Nanoimaging for prion related diseases

References

• Collinge J, Clarke AR. A general model of prion strains and their pathogenicity. Science 2007; 318:930 - 936
   PubMed Web of Science ®Google Scholar
• Baxa U, Wickner RB, Steven AC, Anderson DE, Marekov LN, Yau WM, et al. Characterization of beta-sheet structure in Ure2p1–89 yeast prion fibrils by solid-state nuclear magnetic resonance. Biochemistry 2007; 46:13149 - 162
   PubMed Web of Science ®Google Scholar
• Chan JC, Oyler NA, Yau WM, Tycko R. Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10–39 of the yeast prion protein Ure2p. Biochemistry 2005; 44:10669 - 10680
   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
• Wickner RB, Dyda F, Tycko R. Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure. Proc Natl Acad Sci USA 2008; 105:2403
   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
• Balbach JJ, Petkova AT, Oyler NA, Antzutkin ON, Gordon DJ, Meredith SC, et al. Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance. Biophys J 2002; 83:1205 - 1216
   PubMed Web of Science ®Google Scholar
• Petkova AT, Buntkowsky G, Dyda F, Leapman RD, Yau WM, Tycko R. Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide. J Mol Biol 2004; 335:247 - 260
   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
• Madine J, Doig AJ, Kitmitto A, Middleton DA. Studies of the aggregation of an amyloidogenic alpha-synuclein peptide fragment. Biochem Soc Trans 2005; 33:1113 - 1115
   PubMed Web of Science ®Google Scholar
• Tenidis K, Waldner M, Bernhagen J, Fischle W, Bergmann M, Weber M, et al. Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties. J Mol Biol 2000; 295:1055 - 1071
   PubMed Web of Science ®Google Scholar
• Krebs MR, Wilkins DK, Chung EW, Pitkeathly MC, Chamberlain AK, Zurdo J, et al. Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain. J Mol Biol 2000; 300:541 - 549
   PubMed Web of Science ®Google Scholar
• Ivanova MI, Sawaya MR, Gingery M, Attinger A, Eisenberg D. An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril. Proc Natl Acad Sci USA 2004; 101:10584 - 10589
   PubMed Web of Science ®Google Scholar
• Lopez de la Paz M, Serrano L. Sequence determinants of amyloid fibril formation. Proc Natl Acad Sci USA 2004; 101:87 - 92
   PubMed Web of Science ®Google Scholar
• Esteras-Chopo A, Serrano L, Lopez de la Paz M. The amyloid stretch hypothesis: recruiting proteins toward the dark side. Proc Natl Acad Sci USA 2005; 102:16672 - 16677
   PubMed Web of Science ®Google Scholar
• Keskin O, Ma B, Nussinov R. Hot regions in protein—protein interactions: the organization and contribution of structurally conserved hot spot residues. J Mol Biol 2005; 345:1281 - 1294
   PubMed Web of Science ®Google Scholar
• Sanchez de Groot N, Pallares I, Aviles FX, Vendrell J, Ventura S. Prediction of “hot spots” of aggregation in disease-linked polypeptides. BMC Struct Biol 2005; 5:18
   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
• Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, et al. Structure of the cross-beta spine of amyloid-like fibrils. Nature 2005; 435:773 - 778
   PubMed Web of Science ®Google Scholar
• Kadnar ML, Articov G, Derkatch IL. Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1. PLoS Genet 2010; 6:1000824
   PubMed Web of Science ®Google Scholar
• Ohhashi Y, Ito K, Toyama BH, Weissman JS, Tanaka M. Differences in prion strain conformations result from non-native interactions in a nucleus. Nat Chem Biol 2010; 6:225 - 230
   Google Scholar
• Collins SR, Douglass A, Vale RD, Weissman JS. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol 2004; 2:321
   PubMed Web of Science ®Google Scholar
• Ban T, Hamada D, Hasegawa K, Naiki H, Goto Y. Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J Biol Chem 2003; 278:16462 - 16465
   PubMed Web of Science ®Google Scholar
• Ban T, Goto Y. Direct observation of amyloid growth monitored by total internal reflection fluorescence microscopy. Methods Enzymol 2006; 413:91 - 102
   PubMed Web of Science ®Google Scholar
• Ban T, Hoshino M, Takahashi S, Hamada D, Hasegawa K, Naiki H, et al. Direct observation of Abeta amyloid fibril growth and inhibition. J Mol Biol 2004; 344:757 - 767
   PubMed Web of Science ®Google Scholar
• Hoyer W, Cherny D, Subramaniam V, Jovin TM. Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy. J Mol Biol 2004; 340:127 - 139
   PubMed Web of Science ®Google Scholar
• Kowalewski T, Holtzman DM. In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formation. Proc Natl Acad Sci USA 1999; 96:3688 - 3693
   PubMed Web of Science ®Google Scholar
• Goldsbury C, Kistler J, Aebi U, Arvinte T, Cooper GJ. Watching amyloid fibrils grow by time-lapse atomic force microscopy. J Mol Biol 1999; 285:33 - 39
   PubMed Web of Science ®Google Scholar
• Goldsbury C, Green J. Time-lapse atomic force microscopy in the characterization of amyloid-like fibril assembly and oligomeric intermediates. Methods Mol Biol 2005; 299:103 - 128
   PubMedGoogle Scholar
• Kellermayer MS, Karsai A, Benke M, Soos K, Penke B. Stepwise dynamics of epitaxially growing single amyloid fibrils. Proc Natl Acad Sci USA 2008; 105:141 - 144
   PubMed Web of Science ®Google Scholar
• DePace AH, Weissman JS. Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nat Struct Biol 2002; 9:389 - 396
   PubMedGoogle Scholar
• Prusiner SB. Prions. Proc Natl Acad Sci USA 1998; 95:13363 - 13383
   PubMed Web of Science ®Google Scholar
• Morales R, Abid K, Soto C. The prion strain phenomenon: molecular basis and unprecedented features. Biochim Biophys Acta 2007; 1772:681 - 691
   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
• Tanaka M, Chien P, Yonekura K, Weissman JS. Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins. Cell 2005; 121:49 - 62
   PubMed Web of Science ®Google Scholar
• Jones EM, Surewicz WK. Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell 2005; 121:63 - 72
   PubMed Web of Science ®Google Scholar
• Makarava N, Ostapchenko VG, Savtchenko R, Baskakov IV. Conformational switching within individual amyloid fibrils. J Biol Chem 2009; 284:14386 - 14395
   PubMed Web of Science ®Google Scholar
• van der Wel PC, Lewandowski JR, Griffin RG. Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p. J Am Chem Soc 2007; 129:5117 - 5130
   PubMed Web of Science ®Google Scholar
• Novitskaya V, Makarava N, Bellon A, Bocharova OV, Bronstein IB, Williamson RA, et al. Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay. J Biol Chem 2006; 281:15536 - 15545
   PubMed Web of Science ®Google Scholar
• Petty SA, Decatur SM. Intersheet rearrangement of polypeptides during nucleation of {beta}-sheet aggregates. Proc Natl Acad Sci USA 2005; 102:14272 - 14277
   PubMed Web of Science ®Google Scholar
• Shim SH, Gupta R, Ling YL, Strasfeld DB, Raleigh DP, Zanni MT. Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution. P Natl Acad Sci USA 2009; 106:6614 - 6619
   PubMed Web of Science ®Google Scholar
• Shashilov V, Xu M, Ermolenkov VV, Fredriksen L, Lednev IK. Probing a fibrillation nucleus directly by deep ultraviolet Raman spectroscopy. J Am Chem Soc 2007; 129:6972 - 6973
   PubMed Web of Science ®Google Scholar
• Shashilov VA, Lednev IK. 2D correlation deep UV resonance raman spectroscopy of early events of lysozyme fibrillation: kinetic mechanism and potential interpretation pitfalls. J Am Chem Soc 2008; 130:309 - 317
   PubMed Web of Science ®Google Scholar
• Paulite M, Fakhraai Z, Gunari N, Tanur A, GW. Different Individual Amyloid Fibrils Exhibit Different Beta Sheet Secondary Structures via Near-field Infrared Spectroscopy. Biophys J 2009; 96:87
   Google Scholar
• Paulite M, Fakhraai Z, Akhremitchev BB, Mueller K, Walker GC. Assembly, tuning and use of an apertureless near field infrared microscope for protein imaging. J Vis Exp 2009;
   PubMedGoogle Scholar
• Stockle RM, Suh YD, Deckert V, Zenobi R. Nanoscale chemical analysis by tip-enhanced Raman spectroscopy. Chem Phys Lett 2000; 318:131 - 136
   Web of Science ®Google Scholar
• Hayazawa N, Inouye Y, Sekkat Z, Kawata S. Metallized tip amplification of near-field Raman scattering. Optics Communications 2000; 183:333 - 336
   Web of Science ®Google Scholar
• Pettinger B, Picardi G, Schuster G, Ertl G. Surface enhanced Raman spectroscopy: towards single molecule spectroscopy. Electrochem 2000; 68:942 - 949
   Web of Science ®Google Scholar
• Bailo E, Deckert V. Tip-enhanced Raman scattering. Chem Soc Rev 2008; 37:921 - 930
   PubMed Web of Science ®Google Scholar
• Neacsu CC, Dreyer J, Behr N, Raschke MB. Reply to Comment on “Scanning-probe Raman spectroscopy with single-molecule sensitivity”. Phys Rev B 2007; 75:236402
   Web of Science ®Google Scholar
• Bailo E, Deckert V. Tip-enhanced Raman spectroscopy of single RNA strands: towards a novel direct-sequencing method. Angew Chem Int Ed Engl 2008; 47:1658 - 1661
   PubMed Web of Science ®Google Scholar
• Deckert-Gaudig T, Deckert V. Ultraflat transparent gold nanoplates—ideal substrates for tip-enhanced Raman scattering experiments. Small 2009; 5:432 - 436
   PubMed Web of Science ®Google Scholar
• Deckert-Gaudig T, Rauls E, Deckert V. Aromatic amino acid monolayers sandwiched between gold and silver: a combined tip-enhanced raman and theoretical approach. J Phys Chem C 2010; 114:7412 - 7420
   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
• Harris DA, True HL. New insights into prion structure and toxicity. Neuron 2006; 50:353 - 357
   PubMed Web of Science ®Google Scholar
• Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009; 137:146 - 158
   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
• True HL. The battle of the fold: chaperones take on prions. Trends Genet 2006; 22:110 - 117
   PubMed Web of Science ®Google Scholar
• Legname G, Nguyen HO, Baskakov IV, Cohen FE, Dearmond SJ, Prusiner SB. Strain-specified characteristics of mouse synthetic prions. Proc Natl Acad Sci USA 2005; 102:2168 - 2173
   PubMed Web of Science ®Google Scholar
• Legname G, Nguyen HO, Peretz D, Cohen FE, DeArmond SJ, Prusiner SB. Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc Natl Acad Sci USA 2006; 103:19105 - 19110
   PubMed Web of Science ®Google Scholar
• Sun Y, Makarava N, Lee CI, Laksanalamai P, Robb FT, Baskakov IV. Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size. J Mol Biol 2008; 376:1155 - 1167
   PubMed Web of Science ®Google Scholar
• Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, Hayes SF, et al. The most infectious prion protein particles. Nature 2005; 437:257 - 261
   PubMed Web of Science ®Google Scholar
• Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, Liosatos M, et al. Diffusible, nonfibrillar ligands derived from Abeta1–42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 1998; 95:6448 - 6453
   PubMed Web of Science ®Google Scholar
• Conway KA, Lee SJ, Rochet JC, Ding TT, Harper JD, Williamson RE, et al. Accelerated oligomerization by Parkinson's disease linked alpha-synuclein mutants. Ann NY Acad Sci 2000; 920:42 - 45
   PubMed Web of Science ®Google Scholar
• Scherzinger E, Lurz R, Turmaine M, Mangiarini L, Hollenbach B, Hasenbank R, et al. Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 1997; 90:549 - 558
   PubMed Web of Science ®Google Scholar
• Klein WL, Krafft GA, Finch CE. Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum?. Trends Neurosci 2001; 24:219 - 224
   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
• Goldberg MS, Lansbury PT Jr. Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?. Nat Cell Biol 2000; 2:115 - 119
   PubMedGoogle Scholar
• Orte A, Birkett NR, Clarke RW, Devlin GL, Dobson CM, Klenerman D. Direct characterization of amyloidogenic oligomers by single-molecule fluorescence. P Natl Acad Sci USA 2008; 105:14424 - 14429
   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
• He X, Giurleo JT, Talaga DS. Role of small oligomers on the amyloidogenic aggregation free-energy landscape. J Mol Biol 2009; 395:134 - 154
   PubMed Web of Science ®Google Scholar
• Moore RA, Vorberg I, Priola SA. Species barriers in prion diseases—brief review. Arch Virol 2005; 187 - 202
   Web of Science ®Google Scholar
• Vanik DL, Surewicz KA, Surewicz WK. Molecular basis of barriers for interspecies transmissibility of mammalian prions. Mol Cell 2004; 14:139 - 145
   PubMed Web of Science ®Google 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
• Chen B, Bruce KL, Newnam GP, Gyoneva S, Romanyuk AV, Chernoff YO. Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission. Mol Microbiol 2010; 76:1483 - 1499
   PubMed Web of Science ®Google Scholar
• Chen B, Newnam GP, Chernoff YO. Prion species barrier between the closely related yeast proteins is detected despite coaggregation. Proc Natl Acad Sci USA 2007; 104:2791 - 2796
   PubMed Web of Science ®Google Scholar
• Dobson CM. Principles of protein folding, misfolding and aggregation. Semin Cell Dev Biol 2004; 15:3 - 16
   PubMed Web of Science ®Google Scholar
• Dobson CM. Protein misfolding, evolution and disease. Trends Biochem Sci 1999; 24:329 - 332
   PubMed Web of Science ®Google Scholar
• Petkova AT, Ishii Y, Balbach JJ, Antzutkin ON, Leapman RD, Delaglio F, et al. A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA 2002; 99:16742 - 16747
   PubMed Web of Science ®Google Scholar
• Perutz MF, Johnson T, Suzuki M, Finch JT. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci USA 1994; 91:5355 - 5358
   PubMed Web of Science ®Google Scholar
• Watson D, Castano E, Kokjohn TA, Kuo YM, Lyubchenko Y, Pinsky D, et al. Physicochemical characteristics of soluble oligomeric Abeta and their pathologic role in Alzheimer's disease. Neurol Res 2005; 27:869 - 881
   PubMed Web of Science ®Google Scholar
• Chen S, Ferrone FA, Wetzel R. Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc Natl Acad Sci USA 2002; 99:11884 - 11889
   PubMed Web of Science ®Google Scholar
• Guijarro JI, Sunde M, Jones JA, Campbell ID, Dobson CM. Amyloid fibril formation by an SH3 domain. Proc Natl Acad Sci USA 1998; 95:4224 - 4228
   PubMed Web of Science ®Google Scholar
• Chiti F, Webster P, Taddei N, Clark A, Stefani M, Ramponi G, et al. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci USA 1999; 96:3590 - 3594
   PubMed Web of Science ®Google Scholar
• Bader R, Bamford R, Zurdo J, Luisi BF, Dobson CM. Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation. J Mol Biol 2006; 356:189 - 208
   PubMed Web of Science ®Google Scholar
• Pellarin R, Caflisch A. Interpreting the aggregation kinetics of amyloid peptides. J Mol Biol 2006; 360:882 - 892
   PubMed Web of Science ®Google Scholar
• Knowles TP, Fitzpatrick AW, Meehan S, Mott HR, Vendruscolo M, Dobson CM, et al. Role of intermolecular forces in defining material properties of protein nanofibrils. Science 2007; 318:1900 - 1903
   PubMed Web of Science ®Google Scholar
• Mukhopadhyay S, Krishnan R, Lemke EA, Lindquist S, Deniz AA. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc Natl Acad Sci USA 2007; 104:2649 - 2654
   PubMed Web of Science ®Google Scholar
• Kransnoslobodtsev AV, Shlyakhtenko LS, Ukraintsev E, Zaikova TO, Keana JF, Lyubchenko YL. Nanomedicine and protein misfolding diseases. Nanomedicine 2005; 1:300 - 305
   PubMedGoogle Scholar
• Rubinstein A, Lyubchenko YL, Sherman S. Dynamic properties of pH-dependent structural organization of the amyloidogenic beta-protein (1–40). Prion 2009; 3:31 - 43
   PubMed Web of Science ®Google Scholar
• Sorce B, Sabella S, Sandal M, Samori B, Santino A, Cingolani R, et al. Single-molecule mechanical unfolding of amyloidogenic beta(2)-microglobulin: The force-spectroscopy approach. Chemphyschem 2009; 10:1471 - 1477
   PubMed Web of Science ®Google Scholar
• Sandal M, Valle F, Tessari I, Mammi S, Bergantino E, Musiani F, et al. Conformational equilibria in monomeric alpha-synuclein at the single-molecule level. PLoS Biol 2008; 6:6
   Web of Science ®Google Scholar
• Brucale M, Sandal M, Di Maio S, Rampioni A, Tessari I, Tosatto L, et al. Pathogenic mutations shift the equilibria of alpha-synuclein single molecules towards structured conformers. Chembiochem 2009; 10:176 - 183
   PubMed Web of Science ®Google Scholar
• McAllister C, Karymov MA, Kawano Y, Lushnikov AY, Mikheikin A, Uversky VN, et al. Protein interactions and misfolding analyzed by AFM force spectroscopy. J Mol Biol 2005; 354:1028 - 1042
   PubMed Web of Science ®Google Scholar
• Lyubchenko YL, Sherman S, Shlyakhtenko LS, Uversky VN. Nanoimaging for protein misfolding and related diseases. J Cell Biochem 2006; 99:53 - 70
   Web of Science ®Google Scholar
• Yu J, Lyubchenko YL. Early stages for Parkinson's development: alpha-synuclein misfolding and aggregation. J Neuroimmune Pharm 2009; 4:10 - 16
   PubMed Web of Science ®Google Scholar
• Yu J, Malkova S, Lyubchenko YL. alpha-Synuclein misfolding: single molecule AFM force spectroscopy study. J Mol Biol 2008; 384:992 - 1001
   PubMed Web of Science ®Google Scholar
• Perutz MF, Pope BJ, Owen D, Wanker EE, Scherzinger E. Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques. Proc Natl Acad Sci USA 2002; 99:5596 - 5600
   PubMed Web of Science ®Google Scholar
• Balbirnie M, Grothe R, Eisenberg DS. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Proc Natl Acad Sci USA 2001; 98:2375 - 2380
   PubMed Web of Science ®Google Scholar
• Lyubchenko Y, Kim BH, Krasnoslobodtsev A, Yu J. Nanoimaging for protein misfolding diseases. Wiley Interdisciplinary Reviews: Nanomedicine and Nanobiotechnology 2010;
   PubMed Web of Science ®Google Scholar
• Merkel R, Nassoy P, Leung A, Ritchie K, Evans E. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 999; 397:50 - 53
   Google Scholar