckthun A.. 1990. The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor. EMBO J. 9(7)2315, [PUBMED], [INFOTRIEVE], [CSA]
- Laufen T., Mayer M. P., Beisel C., Klostermeier D., Reinstein J., Bukau B.. 1999. Mechanism of regulation of Hsp70 chaperones by DnaJ co-chaperones. Proc Natl Acad Sci USA. 96: 5452, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Lauring B., Wang S., Sakai H., Davis T. A., Wiedmann B., Kreibich G., Wiedmann M.. 1995. Nascent-polypeptide-associated complex: A bridge between ribosome and cytosol. Cold Spring Harb Symp Quant Biol. 60: 47, [PUBMED], [INFOTRIEVE], [CSA]
- Lewis V. A., Hynes G. M., Zheng D., Saibil H., Willison K.. 1992. T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol. Nature. 358: 249, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Liberek K., Marszalek J., Ang D., Georgopoulos C., Zylicz M.. 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci USA. 88: 2874, [PUBMED], [INFOTRIEVE], [CSA]
- Lill R., Crooke E., Guthrie B., Wickner W.. 1988. The “Trigger factor cycle” includes ribosomes, presecretory proteins and the plasma membrane. Cell. 54: 1013, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Maier R., Eckert B., Scholz C., Lilie H., Schmid F. X.. 2003. Interaction of trigger factor with the ribosome. J Mol Biol. 326(2)585, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Markesich D. C., Gajewski K. M., Nazimiec M. E., Beckingham K.. 2000. Bicaudal encodes the Drosophila beta NAC homolog, a component of the ribosomal translational machinery. Development. 127(3)559, [PUBMED], [INFOTRIEVE]
- Mayer M. P., Brehmer D., Gassler C. S., Bukau B.. 2001. Hsp70 chaperone machines. Adv Protein Chem. 59: 1, [PUBMED], [INFOTRIEVE], [CSA]
- Mayer M. P., Rüdiger S., Bukau B.. 2000. Molecular basis for interactions of the DnaK chaperone with substrates. Biol Chem. 381: 877, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- McCarty J. S., Buchberger A., Reinstein J., Bukau B.. 1995. The role of ATP in the functional cycle of the DnaK chaperone system. J Mol Biol. 249: 126, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Minton A. P.. 2000. Protein folding: thickening the broth. Curr Biol. 10: R97, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Minton K. W., Karmin P., Hahn G. M., Minton A. P.. 1982. Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins. Proc Natl Acad Sci USA. 79: 7107, [PUBMED], [INFOTRIEVE]
- Misselwitz B., Staeck O., Rapoport T. A.. 1998. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol Cell. 2: 593, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Mogk A., Mayer M. P., Deuerling E.. 2002. Mechanisms of Protein Folding: molecular chaperones and their application in biotechnology. ChemBioChem. 3: 807, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Molinari M., Helenius A.. 2000. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science. 288: 331, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Möller I., Beatrix B., Kreibich G., Sakai H., Lauring B., Wiedmann M.. 1998. Unregulated exposure of the ribosomal M-site caused by NAC depletion results in delivery of non-secretory polypeptides to the Sec61 complex. FEBS Letters. 441: 1, [CSA], [CROSSREF]
- Nakatogawa H., Ito K.. 2002. The ribosomal exit tunnel functions as a discriminating gate. Cell. 108(5)629, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Netzer W. J., Hartl F. U.. 1997. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature. 388: 343, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Neupert W.. 1997. Protein import into mitochondria. Annu Rev Biochem. 66: 863, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Neupert W., Brunner M.. 2002. The protein import motor of mitochondria. Nat Rev Mol Cell Biol. 3(8)555, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Nicola A. V., Chen W., Helenius A.. 1999. Co-translational folding of an alphavirus capsid protein in the cytosol of living cells. Nature Cell Biol. 1: 341, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Nissen P., Hansen J., Ban N., Moore P. B., Steitz T. A.. 2000. The structural basis of ribosome activity in peptide bond synthesis. Science. 289: 920, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Ostermann J., Horwich A. L., Neupert W., Hartl F. U.. 1989. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature. 341(6238)125, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Packschies L., Theyssen H., Buchberger A., Bukau B., Goody R. S., Reinstein J.. 1997. GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry. 36(12)3417, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Patzelt H., Kramer G., Rauch T., Schönfeld H. J., Bukau B., Deuerling E.. 2002. Three-sate equilibrium of Escherichi coli trigger Factor. Biol Chem. 383: 1611, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Patzelt H., Rudiger S., Brehmer D., Kramer G., Vorderwulbecke S., Schaffitzel E., Waitz A., Hesterkamp T., Dong L., Schneider-Mergener J., Bukau B., Deuerling E.. 2001. Binding specificity of Escherichia coli trigger factor. Proc Natl Acad Sci USA. 98(25)14244, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Pfanner N., Geissler A.. 2001. Versatility of the mitochondrial protein import machinery. Nat Rev Mol Cell Biol. 2(5)339, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Pfanner N., Wiedemann N.. 2002. Mitochondrial protein import: two membranes, three translocases. Curr Opin Cell Biol. 14(4)400, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Pfund C., Lopez-Hoyo N., Ziegelhoffer T., Schilke B. A., Lopez-Buesa P., Walter W. A., Wiedmann M., Craig E. A.. 1998. The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex. EMBO J. 17: 3981, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Pierpaoli E. V., Sandmeier E., Baici A., Schönfeld H.-J., Gisler S., Christen P.. 1997. The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system. J Mol Biol. 269: 757, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Radford S. E.. 2003. Co-translocational misfolding in the ER of living cells. Nat Struct Biol. 10(3)153, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Reimann B., Bradsher J., Franke J., Hartmann E., Wiedmann M., Prehn S., Wiedmann B.. 1999. Initial characterization of the nascent polypeptide-associated complex in yeast. Yeast. 15(5)397, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Roseman A. M., Chen S., White H., Braig K., Saibil H. R.. 1996. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell. 87: 241, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Rospert S., Dubaquie Y., Gautschi M.. 2002. Nascent-polypeptide-associated complex. Cell Mol Life Sci. 59(10)1632, [PUBMED], [INFOTRIEVE], [CSA]
- Rüdiger S., Buchberger A., Bukau B.. 1997. Interaction of Hsp70 chaperones with substrates. Nat Struct Biol. 4: 342, [CSA], [CROSSREF]
- Rüdiger S., Germeroth L., Schneider-Mergener J., Bukau B.. 1997. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16: 1501, [CSA], [CROSSREF]
- Rye H. S., Burston S. G., Fenton W. A., Beechem J. M., Xu Z., Sigler P. B., Horwich A. L.. 1997. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature. 388(6644)792, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Saibil H. R.. 2000. Conformational changes studied by cryo-electron microscopy. Nature Struct Biol. 7: 711, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Saibil H. R., Horwich A. L., Fenton W. A.. 2001. Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding. Adv Protein Chem. 59: 45, [PUBMED], [INFOTRIEVE], [CSA]
- Sanchez I. E., Morillas M., Zobeley E., Kiefhaber T., Glockshuber R.. 2004. Fast folding of the two-domain semliki forest virus capsid protein explains co-translational proteolytic activity. J Mol Biol. 338(1)159, [PUBMED], [INFOTRIEVE]
- Schaffitzel E., Rüdiger S., Bukau B., Deuerling E.. 2001. Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteins. Biological Chemistry. 382: 1235, [PUBMED], [INFOTRIEVE], [CSA]
- Schatz G., Dobberstein B.. 1996. Common principles of protein translocation across membranes. Science. 271: 1519, [PUBMED], [INFOTRIEVE]
- Schluenzen F., Tocilj A., Zarivach R., Harms J., Gluehmann M., Janell D., Bashan A., Bartels H., Agmon I., Franceschi F., Yonath A.. 2000. Structure of functionally activated small ribosomal subunit at 3.3 angstroms resolution. Cell. 102(5)615, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Schmid D., Baici A., Gehring H., Christen P.. 1994. Kinetics of molecular chaperone action. Science. 263: 971, [PUBMED], [INFOTRIEVE]
- Shi Y., Mosser D. D., Morimoto R. I.. 1998. Molecular chaperones as HSF-specific transcriptional repressors. Genes & Development. 12: 654, [CSA]
- Shtilerman M., Lorimer G. H., Englander S. W.. 1999. Chaperonin function: Folding by forced unfolding. Science. 284: 822, [PUBMED], [INFOTRIEVE], [CROSSREF]
- 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(5)1197, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Stoller G., Ruecknagel K. P., Nierhaus K. H., Schmid F. X., Fischer G., Rahfeld J.-U.. 1995. A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J. 14: 4939, [PUBMED], [INFOTRIEVE], [CSA]
- Teter S. A., Houry W. A., Ang D., Tradler T., Rockabrand D., Fischer G., Blum P., Georgopoulos C., Hartl F. U.. 1999. Polypeptide flux through bacterial Hsp70: DnaK cooperates with Trigger Factor in chaperoning nascent chains. Cell. 97: 755, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Ullers R. S., Luirink J., Harms N., Schwager F., Georgopoulos C., Genevaux P.. 2004. SecB is a bona fide generalized chaperone in Escherichia coli. Proc Natl Acad Sci USA. 101(20)7583, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Valent Q. A., de, Gier J.-W.L., von, Heijne G., Kendall D. A., ten, Hagen-Jongman C. M., Oudega B., Luirink J.. 1997. Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor. Molecular Microbiology. 25(1)53, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Valent Q. A., Kendall D. A., High S., Kusters R., Oudega B., Luirink J.. 1995. Early events in preprotein recognition in E. coli: Interaction of SRP and trigger factor with nascent polypeptides. EMBO J. 14: 5494, [PUBMED], [INFOTRIEVE], [CSA]
- van den, Berg B., Ellis R. J., Dobson C. M.. 1999. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18: 6927, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Viitanen P. V., Lubben T. H., Reed J., Goloubinoff P., O'Keefe D. P., Lorimer G. H.. 1990. Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+dependent. Biochemistry. 29(24)5665, [PUBMED], [INFOTRIEVE]
- Vorderwulbecke S., Kramer G., Merz F., Kurz T. A., Rauch T., Zachmann-Brand B., Bukau B., Deuerling E.. 2004. Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK. FEBS Lett. 559(1–3)181, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Walter P., Johnson A. E.. 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu Rev Cell Biol. 10: 87, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Wang S., Sakai H., Wiedmann M.. 1995. NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center. J Cell Biol. 130: 519, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Welch W. J., Eggers D. K., Hansen W. J., Nagata H.. 1999. Early events in the synthesis and maturation of polypeptides. Molecular Chaperones and Folding Catalysts. Regulation, Cellular Function and Mechanism, Bukau B., Amsterdam, Harwood Academic Publishers. 177
- Wiedmann B., Prehn S.. 1999. The nascent polypeptide-associated complex (NAC) of yeast functions in the targeting process of ribosomes to the ER membrane. FEBS Letters. 458: 51, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Wiedmann B., Sakai H., Davis T. A., Wiedmann M.. 1994. A protein complex required for signal-sequence-specific sorting and translocation. Nature. 370: 434, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Wiedmann B., Sakai H., Davis T. A., Wiedmann M.. 1994. A protein complex required for signal-sequence-specific sorting and translocation. Nature. 370(6489)434, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Wimberly B. T., Brodersen D. E., Clemons, Jr., W. M., Morgan-Warren R. J., Carter A. P., Vonrhein C., Hartsch T., Ramakrishnan V.. 2000. Structure of the 30S ribosomal subunit. Nature. 407: 327, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Xu Z., Horwich A. L., Sigler P. B.. 1997. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature. 388: 741, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Xu Z., Sigler P. B.. 1998. GorEL/GroES: structure and function of a two-stroke folding machine. J Struct Biol. 124: 129, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Yan W., Schilke B., Pfund C., Walter W., Kim S., Craig E. A.. 1998. Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO J. 17: 4809, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Zhu X., Zhao X., Burkholder W. F., Gragerov A., Ogata C. M., Gottesman M., Hendrickson W. A.. 1996. Structural analysis of substrate binding by the molecular chaperone DnaK. Science. 272: 1606, [PUBMED], [INFOTRIEVE]
- Zimmerman S. B., Minton A. P.. 1993. Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu Rev Biophys Biomol Struct. 22: 27, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Zimmerman S. B., Trach S. O.. 1991. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J Mol Biol. 222: 599, [PUBMED], [INFOTRIEVE]