Modulating proteostasis: Peptidomimetic inhibitors and activators of protein folding

Current Pharmaceutical Design

Volumn 15, Issue 21, 2009, Pages 2488-2507

  Hatahet, Feras ^a   Ruddock, Lloyd W ^a  

^a UNIVERSITY OF OULU   (Finland)

Author keywords

Chemical chaperone; Degradation; Molecular chaperone; Peptidomimetic; Pharmacological chaperone; Protein folding; Proteostasis

Indexed keywords

4 PHENYLBUTYRIC ACID; BACITRACIN; BORTEZOMIB; CAPSAICIN; CYCLOLINOPEPTIDE A; CYCLOPHILIN; CYCLOSPORIN A; DILTIAZEM; GELDANAMYCIN; NITAZOXANIDE; NOVOBIOCIN; PEPTIDOMIMETIC AGENT; RHODOPSIN; SANGLIFEHRIN A; TACROLIMUS; TIZOXANIDE; VERAPAMIL;

ANTINEOPLASTIC ACTIVITY; BINDING AFFINITY; CARBOXYLATION; CELL VIABILITY; CLINICAL TRIAL; CRYSTAL STRUCTURE; CYSTIC FIBROSIS; DISULFIDE BOND; DNA REPLICATION; DOWN REGULATION; DRUG ACTIVITY; DRUG DESIGN; DRUG EFFICACY; ENDOPLASMIC RETICULUM; ENZYME INHIBITION; GASTROINTESTINAL INFECTION; GENE DISRUPTION; HOMEOSTASIS; HUMAN; HYDROPHOBICITY; IONIC STRENGTH; ISOMERIZATION; MULTIPLE MYELOMA; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; REVIEW; THALASSEMIA; UPREGULATION; VIRUS INFECTIVITY; X RAY CRYSTALLOGRAPHY;

CATALYSIS; DOWN-REGULATION; HUMANS; MOLECULAR CHAPERONES; MOLECULAR MIMICRY; PEPTIDES; PROTEIN FOLDING; PROTEIN SYNTHESIS INHIBITORS; PROTEIN TRANSPORT; PROTEINS; UP-REGULATION;

EID: 69249103011     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161209788682343     Document Type: Review

References (343)

1. Balch WE, Morimoto RI, Dillin A, Kelly JW. Adapting proteostasis for disease intervention. Science 2008; 319: 916-9.
2. Rapoport TA. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 2007; 450: 663-9.
3. Cheesman C, Ruddock LW, Freedman RB. The refolding and reassembly of Escherichia coli heat-labile enterotoxin B-subunit: Analysis of reassembly-competent and reassembly-incompetent unfolded states. Biochemistry 2004; 43: 1609-17.
4. Luheshi LM, Crowther DC, Dobson CM. Protein misfolding and disease: From the test tube to the organism. Curr Opin Chem Biol 2008; 12: 25-31.
5. Schaeffer RD, Fersht A, Daggett V. Combining experiment and simulation in protein folding: Closing the gap for small model systems. Curr Opin Struct Biol 2008; 18: 4-9.
6. Baldwin RL. Energetics of protein folding. J Mol Biol 2007; 371: 283-301.
7. Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 1989; 6: 87-103.
8. Schubert U, Anton LC, Gibbs J, Norbury CC, Yewdell JW, Bennink JR. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 2000; 404: 770-4.
9. Vabulas RM, Hartl FU. Protein synthesis upon acute nutrient restriction relies on proteasome function. Science 2005; 310: 1960-3.
10. Paget MS, Buttner MJ. Thiol-based regulatory switches. Annu Rev Genet 2003; 37: 91-121.
11. Ilbert M, Horst J, Ahrens S, Winter J, Graf PC, Lilie H, Jakob U. The redox-switch domain of Hsp33 functions as dual stress sensor. Nat Struct Mol Biol 2007; 14: 556-63.
12. Mesecke N, Terziyska N, Kozany C, Baumann F, Neupert W, Hell K, et al. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 2005; 121: 1059-69.
13. Koehler CM, Beverly KN, Leverich EP. Redox pathways of the mitochondrion. Antioxid Redox Signal 2006; 8:813-22.
14. Singh AK, Bhattacharyya-Pakrasi M, Pakrasi HB. Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms. J Biol Chem. 2008; 283: 15762-70.
15. Beeby M, O'Connor BD, Ryttersgaard DR, Boutz DR, Perry LJ, Yeates TO. The genomics of disulfide bonding and protein stabilization in thermophiles. PloS Biol 2005; 3: 1549-58.
16. Berkmen M, Boyd D, Beckwith J. The nonconsecutive bond of Escherichia coli phytase (AppA) renders it dependent on the protein disulfide isomerase, DsbC. J Biol Chem 2005; 280: 11397-94.
17. Kadokura H, Katzen F, Beckwith J. Protein disulfide bond formation in prokaryotes. Annu Rev Biochem 2003; 72: 111-35.
18. Bardwell JC, McGovern K, Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell 1991; 67: 581-9.
19. Bardwell HC, Lee JO, Jander G, Martin N, Belin D, Beckwith J. A pathway for disulfide bond formation in vivo. Proc Natl Acad Sci USA 1993; 90: 1038-42.
20. Frand AR, Kaiser CA. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1998; 1: 161-70.
21. Frand AR, Kaiser CA. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 1999; 4: 469-77.
22. Tu BP, Ho-Schleyer SC, Travers KJ, Weissman JS. Biochemical basis of oxidative folding in the endoplasmic reticulum. Science 2000; 290: 1571-4.
23. Gross E, Sevier CS, Heldman N, Vitu E, Bentzur M, Kaiser CA, et al. Generating disulfides enzymatically: Reaction product and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc Natl Acad Sci USA 2006; 103: 299-304.
24. Missiakas D, Georgopoulos C, Raina S. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J 1994; 13: 2013-20.
25. Missiakas D, Schwager F, Raina S. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J 1995; 14: 3415-24.
26. Appenzeller-Herzog C, Ellgaard L. The human PDI family: Versatility packed into a single fold. Biochim Biophys Acta 2008; 1783: 535-48.
27. Fabianek RA, Hennecke H, Thony-Meyer L. The active site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo. J Bacterial 1998; 180: 1947-50.
28. Andersen CL, Matthey-Dupraz A, Missiakas D, Raina S. A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins. Mol Microbiol 1997; 26: 121-32.
29. Sevier CS, Cuozzo JW, Vala A, Aslund F, Kaiser CA. A flavoprotein defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat Cell Biol 2001; 3: 874-882.
30. Thorpe C, Hoober KL, Raje S, Glynn NM, Burnside J, Turi GK, et al. Sulfhydryl oxidases: Emerging catalysts of protein disulfide bond formation in eukaryotes. Arch Biochem Biophys 2002; 405: 1-12.
31. Chakravarthi S, Jessop CE, Miller M, Stirling CKJ, Bulleid NJ. Intracellular catalysis of disulfide bond formation by the human suldhydryl oxidase, QSOX1. Biochem J 2007; 404: 403-411.
32. Nørgaard P, Westphal V, tachibana C, Alsøe L, Holst B, Winther JR. Functional differences in yeast protein disulfide isomerases. J Cell Biol 2001; 152: 553-62.
33. Ellgaard L, Ruddock LW. The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep 2005; 6: 28-32.
34. Koivu J, Myllyla R, Helaakoski T, Pihlajaniemi T, Tasanen K, Kivirikko KI. A single polypeptide chain acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfideisomerase. J Biol Chem 1987; 2: 6447-9.
35. Wetterau JR, Combs KA, McLean LR, Spinner SN, Aggerbeck LP. Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein. Biochemistry 1991; 30: 9728-35.
36. Wajih N, Hutson SM, Wallin R. Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum- A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2, 3-epoxide reduction. J Biol Chem 2007; 282: 2626-35.
37. Reinhardt C, von Brühl ML, Manukyan D, Grahl L, Lorenz M, Altmann B, et al. Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation. J Clin Invest 2008; 118: 1110-22.
38. Ellerman DA, Myles DG, Primakoff P. A role for sperm surface protein disulfide isomerase activity in gamete fusion: Evidence for the participation of ERp57. Dev Cell 2006; 10: 831-7.
39. Lahav J, Jurk K, Hess O, Barnes MJ, Farndale RW, Luboshitz J, et al. Sustained integrin ligation involves extracellular free sulhydryls and enzymatically catalysed disulfide exchange. Blood 2002; 100: 2472-8.
40. Tsai B, Rodighiero C, Lencer QI, Rapoport T. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 2001; 104: 937-48.
41. Spooner RA, Watson PD, Marsden CJ, Smith DC, Moore KA, Cook JP, et al. Protein disulphide-isomerase reduces ricin to it's A and B chains in the endoplasmic reticulum. Biochem J 2004; 383: 285-93.
42. Magnuson B, Rainey EK, Benjamin T, Baryshev M, Mkrtchian S, Tsai B. ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding. Mol Cell 2005; 20; 289-300.
43. Markovic I, Stantchev TS, Fields KH, Tiffany LJ, Tomic M, Weiss CD, et al. Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1 envelope-mediated T-cell fusion during viral entry. Blood 2004; 103: 1586-94.
44. Ramachandran GN, Mitra AK. An explanation for the rare occurrence of cis peptide units in proteins and polypeptides. J Mol Biol 1976; 107: 85-92.
45. Hinderaker MP, Raines, RT. An electronic effect on protein structure. Protein Sci 2003; 12: 1188-94.
46. Brandts JF, Halvorson HR, Brennan M. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 1975; 14: 4953-63.
47. n-L-Pro-OH. Biopolymers 1976; 15: 2043-57.
48. Scherer G, Kramer ML, Schutkowski M, Reimer U, Fischer G. Barriers to rotation of secondary amide peptide bonds. J Am Chem Soc 1998; 120, 5568-74.
49. Pahlke D, Freund C, Leitner D, Labudde D. Statistically significant dependence of the Xaa-Pro peptide bond conformation on secondary structure and amino acid sequence. BMC Struct Biol 2005; 5: 8.
50. Jabs A, Weiss M, Hilgenfeld R. Non-proline cis-peptide bonds in proteins. J Mol Biol 1999; 286, 291-304.
51. Schiene-Fischer C, Fischer G. Direct measurement indicates a slow cis/ trans isomerization at the secondary amide peptide bond of glycylglycine. J Am Chem Soc 2001; 123: 6227-31.
52. Scholz C, Scherer G, Mayr LM, Schindler T, Fischer G, Schmid FX. Prolyl isomerases do not catalyze isomerization of non-prolyl peptide bonds. Biol Chem. 1998; 379: 361-5.
53. Pal D, Chakrabati P. Cis peptide bonds in proteins: Residues involved, their conformations, interactions and locations. J Mol Biol 1999: 294, 271-88.
54. Guan RJ, Xiang Y, He XL, Wang CG, Wang M, Zhang Y, et al. Structural mechanism governing cis and trans isomeric states and an intramolecular switch for cis/trans isomerization of a non-proline peptide bond observed in crystal structure of scorpion toxins. J Mol Biol 2004; 341:1189-204.
55. Bouckaert J, Dewallef Y, Poortmans F, Wyns L, Loris R. The structural features of concanavalin A governing non-proline peptide isomerization. J Biol Chem 2000; 275: 19778-87.
56. Schiene-Fischer C, Habazettl J, Schmid FX, Fischer G. The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase. Nat Struct Biol 2002; 9: 419-424.
57. Mallis RJ, Brazin KN, Fulton DB, Andreotti AH. Structural characterization of a proline-driven conformational switch within the Itk SH2 domain. Nat Struct Biol 2002; 9: 900-5.
58. Andreotti AH. Native state proline isomerization: An intrinsic molecular switch. Biochemistry 2003; 42: 9515-24.
59. Liou YC, Sun A, Ryo A, Zhou XZ, Yu ZX, Huang HK, et al. Role of the prolyl isomerase Pin1 in protecting against age-dependent neurodegeneration. Nature 2003; 424: 556-61.
60. Lummis SC, Beene DL, Lee LW, Lester HA, Broadhurst RW, Dougherty DA. Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel. Nature 2005; 438: 248-52.
61. Eckert B, Martin A, Balbach J, Schmid FX. Prolyl isomerization as a molecular timer in phage infection. Nat Struct Mol Biol 2005; 2: 619-23.
62. Nelson CJ, Santos-Rosa H, Kouzarides T. Proline isomerization of histone H3 regulates lysine methylation and gene expression. Cell 2006; 126: 905-16.
63. Shaw PE. Peptidyl-prolyl cis/trans isomerases and transcription: Is there a twist in the tail? EMBO Rep 2007; 8: 40-5.
64. Sarkar P, Recichman C, Saleh T, Birge RB, Kalodimos CG. Proline cis-trans isomerization controls autoinhibition of a signaling protein. Mol Cell 2007; 25: 413-26.
65. Saibil HR. Chaperone machines in action. Curr Opin Struct Biol 2008; 18: 35-42.
66. Bakau B, Weissman J, Horwich AL. Molecular chaperones and protein quality control. Cell 2006; 125: 443-451.
67. Brinker A, Pfeifer G, Kerner M, Naylor DF, Hartl FU, Hayer-Hartl M. Dual function of protein confinement in chaperonin-assisted protein folding. Cell 2001; 107: 223-233.
68. Tang YC, Chang HC, Chakraborty K, Hartl FU, Hayer-Hartl M. Essential role of the chaperonin folding compartment in vivo. EMBO J 2008; 27: 1458-68.
69. Sharma S, Chakraborty K, Müller BK, Astola N, Tang YC, Lamb DC, et al. Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell 2008; 133: 142-53.
70. Liberek K, Lewandowska A, Zietkiewicz S. Chaperones in control of protein disaggregation. EMBO J 2008; 27: 328-35.
71. Kerner MJ, Naylor DJ, Ishihama Y, Maier T, Chang HC, Stines AP, et al. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 2005; 122: 209-20.
72. Neupert W, Herrmann JM. Translocation of proteins into mitochondria. Annu Rev Biochem 2007; 76: 723-49.
73. Chiosis G. Targeting chaperones in transformed systems - a focus on Hsp90 and cancer. Expert Opin Ther Targets. 2006; 10: 37-50.
74. Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 1994; 91: 8324-8.
75. Srivastava PK, Menoret A, Basu S, Binder RJ, McQuade KL. Heat shock proteins come of age: Primitive functions acquire new roles in an adaptive world. Immunity 1998; 8: 657-65.
76. Binder RJ, Blachere NE, Srivastava PK. Heat shock protein-chaperoned peptides but not free peptides introduced into the cytosol are presented efficiently by major histocompatibility complex I molecules. J Biol Chem 2001; 276: 17163-71.
77. Shen J, Chen X, Hendershot L, Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell. 2002; 3: 99-111.
78. Helmbrecht K, Zeise E, Rensing L. Chaperones in cell cycle regulation and mitogenic signal transduction. Cell Prolif 2000; 33: 341-65.
79. Aldea M, Garí E, Colomina N. Control of cell cycle and cell growth by molecular chaperones. Cell Cycle 2007; 6: 2599-603.
80. Nollen EA, Morimoto RI. Chaperoning signaling pathways: Molecular chaperones as stress-sensing 'heat shock' proteins. J Cell Sci. 2002; 115: 2809-16.
81. Nishikawa SI, Fewell SW, Kato Y, Brodsky JL, Endo T. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 2001; 153: 1061-70.
82. Rusconi S, Scozzafava A, Mastrolorenzo A, Supuran CT. An update in the development of HIV entry inhibitors. Curr Top Med Chem 2007; 7: 1273-89.
83. Esté JA, Telenti A. HIV entry inhibitors. Lancet 2007; 370: 81-88.
84. Wild C, Greenwell T, Matthews T. A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion. AIDS Res Hum Retroviruses 1993; 9: 1051-3.
85. Kilby JM, Hopkins S, Venetta TM, DiMassimo B, Cloud GA, Lee JY, et al. Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry. Nat Med; 4: 1302-7.
86. Doranz BJ, Filion LG, Diaz-Mitoma F, Sitar DS, Sahai J, Baribaud F, et al. Safe use of the CXCR4 inhibitor ALX40-4C in humans. AIDS Res Hum Retroviruses 2001; 17: 475-86.
87. Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003; 300: 486-9.
88. Estrada LD, Soto C. Inhibition of protein misfolding and aggregation by small rationally-designed peptides. Curr Pharm Des 2006; 12: 2557-67
89. Estrada LD, Soto C. Disrupting β-amyloid aggregation for alzheimer disease treatment. Curr Top Med Chem 2007; 7: 115-26.
90. Kaneko K, Peretz D, Pan KM, Blochberger TC, Wille H, Gabizon R, et al. Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform. Proc Natl Acad Sci USA 1995; 92: 11160-4.
91. Chabry J, Caughey B, Chesebro B. Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides. J Biol Chem 1998; 273: 13203-7.
92. Soto C, Kascsak RJ, Saborío GP, Aucouturier P, Wisniewski T, Prelli F, et al. Reversion of prion protein conformational changes by synthetic beta-sheet breaker peptides. Lancet 2000; 355: 192-7.
93. Nagai Y, Tucker T, Ren H, Kenan DJ, Henderson BS, Keene JD, et al. Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening. J Biol Chem 2000; 275: 10437-42.
94. Kazantsev A, Walker HA, Slepko N, Bear JE, Preisinger E, Steffan JS, et al. A bivalent Huntingtin binding peptide suppresses polyglutamine aggregation and pathogenesis in Drosophila. Nat Genet 2002; 30: 367-76.
95. Nagai Y, Fujikake N, Ohno K, Higashiyama H, Popiel HA, Rahadian J, et al. Prevention of polyglutamine oligomerization and neurodegeneration by the peptide inhibitor QBP1 in Drosophila. Hum Mol Genet 2003; 12: 1253-9.
96. Bodles AM, El Agnaf OM, Greer B, Guthrie DKJ, Irvine GB. Inhibition of fibril formation and toxicity of a fragment of α-synuclein by a N-methylated peptide analogue. Neurosci Lett 2004; 359: 89-93.
97. Sode K, Usuzaka E, Kobayashi N, Ochiai S. Engineered α-synuclein prevents wild type and familial Parkin variant fibril formation. Biochem Biophys Res Commun 2005; 335: 432-6.
98. Kapurniotu A, Schmauder A, Tenidis K. Structure-based design and study of non-amyliodogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity. J Mol Biol 2002; 315: 339-50.
99. Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, Liosatos M, et al. Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 1998; 95: 6448-53.
100. Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, et al. Naturally secreted oligomers of amyloid b protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002; 416: 535-9.
101. Garbi N, Tanaka S, Momburg F, Hammerling GJ. Impaired assembly of the major histocompatability complex class I peptide-loading in mice deficient in the oxidoreductase ERp57. Nat Immunol 2006; 7: 93-102.
102. Mesaeli N, Nakamura K, Zvaritch E, Dickie P, Dziak E, Krause KH, et al. Calreticulin is essential for cardiac development. J Cell Biol 1999; 144: 857-68.
103. Denzel A, Molinari M, Triqueros C, Martin JE, Velmurgan S, Brown S, et al. Early postnatal death and motor disorders in mice congenitally deficient in calnexin expression. Mol Cell Biol 2002; 22: 7398-404.
104. Luo S, Mao C, Lee B, Lee AS. GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development. Mol Cell Biol 2006; 26: 5688-97.
105. Nagai N, Hosokawa M, Itohara S, Adachi E, Matsushita T, Hosokawa N, et al. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. J Cell Biol 2000; 150: 1499-506.
106. Reimold AM, Etkin A, Clauss I, Perkins A, Friend DS, Zhang J, et al. An essential role in liver development for transcription factor XBP-1. Genes Dev 2000; 14: 152-7.
107. Lee K, Tirasophon W, Shen X, Michalak M, Prywes R, Okada T, et al. IRE-1 mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev 2002; 16: 452-66.
108. Zhang K, Wong HN, Song B, Miller CN, Scheuner D, Kaufman RJ. The unfolded protein response sensor IRE1α is required at 2 distinct steps in B cell lymphopoiesis. J Clin Invest. 2005; 115: 268-81.
109. Okiyoneda T, Niibori A, Harada K, Kohno T, Michalak M, Duszyk M, et al. Role of calnexin in the ER quality control and productive folding of CFTR; differential effect of calnexin knockout on wildtype and ΔF508 CFTR. Biochim Biophys Acta 2008; 1783: 1585-94.
110. Stamnes MA, Shieh BH, Chuman L, Harris GL, Zuker CS. The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins. Cell 1991; 65: 219-227.
111. Nagata K. Hsp47: A collagen-specific molecular chaperone. Trends Biochem Sci 1996: 21: 22-26.
112. Kadokura H, Tian H, Zander T, Bardwell JCA, Beckwith J. Snapshots of DsbA in action: Detection of proteins in the process of oxidative folding. Science 2004; 303: 534-7.
113. Yu K, Webb H, Hirst TR. A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae. Mol Microbial 1992; 6: 1949-58.
114. Hirst TR In: Moss J, Iglewski B, Vaughan M and Tu AT Eds, Bacterial toxins and virulence factors in disease, Handbook of natural toxins. New York: Marcel Decker 19P5; vol. 8: pp. 123-184.
115. Spangler BD. Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin. Microbiol Rev 1992; 56: 623-47.
116. Goeckeler JL, Petruso AP, Aquirre J, Clement CC, Chiosis G, Brodsky JL. The yeast Hsp100, Sse1p, exhibits high-affinity peptide binding. FEBS Lett 2008; 582: 2393-6.
117. Wilkinson B, Gilbert HF. Protein disulfide isomerase. Biochim Biophys Acta 2004; 1699: 35-44.
118. Wiertz E, Hill A, Tortorella D, Ploegh H. Cytomegaloviruses use multiple mechanisms to elude the host immune response. Immunol Lett 1997; 57: 213-216.
119. Willey RL, Maldarelli F, Martin MA, Strebel K. Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4. J Virol 1992; 66: 7193-7200.
120. Gidalevitz T, Ben-Zvi A, Ho KH, Brignull HR, Morimoto RI. Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 2006; 311: 1471-74.
121. Goldberger RF, Epstein CJ, Anfinsen CB. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J Biol Chem 1963; 238: 628-35.
122. Gorlacj A, Klappa P, Kietzman T. The endoplasmic reticulum: Folding, calcium homeostasis, signaling and redox control. Antioxid Redox Signal 2006; 8: 1391-418.
123. Park B, Lee S, Kim E, Cho K, Riddell SR, Cho S, et al. Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 2006; 127: 369-82.
124. Gallina A, Hanley TM, Mandel R, Trahey M, Broder CC, Viglianti GA, et al. Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry. J Biol Chem 2002; 277: 50579-88.
125. Jordan PA, Stevens JM, Hubbard GP, Barrett NE, Sage T, Authi KS, et al. A role for the thiol isomerase protein ERP5 in platelet function. Blood 2005; 105: 1500-7.
126. Griffith OW, Meister A. Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine). J Biol Chem 1979; 254: 7558-60.
127. Chakravarthi S, Bulleid NJ. Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway. J Biol Chem 2004; 279: 39872-9.
128. Mandel R, Ryser HJ, Ghani F, Wu M, Peak D. Inhibition of a reductive function of the plasma membrane by bacitracin and antibodies against protein disulfide-isomerase. Proc Natl Acad Sci USA 1993; 90: 4112-6.
129. Ryser HJ, Levy EM, Mandel R, DiSciullo GJ. Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disufide interchange upon virus-receptor interaction. Proc Natl Acad Sci USA 1994; 91: 4559-63.
130. Orlandi PA. Protein-disulfide isomerase-mediated reduction of the A subunit of cholera toxin in a human intestinal cell line. J Biol Chem 1997, 4591-9.
131. Essex DW, Li M, Miller, A, Feinman RD. Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation. Biochemistry 2001; 40: 6070-5.
132. Lahav J, Jurk K, Hess O, Barnes MJ, Farndale RW, Luboshitz J, et al. Sustained integrin ligation involved extracellular free sulhydryls and enzymatically catalysed disulfide exchange. Blood 2002; 10: 2472-8.
133. Janiszewski M, Lopes LR, Carmo AO, Pedro MA, Brandes RP, Santos CX, et al. Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells. J Biol Chem 2005; 280: 40813-9.
134. Goplen D, Wang J, Enger PØ, Tysnes BB, Terzis AJ, Laerum OD, et al. Protein disulfide isomerase expression is related to the invasive properties of malignant glioma. Cancer Res 2006; 66, 9895-902.
135. Ellerman DA, Myles DG, Primakoff P. A role for sperm surface protein disulfide isomerase activity in gamete fusion: Evidence for the participation of Erp57. Dev Cell 2006; 10: 831-7.
136. Lovat PE, Corazzari M, Armstrong JL, Martin S, Pagliarini V, Hill D, et al. Increasing melanoma cell death using inhibitors of protein disulfide isomerases to abrogate survival responses to endoplasmic reticulum stress. Cancer Res 2008; 68: 5363-9.
137. Johnson BA, Anker FL, Meleney FL. Bacitracin: A new antibiotic produced by a member of the B.Subtilis group. Science 1945: 376-7.
138. Meleney FL, Johnson BA. Bacitracin. Am J Med 1949: 794-806.
139. Ming LJ, Epperson JD. Metal binding and structure-activity relationship of the metalloantibiotic peptide bacitracin. J Inorg Biochem 2002; 91: 46-58.
140. Pfeffer S, Höhne W, Branner S, Wilson K, Betzel C X-ray structure of the antibiotic bacitracin A. FEBS Lett 1991; 285: 115-9.
141. Pfeffer-Hennig S. Dauter Z, Hennig M, Höhne W, Wilson K, Betzel C. Three dimensional structure of the antibiotic bacitracin A complexed to two different subtilisin proteases: Novel mode of action of enzyme inhibition. Adv Exp Med Biol 1996; 379: 29-41.
142. Kang JW, De Reymaeker G, Van Schepdael A, Roets E, Hoogmartens J. Analysis of bacitracin by micellar electrokinetic capillary chromatography with mixed micelle in acidic solution. Electrophoresis 2001; 22: 1356-62.
143. Roth RA. Bacitracin: An inhibitor of the insulin degrading activity of glutathione-insulin transhydrogenase. Biochem Biophys Res Commun 1981; 98: 431-438.
144. Rogelj S, Reiter KJ, Kesner L, Li M, Essex D. Enzyme destruction by a protease contaminant in bacitracin. Biochem Biophys Res Commun 2000; 273: 829-32.
145. Hiroi T, Okada K, Imaoka S, Osada M, Funae Y. Bisphenol A bind to protein disulfide isomerase and inhibits its enzymatic and hormone binding activities. Endocrinology 2006; 147: 2773-80.
146. Hashimoto S, Okada K, Imaoka S. Interaction between bisphenol derivatives and protein disulfide isomerase (PDI) and inhibition of PDI functions: Requirement of chemical structure for binding to PDI. J Biochem 2008; 144: 335-42.
147. Müller J, Naguleswaran A, Muller N, Hemphill A. Neospora caninum: Functional inhibition of protein disulfide isomerase by the broad-spectrum anti-parasitic drug nitazoxanide and other thiazolides. Experimental Parasitology 2008; 118: 80-8.
148. Rossignol J. US patent application: US2007/0015803 A1.
149. Müller J, Wastling J, Sanderson S, Müller N, Hemphill A. A novel Giardia lambila nitroreductase, GINR1, interacts with nitazoxanide and other thiazolides. Antimicrob Agents Chemother 2007; 51: 1979-86.
150. Mégraud F, Occhialini A, Rossignol JF. Nitazoxanide, a potential drug for eradication of Helicobacter pylori with no cross-resistance to metronidazole. Antimicrob Agents Chemother 1998; 42: 2836-40.
151. Adagu IS, Nolder D, Warhurst DC, Rossignol JF. In vitro activity of nitazoxanide and related compounds against isolates of Gardia intestinalis, Entamoeba histolytica and Trichomonas vaginalis. J Antimicrob Chemother 2002; 49: 103-11.
152. Pankuch GA, Appelbaum PC. Activities of tizoxanide and nitrazoxanide compared to those of five other thiazolides and three other agents against anaerobic species. Antimicrob Agents Chemother 2006; 50: 1112-7.
153. Cortes HC, Mueller N, Esposito M, Leitão A, Naguleswaran A, Hemphill A. In vitro efficacy of nitro- and bromo-thiazolylsalicylamide compounds (thiazolides) against Besnoitia besnoiti infection in Vero cells. Parasitology 2007; 134: 975-85
154. Korba BE, Montero AB, Farrar K, Gaye K, Mukerjee S, Ayers MS, et al. Nitazoxanide, tizoxanide and other thiazolides are potent inhibitors of hepatitis B virus and hepatitis C virus replication. Antiviral Res 2008; 77: 56-63.
155. Borel JF, Feurer C, Gubler HU, Stahelin H Biological effects of cyclosporin A: A new antilymphocytic ageent. Agents Actions 1976; 6: 468-75.
156. Kino T, hatanaka H, Hashimoto M, Nishiyama M, Goto T, Okuhara M, et al. FK-506, a novel immunosuppressant isolated from a Streptomyces I. Fermentation, isolation and physico-chemical and biological properties. J Antibiot (Tokyo) 1987; 40: 1249-55.
157. Handschumacher RE, Harding MW, Rice J, Drugge RJ, Speicher DW. Cyclophilin: A specific cytosolic binding protein for cyclosporin A. Science 1984; 226: 544-547.
158. Fischer G, Bang H, Mech C Determination of enzymatic catalysis for the cis-trans isomerization of peptide binding in proline containing peptides. Biomed Biochim Acta 1984; 43: 1101-11.
159. Takahashi N, Hayano T, Suzuki M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 1989; 337: 473-5.
160. Fisher G, Wittmann-Liebold B, Lang K, Kiefhaber T, Schmid FX. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 1989; 337: 476-8.
161. Finn RD, Tate J, Mistry J, Coggill PC, Sammut SJ, Hotz HR, et al. The Pfam protein families database. Nucleic Acids Res 2008; 36: D281-8.
162. Dolinski K, Muir S, Cardenas M, Heitman J. All cyclophilins and FK506 binding proteins are individually and collectively dispensable for viability in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 1997; 94: 13093-8.
163. Wang P, Heitman J. The cyclophilins. Genome Biol 2005; 6: 226.
164. Liu J, Farmer JD Jr, Lane WS, Friedman J, Weissman I, Schreiber SL. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 1991; 66: 807-15.
165. Jin L, Harrison SC. Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin. Proc Natl Acad Sci USA 2002; 99: 13522-6.
166. Huai Q, Kim HY, Liu Y, Zhao Y, Mondragon A, Liu JO, et al. Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc Natl Acad Sci USA 2002; 99: 12037-42.
167. Liu J, Albers MW, Wandless TJ, Luan S, Alberg DG, Belshaw PJ, et al. Inhibition of T cell signaling by immunophilin-ligand complexes correlates with loss of calcineurin phosphatase activity. Biochemistry 1992; 31: 3896-901.
168. O'Keefe SJ, Tamura J, Kincaid RL, Tocci MJ, O'Neill EA. FK-506 and CsA-sensitive activation of the interleukin-2 promoter by calcineurin. Nature 1992; 357: 692-4.
169. Foor F, Parent SA, Morin N, Dahl AM, Ramadan N, Chrebet G, et al. Calcineurin mediates inhibition by FK506 and cyclosporin of recovery from alpha-factor arrest in yeast. Nature 1992; 360: 682-684.
170. Breuder T, Hemenway CS, Movva NR, Cardenas ME, Heitman J. Calcineurin is essential in cyclosporin A- and FK506-sensitive yeast strains. Proc Natl Acad Sci USA 1994; 91: 5372-6.
171. Odom A, Muir S, Lim E, Toffaletti DL, Perfect J, Heitman J. Calcineurin is required for virulense of Cryptococcus neoformans. EMBO J 1997; 16: 2576-89.
172. Luban J, Bossolt KL, Franke EK, Kalpana GV, Goff SP. Human immunodeficiency virus type I Gag protein binds to cyclophilins A and B. Cell 1993; 73: 1067-78.
173. Franke EK, Yuan HE, Luban J. Specific incorporation of cyclophilin A into HIA-1 virions. Nature 1994; 372: 359-62.
174. Thali M, Bukovsky A, Kondo E, Rosenwirth B, Walsh CT, Sodroski J, et al. Functional association of cyclophilin A with HIV-1 virions. Nature 1994; 372: 363-5.
175. Luban J. Absconding with the chaperone: Essential cyclophilin-Gag interaction in HIV-1 virions. Cell 1996; 87: 1157-59.
176. Braaten D, Franke EK, Luban J. Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type I before initiation of reverse transcription. J Virol 1996; 70: 3551-60.
177. Braaten D, Luban J. Cyclophilin A regulates HIV-1 infectivity as demonstrate by gene targeting in human T cells. EMBO J 2001; 20: 1300-9.
178. Bosco DA, Eisenmesser EZ, Pochapsky S, Sundquist WI, Kern D. Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A. Proc Natl Acad Sci USA 2002; 99: 5247-52.
179. Yang WM, Inouye CJ, Seto E. Cyclophilin A and FKBP12 interact with YY1 and alter its transcriptional activity. J Biol Chem 1995; 270: 15187-93.
180. Brazin KN, Mallis RJ, Fulton DB, Andreotti AH. Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A. Proc Natl Acad Sci USA 2002; 99: 1899-904.
181. Mallis RJ, Brazin KN, Fulton DB, Andreotti AH. Structural characterization of a proline-driven conformational switch within the Itk SH2 domain. Nat Struct Biol 2002; 9: 900-5.
182. Leverson JD, Ness SA. Point mutations in v-Myb disrupt a cyclophilin-catalysed negative regulatory mechanism. Mol Cell 1998; 1: 203-211.
183. Rycyzyn MA, Clevenger CV. The intranuclear prolactin/cyclophilin B complex as a transcriptional inducer. Proc Natl Acad Sci USA 2002; 99: 6790-5.
184. Obata Y, Yamamoto K, Miyazaki M, Shimotohno K, Kohno S, Matsuyama T. Role of cyclophilin B in activation of interferon regulatory factor-3. J Biol Chem 2005; 280: 18355-60.
185. Lin DT, Lechleiter JD. Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization. J Biol Chem 2002; 277: 31134-41.
186. Nakagawa T, Shimizu S, Watanabe T, Yamaguchi O, Otsu K, Yamagata H, et al. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 2005; 434: 652-8.
187. Baines CP, Kaiser RA, Purcell NH, Blair NS, Osinsja, H, Hambleton MA, et al. Loss of cyclophilin D reveals critical role for mitochondrial permeability transition in cell death. Nature 2005; 434: 658-62.
188. Zydowsky LD, Etzkorn FA, Chang HY, Ferguson SB, Stolz LA, Ho SI, et al. Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition. Protein Sci 1992; 1: 1092-9.
189. Kaufmann HP, Tobschirbel A Über ein oligopeptide aus Leinsamen. Chem Ber 1959; 92: 2805-9.
190. Wieczorek Z, Bengtsson B, Tronjar J, Siemion IZ. Immunosuppressive activity of cyclolinopeptide A. Pept Res 1991; 4: 275-83.
191. Gaymes TJ, Cebrat M, Siemion IZ, Kay JE. Cyclolinopeptide A (CLA) mediate its immunosupressive activity through cyclophilin-dependent calcineurin inactivation. FEBS Lett 1997; 418: 224-7.
192. Górski A, Kasprzycka M, Nowaczyk M, Wieczoreck Z, Siemion IZ, Szelejewski W, et al. Cyclolinopeptide: A novel immunosuppressive agent with potential anti-lipemic activity. Transplant Proc 2001; 33: 553.
193. Sanglier JJ, Quesniaux V, Fehr T, Hofmann H, Mahnke M, memmert K, et al. Sanglifehrins A, B, C and D, novel cyclophilin-binding compounds isolated from Streptomyces sp. A92-308110. I. Taxonomy, fermentation, isolation and biological activity. J Antibiot (Tokyo) 1999; 52: 466-73.
194. Fehr T, Kallen J, Oberer L, Sanglier JJ, Schilling W. Sanglifehrins A, B, C and D, novel cyclophilin-binding compounds isolated from Streptomyces sp. A92-308110. II. Structure elucidation, stereo-chemistry and physico-chemical properties. J Antibiot (Tokyo) 1999; 52: 474-479.
195. Zenke G, Strittmatter U, Fuchs S, Quesniaux VF, Brinkmann V, Schuler W, et al. Sanlifehrin A, novel cyclophilin-binding compound showing immunosuppressive activity with a new mechanism of action. J Immunol 2001; 166: 7165-71.
196. Zhang LH, Liu JO. Sanglifehrin A, a novel cyclophilin-binding immunosuppressant, inhibits IL-2-dependent T cell proliferation at the G1 phase of the cell cycle. J Immunol 2001; 166: 5611-8.
197. Zhang LH, Youn HD, Liu JO. Inhibition of cell cycle progression by the novel cyclophilin ligand sanglifehrin A is mediated through NFkappa B-dependent activation of p53. J Biol Chem 2001; 276: 43534-40.
198. Steinschulte C, Taner T, Thomson AW, Bein G, Hackestein H. Cutting edge: sanglifehrin A, a novel cyclophilin-binding immunosuppressant blocks bioactive IL-12 production by human dendritic cells. J Immunol 2003; 171: 542-6.
199. Kallen J, Sedrani R, Zenke G, Wagner J. Structure of human cyclophilin A in complex with the novel immunosuppresant sanglifehrin A at 1.6Å resolution. J Biol Chem 2005; 280: 21965-71.
200. Sedrani R, Kallen J, Martin Cabrejas LM, Papageorgiou CD, Senia F, Rohrbach S, et al. Sanglifehrin-cyclophilin interaction: degradation work, synthetic macrocyclic analogues, x-ray structure, and binding data. J Am Chem Soc 2003; 125: 3349-59.
201. Hackstein H, Steinschulte C, Fiedel S, Eisele A, Rathke V, Stadlbauer T, et al. Sanflifehrin A blocks key dendritic cell functions in vivo and promotes long-term allograft survival together with low-dose CsA. Am J Transplant 2007; 7: 789-98.
202. Woltman AM, Schlagwein N, van der Kooij SW, van Kooten C. A novel cyclophilin-binding drug sanglifehrin A specifically affects antigen uptake receptor expression and endocytic capacity of human dendritic cells. J Immunol 2004; 172: 6482-9.
203. Wang XJ, Etzkorn FA. Peptidyl-prolyl isomerase inhibitors. Biopolymers 2006; 84: 125-46.
204. Kallen J, Walkinshaw MD. The X-ray structure of a tetrapeptide bound to the active site of human cyclophilin A. FEBS Letts 1992; 300: 286-90.
205. Ke H, Mayrose D, Cao W. Crystal structure of cyclophilin A complexed with substrate Ala-Pro suggests a solvent-assisted mechanism of cis-trans isomerization. Proc Natl Acad Sci USA 1993; 90: 3324-8.
206. Zhao Y, Ke H Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes. Biochemistry 1996; 35: 7362-8.
207. Zhao Y, Ke H. Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization. Biochemistry 1996; 35: 7356-61.
208. Hart SA, Etzkorn FA. Cyclophilin inhibition by a (Z)-Alkene cis-Proline mimic. J Org Chem 1999; 64: 2998-9.
209. Germanas JP, Kim K, Dumas JP. Toward rationally designed peptidyl-prolyl isomerase inhibitors. Adv Amino Acid Mimetics Peptidomimetics 1997; 1: 233-50.
210. Wang HC, Jim K, Bakhitiar R, Germanas JP Structure-activity studies of ground- and transition-state analogue inhibitors of cyclophilin. J Med Chem 2001; 44: 2593-600.
211. 2R-CH)Pro as potential inhibitors of the human cyclophilin hCyp-18. Tetrahedron Lett 2001; 42: 6295-7.
212. Demange L, Moutiez M, Dugave CJ. Synthesis and evaluation of Glypsi(PO(2)R-N)Pro-containing pseudopeptides as novel inhibitors of the human cyclophilin hCyp-18. J Med Chem 2002; 45: 3928-33.
213. Wu YQ, Belyakov S, Choi C, Limburg D, Thomas IV BE, Vaal M, et al. Synthesis and biological evolution of non-peptidic cyclophilin ligands. J Med Chem 2003; 46: 1112-5.
214. Li Q, Moutiez M, Charbonnier JB, Vaudry K, Ménez A, Quéméneur E, et al. Design of a Gag pentapeptide analogue that binds human cyclophilin A more effectively than the entire capsid protein: New insights for the development of novel anti-HIV1 drugs. J Med Chem 2000; 43: 1770-9.
215. Fox DS, Cruz MC, Sia RA, Ke H, Cox GM, Cardenas ME, et al. Calcineurin regulatory subunit is essential for virulence and mediates interactions with FKBP12-FK506 in Cryptococcus neoformans. Mol Microbiol 2001; 39: 835-49.
216. Rahfeld JU, Rücknagel KP, Schelbert B, Ludwig B, Hacker J, Mann K, et al. Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin. FEBS Lett 1994; 352: 180-4.
217. Lu KP, Zhou XZ. The prolyl isomerase PIN1: A pivotal new twist in phosphorylation signaling and disease. Nature Rev 2007; 8: 904-916.
218. Lu PJ, Zhou XZ, Shen M, Lu KP. A function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 1999; 283: 1325-8.
219. Yaffe MB, Schutkowski M, Shen M, Zhou XZ, Stukenberg PT, Rahfeld JU, et al. Sequence-specific and phosphorylation-dependent proline isomerization: A potential mitotic regulatory mechanism. Science 1997; 278: 1957-60.
220. Ranganathan R, Lu KP, Hunter T, Noel JP. Structural and functional analysis of the mitotic peptidyl-prolyl isomerase Pin1 suggests that substrate recognition is phosphorylation dependent. Cell 1997; 89: 875-86.
221. Wintjens R, Wieruszeski JM, Drobecq H, Rousselot-Paillet P, Buée L, Lippens G, et al. 1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides. J Biol Chem 2001; 276: 25150-6
222. Verdecia MA, Bowman ME, Lu KP, Hunter T, Noel JP. Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat Struct Biol 2000; 7: 639-43.
223. Hennig L, Christner C, Kipping M, Schelbert B, Rücknagel KP, Grabley S, et al. Selective inactivation of parvulin-like peptidylprolyl cis/trans isomerases by juglone. Biochemistry 1998; 37: 5953-60
224. Webb JL. Enzyme and Metabolic Inhibitors. New York: Academic Press 1966; vol. 3.
225. Chao SH, Greenleaf AL, Price DH. Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription. Nucleic Acids Res 2001; 29: 767-73.
226. Cenas N, Prast S, Nivinskas H, Sarlauskas J, Arnér ES. Interactions of nitroaromatic compounds with the mammalian selenoprotein thioredoxin reductase and the relation to induction of apoptosis in human cancer cells. J Biol Chem 2006; 281: 5593-603.
227. Inbaraj JJ, Chignell CF. Cytotoxic action of juglone and plumbagin: A mechanistic study using HaCaT keratinocytes. Chem Res Toxicol 2004; 17: 55-62.
228. Fila C, Metz C, van der Sluijs P. Juglone inactivates cysteine-rich proteins required for progression through mitosis. J Biol Chem 2008; 283: 21714-24.
229. Zhang Y, Fussel S, Reimer U, Schutkowski M, Fischer G. Substrate-based design of reversible Pin1 inhibitors. Biochemistry 2002; 41: 11868-77
230. Wang XJ, Xu B, Neiler FK, Mullins AB, Etzkorn FA. Conformationally locked isostere of phosphoSer-cis-Pro inhibits Pin1 23-fold better than phosphoSer-trans-Pro isostere. J Am Chem Soc 2004; 126: 15533-42.
231. Zhao S, Etzkorn FA. A phosphorylated prodrug for the inhibition of Pin1. Bioorg Med Chem Lett 2007; 17: 6615-18.
232. Uchida T, Takamiya M, Takahashi M, Miyashita H, Ikeda H, Terada T, et al. Pin1 and Par14 peptidyl prolyl isomerase inhibitors block cell proliferation. Chem Biol 2003; 10: 15-24.
233. Wildemann D, Erdmann F, Alvarez BH, Stoller G, Zhou XZ, Fanghänel J, et al. Nanomolar inhibitors of the peptidyl prolyl cis/ trans isomerase Pin1 from combinatorial peptide libraries. J Med Chem 2006; 49: 2147-50.
234. Blond-Elguindi S, Cwirla SE, Dower WJ, Lipshutz RJ, Sprang SR, Sambrook JF, et al. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 1993; 75: 717-28.
235. Powers MV, Workman P. Inhibitors of the heat shock response: Biology and pharmacology. FEBS Lett 2007; 581: 3758-69.
236. Didelot C, Lanneau D, Brunet M, Joly AL, De Thonel A, Chiosis G, et al. Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins. Curr Med Chem 2007; 14: 2839-47.
237. Brodsky JL, Chiosis G. Hsp70 molecular chaperones: Emerging roles in human disease and identification of small molecule modulators. Curr Top Med Chem 2006; 6: 1215-25.
238. Nadler SG, Tepper MA, Schacter B, Mazzucco CE. Interaction of the immunosuppressant deoxyspergualin with a member of the Hsp70 family of heat shock proteins. Science 1992; 258: 484-6.
239. Nadeau K, Nadler SG, Saulnier M, Tepper MA, Walsh CT. Quantification of the interaction of the immunosuppressant deoxyspergualin and analogs with Hsc70 and Hsp90. Biochemistry 1994; 33: 2561-7.
240. Nadler SG, Dischino DD, Malacko AR, Cleaveland JS, Fujihara SM, Marquardt H. Identification of a binding site on Hsc70 for the immunosuppressant 15-deoxyspergualin. Biochem Biophys Res Commun 1998; 253: 176-80.
241. Freeman BC, Myers MP, Schumacher R, Morimoto RI. Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J 1995; 14: 2281-92.
242. Fewell SW, Day BW, Brodsky JL. Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis. J Biol Chem 2001; 276: 910-4.
243. Fewell SW, Smith CM, Lyon MA, Dumitrescu TP, Wipf P, Day BW, et al. Small molecule modulators of endogenous and cochaperone-stimulated Hsp70 ATPase activity. J Biol Chem 2004; 279: 51131-40.
244. Jiang C, Fang SL, Xiao YF, O'Connor SP, Nadler SG, Lee DW, et al. Partial restoration of cAMP-stimulated CFTR chloride channel activity in ΔF508 cells by deoxyspergualin. Am J Physiol 1998; 275: C171-8.
245. Ramya TN, Karmodiya K, Surolia A, Suorlia N. 15-deoxyspergualin primarily targets the trafficking of apicoplast proteins in Plasmodium falciparum. J Biol Chem 2007; 282: 6388-97.
246. Schmitt E, Parcellier A, Gurbuxani S, Cande C, Hammann A, Morales MC, et al. Chemosensitization by a non-apoptogenic heat shock protein 70-binding apoptosis-inducing factor mutant. Cancer Res 2003; 63: 8233-40.
247. Schmitt E, Maingret L, Puig PE, Rerole AL, Ghiringhelli F, Hammann A, et al. Heat shock protein 70 neutralization exerts potent antitumor effects in animal models of colon cancer and melanoma. Cancer Res 2006; 66: 4191-7.
248. Liebscher M, Jahreis G, Lücke C, Grabley S, Raina S, Schiene-Fischer C. Fatty acyl benzamido antibacterials based on inhibition of DnaK-catalysed protein folding. J Biol Chem 2007; 282: 4437-46.
249. Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005; 5: 761-772.
250. Calderwood SK, Khaleque MA, Sawyer DB, Ciocca DR. Heat shock proteins in cancer: Chaperones of tumorigenesis. Trends Biochem Sci 2006; 31: 164-171.
251. Lewis RJ, Singh OM, Smith CV, Skarynski T, Maxwell A, Wonacott AJ, et al. The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by x-ray crystallography. EMBO J 1996; 15: 1412-20.
252. Sharma SV, Agatsuma T, Nakano H. Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol. Oncogene 1998; 16: 2639-45.
253. Guarnieri MT, Zhang L, Shen J, Zhao R. The Hsp90 inhibitor radicicol interacts with the ATP-binding pocket of bacterial sensor kinase PhoQ. J Mol Biol 2008; 379: 82-93.
254. Blagg BSJ, Kerr TD. Hsp90 inhibitors: Small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation. Med Res Rev 2006; 26: 310-38.
255. Sharp S, Workman P. Inhibitors of the HSP90 molecular chaperone: Current Status. Adv Cancer Res 2006; 95: 323-48.
256. Taldone T, Gozman A, Maharaj R, Chiosis G. Trageting Hsp90: small-molecule inhibitors and their clinical development. Curr Opin Pharmacol 2008; epub ahead of print.
257. Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH Identification and structural characterization of the ATP/ADPbinding site in the Hsp90 molecular chaperone. Cell 1997; 90: 65-75.
258. Felts SJ, Owen BA, Nguyen P, Trepel J, Donner DB, Toft DO. The hsp-90 related protein TRAP1 is a mitochondrial protein with distinct functional properties. J Biol Chem 2000; 275: 3305-12.
259. Supko JG, Hickman RL, Grever MR, Malspeis L. Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent. Cancer Chemother Phramacol 1995; 36: 305-15.
260. Schulte TW, Neckers LM. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to Hsp90 and shares important biological activities with geldanamycin. Cancer Chemother Pharmacol 1998; 42: 273-9.
261. Sydor JR, Normant E, Pien CS, Porter JR, Ge J, Grenier L, et al. Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90. Proc Natl Acad Sci USA 2006; 103: 17408-13.
262. Martin CJ, Gaisser S, Challis IR, Carletti I, Wilkinson B, Gregory M, et al. Molecular characterization of macbecin as an Hsp90 inhibitor. J Med Chem 2008; 51: 2853-7.
263. Gellert M, O'Dea MH, Itoh T, Tomizawa J. Novobiocin and coumermycin inihibit DNA supercoiling catalysed by DNA gyrase. Proc Natl Acad Sci USA 1976; 73: 4474-8.
264. Marcu MG, Schulte TW, Neckers L. Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J Natl Cancer Inst 2000; 92: 242-8.
265. Marcu MG, Chadli A, Bouhouche I, Catelli M, Neckers LM. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J Biol Chem 2000; 275: 37181-6.
266. Yu XM, Shen G, Neckers L, Blake H, Holzbeirlein J, Cronk B, et al. Hsp90 inhibitors identified from a library of novobiocin analogues. J Am Chem Soc 2005; 127: 12778-9.
267. Burlison JA, Neckers L, Smith AB, Maxwell A, Blagg BSJ. Novobiocin: Redesigning a DNA gyrase inhibitor for selective inhibition of Hsp90. J Am Chem Soc 2006; 128: 15529-36.
268. Le Bras G, Radanyi C, Peyrat JF, Brion JD, Alami M, Marsaud V, et al. New novobiocin analogues as antiproliferative agents in breast cancer cells and potential inhibitors of heat shock protein 90. J Med Chem 2007; 50: 6189-200.
269. Burlison JA, Avila C, Vielhauer G, Lubbers DJ, Holzbeierlein J, Blagg BSJ. Development of novobiocin analogues that manifest anti-proliferative activity against several cancer cell lines. J Org Chem 2008; 73: 2130-7.
270. Radanyi C, Le Bras G, Messaoudi S, Bouclier C, Peyrat JF, Brion JD, et al. Synthesis and biological activity of simplified denoviose-coumarins related to novobiocin as potent inhibitors of heat-shock protein 90 (hsp90). Bioorg Med Chem Lett 2008; 18: 2495-8
271. Hutchinson KA, Fox IH. Purification and characterization of the adenosine A2-like binding site from human placental membrane. J Biol Chem 1989; 264: 19898-903.
272. Hutchinson KA, Nevins B, Perini F, Fox IH. Soluble and membrane-associated human low affinity adenosine binding protein (adenotin): Properties and homology with mammalian and avian stress proteins. Biochemistry 1990; 29: 5138-44.
273. Rosser MFN, Nicchitta CV. Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone GRP94. J Biol Chem 2000; 275: 22798-805.
274. Soldano KL, Jivan A, Nicchitta CV, Gewirth DT. Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation. J Biol Chem 2003; 279: 48330-8.
275. Plescia J, Salz W, Xia F, Pennati M, Zaffaroni N, Daidone MG, et al. Rational design of shepherdin, a novel anticancer agent. Cancer Cell 2005; 7: 457-68.
276. Gyurkocza B, Plescia J, Raskett CM, Garlick DS, Lowry PA, Carter BZ, et al. Antileukemic activity of shepherdin and molecular diversity of hsp90 chaperones. J Natl Cancer Inst 2006; 98: 1068-77
277. Kang BH, Plescia J, Dohi T, Rosa J, Doxsey SJ, Altieri DC. Regulation of tumor cell mitochondrial homeostasis by an organelle-specific HSp90 chaperone network. Cell 2007; 131: 257-70.
278. Kerem B, Rommens JM, Buchanan JA, Markiewicz D, Cox TK, Chakravarti A, et al. Identification of the cystic fibrosis gene: Genetic analysis. Science 1989 245: 1073-80.
279. Denning GM, Anderson MP, Amara JF, Marshall J, Smith AE, Welsh MJ. Processing of mutant cystic fibrosis conductance regulator is temperature-sensitive. Nature 1992; 358: 761-4.
280. Barbe MF, Tytell M, Gower DJ, Welch WJ. Hyperthermia protects against light damage in the rat retina. Science 1988; 241: 1817-20.
281. Sawano H, Koumoto Y, Ohta K, Sasaki Y, Segawa S, Tachibana H. Efficient in vitro refolding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol. FEBS Lett 1992; 303: 11-4.
282. Brown CR, Hong-Brown LQ, Biwersi J, Verkman AS, Welch WJ. Chemical chaperones correct the mutant phenotype of the ΔF508 cystic fibrosis transmembrane conductance regulator protein. Cell Stress Chaperones 1996; 1: 117-25.
283. Sato S, Ward CL, Krouse ME, Wine JJ, Kopito RR. Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J Biol Chem 1996; 271: 635-8.
284. Howard M, Fischer H, Roux J, Santos BC, Gullans SR, Yancey PH, et al. Mammalian osmolytes and S-nitrosoglutathione promote ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) protein maturation and function. J Biol Chem 2003; 278: 31359-67.
285. Zhang XM, Wang XT, Yue H, Leung SW, Thibodeau PH, Thomas PJ, et al. Organic solutes rescue the functional defect in ΔF508 cystic fibrosis transmembrane conductance regulator. J Biol Chem 2003; 278: 51232-42.
286. Tamarappoo BK, Verkman AS. Defective aquaporin-2 trafficking in nephrogenic diabetes insipidus and correction by chemical chaperones. J Clin Invest 1998; 101: 2257-67.
287. Burrows JA, Willis LK, Perlmutter DH. Chemical chaperones mediate increased secretion of mutant α1-antitrypsin (α1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphyseme in alpha 1-AT deficiency. Proc Natl Acad Sci USA 2000; 97: 1796-801.
288. Yoshida H, Yoshizawa T, Shibasaki F, Shoji S, Kanazawa I. Chemical chaperones reduce aggregate formation and cell death caused by the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch. Neurobiol Dis 2002; 10: 88-99.
289. Ozcan U, Yilmaz E, Ozcan L, Furuhashi M, Vaillancourt E, Smith RO, et al. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 2006; 313: 1137-40.
290. Maestri NE, Brusilow SW, Clissold DB, Bassett SS. Long-term treatment of girls with ornithine transcarbamylase deficiency. N Engl J Med 1996; 335: 855-9.
291. Collins AF, Pearson HA, Giardina P, McDonagh KT, Brusilow SW, Dover GJ. Oral sodium phenylbutyrate therapy in homozygous beta thalassemia: A clinical trial. Blood 1995; 85: 43-9.
292. Poupon RE, Bonnand AM, Chrétien Y, Poupon R. Ten-year survival in ursodeoxycholic acid-treated patients with primary biliary cirrhosis: The UDCA-PBC study group. Hepatology 1999; 29: 1668-71.
293. Sorger, PK. Heat shock factor and the heat shock response. Cell 1991; 65: 363-6.
294. Westerheide SD, Morimoto RI. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J Biol Chem 2005; 280: 33097-100.
295. Malhotra JD, Kaufman RJ. The endoplasmic reticulum and the unfolded protein response. Semin Cell Dev Biol 2007; 18: 716-31.
296. Schröder M. Endoplasmic reticulum stress reponses. Cell Mol Life Sci 2008; 65: 862-94.
297. Pirkkala L, Nykänen P, Sistonen L Roles of the heat shock transcription factors in regulation of the heat shock response and beyond. FASEB J 2001;15:1118-31.
298. Wegele H, Müller L, Buchner J. Hsp70 and Hsp90 - a relay team for protein folding. Rev Physiol Biochem Pharmacol 2004; 151: 1-44.
299. Lee BS, Chen J, Angelidis C, Jurivich DA, Morimoto RI. Pharmacological modulation of heat shock factor 1 by anti-inflammatory drugs results in protection against stress-induced cellular damage. Proc Natl Acad Sci USA 1995; 92: 7207-11.
300. Westerheide SD, Bosman JD, Mbadugha BN, Kawahara TL, Matsumoto G, Kim S, et al. Celastrols as inducers of the heat shock response and cytoprotection. J Biol Chem 2004; 279: 56053-60.
301. Trott A, West JD, Klaić L, Westerheide SD, Silverman RB, Morimoto RI, et al. Activation of heat shock and antioxidant responses by the natural product celastrol: Transcriptional signatures of a thiol-targeted molecule. Mol Biol Cell 2008; 19: 1104-12.
302. Yang H, Chen D, Cui QC, Yuan X, Dou QP. Celastrol, a triterpene extracted from the Chinese "Thunder of God Vine" is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice. Cancer Res 2006; 66: 4758-65.
303. Bagatell R, Paine-Murrieta GD, Taylor CW, Pulcini EJ, Akinaga S, Benjamin IJ, et al. Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents. Clin Cancer Res 2000; 6: 3312-8.
304. Lawson B, Brewer JW, Hendershot LM. Geldanamycin, an hsp90/GRP94-binding drug, induces increased transcription of endoplasmic reticulum (ER) chaperones via the ER stress pathway. J Cell Physiol. 1998; 174: 170-8.
305. Xiao X, Zuo X, Davis AA, McMillan DR, Curry BB, Richardson JA, et al. HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice. EMBO J 1999; 18: 5943-52.
306. Dai C, Whitesell L, Rogers AB, Lindquist S. Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis. Cell 2007; 130: 1005-18.
307. Mu TW, Fowler DM, Kelly JW. Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasis. PloS Biology 2008; 6: E26.
308. Wang X, Venable J, LaPointe P, Hutt DM, Koulov AV, Coppinger J, et al. Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 2006; 127: 803-15.
309. Vij N, Fang S, Zeitlin PL. Selective inhibition of endoplasmic reticulum-associated degradation rescues ΔF508-cystic fibrosis transmembrane regulator and suppresses interleukin-8 levels: Therapeutic implications. J Biol Chem 2006; 281: 17369-78.
310. Shen X, Ellis RE, Lee K, Liu CY, Yang K, Solomon A, et al. Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 2001;107: 893-903
311. Shah N, Kuntz DA, Rose DR. Comparison of kifuensine and 1-deoxymannojirimycin binding to class I and II α-mannosidases demonstrates different saccharide distortions in inverting and retaining catalytic mechanisms. Biochemistry 2003; 42: 13812-6.
312. Ruddock LW, Molinari M. N-glycan processing in ER quality control. J Cell Sci 2006; 119: 4373-80.
313. Richardson PG, Mitsiades C, Hideshima T, Anderson KC. Bortezomib: Proteasome inhibition as an effective anticancer therapy. Annu Rev Med 2006; 57: 33-47.
314. Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 1995; 268: 726-31.
315. Meng L, Mohan R, Kwok BH, Elofsson M, Sin N, Crews CM. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinfammatory activity. Proc Natl Acad Sci USA 1999; 96: 10403-8.
316. Kim D, Kim SH, Li HC. Proteasome inhibitors MG132 and lactacystin hyperphosphophorylate HSF1 and induce hsp70 and hsp27 expression. Biochem Biophys Res Commun 1999; 254: 264-8.
317. Mitsiades N, Mitsiades CS, Poulaki V, Chauhan D, Fanourakis G, Gu X, et al. Molecular sequelae of proteasome inhibition in human multiple myeloma cells. Proc Natl Acad Sci USA 2002; 99: 14374-9.
318. Kitiphongspattana K, Mathews CE, Leiter EH, Gaskins HR. Proteasome inhibition alters glucose-stimulated (pro)insulin secretion and turnover in pancreatic β-cells. J Biol Chem 2005; 280: 15727-34.
319. Wyttenbach A, Carmichael J, Swartz J, Furlong RA, Narain Y, Rankin J, et al. Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease. Proc Natl Acad Sci USA 2000; 97: 2898-903.
320. Drexler HC. Activation of the cell death program by inhibition of proteasome function. Proc natl Acad Sci USA 1997; 94: 855-60.
321. Adams J, Palombella VJ, Sausville EA, Johnson J, Destree A, Lazarus DD, et al. Proteasome inhibitors: A novel class of potent and effective antitumor agents. Cancer Res 1999; 59: 2615-22.
322. McNaught KS, Perl DP, Brownell AL, Olanow CW. Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease. Ann Neurol 2004; 56: 149-62.
323. Kumita JR, Johnson RJ, Alcocer MJ, Dumoulin M, Holmqvist F, McCammon MG, et al. Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris. FEBS Journal 2006; 273: 711-720.
324. Fan JQ, Ishii S. Cell-base screening of active-site specific chaperone for the treatment of Fabry disease. Methods Enzymol. 2003; 363: 412-420.
325. Fan JQ. A counterintuitive approach to treat enzyme deficiences: Use of enzyme inhibitors for restoring mutant enzyme activity. Biol Chem 2008; 389: 1-11.
326. Bernier V, Morello JP, Zarruk A, Debrand N, Salahpour A, Lonergan M, et al. Pharmacologic chaperones as a potential treatment for X-linked nephrogenic diabetes insipidus. J Am Soc Nephrol 2006; 17: 232-43.
327. Noorwez SM, Kuksa V, Imanishi Y, Zhu L, Filipek S, Palczewski K, Kaushal S. Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinis pigmentosa. J Biol Chem 2003; 278: 14442-50.
328. Noorwez SM, Malhotra R, McDowell JH, Smith KA, Bkrebs MP, Kaushal S. Retinoids assist the cellular folding of the autosomal dominant retinitis igmentosa opsin mutant P23H. J Biol Chem 2004; 279: 16278-84.
329. Morello JP, Salahpour A, Laperrière A, Bernier V, Arthus MF, Longergan M, et al. Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants. J Clin Invest 2000; 105: 887-95.
330. Wang Y, Bartlett MC, Loo TP, Clarke DM. Specific rescue of cystic fibrosis transmembrane conductance regulator processing mutants using pharmacological chaperones. Mol Pharmacol 2006; 70: 297-302.
331. Petäjä-Repo UE, Hogue M, Bhalla S, Laperrière A, Morello JP, Bouvier M. Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation. EMBO J 2002; 21: 1628-37.
332. Leskelä TT, Markkanen PM, Pietilä EM, Tuusa JT, Petäjä-Repo UE. Opioid receptor pharmacological chaperones act by binding and stabilizing newly synthesised receptors in the endoplasmic reticulum. J Biol Chem 2007; 282: 23171-83.
333. Loo TW, Clarke DM. Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators. J Biol Chem 1997; 272: 709-12.
334. Pedemonte N, Lukacs GL, Du K, Caci E, Zegarra-Moran O, Galietta LJ, et al. Small molecule correctors of defective ΔF508-CFTR cellular processing identified by high-throughput screening. J Clin Invest 2005; 115: 2564-71.
335. Wang Y, Loo TW, Bartlett MC, Clarke DM. Correctors promote maturation of cystic fibrosis transmembrane conductance regulator (CFTR)-processing mutants by binding to the protein. J Biol Chem 2007; 282: 33247-51.
336. LooTP, Bartlett MC, Clarke DM. Correctors promote folding of the CFTR in the endoplasmic reticulum. Biochem J 2008; 413: 29-36.
337. Curran ME, Splawski I, Timothy KW, Vincent GM, Green ED, Keating MT. A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome. Cell 1995; 80: 795-803.
338. Sanquinetti MC, Jiang C, Curran ME, Keating MT. A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the lKr potassium channel. Cell 1995; 81: 299-307.
339. Fickert E, Obejero-Paz CA, Zhao S, Brown AM. The binding site for channel blockers that rescue misprocessed human long QT syndrome type 2 ether-a-gogo related gene (HERG) mutations. J Biol Chem 2002; 277: 4989-98.
340. Janovick JA, Goulet M, Bush E, Greer J, Wettlaufer DG, Conn PM. Structure-activity relations of successful pharmacologic chaperones for rescue of naturally occurring and manufactured mutants of the gonadotropin-releasing hormone receptor. J Pharmacol Exp Ther 2003; 305: 608-14.
341. Janovick JA, Brothers SP, Cornea A, Bush E, Goulet MT, Ashton WT, et al. Refolding of misfolded mutant GPCR: Post-translational pharmacoperone action in vitro. Mol Cell Endocrinol. 2007; 272: 77-85.
342. Klappa P, Ruddock LW, Darby NJ, Freedman RB. The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J 1998; 17: 927-35.
343. Koivunen P, Salo KEH, Myllyharju J, Ruddock, LW. Three binding sites in protein disulfide isomerase co-operate in collagen prolyl 4-hydroxylase tetramer assembly. J Biol Chem 2005; 280: 5227-35.