Introduction and technical survey: protein aggregation and fibrillogenesis.

作者: J. Robin Harris , Nathaniel G. N. Milton

DOI: 10.1007/978-94-007-5416-4_1

关键词: Data scienceClinical scienceFibrillogenesisBiophysicsProtein aggregationComputer scienceProtein oligomerizationProtein multimerization

摘要: In this chapter we provided the overall background to subject of protein aggregation and fibrillogenesis in amyloidogenesis, with introduction brief discussion various topics that are included coming chapters. The division book into basic science clinical sections enables correlation be made. many proteins peptides have currently been found undergo tabulated. A broad technical survey is made, indicate vast array techniques available study aspects oligomerization, fibrillogenesis. These split three groups tabulated, as microscopical techniques, analytical biophysical methods, biochemical cellular techniques. few discussed, but most cases only a link relevant recent literature provided.

参考文章(184)
Partha Pratim Bose, Urmimala Chatterjee, Ina Hubatsch, Per Artursson, Thavendran Govender, Hendrik G. Kruger, Margareta Bergh, Jan Johansson, Per I. Arvidsson, In vitro ADMET and physicochemical investigations of poly-N-methylated peptides designed to inhibit Aβ aggregation Bioorganic & Medicinal Chemistry. ,vol. 18, pp. 5896- 5902 ,(2010) , 10.1016/J.BMC.2010.06.087
Kathleen A. Maguire-Zeiss, Howard J. Federoff, Future directions for immune modulation in neurodegenerative disorders: focus on Parkinson's disease. Journal of Neural Transmission. ,vol. 117, pp. 1019- 1025 ,(2010) , 10.1007/S00702-010-0431-6
Enrico Rennella, Alessandra Corazza, Sofia Giorgetti, Federico Fogolari, Paolo Viglino, Riccardo Porcari, Laura Verga, Monica Stoppini, Vittorio Bellotti, Gennaro Esposito, Folding and Fibrillogenesis: Clues from β2-Microglobulin Journal of Molecular Biology. ,vol. 401, pp. 286- 297 ,(2010) , 10.1016/J.JMB.2010.06.016
Anna-Lena Göransson, K. Peter R. Nilsson, Katarina Kågedal, Ann-Christin Brorsson, Identification of distinct physiochemical properties of toxic prefibrillar species formed by Aβ peptide variants. Biochemical and Biophysical Research Communications. ,vol. 420, pp. 895- 900 ,(2012) , 10.1016/J.BBRC.2012.03.097
Marie Ø. Pedersen, Katrine Mikkelsen, Manja A. Behrens, Jan S. Pedersen, Jan J. Enghild, Troels Skrydstrup, Anders Malmendal, Niels Chr. Nielsen, NMR reveals two-step association of Congo Red to amyloid β in low-molecular-weight aggregates. Journal of Physical Chemistry B. ,vol. 114, pp. 16003- 16010 ,(2010) , 10.1021/JP108035Y
B. Chen, K. R. Thurber, F. Shewmaker, R. B. Wickner, R. Tycko, Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 106, pp. 14339- 14344 ,(2009) , 10.1073/PNAS.0907821106
Karen E. Marshall, Kyle L. Morris, Deborah Charlton, Nicola O’Reilly, Laurence Lewis, Helen Walden, Louise C. Serpell, Hydrophobic, aromatic, and electrostatic interactions play a central role in amyloid fibril formation and stability. Biochemistry. ,vol. 50, pp. 2061- 2071 ,(2011) , 10.1021/BI101936C
Fernanda Ricchelli, Raffaella Buggio, Denise Drago, Mario Salmona, Gianluigi Forloni, Alessandro Negro, Giuseppe Tognon, Paolo Zatta, Aggregation/fibrillogenesis of recombinant human prion protein and Gerstmann-Sträussler-Scheinker disease peptides in the presence of metal ions Biochemistry. ,vol. 45, pp. 6724- 6732 ,(2006) , 10.1021/BI0601454
F ROUSSEAU, J SCHYMKOWITZ, L SERRANO, Protein aggregation and amyloidosis: confusion of the kinds? Current Opinion in Structural Biology. ,vol. 16, pp. 118- 126 ,(2006) , 10.1016/J.SBI.2006.01.011