Countering amyloid polymorphism and drug resistance with minimal drug cocktails

References

• Cushman M, Johnson BS, King OD, Gitler AD, Shorter J. Prion-like disorders: blurring the divide between transmissibility and infectivity. J Cell Sci 2010; 123:1191 - 1201
   PubMed Web of Science ®Google Scholar
• Soto C, Estrada LD. Protein misfolding and neurodegeneration. Arch Neurol 2008; 65:184 - 189
   PubMed Web of Science ®Google Scholar
• Forman MS, Trojanowski JQ, Lee VM. Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs. Nat Med 2004; 10:1055 - 1063
   PubMed Web of Science ®Google Scholar
• Fandrich M. On the structural definition of amyloid fibrils and other polypeptide aggregates. Cell Mol Life Sci 2007; 64:2066 - 2078
   PubMed Web of Science ®Google Scholar
• Nelson R, Eisenberg D. Structural models of amyloid-like fibrils. Adv Protein Chem 2006; 73:235 - 282
   PubMedGoogle Scholar
• Chiti F, Dobson CM. Protein misfolding, functional amyloid and human disease. Annu Rev Biochem 2006; 75:333 - 366
   PubMed Web of Science ®Google Scholar
• Fink AL. Natively unfolded proteins. Curr Opin Struct Biol 2005; 15:35 - 41
   PubMed Web of Science ®Google Scholar
• Aguzzi A, Rajendran L. The transcellular spread of cytosolic amyloids, prions and prionoids. Neuron 2009; 64:783 - 790
   PubMed Web of Science ®Google Scholar
• Meyer-Luehmann M, Coomaraswamy J, Bolmont T, Kaeser S, Schaefer C, Kilger E, et al. Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science 2006; 313:1781 - 1784
   PubMed Web of Science ®Google Scholar
• Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 2009; 284:12845 - 12852
   PubMed Web of Science ®Google Scholar
• Clavaguera F, Bolmont T, Crowther RA, Abramowski D, Frank S, Probst A, et al. Transmission and spreading of tauopathy in transgenic mouse brain. Nat Cell Biol 2009; 11:909 - 913
   PubMed Web of Science ®Google Scholar
• Li JY, Englund E, Holton JL, Soulet D, Hagell P, Lees AJ, et al. Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation. Nat Med 2008; 14:501 - 503
   PubMed Web of Science ®Google Scholar
• Kordower JH, Chu Y, Hauser RA, Freeman TB, Olanow CW. Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat Med 2008; 14:504 - 506
   PubMed Web of Science ®Google Scholar
• Luk KC, Song C, O'Brien P, Stieber A, Branch JR, Brunden KR, et al. Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. Proc Natl Acad Sci USA 2009; 106:20051 - 20056
   PubMed Web of Science ®Google Scholar
• Desplats P, Lee HJ, Bae EJ, Patrick C, Rockenstein E, Crews L, et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc Natl Acad Sci USA 2009; 106:13010 - 13015
   PubMed Web of Science ®Google Scholar
• Ren PH, Lauckner JE, Kachirskaia I, Heuser JE, Melki R, Kopito RR. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 2009; 11:219 - 225
   PubMed Web of Science ®Google Scholar
• Legname G, Baskakov IV, Nguyen HO, Riesner D, Cohen FE, DeArmond SJ, et al. Synthetic mammalian prions. Science 2004; 305:673 - 676
   PubMed Web of Science ®Google Scholar
• Colby DW, Giles K, Legname G, Wille H, Baskakov IV, DeArmond SJ, et al. Design and construction of diverse mammalian prion strains. Proc Natl Acad Sci USA 2009; 106:20417 - 20422
   PubMed Web of Science ®Google Scholar
• Shorter J. Emergence and natural selection of drug-resistant prions. Mol Biosyst 2010; 6:1115 - 1130
   Google Scholar
• Prusiner SB. Prions. Proc Natl Acad Sci USA 1998; 95:13363 - 13383
   PubMed Web of Science ®Google Scholar
• Shorter J, Lindquist S. Prions as adaptive conduits of memory and inheritance. Nat Rev Genet 2005; 6:435 - 450
   PubMed Web of Science ®Google Scholar
• Collinge J, Clarke AR. A general model of prion strains and their pathogenicity. Science 2007; 318:930 - 936
   PubMed Web of Science ®Google Scholar
• Prusiner SB. The prion diseases. Brain Pathol 1998; 8:499 - 513
   PubMed Web of Science ®Google Scholar
• Wang F, Wang X, Yuan CG, Ma J. Generating a prion with bacterially expressed recombinant prion protein. Science 2010; 327:1132 - 1135
   PubMed Web of Science ®Google Scholar
• Ross CA, Poirier MA. Opinion: What is the role of protein aggregation in neurodegeneration?. Nat Rev Mol Cell Biol 2005; 6:891 - 898
   PubMed Web of Science ®Google Scholar
• 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 - 489
   PubMed Web of Science ®Google Scholar
• Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 2007; 8:101 - 112
   PubMed Web of Science ®Google Scholar
• Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 2002; 418:291
   PubMed Web of Science ®Google Scholar
• Ahmed M, Davis J, Aucoin D, Sato T, Ahuja S, Aimoto S, et al. Structural conversion of neurotoxic amyloid-beta(1–42) oligomers to fibrils. Nat Struct Mol Biol 2010; 17:561 - 567
   PubMed Web of Science ®Google Scholar
• Tanaka M, Chien P, Naber N, Cooke R, Weissman JS. Conformational variations in an infectious protein determine prion strain differences. Nature 2004; 428:323 - 328
   PubMed Web of Science ®Google Scholar
• Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 2005; 307:262 - 265
   PubMed Web of Science ®Google Scholar
• Nekooki-Machida Y, Kurosawa M, Nukina N, Ito K, Oda T, Tanaka M. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc Natl Acad Sci USA 2009; 106:9679 - 9684
   PubMed Web of Science ®Google Scholar
• Krishnan R, Lindquist SL. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 2005; 435:765 - 772
   PubMed Web of Science ®Google Scholar
• Fandrich M, Meinhardt J, Grigorieff N. Structural polymorphism of Alzheimer Abeta and other amyloid fibrils. Prion 2009; 3:89 - 93
   PubMed Web of Science ®Google Scholar
• Colby DW, Wain R, Baskakov IV, Legname G, Palmer CG, Nguyen HO, et al. Protease-sensitive synthetic prions. PLoS Pathog 2010; 6:1000736
   PubMed Web of Science ®Google Scholar
• Tanaka M, Collins SR, Toyama BH, Weissman JS. The physical basis of how prion conformations determine strain phenotypes. Nature 2006; 442:585 - 589
   PubMed Web of Science ®Google Scholar
• Baxa U, Speransky V, Steven AC, Wickner RB. Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein. Proc Natl Acad Sci USA 2002; 99:5253 - 5260
   PubMed Web of Science ®Google Scholar
• Gitler AD, Shorter J. Prime time for alpha-synuclein. J Neurosci 2007; 27:2433 - 2434
   PubMed Web of Science ®Google Scholar
• Gorbatyuk OS, Li S, Nash K, Gorbatyuk M, Lewin AS, Sullivan LF, et al. In vivo RNAi-mediated alpha-synuclein silencing induces nigrostriatal degeneration. Mol Ther 2010; 18:1450 - 1457
   PubMed Web of Science ®Google Scholar
• Bramblett GT, Goedert M, Jakes R, Merrick SE, Trojanowski JQ, Lee VM. Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron 1993; 10:1089 - 1099
   PubMed Web of Science ®Google Scholar
• Barten DM, Albright CF. Therapeutic strategies for Alzheimer's disease. Mol Neurobiol 2008; 37:171 - 186
   PubMed Web of Science ®Google Scholar
• Citron M. Alzheimer's disease: strategies for disease modification. Nat Rev Drug Discov 2010; 9:387 - 398
   PubMed Web of Science ®Google Scholar
• Crowe A, Huang W, Ballatore C, Johnson RL, Hogan AM, Huang R, et al. Identification of aminothienopyridazine inhibitors of tau assembly by quantitative high-throughput screening. Biochemistry 2009; 48:7732 - 7745
   PubMed Web of Science ®Google Scholar
• Schenk D. Amyloid-beta immunotherapy for Alzheimer's disease: the end of the beginning. Nat Rev Neurosci 2002; 3:824 - 828
   PubMed Web of Science ®Google Scholar
• Spencer B, Rockenstein E, Crews L, Marr R, Masliah E. Novel strategies for Alzheimer's disease treatment. Expert Opin Biol Ther 2007; 7:1853 - 1867
   PubMed Web of Science ®Google Scholar
• Vashist S, Cushman M, Shorter J. Applying Hsp104 to protein-misfolding disorders. Biochem Cell Biol 2010; 88:1 - 13
   PubMed Web of Science ®Google Scholar
• Shorter J. Hsp104: a weapon to combat diverse neurodegenerative disorders. Neurosignals 2008; 16:63 - 74
   PubMed Web of Science ®Google Scholar
• Lo Bianco C, Shorter J, Regulier E, Lashuel H, Iwatsubo T, Lindquist S, et al. Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease. J Clin Invest 2008; 118:3087 - 3097
   PubMed Web of Science ®Google Scholar
• Vacher C, Garcia-Oroz L, Rubinsztein DC. Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington's disease. Hum Mol Genet 2005; 14:3425 - 3433
   PubMed Web of Science ®Google Scholar
• Bainbridge JW, Smith AJ, Barker SS, Robbie S, Henderson R, Balaggan K, et al. Effect of gene therapy on visual function in Leber's congenital amaurosis. N Engl J Med 2008; 358:2231 - 2239
   PubMed Web of Science ®Google Scholar
• Maguire AM, Simonelli F, Pierce EA, Pugh EN Jr, Mingozzi F, Bennicelli J, et al. Safety and efficacy of gene transfer for Leber's congenital amaurosis. N Engl J Med 2008; 358:2240 - 2248
   PubMed Web of Science ®Google Scholar
• Feigin A, Kaplitt MG, Tang C, Lin T, Mattis P, Dhawan V, et al. Modulation of metabolic brain networks after subthalamic gene therapy for Parkinson's disease. Proc Natl Acad Sci USA 2007; 104:19559 - 19564
   PubMed Web of Science ®Google Scholar
• Kaplitt MG, Feigin A, Tang C, Fitzsimons HL, Mattis P, Lawlor PA, et al. Safety and tolerability of gene therapy with an adeno-associated virus (AAV) borne GAD gene for Parkinson's disease: an open label, phase I trial. Lancet 2007; 369:2097 - 2105
   PubMed Web of Science ®Google Scholar
• Stoessl AJ. Gene therapy for Parkinson's disease: early data. Lancet 2007; 369:2056 - 2058
   PubMed Web of Science ®Google Scholar
• Wells JA, McClendon CL. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 2007; 450:1001 - 1009
   PubMed Web of Science ®Google Scholar
• Roberts BE, Shorter J. Escaping amyloid fate. Nat Struct Mol Biol 2008; 15:544 - 546
   PubMed Web of Science ®Google Scholar
• Pardridge WM. The blood-brain barrier: bottleneck in brain drug development. NeuroRx 2005; 2:3 - 14
   PubMedGoogle Scholar
• Ballatore C, Brunden KR, Piscitelli F, James MJ, Crowe A, Yao Y, et al. Discovery of brain-penetrant, orally bioavailable aminothienopyridazine inhibitors of tau aggregation. J Med Chem 2010; 53:3739 - 3747
   PubMed Web of Science ®Google Scholar
• Ladiwala AR, Lin JC, Bale SS, Marcelino-Cruz AM, Bhattacharya M, Dordick JS, et al. Resveratrol selectively remodels soluble oligomers and fibrils of amyloid a{beta} into off-pathway conformers. J Biol Chem 2010; 285:24228 - 24237
   PubMed Web of Science ®Google Scholar
• Wang H, Duennwald ML, Roberts BE, Rozeboom LM, Zhang YL, Steele AD, et al. Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs. Proc Natl Acad Sci USA 2008; 105:7159 - 7164
   PubMed Web of Science ®Google Scholar
• Roberts BE, Duennwald ML, Wang H, Chung C, Lopreiato NP, Sweeny EA, et al. A synergistic small-molecule combination directly eradicates diverse prion strain structures. Nat Chem Biol 2009; 5:936 - 946
   PubMed Web of Science ®Google Scholar
• Ehrnhoefer DE, Duennwald M, Markovic P, Wacker JL, Engemann S, Roark M, et al. Green tea (−)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models. Hum Mol Genet 2006; 15:2743 - 2751
   PubMed Web of Science ®Google Scholar
• Ehrnhoefer DE, Bieschke J, Boeddrich A, Herbst M, Masino L, Lurz R, et al. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat Struct Mol Biol 2008; 15:558 - 566
   PubMed Web of Science ®Google Scholar
• Bieschke J, Russ J, Friedrich RP, Ehrnhoefer DE, Wobst H, Neugebauer K, et al. EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. Proc Natl Acad Sci USA 2010; 107:7710 - 7715
   PubMed Web of Science ®Google Scholar
• Masuda M, Suzuki N, Taniguchi S, Oikawa T, Nonaka T, Iwatsubo T, et al. Small molecule inhibitors of alpha-synuclein filament assembly. Biochemistry 2006; 45:6085 - 6094
   PubMed Web of Science ®Google Scholar
• Blanchard BJ, Chen A, Rozeboom LM, Stafford KA, Weigele P, Ingram VM. Efficient reversal of Alzheimer's disease fibril formation and elimination of neurotoxicity by a small molecule. Proc Natl Acad Sci USA 2004; 101:14326 - 14332
   PubMed Web of Science ®Google Scholar
• Hammarstrom P, Wiseman RL, Powers ET, Kelly JW. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 2003; 299:713 - 716
   PubMed Web of Science ®Google Scholar
• Colby DW, Giles K, Legname G, Wille H, Baskakov IV, DeArmond SJ, et al. Design and construction of diverse mammalian prion strains. Proc Natl Acad Sci USA 2009; 106:20417 - 20422
   PubMed Web of Science ®Google Scholar
• Kodali R, Williams AD, Chemuru S, Wetzel R. Aβ(1–40) forms five distinct amyloid structures β-whose sheet contents and fibril stabilities correlate. J Mol Biol 2010; 401:503 - 517
   PubMed Web of Science ®Google Scholar
• Wiltzius JJ, Landau M, Nelson R, Sawaya MR, Apostol MI, Goldschmidt L, et al. Molecular mechanisms for protein-encoded inheritance. Nat Struct Mol Biol 2009; 16:973 - 978
   PubMed Web of Science ®Google Scholar
• Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, et al. Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 2007; 447:453 - 457
   PubMed Web of Science ®Google Scholar
• Del Mar C, Greenbaum EA, Mayne L, Englander SW, Woods VL Jr. Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level. Proc Natl Acad Sci USA 2005; 102:15477 - 15482
   PubMed Web of Science ®Google Scholar
• Paravastu AK, Qahwash I, Leapman RD, Meredith SC, Tycko R. Seeded growth of beta-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure. Proc Natl Acad Sci USA 2009; 106:7443 - 7448
   PubMed Web of Science ®Google Scholar
• Mobley DL, Dill KA. Binding of small-molecule ligands to proteins: “what you see” is not always “what you get”. Structure 2009; 17:489 - 498
   PubMed Web of Science ®Google Scholar
• Shkundina IS, Ter-Avanesyan MD. Prions. Biochemistry (Mosc) 2007; 72:1519 - 1536
   PubMed Web of Science ®Google Scholar
• Toyama BH, Kelly MJ, Gross JD, Weissman JS. The structural basis of yeast prion strain variants. Nature 2007; 449:233 - 237
   PubMed Web of Science ®Google Scholar
• Shorter J, Lindquist S. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol Cell 2006; 23:425 - 438
   PubMed Web of Science ®Google Scholar
• True HL, Lindquist SL. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 2000; 407:477 - 483
   PubMed Web of Science ®Google Scholar
• True HL, Berlin I, Lindquist SL. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 2004; 431:184 - 187
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Chernoff YO, Kushnirov VV, Inge-Vechtomov SG, Liebman SW. Genesis and variability of [PSI+] prion factors in Saccharomyces cerevisiae. Genetics 1996; 144:1375 - 1386
   PubMed Web of Science ®Google Scholar
• Liu JJ, Sondheimer N, Lindquist SL. Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]. Proc Natl Acad Sci USA 2002; 99:16446 - 16453
   PubMed Web of Science ®Google Scholar
• Glover JR, Kowal AS, Schirmer EC, Patino MM, Liu JJ, Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 1997; 89:811 - 819
   PubMed Web of Science ®Google Scholar
• Li L, Lindquist S. Creating a protein-based element of inheritance. Science 2000; 287:661 - 664
   PubMed Web of Science ®Google Scholar
• Shorter J, Lindquist S. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J 2008; 27:2712 - 2724
   PubMed Web of Science ®Google Scholar
• Sondheimer N, Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast. Mol Cell 2000; 5:163 - 172
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Bradley ME, Hong JY, Liebman SW. Prions affect the appearance of other prions: the story of [PIN+]. Cell 2001; 106:171 - 182
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Bradley ME, Masse SV, Zadorsky SP, Polozkov GV, Inge-Vechtomov SG, et al. Dependence and independence of [PSI+] and [PIN+]: a two-prion system in yeast?. EMBO J 2000; 19:1942 - 1952
   PubMed Web of Science ®Google Scholar
• Osherovich LZ, Weissman JS. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI+] prion. Cell 2001; 106:183 - 194
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Uptain SM, Outeiro TF, Krishnan R, Lindquist SL, Liebman SW. Effects of Q/N-rich, polyQ and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci USA 2004; 101:12934 - 12939
   PubMed Web of Science ®Google Scholar
• Tessier PM, Lindquist S. Prion recognition elements govern nucleation, strain specificity and species barriers. Nature 2007; 447:556 - 561
   PubMed Web of Science ®Google Scholar
• Tessier PM, Lindquist S. Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+]. Nat Struct Mol Biol 2009; 16:598 - 605
   PubMed Web of Science ®Google Scholar
• Shewmaker F, Wickner RB, Tycko R. Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure. Proc Natl Acad Sci USA 2006; 103:19754 - 19759
   PubMed Web of Science ®Google Scholar
• Diaz-Avalos R, King CY, Wall J, Simon M, Caspar DL. Strain-specific morphologies of yeast prion amyloid fibrils. Proc Natl Acad Sci USA 2005; 102:10165 - 10170
   PubMed Web of Science ®Google Scholar
• Rambold AS, Miesbauer M, Olschewski D, Seidel R, Riemer C, Smale L, et al. Green tea extracts interfere with the stress-protective activity of PrP and the formation of PrP. J Neurochem 2008; 107:218 - 229
   PubMed Web of Science ®Google Scholar
• Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, Serpell L, et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 2000; 289:1317 - 1321
   PubMed Web of Science ®Google Scholar
• Shorter J, Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 2004; 304:1793 - 1797
   PubMed Web of Science ®Google Scholar
• Bradley ME, Liebman SW. Destabilizing interactions among [PSI+] and [PIN+] yeast prion variants. Genetics 2003; 165:1675 - 1685
   PubMed Web of Science ®Google Scholar
• Kochneva-Pervukhova NV, Chechenova MB, Valouev IA, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD. [PSI+] prion generation in yeast: characterization of the ‘strain’ difference. Yeast 2001; 18:489 - 497
   PubMed Web of Science ®Google Scholar
• Li J, Browning S, Mahal SP, Oelschlegel AM, Weissmann C. Darwinian evolution of prions in cell culture. Science 2010; 327:869 - 872
   PubMed Web of Science ®Google Scholar
• Ghaemmaghami S, Ahn M, Lessard P, Giles K, Legname G, DeArmond SJ, et al. Continuous quinacrine treatment results in the formation of drug-resistant prions. PLoS Pathog 2009; 5:1000673
   PubMed Web of Science ®Google Scholar
• Waxman EA, Emmer KL, Giasson BI. Residue Glu83 plays a major role in negatively regulating alpha-synuclein amyloid formation. Biochem Biophys Res Commun 2010; 391:1415 - 1420
   PubMed Web of Science ®Google Scholar
• Hauber I, Hohenberg H, Holstermann B, Hunstein W, Hauber J. The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection. Proc Natl Acad Sci USA 2009; 106:9033 - 9038
   PubMed Web of Science ®Google Scholar
• Munch J, Rucker E, Standker L, Adermann K, Goffinet C, Schindler M, et al. Semen-derived amyloid fibrils drastically enhance HIV infection. Cell 2007; 131:1059 - 1071
   PubMed Web of Science ®Google Scholar
• Mereles D, Buss SJ, Hardt SE, Hunstein W, Katus HA. Effects of the main green tea polyphenol epigallocatechin-3-gallate on cardiac involvement in patients with AL amyloidosis. Clin Res Cardiol 2010; 99:483 - 490
   PubMed Web of Science ®Google Scholar
• Kocisko DA, Engel AL, Harbuck K, Arnold KM, Olsen EA, Raymond LD, et al. Comparison of protease-resistant prion protein inhibitors in cell cultures infected with two strains of mouse and sheep scrapie. Neurosci Lett 2005; 388:106 - 111
   PubMed Web of Science ®Google Scholar
• Radhakrishnan ML, Tidor B. Optimal drug cocktail design: methods for targeting molecular ensembles and insights from theoretical model systems. J Chem Inf Model 2008; 48:1055 - 1073
   PubMed Web of Science ®Google Scholar
• Staszewski S, Morales-Ramirez J, Tashima KT, Rachlis A, Skiest D, Stanford J, et al. Efavirenz plus zidovudine and lamivudine, efavirenz plus indinavir and indinavir plus zidovudine and lamivudine in the treatment of HIV-1 infection in adults. Study 006 Team. N Engl J Med 1999; 341:1865 - 1873
   PubMed Web of Science ®Google Scholar
• Cowen LE, Singh SD, Kohler JR, Collins C, Zaas AK, Schell WA, et al. Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease. Proc Natl Acad Sci USA 2009; 106:2818 - 2823
   PubMed Web of Science ®Google Scholar
• Mu TW, Ong DS, Wang YJ, Balch WE, Yates JR 3rd, Segatori L, et al. Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell 2008; 134:769 - 781
   PubMed Web of Science ®Google Scholar