Role of molecular chaperones in inclusion body formation
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[1] J. Corchero,et al. The position of the heterologous domain can influence the solubility and proteolysis of beta-galactosidase fusion proteins in E. coli. , 1996, Journal of biotechnology.
[2] C. Georgopoulos,et al. Sequence analysis and phenotypic characterization of groEL mutations that block lambda and T4 bacteriophage growth , 1993, Journal of bacteriology.
[3] U. Rinas,et al. Engineering Regulable Escherichia coliβ-Galactosidases as Biosensors for Anti-HIV Antibody Detection in Human Sera* , 2001, The Journal of Biological Chemistry.
[4] A. Goldberg,et al. Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli. , 1992, The EMBO journal.
[5] A. Villaverde,et al. Construction and deconstruction of bacterial inclusion bodies. , 2002, Journal of biotechnology.
[6] Walid A Houry,et al. In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System , 1997, Cell.
[7] Susan Lindquist,et al. Protein disaggregation mediated by heat-shock protein Hspl04 , 1994, Nature.
[8] F. Baneyx,et al. Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli β‐galactosidase , 1996, Protein science : a publication of the Protein Society.
[9] B. Bukau,et al. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol , 2001, Molecular microbiology.
[10] A. Villaverde,et al. Protein aggregation as bacterial inclusion bodies is reversible , 2001, FEBS letters.
[11] R. Kopito,et al. Aggresomes: A Cellular Response to Misfolded Proteins , 1998, The Journal of cell biology.
[12] F. Marston. The purification of eukaryotic polypeptides synthesized in Escherichia coli. , 1986, The Biochemical journal.
[13] C. Dobson,et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases , 2002, Nature.
[14] P. Goloubinoff,et al. Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones. , 2001, Journal of structural biology.
[15] J. Tkach,et al. Crowbars and ratchets: hsp100 chaperones as tools in reversing protein aggregation. , 2001, Biochemistry and cell biology = Biochimie et biologie cellulaire.
[16] J. Corchero,et al. Distinct chaperone affinity to folding variants of homologous recombinant proteins , 1999, Biotechnology Letters.
[17] M. Gaestel,et al. Binding of non‐native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation , 1997, The EMBO journal.
[18] D Baker,et al. Mechanisms of protein folding. , 2001, Current opinion in structural biology.
[19] A. Villaverde,et al. Fine architecture of bacterial inclusion bodies , 2000, FEBS letters.
[20] F. Hartl,et al. Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms. , 1998, Trends in biochemical sciences.
[21] T. Tsuchido,et al. Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants. , 2002, European journal of biochemistry.
[22] B. Bukau,et al. Size-dependent Disaggregation of Stable Protein Aggregates by the DnaK Chaperone Machinery* , 2000, The Journal of Biological Chemistry.
[23] S. Lindquist,et al. Chaperone-supervised conversion of prion protein to its protease-resistant form. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[24] A. Goldberg,et al. The Molecular Chaperone DnaJ Is Required for the Degradation of a Soluble Abnormal Protein in Escherichia coli * , 2001, The Journal of Biological Chemistry.
[25] A. Fink. Protein aggregation: folding aggregates, inclusion bodies and amyloid. , 1998, Folding & design.
[26] G. Farr,et al. GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated , 2001, Cell.
[27] Eliora Z Ron,et al. Protein aggregation in Escherichia coli: role of proteases. , 2002, FEMS microbiology letters.
[28] F. Hartl,et al. Chaperonin-mediated de novo generation of prion protein aggregates. , 2001, Journal of molecular biology.
[29] J. Corchero,et al. Dynamics of in vivo protein aggregation: building inclusion bodies in recombinant bacteria. , 1998, FEMS microbiology letters.
[30] S. Gottesman,et al. Role of the Heat Shock Protein DnaJ in the Lon-dependent Degradation of Naturally Unstable Proteins* , 1996, The Journal of Biological Chemistry.
[31] B. Bukau,et al. Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology. , 2002, Journal of biotechnology.
[32] E. Craig,et al. Getting Newly Synthesized Proteins into Shape , 2000, Cell.
[33] F. Baneyx,et al. Roles of the Escherichia coli Small Heat Shock Proteins IbpA and IbpB in Thermal Stress Management: Comparison with ClpA, ClpB, and HtpG In Vivo , 1998, Journal of bacteriology.
[34] A. Fink,et al. Nativelike secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR. , 1994, Biochemistry.
[35] T. Wileman,et al. Aggresomes Resemble Sites Specialized for Virus Assembly , 2001, The Journal of cell biology.
[36] A. Zvi,et al. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[37] P. Lund,et al. The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock. , 2002, Microbiology.
[38] J. Buchner,et al. The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network* , 1998, The Journal of Biological Chemistry.
[39] J. Corchero,et al. Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble forms. , 1999, Biochimica et biophysica acta.
[40] P. Blum,et al. DnaK-Mediated Alterations in Human Growth Hormone Protein Inclusion Bodies , 1992, Bio/Technology.
[41] M. Zółkiewski,et al. ClpB Cooperates with DnaK, DnaJ, and GrpE in Suppressing Protein Aggregation , 1999, The Journal of Biological Chemistry.
[42] S. Rüdiger,et al. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB , 1999, The EMBO journal.
[43] George Georgiou,et al. Structure and Morphology of Protein Inclusion Bodies in Escherichia Coli , 1991, Bio/Technology.