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Abstract AI-Helper 아이콘AI-Helper

For most of proteins to be active, they need well-defined three-dimensional structures alone or in complex. Folding is a process through which newly synthesized proteins get to the native state. Protein folding inside cells is assisted by various chaperones and folding factors, and misfolded protein...

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참고문헌 (52)

  1. Baram, D. and Yonath, A. (2005) From peptide-bond formation to cotranslational folding: dynamic, regulatory and evolutionary aspects. FEBS Lett. 579, 948-954 

  2. Barouch, W., Prasad, K., Greene, L. and Eisenberg, E. (1997) Auxilin-induced interaction of the molecular chaperone Hsc70 with clathrin baskets. Biochemistry 36, 4303-4308 

  3. Barral, J. M., Broadley, S. A., Schaffar, G. and Hartl, F. U. (2004) Roles of molecular chaperones in protein misfolding diseases. Semin. Cell Dev. Biol. 15, 17-29 

  4. Bossy-Wetzel, E., Schwarzenbacher, R. and Lipton, S. A. (2004) Molecular pathways to neurodegeneration. Nat. Med. 10 (suppl), S2-S9 

  5. Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., Horwich, A. L. and Sigler, P. B. (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature 371, 578-586 

  6. Bu, G. and Schwartz, A. L. (1998) RAP, a novel type of ER chaperone. Trends Cell Biol. 8, 272-276 

  7. Bukau, B. and Horwich, A. L. (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366 

  8. Caughey, B. and Lansbury, P. T. (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298 

  9. Chiti, F., Stefani, M., Taddei, N., Ramponi, G. and Dobson, C. M. (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424, 805-808 

  10. Dill, K. A. and Chan, H. S. (1997) From Levinthal to pathways to funnels. Nat. Struct. Biol. 4, 10-19 

  11. Dobson, C. M. (2003) Protein folding and misfolding. Nature 426, 884-890 

  12. Dobson, C. M. (2004) Principles of protein folding, misfolding and aggregation. Semin. Cell Dev. Biol. 15, 3-16 

  13. Ellgaard, L. and Frickel, E. M. (2003) Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell Biochem. Biophys. 39, 223-247 

  14. Ellis, R. J. (2001a) Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr. Opin. Struct. Biol. 11, 114-119 

  15. Ellis, R. J. (2001b) Molecular chaperones: inside and outside the Anfinsen cage. Curr. Biol. 11, R1038-1040 

  16. Fersht, A. R. (1999) Folding pathways and energy landscapes; in Structure and mechanism in protein science: A guide to enzyme catalysis and protein folding, Julet, M. R. and Hadler, G. L. (eds.), pp. 573-614, W H Freeman and Co., New York, USA 

  17. Fersht, A. R. and Daggett, V. (2002) Protein folding and unfolding at atomic resolution. Cell 108, 573-582 

  18. Flaherty, K. M., McKay, D. B., Kabsch, W. and Holmes, K. C. (1991) Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc. Natl. Acad. Sci. USA 88, 5041-5045 

  19. Freedman, R. B., Bulleid, N. J., Hawkins, H. C. and Paver, J. L. (1989) Role of protein disulphide-isomerase in the expression of native proteins. Biochem. Soc. Symp. 55, 167-192 

  20. Frydman, J. and Hartl, F. U. (1996) Principles of chaperoneassisted protein folding: differences between in vitro and in vivo mechanisms. Science 272, 1497-1502 

  21. Grantcharova, V., Alm, E. J., Baker, D. and Horwich, A. L. (2001) Mechanisms of protein folding. Curr. Opin. Struct. Biol. 11, 70-82 

  22. Hardesty, B. and Kramer, G. (2001) Folding of a nascent peptide on the ribosome. Prog. Nucleic Acid Res. Mol. Biol. 66, 41-66 

  23. Hartl, F. U. and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858 

  24. Jimenez, J. L., Guijarro, J. I., Orlova, E., Zurdo, J., Dobson, C. M., Sunde, M. and Saibil, H. R. (1999) Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18, 815-821 

  25. Kagan, B. L., Azimov, R. and Azimova, R. (2004) Amyloid peptide channels. J. Membr. Biol. 202, 1-10 

  26. Karzai, A. W. and McMacken, R. (1996) A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J. Biol. Chem. 271, 11236- 11246 

  27. Laufen, T., Mayer, M. P., Beisel, C., Klostermeier, D., Mogk, A., Reinstein, J. and Bukau, B. (1999) Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones. Proc. Natl. Acad. Sci. USA 96, 5452-5457 

  28. Lee, C., Schwartz, M. P., Prakash, S., Iwakura, M. and Matouschek, A. (2001) ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7, 627-637 

  29. Lomas, D. A. and Carrell, R. W. (2002) Serpinopathies and the conformational dementias. Nat. Rev. Genet. 3, 759-768 

  30. Lomas, D. A., Evans, D. L., Finch, J. T. and Carrell, R. W. (1992) The mechanism of Z a1-antitrypsin accumulation in the liver. Nature 357, 605-607 

  31. Matouschek, A. (2003) Protein unfolding--an important process in vivo? Curr. Opin. Struct. Biol. 13, 98-109 

  32. Mayer, M. P. and Bukau, B. (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62, 670-684 

  33. McParland, V. J., Kalverda, A. P., Homans, S. W. and Radford, S. E. (2002) Structural properties of an amyloid precursor of $\beta_{2}$ - microglobulin. Nat. Struct. Biol. 9, 326-331 

  34. Meunier, L., Usherwood, Y. K., Chung, K. T. and Hendershot, L. M. (2002) A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol. Biol. Cell 13, 4456-4469 

  35. Munro, S. and Pelham, H. R. (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 

  36. Nagata, K. (1996) Hsp47: a collagen-specific molecular chaperone. Trends Biochem. Sci. 21, 22-26 

  37. Petkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F. and Tycko, R. (2002) A structural model for Alzheimer's $\beta$ -amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl. Acad. Sci. USA 99, 16742-16747 

  38. Pilon, M., Schekman, R. and Romisch, K. (1997) Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J. 16, 4540-4548 

  39. Plemper, R. K. and Wolf, D. H. (1999) Retrograde protein translocation: ERADication of secretory proteins in health and disease. Trends Biochem. Sci. 24, 266-270 

  40. Prusiner, S. B., Scott, M. R., DeArmond, S. J. and Cohen, F. E. (1998) Prion protein biology. Cell 93, 337-348 

  41. Rudiger, S., Germeroth, L., Schneider-Mergener, J. and Bukau, B. (1997) Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16, 1501-1507 

  42. Sakahira, H., Breuer, P., Hayer-Hartl, M. K. and Hartl, F. U. (2002) Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc. Natl. Acad. Sci. USA 99, 16412-16418 

  43. Selkoe, D. J. (2003) Folding proteins in fatal ways. Nature 426, 900-904 

  44. Siegers, K., Bolter, B., Schwarz, J. P., Bottcher, U. M., Guha, S. and Hartl, F. U. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J. 22, 5230-5240 

  45. Sitia, R. and Braakman, I. (2003) Quality control in the endoplasmic reticulum protein factory. Nature 426, 891-894 

  46. Staniforth, R. A., Giannini, S., Higgins, L. D., Conroy, M. J., Hounslow, A. M., Jerala, R., Craven, C. J. and Waltho, J. P. (2001) Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J. 20, 4774-4781 

  47. Stefani, M. (2004) Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta 1739, 5-25 

  48. Sunde, M. and Blake, C. (1997) The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50, 123-159 

  49. Thulasiraman, V., Yang, C. F. and Frydman, J. (1999) In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO J. 18, 85-95 

  50. Welch, W. J. (2004) Role of quality control pathways in human diseases involving protein misfolding. Semin. Cell Dev. Biol. 15, 31-38 

  51. Yu, M. H., Lee, K. N. and Kim, J. (1995) The Z type variation of human a1-antitrypsin causes a protein folding defect. Nat. Struct. Biol. 2, 363-367 

  52. Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E. and Hendrickson, W. A. (1996) Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272, 1606-1614 

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