Crossref
journal-article
Springer Science and Business Media LLC
Nature (297)
References
30
Referenced
307
-
Dobson, C. M. Protein folding and misfolding. Nature 426, 884–890 (2003)
(
10.1038/nature02261
) / Nature by CM Dobson (2003) -
Sunde, M. & Blake, C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Advan. Protein Chem. 50, 123–159 (1997)
(
10.1016/S0065-3233(08)60320-4
) / Advan. Protein Chem. by M Sunde (1997) -
Selkoe, D. J. Folding proteins in fatal ways. Nature 426, 900–904 (2003)
(
10.1038/nature02264
) / Nature by DJ Selkoe (2003) -
Wickner, R. B. et al. Prions: proteins as genes and infectious entities. Genes Dev. 18, 470–485 (2004)
(
10.1101/gad.1177104
) / Genes Dev. by RB Wickner (2004) -
Chapman, M. R. et al. Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 295, 851–855 (2002)
(
10.1126/science.1067484
) / Science by MR Chapman (2002) -
Kelly, J. W. & Balch, W. E. Amyloid as a natural product. J. Cell Biol. 161, 461–462 (2003)
(
10.1083/jcb.200304074
) / J. Cell Biol. by JW Kelly (2003) -
Si, K., Lindquist, S. & Kandel, E. R. A neuronal isoform of the Aplysia CPEB has prion-like properties. Cell 115, 879–891 (2003)
(
10.1016/S0092-8674(03)01020-1
) / Cell by K Si (2003) -
Stefani, M. & Dobson, C. M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81, 678–699 (2003)
(
10.1007/s00109-003-0464-5
) / J. Mol. Med. by M Stefani (2003) -
Jiménez, J. L. et al. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18, 815–821 (1999)
(
10.1093/emboj/18.4.815
) / EMBO J. by JL Jiménez (1999) -
Zurdo, J., Guijarro, J. I., Jiménez, J. L., Saibil, H. R. & Dobson, C. M. Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. J. Mol. Biol. 311, 325–340 (2001)
(
10.1006/jmbi.2001.4858
) / J. Mol. Biol. by J Zurdo (2001) -
Zurdo, J., Guijarro, J. I. & Dobson, C. M. Preparation and characterization of purified amyloid fibrils. J. Am. Chem. Soc. 123, 8141–8142 (2001)
(
10.1021/ja016229b
) / J. Am. Chem. Soc. by J Zurdo (2001) -
Ventura, S. et al. Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. Proc. Natl Acad. Sci. USA 101, 7258–7263 (2004)
(
10.1073/pnas.0308249101
) / Proc. Natl Acad. Sci. USA by S Ventura (2004) -
Englander, S. W. & Krishna, M. M. G. Hydrogen exchange. Nature Struct. Biol. 8, 741–742 (2001)
(
10.1038/nsb0901-741
) / Nature Struct. Biol. by SW Englander (2001) -
Kheterpal, I., Zhou, S., Cook, K. D. & Wetzel, R. Aβ amyloid fibrils possess a core structure highly resistant to hydrogen exchange. Proc. Natl Acad. Sci. USA 97, 13597–13601 (2000)
(
10.1073/pnas.250288897
) / Proc. Natl Acad. Sci. USA by I Kheterpal (2000) -
Hoshino, M. et al. Mapping the core of the β2-microglobulin amyloid fibril by H/D exchange. Nature Struct. Biol. 9, 332–336 (2002)
(
10.1038/nsb792
) / Nature Struct. Biol. by M Hoshino (2002) -
Olofsson, A., Ippel, J. H., Wijmenga, S. S., Lundgren, E. & Oehman, A. Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy. J. Biol. Chem. 279, 5699–5707 (2004)
(
10.1074/jbc.M310605200
) / J. Biol. Chem. by A Olofsson (2004) -
Petkova, A. T. et al. Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 307, 262–265 (2005)
(
10.1126/science.1105850
) / Science by AT Petkova (2005) -
Polverino de Laureto, P. et al. Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis. J. Mol. Biol. 334, 129–141 (2003)
(
10.1016/j.jmb.2003.09.024
) / J. Mol. Biol. by P Polverino de Laureto (2003) -
Miranker, A., Robinson, C. V., Radford, S. E., Aplin, R. T. & Dobson, C. M. Detection of transient protein folding populations by mass spectrometry. Science 262, 896–900 (1993)
(
10.1126/science.8235611
) / Science by A Miranker (1993) -
Yamaguchi, K. et al. Core and heterogeneity of β2-microglobulin amyloid fibrils as revealed by H/D exchange. J. Mol. Biol. 338, 559–571 (2004)
(
10.1016/j.jmb.2004.02.067
) / J. Mol. Biol. by K Yamaguchi (2004) -
Kheterpal, I. et al. Aβ protofibrils possess a stable core structure resistant to hydrogen exchange. Biochemistry 42, 14092–14098 (2003)
(
10.1021/bi0357816
) / Biochemistry by I Kheterpal (2003) -
Ban, T., Hamada, D., Hasegawa, K., Naiki, H. & Goto, Y. Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J. Biol. Chem. 278, 16462–16465 (2003)
(
10.1074/jbc.C300049200
) / J. Biol. Chem. by T Ban (2003) -
Goldsbury, C., Kistler, J., Aebi, U., Arvinte, T. & Cooper, G. J. S. Watching amyloid fibrils grow by time-lapse atomic force microscopy. J. Mol. Biol. 285, 33–39 (1999)
(
10.1006/jmbi.1998.2299
) / J. Mol. Biol. by C Goldsbury (1999) -
Hall, D. & Edskes, H. Silent prions lying in wait: a two-hit model of prion/amyloid formation and infection. J. Mol. Biol. 336, 775–786 (2004)
(
10.1016/j.jmb.2003.12.004
) / J. Mol. Biol. by D Hall (2004) -
Hammarstroem, P., Wiseman, R. L., Powers, E. T. & Kelly, J. W. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 299, 713–716 (2003)
(
10.1126/science.1079589
) / Science by P Hammarstroem (2003) -
Sekijima, Y. et al. The biological and chemical basis for tissue-selective amyloid disease. Cell 121, 73–85 (2005)
(
10.1016/j.cell.2005.01.018
) / Cell by Y Sekijima (2005) -
Cohen, F. E. & Kelly, J. W. Therapeutic approaches to protein-misfolding diseases. Nature 426, 905–909 (2003)
(
10.1038/nature02265
) / Nature by FE Cohen (2003) -
Hamada, D., Yanagihara, I. & Tsumoto, K. Engineering amyloidogenicity towards the development of nanofibrillar materials. Trends Biotechnol. 22, 93–97 (2004)
(
10.1016/j.tibtech.2003.12.003
) / Trends Biotechnol. by D Hamada (2004) -
MacPhee, C. E. & Woolfson, D. N. Engineered and designed peptide-based fibrous biomaterials. Curr. Opin. Solid State Mater. Sci. 8, 141–149 (2004)
(
10.1016/j.cossms.2004.01.010
) / Curr. Opin. Solid State Mater. Sci. by CE MacPhee (2004) -
Dobson, C. M. In the footsteps of alchemists. Science 304, 1261–1262 (2004)
(
10.1126/science.1093078
) / Science by CM Dobson (2004)
Dates
Type | When |
---|---|
Created | 20 years, 1 month ago (July 27, 2005, 3:11 p.m.) |
Deposited | 2 years, 3 months ago (May 18, 2023, 1:48 p.m.) |
Indexed | 1 month ago (July 28, 2025, 2:48 a.m.) |
Issued | 20 years, 1 month ago (July 28, 2005) |
Published | 20 years, 1 month ago (July 28, 2005) |
Published Print | 20 years, 1 month ago (July 28, 2005) |
@article{Carulla_2005, title={Molecular recycling within amyloid fibrils}, volume={436}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/nature03986}, DOI={10.1038/nature03986}, number={7050}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Carulla, Natàlia and Caddy, Gemma L. and Hall, Damien R. and Zurdo, Jesús and Gairí, Margarida and Feliz, Miguel and Giralt, Ernest and Robinson, Carol V. and Dobson, Christopher M.}, year={2005}, month=jul, pages={554–558} }