Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases-progress and prognosis

Cold Spring Harbor Perspectives in Biology

Volumn 3, Issue 12, 2011, Pages

  Lindquist, Susan L ^a   Kelly, Jeffery W ^b  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CFTR PROTEIN, HUMAN; HEAT SHOCK PROTEIN; SOMATOMEDIN C; TRANSMEMBRANE CONDUCTANCE REGULATOR;

ANIMAL; BIOLOGICAL MODEL; CYSTIC FIBROSIS; ENDOPLASMIC RETICULUM; GENETICS; HEAT SHOCK RESPONSE; HOMEOSTASIS; HUMAN; KINETICS; METABOLISM; PHYSIOLOGICAL STRESS; PHYSIOLOGY; PROTEIN FOLDING; PROTEOSTASIS DEFICIENCY; REVIEW; SECRETORY PATHWAY; SIGNAL TRANSDUCTION;

ANIMALS; CYSTIC FIBROSIS; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; HEAT-SHOCK RESPONSE; HOMEOSTASIS; HUMANS; INSULIN-LIKE GROWTH FACTOR I; KINETICS; MODELS, BIOLOGICAL; PROTEIN FOLDING; PROTEOSTASIS DEFICIENCIES; SECRETORY PATHWAY; SIGNAL TRANSDUCTION; STRESS, PHYSIOLOGICAL;

EID: 84863903065     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a004507     Document Type: Article

References (235)

1. Adamski-Werner SL, Palaninathan SK, Sacchettini JC, Kelly JW. 2004. Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis. J Med Chem 47: 355-374.
2. Akerfelt M, Morimoto RI, Sistonen L. 2010. Heat shock factors: Integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 11: 545-555.
3. Albanese V, Reissmann S, Frydman J. 2010. A ribosomeanchored chaperone network that facilitates eukaryotic ribosome biogenesis. J Cell Biol 189: 69-81.
4. Alfonso P, Pampin S, Estrada J, Rodriguez-Rey JC, Giraldo P, Sancho J, Pocovi M. 2005. Miglustat (NB-DNJ) works as a chaperone for mutated acid β-glucosidase in cells transfected with several Gaucher disease mutations. Blood Cells Molecules Diseases 35: 268-276.
5. Andrade C. 1952. A peculiar form of peripheral neuropathy; Familiar atypical generalized amyloidosis with special involvement of the peripheral nerves. Brain 75: 408-427.
6. Anfinsen CB. 1973. Principles that govern the folding of protein chains. Science 181: 223-230.
7. Arantes-Oliveira N, Apfeld J, Dillin A, Kenyon C. 2002. Regulation of life-span by germ-line stem cells in Caenorhabditis elegans. Science 295: 502-505.
8. Arias E, Cuervo AM. 2011. Chaperone-mediated autophagy in protein quality control. Curr Opin Cell Biol 23: 184-189.
9. Asano N, Ishii S, Kizu H, Ikeda K, Yasuda K, Kato A, Martin OR, Fan J-Q. 2000. In vitro inhibition and intracellular enhancement of lysosomal α-galactosidase A activity in Fabry lymphoblasts by 1-deoxygalactonojirimycin and its derivatives. Eur J Biochem 267: 4179-4186.
10. Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM. 2002. Chaperone suppression of α-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295: 809-810.
11. Bagatell R, Whitesell L. 2004. Altered Hsp90 function in cancer: A unique therapeutic opportunity. Molecular Cancer Therapeutics 3: 1021-1030.
12. 2+ binding domains. J Biol Chem 266: 21458-21465.
13. Balch WE, Morimoto RI, Dillin A, Kelly JW. 2008. Adapting proteostasis for disease intervention. Science 319: 916-919.
14. Baures PW, Peterson SA, Kelly JW. 1998. Discovering transthyretin amyloid fibril inhibitors by limited screening. Bioorg Med Chem 6: 1389-1401.
15. Baures PW, Oza VB, Peterson SA, Kelly JW. 1999. Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the nonsteroidal anti-inflammatory drug flufenamic acid. Bioorg Med Chem 7: 1339-1347.
16. Behrends C, Langer Carola A, Boteva R, Bottcher Ulrike M, Stemp Markus J, Schaffar G, Rao Bharathi V, Giese A, Kretzschmar H, Siegers K, et al. 2006. Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Mol Cell 23: 887-897.
17. Ben-Zvi A, Miller EA, Morimoto RI. 2009. Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging. Proc Natl Acad Sci 6: 1-6.
18. Bieschke J, Zhang Q, Bosco DA, Lerner RA, Powers ET, Wentworth P Jr, Kelly JW. 2006. Small molecule oxidation products trigger disease-associated protein misfolding. Acc Chem Res 39: 611-619.
19. Blake CCF, Geisow MJ, Oatley SJ. 1978. Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by fourier refinement at 1.8 angstroms. J Mol Biol 121: 339-356.
20. Bosco DA, Fowler DM, Zhang Q, Nieva J, Powers ET, Wentworth P, Lerner RA, Kelly JW. 2006. Elevated levels of oxidized cholesterol metabolites in Lewy body disease brains accelerate α-synuclein fibrilization. [Erratum to document cited in CA145:005691.] Nat Chem Biol 2: 346.
21. Brandt F, Carlson L-A, Hartl FU, Baumeister W, Gruenewald K. 2010. The three-dimensional organization of polyribosomes in intact human cells. Mol Cell 39: 560-569.
22. Brockmeier A, Brockmeier U, Williams DB. 2009. Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function. J Biol Chem 284: 3433-3444.
23. Brodsky JL, McCracken AA. 1997. ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together. Trends Cell Biol 7: 151-156.
24. Chaney MO, Baudry J, Esh C, Childress J, Luehrs DC, Kokjohn TA, Roher AE. 2003. Aβ, aging, and Alzheimer's disease: A tale, models, and hypotheses. Neurol Res 25: 581-589.
25. Chang HH, Asano N, Ishii S, Ichikawa Y, Fan JQ. 2006. Hydrophilic iminosugar active-site-specific chaperones increase residual glucocerebrosidase activity in fibroblasts from Gaucher patients. FEBS J 273: 4082-4092.
26. Chang L, Bertelsen EB, Wisen S, Larsen EM, Zuiderweg ERP, Gestwicki JE. 2008. High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK. Anal Biochem 372: 167-176.
27. Chang L, Thompson AD, Ung P, Carlson HA, Gestwicki JE. 2010. Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK). J Biol Chem 285: 21282-21291.
28. Chang L, Miyata Y, Ung PMU, Bertelsen EB, McQuade TJ, Carlson HA, Zuiderweg ERP, Gestwicki JE. 2011. Chemical screens against a reconstituted multiprotein complex: Myricetin blocks dnaj regulation of dnak through an allosteric mechanism. Chem Biol 18: 210-221.
29. Chen X, Yin XM. 2011. Coordination of autophagy and the proteasome in resolving endoplasmic reticulum stress. Vet Pathol 48: 245-253.
30. Choi S-W, Reixach N, Connelly S, Johnson SM, Wilson IA, Kelly JW. 2010a. A substructure combination strategy to create potent and selective transthyretin kinetic stabilizers that prevent amyloidogenesis and cytotoxicity. J Am Chem Soc 132: 1359-1370.
31. Choi S, Connelly S, Reixach N, Wilson IA, Kelly JW. 2010b. Chemoselective small molecules that covalently modify one lysine in a non-enzyme protein in plasma. Nat Chem Biol 6: 133-139.
32. Cohen E, Dillin A. 2008. The insulin paradox: Aging, proteotoxicity and neurodegneration. Nat Rev Neurosci 9: 759-767.
33. Cohen FE, Kelly JW. 2003. Therapeutic approaches to protein-misfolding diseases. Nature 426: 905-909.
34. Cohen E, Bieschke J, Perciavalle RM, Kelly JW, Dillin A. 2006. Opposing activities protect against age-onset proteotoxicity. Science 313: 1604-1610.
35. Cohen E, Paulsson JF, Blinder P, Burstyn-Cohen T, Du D, Estepa G, Adame A, Pham HM, Holzenberger M, Kelly JW, et al. 2009. Reduced IGF-1 signaling delays age-associated proteotoxicity in mice. Cell 139: 1157-1169.
36. Cohen E, Du D, Joyce D, Kapernick EA, Volovik Y, Kelly JW, Dillin A. 2010. Temporal requirements of insulin/IGF-1 signaling for proteotoxicity protection. Aging Cell 9: 126-134.
37. Colon W, Kelly JW. 1992. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31: 8654-8660.
38. Compain P, Martin OR, Boucheron C, Godin G, Yu L, Ikeda K, Asano N. 2006. Design and synthesis of highly potent and selective pharmacological chaperones for the treatment of Gaucher's disease. Chembiochemistry 7: 1356-1359.
39. Connelly S, Choi S, Johnson SM, Kelly JW, Wilson IA. 2010. Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses. Curr Opin Struct Biol 20: 54-62.
40. Cornwell GG 3 rd, Sletten K, Johansson B, Westermark P. 1988. Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin. Biochem Biophys Res Commun 154: 648-653.
41. Cowen LE, Singh SD, Kohler JR, Collins C, Zaas A, Schell WA, Aziz H, Mylonakis E, Perfect JR, Whitesell L, et al. 2009. Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease. Proc Nat Acad Sci 106: 2818-2823.
42. Culyba EK, Price JL, Hanson SR, Dhar A, Wong C-H, Gruebele M, Powers ET, Kelly JW. 2011. Protein native-state stabilization by placing aromatic side chains in n-glycosylated reverse turns. Science 331: 571-575.
43. Dai C, Whitesell L, Rogers AB, Lindquist S. 2007. Heatshock factor 1 is a powerful multifaceted modifier of carcinogenesis. Cell 130: 1005-1018.
44. Deechongkit S, Nguyen H, Powers ET, Dawson PE, Gruebele M, Kelly JW. 2004. Context-dependent contributions of backbone hydrogen bonding to β-sheet folding energetics. Nature 430: 101-105.
45. DeMartino GN, Gillette TG. 2007. Proteasomes: Machines for all reasons. Cell 129: 659-662.
46. Didomenico BJ, Bugaisky GE, Lindquist S. 1982. The heatshock is self-regulated at both the transcriptional and posttranslational levels. Cell 31: 593-603.
47. Dill KA, Chan HS. 1997. FromLevinthal to pathway funnels. Nat Struct Biol 4: 10-19.
48. Dillin A, Crawford DK, Kenyon C. 2002. Timing Requirements for Insulin/IGF-1 Signaling in C. elegans. Science 298: 830-834.
49. Douglas PM, Dillin A. 2010. Protein homeostasis and aging in neurodegeneration. J Cell Biol 190: 719-729.
50. Douglas NR, Reissmann S, Zhang J, Chen B, Jakana J, Kumar R, Chiu W, Frydman J. 2011. Dual action of ATP hydrolysis couples lid closure to substrate release into the group ii chaperonin chamber. Cell 144: 240-252.
51. Drummond DA, Wilke CO. 2008. Mistranslation-induced protein misfolding as a dominant constraint on codingsequence evolution. Cell 134: 341-352.
52. Du D, Murray AN, Cohen E, Kim H-E, Simkovsky R, Dillin A, Kelly JW. 2011. A kinetic aggregation assay allowing selective and sensitive amyloid-β quantification in cells and tissues. Biochemistry 50: 1607-1617.
53. Dvir H, Harel M, McCarthy AA, Toker L, Silman I, Futerman AH, Sussman JL. 2003. X-ray structure of human acid-β-glucosidase, the defective enzyme in Gaucher disease. EMBO Rep 4: 704-709.
54. Dyson HJ, Wright PE. 2005. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6: 197-208.
55. Edlich F, Fischer G. 2006. Pharmacological targeting of catalyzed protein folding: The example of peptide bond cis/trans isomerases. Handb Exp Pharmacol 172: 359-404.
56. Ellgaard L, Molinari M, Helenius A. 1999. Setting the standards: Quality control in the secretory pathway. Science 286: 1882-1888.
57. Ellis RJ, Hartl FU. 1999. Principles of protein folding in the cellular environment. Curr Op Struct Biol 9: 102-110.
58. Ellis RJ, Minton AP. 2006. Protein aggregation in crowded environments. Biol Chem 387: 485-497.
59. Evans CG, Chang L, Gestwicki JE. 2010. Heat shock protein 70 (Hsp70) as an emerging drug target. J Med Chem 53: 4585-4602.
60. Fan J-Q. 2001. Potential drug therapies for lysosomal storage disorders. Frontiers Biotechnol Pharmaceuticals 2: 275-291.
61. Fan JQ. 2003. A contradictory treatment for lysosomal storage disorders: Inhibitors enhance mutant enzyme activity. Trends Pharmacol Sci 24: 355-360.
62. Fan JQ, Ishii S, Asano N, Suzuki Y. 1999. Accelerated transport and maturation of lysosomal α-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor. Nature Med 5: 112-115.
63. Fewell SW, Travers KJ, Weissman JS, Brodsky JL. 2001. The action of molecular chaperones in the early secretory pathway. Annu Rev Genet 35: 149-191.
64. Finley D. 2009. Recognition and processing of ubiquitinprotein conjugates by the proteasome. Annu Rev Biochem 78: 477-513.
65. Fischer G, Schmid FX. 1999. Peptidyl-prolyl cis/trans isomerases, pp. 461-489. Harwood, Newark, NJ.
66. Foss TR, Wiseman RL, Kelly JW. 2005. The pathway by which the tetrameric protein transthyretin dissociates. Biochemistry 44: 15525-15533.
67. Frustaci A, Chimenti C, Ricci R, Natale L, Russo MA, Pieroni M, Eng CM, Desnick RJ. 2001. Brief report: Improvement in cardiac function in the cardiac variant of Fabry's disease with galactose-infusion therapy. New Eng J Med 345: 25-32.
68. Futerman AH, van Meer G. 2004. The cell biology of lysosomal storage disorders. Nat Rev Mol Cell Biol 5: 554-565.
69. Geller R, Vignuzzi M, Andino R, Frydman J. 2007. Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev 21: 195-205.
70. Genereux JC, Wiseman RL. 2011. Chemically targeting the emergent properties of a chaperone complex. Chem Biol 18: 144-145.
71. Ghosh R, Lipson KL, Sargent KE, Mercurio AM, Hunt JS, Ron D, Urano F. 2010. Transcriptional regulation of VEGF-A by the unfolded protein response pathway. PLoS One 5: e9575.
72. Gidalevitz T, Ben-Zvi A, Ho KH, Brignull HR, Morimoto RI. 2006. Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311: 1471-1474.
73. Glasser SP. 2006. Antihypertensive safety and efficacy and physician and patient satisfaction: Results from a phase 4 practice-based clinical experience trial with diltiazem LA. Adv Ther 23: 284-294.
74. Green NS, Palaninathan SK, Sacchettini JC, Kelly JW. 2003. Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization. J Am Chem Soc 125: 13404-13414.
75. Green NS, Foss TR, Kelly JW. 2005. Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosis. Proc Natl Acad Sci 102: 14545-14550.
76. Gusella JF, MacDonald ME. 2009. Huntington's disease: The case for genetic modifiers. Genome Med 1: 80.
77. Hammarstrom P, Jiang X, Hurshman AR, Powers ET, Kelly JW. 2002. Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity. Proc Natl Acad Sci 99: 16427-16432.
78. Hammarstrom P, Wiseman RL, Powers ET, Kelly JW. 2003. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 299: 713-716.
79. Harding HP, Zhang Y, Zeng H, Novoa I, Lu PD, Calfon M, Sadri N, Yun C, Popko B, Paules R, et al. 2003. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 11: 619-633.
80. Hartl FU, Hayer-Hartl M. 2009. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 16: 574-581.
81. Haslbeck M, Franzmann T, Weinfurtner D, Buchner J. 2005. Some like it hot: The structure and function of small heat-shock proteins. Nature StructMol Biol 12: 842-846.
82. Hidvegi T, Ewing M, Hale P, Dippold C, Beckett C, Kemp C, Maurice N, Mukherjee A, Goldbach C, Watkins S, et al. 2010. An autophagy-enhancing drug promotes degradation of mutant α1-antitrypsin z and reduces hepatic fibrosis. Science 329: 229-232.
83. Hsu A, Murphy CT, Kenyon C. 2003. Regulation of aging and age-related disease byDAF-16 and heat-shock factor. Science 300: 1142-1145.
84. Hurshman AR, White JT, Powers ET, Kelly JW. 2004. Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. Biochemistry 43: 7365-7381.
85. Hurshman Babbes AR, Powers ET, Kelly JW. 2008. Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: The relationship between stability and amyloidosis. Biochemistry 47: 6969-6984.
86. Hutt DM, Herman D, Rodrigues APC, Noel S, Pilewski JM, Matteson J, Hoch B, Kellner W, Kelly JW, Schmidt A, et al. 2010. Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis. Nature Chem Biol 6: 25-33.
87. Ishii S, Kase R, Sakuraba H, Suzuki Y. 1993. Characterization of a mutant α-galactosidase gene-product for the late-onset cardiac form of Fabry disease. Biochem Biophys Res Commun 197: 1585-1589.
88. Jacobson DR, Pastore RD, Yaghoubian R, Kane I, Gallo G, Buck FS, Buxbaum JN. 1997. Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans. N Engl J Med 336: 466-473.
89. Jager M, Nguyen H, Crane JC, Kelly JW, Gruebele M. 2001. The folding mechanism of a α-sheet: The WWdomain. J Mol Biol 311: 373-393.
90. Jager M, Deechongkit S, Koepf EK, Nguyen H, Gao J, Powers ET, Gruebele M, Kelly JW. 2008. 2008 Vincent du Vigneaud award lecture. Understanding the mechanism of α-sheet folding from a chemical and biological perspective. Biopolymers 90: 751-758.
91. Jahn TR, Radford SE. 2008. Folding versus aggregation: Polypeptide conformations on competing pathways. Arch Biochem Biophys 469: 100-117.
92. Jankowsky JL, Slunt HH, Ratovitski T, Jenkins NA, Copeland NG, Borchelt DR. 2001. Coexpression of multiple transgenes in mouse CNS: A comparison of strategies. Biomol Eng 17: 157-165.
93. Jarosz DF, Taipale M, Lindquist S. 2010. Protein homeostasis and the phenotypic manifestation of genetic diversity: Principles and mechanisms. Annu Rev Genet 44: 189-216.
94. Jiang X, Buxbaum JN, Kelly JW. 2001a. The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis. Proc Natl Acad Sci 98: 14943-14948.
95. Jiang X, Smith CS, Petrassi HM, Hammarstrom P, White JT, Sacchettini JC, Kelly JW. 2001b. An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured. Biochemistry 40: 11442-11452.
96. Jinwal UK, Miyata Y, Koren J III, Jones JR, Trotter JH, Chang L, O'Leary J, Morgan D, Lee DC, Shults CL, et al. 2009. Chemical manipulation of Hsp70 ATPase activity regulates Tau stability. J Neurosci 29: 12079-12088.
97. Johnson AE. 2009. The structural and functional coupling of two molecular machines, the ribosome and the translocon. J Cell Biol 185: 765-767.
98. Johnson SM, Petrassi HM, Palaninathan SK, Mohamedmohaideen NN, Purkey HE, Nichols C, Chiang KP, Walkup T, Sacchettini JC, Sharpless KB, et al. 2005a. Bisaryloxime ethers as potent inhibitors of transthyretin amyloid fibril formation. J Med Chem 48: 1576-1587.
99. Johnson SM, Wiseman RL, Sekijima Y, Green NS, Adamski-Werner SL, Kelly JW. 2005b. Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses. Acc Chem Res 38: 911-921.
100. Johnson SM, Connelly S, Wilson IA, Kelly JW. 2008a. Bbiochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors. J Med Chem 51: 260-270.
101. Johnson SM, Connelly S, Wilson IA, Kelly JW. 2008b. Toward optimization of the linker substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies. J Med Chem 51: 6348-6358.
102. Johnson SM, Connelly S, Wilson IA, Kelly JW. 2009. Toward optimization of the second aryl substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies. J Med Chem 52: 1115-1125.
103. Johnson SM, Wiseman RL, Reixach N, Paulsson JF, Choi S, Powers ET, Buxbaum JN, Kelly JW. 2010. Understanding and ameliorating the TTR amyloidoses, pp. 967-1003. John Wiley & Sons, Hoboken, NJ.
104. Junker M, Besingi RN, Clark PL. 2009. Vectorial transport and folding of an autotransporter virulence protein during outer membrane secretion. Mol Microbiol 71: 1323-1332.
105. Kampinga HH, Craig EA. 2010. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 11: 579-592.
106. Kauzmann W. 1959. Some factors in the interpretation of protein denaturation. In Advances in protein chemistry (ed. CB Anfinsen, et al.), Vol. 14, pp. 1-63. Academic Press, New York.
107. Kenyon C. 2005. The plasticity of aging: Insights from longlived mutants. Cell 120: 449-460.
108. Kirstein-Miles J, Morimoto RI. 2010a. Caenorhabditis elegans as a model system to study intercompartmental proteostasis: Interrelation of mitochondrial function, longevity, and neurodegenerative diseases. Dev Dyn 239: 1529-1538.
109. Kirstein-Miles J, Morimoto RI. 2010b. Peptides signal mitochondrial stress. Cell Metab 11: 177-178.
110. Kitamura A, Kubota H, Pack C-G, Matsumoto G, Hirayama S, Takahashi Y, Kimura H, Kinjo M, Morimoto RI, Nagata K. 2006. Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state. Nature Cell Biol 8: 1163-1169.
111. Klabunde T, Petrassi HM, Oza VB, Raman P, Kelly JW, Sacchettini JC. 2000. Rational design of potent human transthyretin amyloid disease inhibitors. Nat Struct Biol 7: 312-321.
112. Kon M, Cuervo AM. 2010. Autophagy: An alternative degradation mechanism for misfolded proteins, pp. 113-129. John Wiley & Sons, Hoboken, NJ.
113. Koonin EV. 2010. The origin and early evolution of eukaryotes in the light of phylogenomics. Genome Biology 11: 209.
114. Koren J III, Jinwal UK, Jin Y, O'Leary J, Jones JR, Johnson AG, Blair LJ, Abisambra JF, Chang L, Miyata Y, et al. 2010. Facilitating Akt clearance via manipulation of Hsp70 activity and levels. J Biol Chem 285: 2498-2505.
115. Korkotian E, Schwarz A, Pelled D, Schwarzmann G, Segal M, Futerman AH. 1999. Elevation of intracellular glucosylceramide levels results in an increase in endoplasmic reticulumdensity and in functional calcium stores in cultured neurons. J Biol Chem 274: 21673-21678.
116. Koulov AV, La PP, Lu B, Razvi A, Coppinger J, Dong M-Q, Matteson J, Laister R, Arrowsmith C, Yates JR III, et al. 2010. Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis. Mol Biol Cell 21: 871-884.
117. Kruse KB, Brodsky JL, McCracken AA. 2006. Autophagy. An ER protein quality control process. Autophagy 2: 135-137.
118. Kuntz ID Jr, Kauzmann W. 1974. Hydration of proteins and polypeptides. Adv Protein Chem 28: 239-345.
119. Lai Z, Colon W, Kelly JW. 1996. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate which can self-assemble into amyloid. Biochemistry 35: 6470-6482.
120. Lamark T, Johansen T. 2010. Autophagy: Links with the proteasome. Curr Opin Cell Biol 22: 192-198.
121. Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, Liosatos M, Morgan TE, Rozovsky I, Trommer B, Viola KL, et al. 1998. Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci 95: 6448-6453.
122. Larkin A, Imperiali B. 2011. The expanding horizons of asparagine-linked glycosylation. Biochemistry 50: 4411-4426.
123. Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT. 2002. Neurodegenerative disease: Amyloid pores from pathogenic mutations. Nature 418: 291.
124. Lecker SH, Goldberg AL, Mitch WE. 2006. Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. J Am Soc Nephrol 17: 1807-1819.
125. Lee B-H, Lee MJ, Park S, Oh D-C, Elsasser S, Chen P-C, Gartner C, Dimova N, Hanna J, Gygi SP, et al. 2010. Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 467: 179-184.
126. Li H, Korennykh AV, Behrman SL, Walter P. 2010. Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering. Proc Natl Acad Sci 107: 16113-16118, S16113/16111-S16113/16115.
127. Li J, Richter K, Buchner J. 2011. Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat Struct Mol Biol 18: 61-66.
128. Lieberman RL, Wustman BA, Huertas P, Powe AC, Pine CW, Khanna R, Schlossmacher MG, Ringe D, Petsko GA. 2007. Structure of acid β-glucosidase with pharmacological chaperone provides insight into Gaucher disease. Nature Chem Biol 3: 101-107.
129. Lin H, Sugimoto Y, Ohsaki Y, Ninomiya H, Oka A, Taniguchi M, Ida H, Eto Y, Ogawa S, Matsuzaki Y, et al. 2004. N-Octyl-[β]-valienamine up-regulates activity of F213I mutant [β]-glucosidase in cultured cells: A potential chemical chaperone therapy for Gaucher disease. Biochim Biophys Acta (BBA)-Molecular Basis of Disease 1689: 219-228.
130. Liu K, Cho HS, Lashuel HA, Kelly JW, Wemmer DE. 2000. A glimpse of a possible amyloidogenic intermediate of transthyretin. Nat Struct Biol 7: 754-757.
131. Liu XL, Done SC, Yan K, Kilpelaeinen P, Pikkarainen T, Tryggvason K. 2004. Defective trafficking of nephrin missense mutants rescued by a chemical chaperone. J Am Soc Nephrol 15: 1731-1738.
132. Lloyd-Evans E, Pelled D, Riebeling C, Bodennec J, de-Morgan A, Waller H, Schiffmann R, Futerman AH. 2003. Glucosylceramide and glucosylsphingosine modulate calcium mobilization from brain microsomes via different mechanisms. J Biol Chem 278: 23594-23599.
133. Lomas DA, Perlmutter DH. 2010. α-1-antitrypsin deficiency, pp. 403-423, 401 plate. John Wiley&Sons, Hoboken, NJ.
134. Maier T, Ferbitz L, Deuerling E, Ban N. 2005. A cradle for new proteins: Trigger factor at the ribosome. Curr Opin Struct Biol 15: 204-212.
135. Marciniak SJ, Ron D. 2006. Endoplasmic reticulum stress signaling in disease. Physiol Rev 86: 1133-1149.
136. McCracken AA, Brodsky JL. 2003. Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). Bio Essays 25: 868-877.
137. McCracken AA, Werner ED, Brodsky JL. 1998. Endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate. Adv Mol Cell Biol 27: 165-200.
138. McCutchen SL, Lai Z, Miroy G, Kelly JW, Colon W. 1995. Comparison of lethal and non-lethal transthyretin variants and their relationship to amyloid disease. Biochemistry 34: 13527-13536.
139. McDonald E, Workman P, Jones K. 2006. Inhibitors of the HSP90 molecular chaperone: Attacking the master regulator in cancer. Curr Top Med Chem 6: 1091-1107.
140. Merz F, Boehringer D, Schaffitzel C, Preissler S, Hoffmann A, Maier T, Rutkowska A, Lozza J, Ban N, Bukau B, et al. 2008. Molecular mechanism and structure of trigger factor bound to the translating ribosome. EMBO J 27: 1622-1632.
141. Miller SR, Sekijima Y, Kelly JW. 2004. Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants. Lab Invest 84: 545-552.
142. Miroy GJ, Lai Z, Lashuel HA, Peterson SA, Strang C, Kelly JW. 1996. Inhibiting transthyretin amyloid fibril formation via protein stabilization. Proc Natl Acad Sci 93: 15051-15056.
143. Miyata Y, Chang L, Bainor A, McQuade TJ, Walczak CP, Zhang Y, Larsen MJ, Kirchhoff P, Gestwicki JE. 2010. High-throughput screen for Escherichia coli heat shock protein 70 (Hsp70/DnaK): ATPase assay in low volume by exploiting energy transfer. J Biomol Screening 15: 1211-1219.
144. Morimoto RI. 1998. Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 12: 3788-3796.
145. Morimoto RI, Cuervo AM. 2009. Protein homeostasis and aging: Taking care of proteins fromthe cradle to the grave. J Gerontol, Ser A 64A: 167-170.
146. Morley JF, Morimoto RI. 2004. Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. Mol Biol Cell 15: 657-664.
147. Morley JF, Brignull HR, Weyers JJ, Morimoto RI. 2002. The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc Natl Acad Sci 99: 10417-10422.
148. Mu T-W, Fowler DM, Kelly JW. 2008a. Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasis. PLoS Biol 6: 253-265.
149. Mu T-W, Ong DST, Wang Y-J, Balch WE, Yates JR 3rd, Segatori L, Kelly JW. 2008b. Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell 134: 769-781.
150. Mulder AM, Yoshioka C, Beck AH, Bunner AE, Milligan RA, Potter CS, Carragher B, Williamson JR. 2010. Visualizing ribosome biogenesis: Parallel assembly pathways for the 30S subunit. Science 330: 673-677.
151. Namba Y, Tomonaga M, Ohtsuka K, Oda M, Ikeda K. 1991. HSP 70 is associated with abnormal cytoplasmic inclusions characteristic of neurodegenerative diseases. Brain Nerve 43: 57-60.
152. Oliveberg M, Wolynes PG. 2005. The experimental survey of protein-folding energy landscapes. Q Rev Biophys 38: 245-288.
153. Olzscha H, Schermann SM, Woerner AC, Pinkert S, Hecht MH, Tartaglia GG, Vendruscolo M, Hayer-Hartl M, Hartl FU, Vabulas RM. 2011. Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144: 67-78.
154. 2+ increases enhance mutant glucocerebrosidase proteostasis. Nat Chem Biol 6: 424-432.
155. Onuchic JN, Wolynes PG. 2004. Theory of protein folding. Curr Opin Struct Biol 14: 70-75.
156. Orlowski RZ, Kuhn DJ. 2008. Proteasome inhibitors in cancer therapy: Lessons from the first decade. Clin Cancer Res 14: 1649-1657.
157. Oza VB, Petrassi HM, Purkey HE, Kelly JW. 1999. Synthesis and evaluation of anthranilic acid-based transthyretin amyloid fibril inhibitors. Bioorg Med Chem Lett 9: 1-6.
158. Oza VB, Smith C, Raman P, Koepf EK, Lashuel HA, Petrassi HM, Chiang KP, Powers ET, Sachettinni J, Kelly JW. 2002. Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors. J Med Chem 45: 321-332.
159. Ozcan U, Yilmaz E, Ozcan L, Furuhashi M, Vaillancourt E, Smith Ross O, Gorgun Cem Z, Hotamisligil GS. 2006. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 313: 1137-1140.
160. Pelled D, Trajkovic-Bodennec S, Lloyd-Evans E, Sidransky E, Schiffmann R, Futerman AH. 2005. Enhanced calcium release in the acute neuronopathic form of Gaucher disease. Neurobiol Dis 18: 83-88.
161. Perlmutter DH. 2011. α-1-antitrypsin deficiency: importance of proteasomal and autophagic degradative pathways in disposal of liver disease-associated protein aggregates. Annu Rev Med 62: 333-345.
162. Petrassi HM, Klabunde T, Sacchettini J, Kelly JW. 2000. Structure-based design of N-phenyl phenoxazine transthyretin amyloid fibril inhibitors. J Am Chem Soc 122: 2178-2192.
163. Petrassi HM, Johnson SM, Purkey HE, Chiang KP, Walkup T, Jiang X, Powers ET, Kelly JW. 2005. Potent and selective structure-based dibenzofuran inhibitors of transthyretin amyloidogenesis: Kinetic stabilization of the native state. J Am Chem Soc 127: 6662-6671.
164. Powers ET, Balch WE. 2008. Costly mistakes: Translational infidelity and protein homeostasis. Cell 134: 204-206.
165. Powers ET, Morimoto RI, Dillin A, Kelly JW, Balch WE. 2009. Biological and chemical approaches to diseases of proteostasis deficiency. Annu Rev Biochem 78: 23.21-23.33.
166. Prahlad V, Cornelius T, Morimoto RI. 2008. Regulation of the cellular heat shock response in Caenorhabditis elegans by thermosensory neurons. Science 320: 811-814.
167. Purkey HE, Dorrell MI, Kelly JW. 2001. Evaluating the binding selectivity of transthyretin amyloid fibril inhibitors in blood plasma. Proc Natl Acad Sci 98: 5566-5571.
168. Purkey HE, Palaninathan SK, Kent KC, Smith C, Safe SH, Sacchettini JC, Kelly JW. 2004. Hydroxylated polychlorinated biphenyls selectively bind transthyretin in blood and inhibit amyloidogenesis: Rationalizing rodent PCB toxicity. Chem Biol 11: 1719-1728.
169. Qu BH, Strickland EH, Thomas PJ. 1997. Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding. J Biol Chem 272: 15739-15744.
170. Razavi H, Palaninathan SK, Powers ET, Wiseman RL, Purkey HE, Mohamedmohaideen NN, Deechongkit S, Chiang KP, Dendle MTA, Sacchettini JC, et al. 2003. Benzoxazoles as transthyretin amyloid fibril inhibitors: Synthesis, evaluation, and mechanism of action. Angewandte Chemie, International Edition 42: 2758-2761.
171. Razavi H, Powers ET, Purkey HE, Adamski-Werner SL, Chiang KP, Dendle MTA, Kelly JW. 2005. Design, synthesis, and evaluation of oxazole transthyretin amyloidogenesis inhibitors. Bioorg Med Chem Lett 15: 1075-1078.
172. Richardson PG. 2004. A review of the proteasome inhibitor bortezomib in multiple myeloma. Expert Opin Pharmacother 5: 1321-1331.
173. Richardson PG, Mitsiades C. 2005. Bortezomib: Proteasome inhibition as an effective anticancer therapy. Future Oncol 1: 161-171.
174. Richter K, Buchner J. 2011. Closing in on the Hsp90 chaperone-client relationship. Structure 19: 445-446.
175. Rieger TR, Morimoto RI, Hatzimanikatis V. 2005. Mathematical modeling of the eukaryotic heat-shock response: Dynamics of the hsp70 promoter. Biophys J 88: 1646-1658.
176. Riordan JR. 1999. Cystic fibrosis as a disease of misprocessing of the cystic fibrosis transmembrane conductance regulator glycoprotein. Am J Hum Genet 64: 1499-1504.
177. Riordan JR. 2008. CFTR function and prospects for therapy. Annu Rev Biochem 77: 701-726.
178. Ron D, Walter P. 2007. Signal integration in the endoplasmic reticulum unfolded protein response. Nature Rev Mol Cell Biol 8: 519-529.
179. Sawkar AR, Cheng W-C, Beutler E, Wong C-H, Balch WE, Kelly JW. 2002. Chemical chaperones increase the cellular activity of N370S b-glucosidase: A therapeutic strategy for Gaucher disease. Proc Natl Acad Sci 99: 15428-15433.
180. Sawkar AR, Adamski-Werner SL, Cheng W-C, Wong C-H, Beutler E, Zimmer K-P, Kelly JW. 2005. Gaucher disease-associated glucocerebrosidases show mutationdependent chemical chaperoning profiles. Chem Biol 12: 1235-1244.
181. Sawkar AR, D'Haeze W, Kelly JW. 2006a. Therapeutic strategies to ameliorate lysosomal storage disorders-a focus on Gaucher disease. Cell Mol Life Sci 63: 1179-1192.
182. Sawkar AR, Schmitz M, Zimmer K-P, Reczek D, Edmunds T, Balch WE, Kelly JW. 2006b. Chemical chaperones and permissive temperatures alter the cellular localization of Gaucher disease associated glucocerebrosidase variants. ACS Chem Biol 1: 235-251.
183. Schroder M, Kaufman RJ. 2005. The mammalian unfolded protein response. Ann Rev Biochem 74: 739-789.
184. Schue A. 2009. The mitochondrial hypothesis of age. Labor-Praxis 33: 36-37.
185. Sekijima Y, Wiseman RL, Matteson J, Hammarstrom P, Miller SR, Sawkar AR, Balch WE, Kelly JW. 2005. The biological and chemical basis for tissue-selective amyloid disease. Cell 121: 73-85.
186. Sekijima Y, Dendle MA, Kelly JW. 2006. Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis. Amyloid 13: 236-249.
187. Selkoe DJ. 2004. Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases. Nat Cell Biol 6: 1054-1061.
188. Selkoe DJ. 2008. Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior. Behav Brain Res 192: 106-113.
189. Shan S-o, Walter P. 2005. Cotranslational protein targeting by the signal recognition particle. FEBS Lett 579: 921-926.
190. Shang J, Gao N, Kaufman RJ, Ron D, Harding HP, Lehrman MA. 2007. Translation attenuation by PERK balances ER glycoprotein synthesis with lipid-linked oligosaccharide flux. J Cell Biol 176: 605-616.
191. Singer MA, Lindquist S. 1998. Multiple effects of trehalose on protein folding in vitro and in vivo. Mol Cell 1: 639-648.
192. Smaili S, Hirata H, Ureshino R, Monteforte PT, Morales AP, Muler ML, Terashima J, Oseki K, Rosenstock TR, Lopes GS, et al. 2009. Calcium and cell death signaling in neurodegeneration and aging. Ann Acad Bras Cienc 81: 467-475.
193. Smith DM, Fraga H, Reis C, Kafri G, Goldberg AL. 2011. ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle. Cell 144: 526-538.
194. Steet RA, Chung S, Wustman B, Powe A, Do H, Kornfeld SA. 2006. The iminosugar isofagomine increases the activity of N370S mutant acid β-glucosidase in Gaucher fibroblasts by several mechanisms. PNAS 103: 13813-13818.
195. Taipale M, Jarosz DF, Lindquist S. 2010. HSP90 at the hub of protein homeostasis: Emerging mechanistic insights. Nat Rev Mol Cell Biol 11: 515-528.
196. Tam S, Geller R, Spiess C, Frydman J. 2006. The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nature Cell Biol 8: 1155-1162.
197. Tang Y-C, Chang H-C, Hayer-Hartl M, Hartl FU. 2007. Snapshot: Molecular chaperones, part II. Cell 128: 412.
198. Tang Y-C, Chang H-C, Chakraborty K, Hartl FU, Hayer-Hartl M. 2008. Essential role of the chaperonin folding compartment in vivo. EMBO J 27: 1458-1468.
199. Tanzi RE, Bertram L. 2005. Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective. Cell 120: 545-555.
200. Tatsuta T, Langer T. 2008. Quality control of mitochondria: Protection against neurodegeneration and ageing. EMBO J 27: 306-314.
201. Tojo K, Sekijima Y, Kelly JW, Ikeda S-i. 2006. Diflunisal stabilizes familial amyloid polyneuropathy-associated transthyretin variant tetramers in serum against dissociation required for amyloidogenesis. Neurosci Res 56: 441-449.
202. Trepel J, Mollapour M, Giaccone G, Neckers L. 2010. Targeting the dynamic HSP90 complex in cancer. Nat Rev Cancer 10: 537-549.
203. Tsaytler P, Harding HP, Ron D, Bertolotti A. 2011. Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis. Science 332: 91-94.
204. Vidal M, Cusick ME, Barabasi A-L. 2011. Interactome networks and human disease. Cell 144: 986-998.
205. Voellmy R, Boellmann F. 2007. Chaperone regulation of the heat shock protein response. Adv Exp Med Biol 594: 89-99.
206. Voisine C, Pedersen JS, Morimoto RI. 2010. Chaperone networks: Tipping the balance in protein folding diseases. Neurobiol Dis 40: 12-20.
207. Volchuk A, Ron D. 2010. The endoplasmic reticulum stress response in the pancreatic β-cell. Diabetes, Obes Metab 12: 48-57.
208. Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ, Selkoe DJ. 2002. Naturally secreted oligomers of amyloid b protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416: 535-539.
209. Wang X, Venable J, LaPointe P, Hutt DM, Koulov AV, Coppinger J, Gurkan C, Kellner W, Matteson J, Plutner H, et al. 2006. Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127: 803-815.
210. Weissman L, de S-PNC, Stevnsner T, Bohr VA. 2007. DNA repair, mitochondria, and neurodegeneration. Neuroscience 145: 1318-1329.
211. Wek RC, Jiang HY, Anthony TG. 2006. Coping with stress: eIF2 kinases and translational control. Biochem Soc Trans 34: 7-11.
212. Werner ED, Brodsky JL, McCracken AA. 1996. Proteasomedependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate. Proc Natl Acad Sci 93: 13797-13801.
213. Westerheide SD, Bosman JD, Mbadugha BNA, Kawahara TLA, Matsumoto G, Kim S, Gu W, Devlin JP, Silverman RB, Morimoto RI. 2004. Celastrols as inducers of the heat shock response and cytoprotection. J Biol Chem 279: 56053-56060.
214. Westerheide SD, Morimoto RI. 2005. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J Biol Chem 280: 33097-33100.
215. Westerheide SD, Anckar J, Stevens SM Jr, Sistonen L, Morimoto RI. 2009. Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 323: 1063-1066.
216. Westermark P, Sletten K, Johansson B, Cornwell GG. 1990. Fibril in senile Systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci 87: 2843-2845.
217. Whitesell L, Lindquist SL. 2005. HSP90 and the chaperoning of cancer. Nat Rev Cancer 5: 761-772.
218. Whitesell L, Lindquist S. 2009. Inhibiting the transcription factor HSF1 as an anticancer strategy. Expert Opin Ther Targets 13: 469-478.
219. Williams DB. 2006. Beyond lectins: The calnexin/calreticulin chaperone system of the endoplasmic reticulum. J Cell Sci 119: 615-623.
220. Wiseman RL, Kelly JW. 2011. Cell biology. Phosphatase inhibition delays translational recovery. Science 332: 44-45.
221. Wiseman RL, Johnson SM, Kelker MS, Foss T, Wilson IA, Kelly JW. 2005. Kinetic stabilization of an oligomeric protein by a single ligand binding event. J Am Chem Soc 127: 5540-5551.
222. Wiseman RL, Haynes CM, Ron D. 2010. SnapShot: The unfolded protein response. Cell 140: 590-590. e592.
223. Wisen S, Bertelsen EB, Thompson AD, Patury S, Ung P, Chang L, Evans CG, Walter GM, Wipf P, Carlson HA, et al. 2010. Binding of a small molecule at a protein-protein interface regulates the chaperone activity of Hsp70-Hsp40. ACS Chem Biol 5: 611-622.
224. Wong E, Cuervo AM. 2010. Autophagy gone awry in neurodegenerative diseases. Nat Neurosci 13: 805-811.
225. Yamashita T, Asl KH, Yazaki M, Benson MD. 2005. A prospective evaluation of the transthyretin Ile122 allele frequency in an African-American population. Amyloid 12: 127-130.
226. Yoshida Y. 2003. Quality control of proteins in secretory pathway by N-glycans. Kagaku Kogyo 54: 771-776.
227. Yost HJ, Petersen RB, Linquist S. 1990. RNA metabolism: Strategies for regulation in the heat shock response. Trends Genet 6: 223-227.
228. Young JC, Agashe VR, Siegers K, Hartl FU. 2004. Pathways of chaperone-mediated protein folding in the cytosol. Nature Rev Mol Cell Biol 5: 781-791.
229. Yu L, Ikeda K, Kato A, Adachi I, Godin G, Compain P, Martin O, Asano N. 2006. α-1-C-octyl-1-deoxynojirimycin as a pharmacological chaperone for Gaucher disease. Bioorganic Medicinal Chem 14: 7736-7744.
230. Yu Z, Sawkar AR, Kelly JW. 2007a. Pharmacologic chaperoning as a strategy to treat Gaucher disease. FEBS J 274: 4944-4950.
231. Yu ZQ, Sawkar AR, Whalen LJ, Wong CH, Kelly JW. 2007b. Isofagomine-and 2,5-anhydro-2,5-imino-D-glucitol-based glucocerebrosidase pharmacological chaperones for Gaucher disease intervention. J Medicinal Chem 50: 94-100.
232. Zhang Q, Powers ET, Nieva J, Huff ME, Dendle MA, Bieschke J, Glabe CG, Eschenmoser A, Wentworth P Jr, Lerner RA, et al. 2004. Metabolite-initiated protein misfolding may trigger Alzheimer's disease. Proc Natl Acad Sci 101: 4752-4757.
233. Zhang J, Baker ML, Schroeder GF, Douglas NR, Reissmann S, Jakana J, Dougherty M, Fu CJ, Levitt M, Ludtke SJ, et al. 2010. Mechanism of folding chamber closure in a group II chaperonin. Nature 463: 379-383.
234. Zhao H, Grabowski GA. 2002. Gaucher disease: Perspectives on a prototype lysosomal disease. Cell Molec Life Sci 59: 694-707.
235. Zhu K, Dunner K, McConkey DJ. 2010. Proteasome inhibitors activate autophagy as a cytoprotective response in human prostate cancer cells. Oncogene 29: 451-462.