REFERENCES
- Alberti S., Esser C., Hohfeld J.. 2003. BAG-1–a nucleotide exchange factor of Hsc70 with multiple cellular functions. Cell Stress Chaperones. 8: 225–231. [PUBMED], [INFOTRIEVE], [CSA]
- Apel K. and Hirt H.. 2004. Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu Rev Plant Physiol Plant Mol Biol. 55: 373–399
- Aslund F., Zheng M., Beckwith J., Storz G.. 1999. Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc Natl Acad Sci USA. 96: 6161–6165. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Azevedo D., Tacnet F., Delaunay A., Rodrigues-Pousada C., Toledano M. B.. 2003. Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling. Free Radic Biol Med. 35: 889–900. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Barbirz S., Jakob U., Glocker M. O.. 2000. Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone. J Biol Chem. 275: 18759–18766. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Bentley N. J., Fitch I. T., Tuite M. F.. 1992. The small heat-shock protein Hsp26 of Saccharomyces cerevisiae assembles into a high molecular weight aggregate. Yeast. 8: 95–106. [PUBMED], [INFOTRIEVE], [CSA]
- Berlett B. S. and Stadtman E. R.. 1997. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem. 272: 20313–20316. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Bottomley M. J., Batten M. R., Lumb R. A., Bulleid N. J.. 2001. Quality control in the endoplasmic reticulum: PDI mediates the ER retention of unassembled procollagen C-propeptides. Curr Biol. 11: 1114–1118. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Brodsky J. L., McCracken A. A.. 1999. ER protein quality control and proteasome-mediated protein degradation. Semin Cell Dev Biol. 10: 507–513. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Buchner J., Schmidt M., Fuchs M., Jaenicke R., Rudolph R., Schmid F. X., Kiefhaber T.. 1991. GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry. 30: 1586–1591. [PUBMED], [INFOTRIEVE]
- Bukau B. and Horwich A. L.. 1998. The Hsp70 and Hsp60 chaperone machines. Cell. 92: 351–366. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Cabiscol E., Tamarit J., Ros J.. 2000. Oxidative stress in bacteria and protein damage by reactive oxygen species. Int Microbiol. 3: 3–8. [PUBMED], [INFOTRIEVE], [CSA]
- Calabrese V., Scapagnini G., Colombrita C., Ravagna A., Pennisi G., Giuffrida Stella A. M., Galli F., Butterfield D. A.. 2003. Redox regulation of heat shock protein expression in aging and neurodegenerative disorders associated with oxidative stress: a nutritional approach. Amino Acids. 25: 437–444. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Chessler S. D., Byers P. H.. 1993. BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta. J Biol Chem. 268: 18226–18233. [PUBMED], [INFOTRIEVE]
- Chuang S. E., Blattner F. R.. 1993. Characterization of twenty-six new heat shock genes of Escherichia coli. J Bacteriol. 175: 5242–5252. [PUBMED], [INFOTRIEVE]
- Chung H. Y., Kim H. J., Kim J. W., Yu B. P.. 2001. The inflammation hypothesis of aging: molecular modulation by calorie restriction. Ann N Y Acad Sci. 928: 327–335. [PUBMED], [INFOTRIEVE], [CSA]
- Craig E. A.. 1985. The heat shock response. CRC Crit Rev Biochem. 18: 239–280. [PUBMED], [INFOTRIEVE]
- Datta S. A., Rao C. M.. 1999. Differential temperature-dependent chaperone-like activity of alphaA- and alphaB-crystallin homoaggregates. J Biol Chem. 274: 34773–34778. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Jong W. W., Caspers G. J., Leunissen J. A.. 1998. Genealogy of the alpha-crystallin–small heat-shock protein superfamily. Int J Biol Macromol. 22: 151–162. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Delaunay A., Isnard A. D., Toledano M. B.. 2000. H2O2 sensing through oxidation of the Yap1 transcription factor. Embo J. 19: 5157–5166. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Derman A. I., Prinz W. A., Belin D., Beckwith J.. 1993. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science. 262: 1744–1747. [PUBMED], [INFOTRIEVE]
- 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: 693–696. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Diamant S., Goloubinoff P.. 1998. Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration. Biochemistry. 37: 9688–9694. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Ding H., Demple B.. 1997. In vivo kinetics of a redox-regulated transcriptional switch. Proc Natl Acad Sci USA. 94: 8445–8449. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Ehrnsperger M., Graber S., Gaestel M., Buchner J.. 1997. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. Embo J. 16: 221–229. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Ellgaard L., Helenius A.. 2003. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol. 4: 181–191. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Ellis R. J.. 2003. Protein folding: importance of the Anfinsen cage. Curr Biol. 13: R881–R883. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Ellis R. J., Hartl F. U.. 1999. Principles of protein folding in the cellular environment. Curr Opin Struct Biol. 9: 102–110. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Fink A. L.. 1999. Chaperone-mediated protein folding. Physiol Rev. 79: 425–449. [PUBMED], [INFOTRIEVE], [CSA]
- Frand A. R., Cuozzo J. W., Kaiser C. A.. 2000. Pathways for protein disulphide bond formation. Trends Cell Biol. 10: 203–210. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Frand A. R., Kaiser C. A.. 1998. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell. 1: 161–170. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Freedman R. B., Klappa P., Ruddock L. W.. 2002. Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep. 3: 136–140. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Gamer J., Multhaup G., Tomoyasu T., McCarty J. S., Rudiger S., Schonfeld H. J., Schirra C., Bujard H., Bukau B.. 1996. A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. Embo J. 15: 607–617. [PUBMED], [INFOTRIEVE], [CSA]
- Gething M. J., Sambrook J.. 1992. Protein folding in the cell. Nature. 355: 33–45. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Giese K. C., Vierling E.. 2002. Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro. J Biol Chem. 277: 46310–46318. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Gilbert H. F.. 1990. Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol. 63: 69–172. [PUBMED], [INFOTRIEVE]
- Gillece P., Luz J. M., Lennarz W. J., de La, Cruz F. J., Romisch K.. 1999. Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J Cell Biol. 147: 1443–1456. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Goldberger R. F., Epstein C. J., Anfinsen C. B.. 1963. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J Biol Chem. 238: 628–635. [PUBMED], [INFOTRIEVE]
- Goloubinoff P., Diamant S., Weiss C., Azem A.. 1997. GroES binding regulates GroEL chaperonin activity under heat shock. FEBS Lett. 407: 215–219. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Gophna U., Ron E. Z.. 2003. Virulence and the heat shock response. Int J Med Microbiol. 292: 453–461. [PUBMED], [INFOTRIEVE], [CSA]
- Graf P. C., Jakob U.. 2002. Redox-regulated molecular chaperones. Cell Mol Life Sci. 59: 1624–1631. [PUBMED], [INFOTRIEVE], [CSA]
- Graf P. C., Martinez-Yamout M., Van Haerents S., Lilie H., Dyson H. J., Jakob U.. 2004. Activation of the redox-regulated chaperone Hsp33 by domain unfolding. J Biol Chem. 279: 20529–20538. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Graumann J., Lilie H., Tang X., Tucker K. A., Hoffmann J. H., Vijayalakshmi J., Saper M., Bardwell J. C., Jakob U.. 2001. Activation of the redox-regulated molecular chaperone Hsp33–a two-step mechanism. Structure (Camb). 9: 377–387. [CSA], [CROSSREF]
- Grimshaw J. P., Jelesarov I., Schonfeld H. J., Christen P.. 2001. Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system. J Biol Chem. 276: 6098–60104. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Grimshaw J. P., Jelesarov I., Siegenthaler R. K., Christen P.. 2003. Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures. J Biol Chem. 278: 19048–19053. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Groemping Y., Reinstein J.. 2001. Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response. J Mol Biol. 314: 167–178. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Harrison C.. 2003. GrpE, a nucleotide exchange factor for DnaK. Cell Stress Chaperones. 8: 218–224. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Harrison C. J., Hayer-Hartl M., Di Liberto M., Hartl F., Kuriyan J.. 1997. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science. 276: 431–435. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Hartl F. U., Hayer-Hartl M.. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 295: 1852–1858. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Haslbeck M.. 2002. sHsps and their role in the chaperone network. Cell Mol Life Sci. 59: 1649–1657. [PUBMED], [INFOTRIEVE], [CSA]
- Haslbeck M., Braun N., Stromer T., Richter B., Model N., Weinkauf S., Buchner J.. 2004. Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. Embo J. 23: 638–649. [PUBMED], [INFOTRIEVE], [CSA]
- Haslbeck M., Walke S., Stromer T., Ehrnsperger M., White H. E., Chen S., Saibil H. R., Buchner J.. 1999. Hsp26: a temperature-regulated chaperone. Embo J. 18: 6744–6751. [PUBMED], [INFOTRIEVE], [CSA]
- Hirst T. R.. 2001. Cholera. A toxin with emerging therapeutic potential. Lancet. 358(Suppl)S7, [PUBMED], [INFOTRIEVE]
- Hoffmann J. H., Linke K., Graf P. C., Lilie H., Jakob U.. 2004. Identification of a redox-regulated chaperone network. Embo J. 23: 160–168. [PUBMED], [INFOTRIEVE], [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: 147–154. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Imlay J. A.. 2003. Pathways of oxidative damage. Annu Rev Microbiol. 57: 395–418. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Jakob U., Eser M., Bardwell J. C.. 2000. Redox switch of hsp33 has a novel zinc-binding motif. J Biol Chem. 275: 38302–38310. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Jakob U., Gaestel M., Engel K., Buchner J.. 1993. Small heat shock proteins are molecular chaperones. J Biol Chem. 268: 1517–1520. [PUBMED], [INFOTRIEVE]
- Jakob U., Muse W., Eser M., Bardwell J. C.. 1999. Chaperone activity with a redox switch. Cell. 96: 341–352. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Janda I., Devedjiev Y., Derewenda U., Dauter Z., Bielnicki J., Cooper D. R., Graf P. C., Joachimiak A., Jakob U., Derewenda Z. S.. 2004. The crystal structure of the reduced, Zn(2+)-bound form of the B. subtilis Hsp33 Chaperone and Its Implications for the activation mechanism. Structure (Camb). 12: 1901–1907. [CROSSREF]
- John D. C., Bulleid N. J.. 1994. Prolyl 4-hydroxylase: defective assembly of alpha-subunit mutants indicates that assembled alpha-subunits are intramolecularly disulfide bonded. Biochemistry. 33: 14018–14025. [PUBMED], [INFOTRIEVE]
- John D. C., Grant M. E., Bulleid N. J.. 1993. Cell-free synthesis and assembly of prolyl 4-hydroxylase: the role of the beta-subunit (PDI) in preventing misfolding and aggregation of the alpha-subunit. Embo J. 12: 1587–1595. [PUBMED], [INFOTRIEVE]
- Kang J. G., Paget M. S., Seok Y. J., Hahn M. Y., Bae J. B., Hahn J. S., Kleanthous C., Buttner M. J., Roe J. H.. 1999. RsrA, an anti-sigma factor regulated by redox change. Embo J. 18: 4292–4298. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Kim S. J., Jeong D. G., Chi S. W., Lee J. S., Ryu S. E.. 2001. Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity. Nat Struct Biol. 8: 459–466. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Klappa P., Ruddock L. W., Darby N. J., Freedman R. B.. 1998. The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. Embo J. 17: 927–935. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Kyselova P., Zourek M., Rusavy Z., Trefil L., Racek J.. 2002. Hyperinsulinemia and oxidative stress. Physiol Res. 51: 591–595. [PUBMED], [INFOTRIEVE], [CSA]
- Lee G. J., Roseman A. M., Saibil H. R., Vierling E.. 1997. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. Embo J. 16: 659–671. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Lee G. J., Vierling E.. 2000. A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. Plant Physiol. 122: 189–198. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Lencer W. I., Constable C., Moe S., Jobling M. G., Webb H. M., Ruston S., Madara J. L., Hirst T. R., Holmes R. K.. 1995. Targeting of cholera toxin and Escherichia coli heat labile toxin in polarized epithelia: role of COOH-terminal KDEL. J Cell Biol. 131: 951–962. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Leslie N. R., Bennett D., Lindsay Y. E., Stewart H., Gray A., Downes C. P.. 2003. Redox regulation of PI 3-kinase signalling via inactivation of PTEN. Embo J. 22: 5501–5510. [PUBMED], [INFOTRIEVE], [CSA], [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: 2874–2878. [PUBMED], [INFOTRIEVE], [CSA]
- Linke K., Jakob U.. 2003. Not every disulfide lasts forever: disulfide bond formation as a redox switch. Antioxid Redox Signal. 5: 425–434. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Linke K., Wolfram T., Bussemer J., Jakob U.. 2003. The roles of the two zinc binding sites in DnaJ. J Biol Chem. 278: 44457–4466. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Llorca O., Galan A., Carrascosa J. L., Muga A., Valpuesta J. M.. 1998. GroEL under heat-shock. Switching from a folding to a storing function. J Biol Chem. 273: 32587–32594. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Lumb R. A., Bulleid N. J.. 2002. Is protein disulfide isomerase a redox-dependent molecular chaperone?. Embo J. 21: 6763–6770. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Lund P. A.. 2001. Microbial molecular chaperones. Adv Microb Physiol. 44: 93–140. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Martin J., Langer T., Boteva R., Schramel A., Horwich A. L., Hartl F. U.. 1991. Chaperonin-mediated protein folding at the surface of groEL through a ‘molten globule’-like intermediate. Nature. 352: 36–42. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Mayer M., Kies U., Kammermeier R., Buchner J.. 2000a. BiP and PDI cooperate in the oxidative folding of antibodies in vitro. J Biol Chem. 275: 29421–29425. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Mayer M. P., Rudiger S., Bukau B.. 2000b. Molecular basis for interactions of the DnaK chaperone with substrates. Biol Chem. 381: 877–885. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Mayer M. P., Schroder H., Rudiger S., Paal K., Laufen T., Bukau B.. 2000c. Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat Struct Biol. 7: 586–593. [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: 126–137. [CROSSREF]
- McCracken A. A., Brodsky J. L.. 2003. Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). Bioessays. 25: 868–877. [CSA], [CROSSREF]
- Mekalanos J. J., Collier R. J., Romig W. R.. 1979. Enzymic activity of cholera toxin. II. Relationships to proteolytic processing, disulfide bond reduction, and subunit composition. J Biol Chem. 254: 5855–5861. [PUBMED], [INFOTRIEVE]
- Mendoza J. A., Rogers E., Lorimer G. H., Horowitz P. M.. 1991. Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J Biol Chem. 266: 13044–13049. [PUBMED], [INFOTRIEVE]
- Meunier L., Usherwood Y. K., Chung K. T., 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. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Mogk A., Deuerling E., Vorderwulbecke S., Vierling E., Bukau B.. 2003a. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol Microbiol. 50: 585–595. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Mogk A., Schlieker C., Friedrich K. L., Schonfeld H. J., Vierling E., Bukau B.. 2003b. Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J Biol Chem. 278: 31033–31042. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Mogk A., Tomoyasu T., Goloubinoff P., Rudiger S., Roder D., Langen H., Bukau B.. 1999. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. Embo J. 18: 6934–6949. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Molinari M., Galli C., Piccaluga V., Pieren M., Paganetti P.. 2002. Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER. J Cell Biol. 158: 247–257. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Muffler A., Barth M., Marschall C., Hengge-Aronis R.. 1997. Heat shock regulation of sigmaS turnover: a role for DnaK and relationship between stress responses mediated by sigmaS and sigma32 in Escherichia coli. J Bacteriol. 179: 445–452. [PUBMED], [INFOTRIEVE]
- Noiva R.. 1999. Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum. Semin Cell Dev Biol. 10: 481–493. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Parsell D. A., R. T., Sauer. 1989. Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation. Genes Dev. 3: 1226–1232. [PUBMED], [INFOTRIEVE]
- Pihlajaniemi T., Helaakoski T., Tasanen K., Myllyla R., Huhtala M. L., Koivu J., Kivirikko K. I.. 1987. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. Embo J. 6: 643–649. [PUBMED], [INFOTRIEVE], [CSA]
- Prockop D. J., Kivirikko K. I.. 1995. Collagens: molecular biology, diseases, and potentials for therapy. Annu Rev Biochem. 64: 403–434. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Quan H., Fan G., Wang C. C.. 1995. Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site. J Biol Chem. 270: 17078–17080. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Raman B., Siva Kumar L. V., Ramakrishna T., Mohan Rao C.. 2001. Redox-regulated chaperone function and conformational changes of Escherichia coli Hsp33. FEBS Lett. 489: 19–24. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Rao C. M., Raman B., Ramakrishna T., Rajaraman K., Ghosh D., Datta S., Trivedi V. D., Sukhaswami M. B.. 1998. Structural perturbation of alpha-crystallin and its chaperone-like activity. Int J Biol Macromol. 22: 271–281. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Requena J. R., Chao C. C., Levine R. L., Stadtman E. R.. 2001. Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proc Natl Acad Sci USA. 98: 69–74. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Richmond C. S., Glasner J. D., Mau R., Jin H., Blattner F. R.. 1999. Genome-wide expression profiling in Escherichia coli K-12. Nucleic Acids Res. 27: 3821–3835. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Richter K., Buchner J.. 2001. Hsp90: chaperoning signal transduction. J Cell Physiol. 188: 281–290. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G., Ducasse C., Paul C., Wieske M., Arrigo A. P., Buchner J., Gaestel M.. 1999. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. J Biol Chem. 274: 18947–18956. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Rosen R., Ron E. Z.. 2002. Proteome analysis in the study of the bacterial heat-shock response. Mass Spectrometry Reviews. 21: 244–265. [PUBMED], [INFOTRIEVE], [CSA]
- Rudiger S., Schneider-Mergener J., Bukau B.. 2001. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. Embo J. 20: 1042–1050. [PUBMED], [INFOTRIEVE], [CSA]
- Salmeen A., Andersen J. N., Myers M. P., Meng T. C., Hinks J. A., Tonks N. K., Barford D.. 2003. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature. 423: 769–773. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Schmid D., Baici A., Gehring H., Christen P.. 1994. Kinetics of molecular chaperone action. Science. 263: 971–973. [PUBMED], [INFOTRIEVE]
- Schmidt M., Buchner J., Todd M. J., Lorimer G. H., Viitanen P. V.. 1994. On the role of groES in the chaperonin-assisted folding reaction. Three case studies. J Biol Chem. 269: 10304–10311. [PUBMED], [INFOTRIEVE]
- Shin H. C., Song M. C., Scheraga H. A.. 2002. Effect of protein disulfide isomerase on the rate-determining steps of the folding of bovine pancreatic ribonuclease A. FEBS Lett. 521: 77–80. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Siegenthaler R. K., Grimshaw J. P., Christen P.. 2004. Immediate response of the DnaK molecular chaperone system to heat shock. FEBS Lett. 562: 105–110. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Sitia R., Braakman I.. 2003. Quality control in the endoplasmic reticulum protein factory. Nature. 426: 891–894. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Sitia R., Molteni S. N.. 2004. Stress, protein (mis)folding, and signaling: the redox connection. Sci STKE. 2004: pe27, [PUBMED], [INFOTRIEVE], [CROSSREF]
- Stadtman E. R., Moskovitz J., Levine R. L.. 2003. Oxidation of methionine residues of proteins: biological consequences. Antioxid Redox Signal. 5: 577–582. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Stromer T., Ehrnsperger M., Gaestel M., Buchner J.. 2003. Analysis of the interaction of small heat shock proteins with unfolding proteins. J Biol Chem. 278: 18015–18021. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Stromer T., Fischer E., Richter K., Haslbeck M., Buchner J.. 2004. Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domail is important for oligomer assembly and the binding of unfolding proteins. J Biol Chem. 279: 11222–11228. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Takemoto T., Zhang Q. M., S., Yonei. 1998. Different mechanisms of thioredoxin in its reduced and oxidized forms in defense against hydrogen peroxide in Escherichia coli. Free Radic Biol Med. 24: 556–562. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- 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: 755–765. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Tomoyasu T., Mogk A., Langen H., Goloubinoff P., Bukau B.. 2001. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol Microbiol. 40: 397–413. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Tomoyasu T., Ogura T., Tatsuta T., Bukau B.. 1998. Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli. Mol Microbiol. 30: 567–581. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Tsai B., Rapoport T. A.. 2002. Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1. J Cell Biol. 159: 207–216. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Tsai B., Rodighiero C., Lencer W. I., Rapoport T. A.. 2001. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell. 104: 937–948. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Tu B. P., Ho-Schleyer S. C., Travers K. J., Weissman J. S.. 2000. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science. 290: 1571–1574. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Tu B. P., Weissman J. S.. 2004. Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol. 164: 341–346. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Ueda S., Masutani H., Nakamura H., Tanaka T., Ueno M., Yodoi J.. 2002. Redox control of cell death. Antioxid Redox Signal. 4: 405–414. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- van Boekel M. A., de, Lange F., de, Grip W. J., de Jong W. W.. 1999. Eye lens alphaA- and alphaB-crystallin: complex stability versus chaperone-like activity. Biochim Biophys Acta. 1434: 114–123. [PUBMED], [INFOTRIEVE]
- van Montfort R. L., Basha E., Friedrich K. L., Slingsby C., Vierling E.. 2001. Crystal structure and assembly of a eukaryotic small heat shock protein. Nat Struct Biol. 8: 1025–1030. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- van Montfort R. L., Congreve M., Tisi D., Carr R., Jhoti H.. 2003. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature. 423: 773–777. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Vijayalakshmi J., Mukhergee M. K., Graumann J., Jakob U., Saper M. A.. 2001. The 2.2 A crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity. Structure (Camb). 9: 367–375. [CSA], [CROSSREF]
- Vuori K., Pihlajaniemi T., Myllyla R., Kivirikko K. I.. 1992. Site-directed mutagenesis of human protein disulphide isomerase: effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cells. Embo J. 11: 4213–4217. [PUBMED], [INFOTRIEVE], [CSA]
- Walmsley A. R., Batten M. R., Lad U., Bulleid N. J.. 1999. Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase. J Biol Chem. 274: 14884–14892. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Walter S., Buchner J.. 2002. Molecular chaperones—cellular machines for protein folding. Angew Chem Int Ed Engl. 41: 1098–1113. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Wegele H., Muller L., Buchner J.. 2004. Hsp70 and Hsp90-a relay team for protein folding. Rev Physiol Biochem Pharmacol. 151: 1–44. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Weissman J. S., Kim P. S.. 1993. Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature. 365: 185–188. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Wetterau J. R., Combs K. A., Spinner S. N., Joiner B. J.. 1990. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J Biol Chem. 265: 9801–9807. [PUBMED], [INFOTRIEVE]
- Winter J., Klappa P., Freedman R. B., Lilie H., Rudolph R.. 2002. Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin. J Biol Chem. 277: 310–317. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Wintrode P. L., Friedrich K. L., Vierling E., Smith J. B., Smith D. L.. 2003. Solution structure and dynamics of a heat shock protein assembly probed by hydrogen exchange and mass spectrometry. Biochemistry. 42: 10667–10673. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Won H. S., Low L. Y., Guzman R. D., Martines-Yamout M., Jakob U., Dyson H. J.. 2004. The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold. J Mol Biol. 341: 893–899. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Woo H. A., Chae H. Z., Hwang S. C., Yang K. S., Kang S. W., Kim K., Rhee S. G.. 2003. Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science. 300: 653–656. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Yeh J. I., Claiborne A., Hol W. G.. 1996. Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution. Biochemistry. 35: 9951–9957. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Young J. C., Barral J. M., Hartl F. U.. 2003. More than folding: localized functions of cytosolic chaperones. Trends Biochem Sci.. 28: 541–547. [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Zhang R. G., Scott D. L., Westbrook M. L., Nance S., Spangler B. D., Shipley G. G., Westbrook E. M.. 1995. The three-dimensional crystal structure of cholera toxin. J Mol Biol. 251: 563–573. [PUBMED], [INFOTRIEVE], [CROSSREF]
- Zheng M., Aslund F., Storz G.. 1998. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science. 279: 1718–1721. [PUBMED], [INFOTRIEVE], [CROSSREF]