By Vladimir N. Uversky, Anthony Fink
Examine exhibits that almost all neurodegenerative illnesses, systemic amyloidoses etc, come up from the misfolding and aggregation of an underlying protein. this can be the 1st publication to debate major achievements in protein structure-function relationships in biochemistry, molecular biology and molecular medication. The authors summarize contemporary development within the figuring out of the relationships among protein misfolding, aggregation and improvement of protein deposition issues.
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Additional resources for Protein Misfolding, Aggregation and Conformational Diseases: Part A: Protein Aggregation and Conformational Diseases (Protein Reviews)
Acad. Sci. USA 100:6446–6451. S. (2004). The nonconserved wrapping of conserved protein folds deﬁnes a trend towards increasing connectivity in proteomic networks. Proc. Natl. Acad. Sci. USA 101:2823–2827. L. (1995a). Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24:495–522. L. (1995b). Molten globules. Methods Mol. Biol. 40:343–360. L. (1998). Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold. Des. 3:9–15. , and Damaschun, G. (1995).
330:943–954. L. (2002a). Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid ﬁbril formation at physiological pH. J. Biol. Chem. 277:12657–12665. L. (2002b). Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid ﬁbrillation: evidence for an off-pathway oligomer at acidic pH. J. Biol. Chem. 277:12666–12679. C. (1997). Common core structure of amyloid ﬁbrils by synchrotron X-ray diffraction. J.
Conformation-dependent environments in folding proteins. J. Chem. Phys. 114:2489–2502. Fernandez, A. (2002). Insufﬁcient hydrogen-bond desolvation and prion-related disease. Eur. J. Biochem. 269: 4165–4168. N. Uversky et al. Fernandez, A. (2004). Packing defects in folded proteins: what cannot be kept dry must be conserved. J. Mol. Biol. 337:477–483. S. (2003). Proteins with H-bond packing defects are highly interactive with lipid bilayers: implications for amyloidogenesis. Proc. Natl. Acad. Sci.