Conformational constraints for amyloid fibrillation: the importance of being unfolded.

By Vladimir N Uversky, A. Fink. Biochimica et Biophysica Acta, 2004

1,017 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/61210fd843ca7530a7758fa79a3b68ef6a0f0a5d

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Citations in the corpus

Analysis of molecular recognition features (MoRFs). (2006, background): “43,85,86 It has been also hypothesized that PPII, being transiently populated by a polypeptide chain in a major amyloidogenic conformation, pre-molten globule state 87 may play a crucial role in the protein fibrillogenesis.”
PASTA 2.0: an improved server for protein aggregation prediction (2014, background): “Within this context, an intermediate partially disordered or flexible state was previously hypothesized in an aggregation model (24).”
A decade and a half of protein intrinsic disorder: Biology still waits for physics (2013, background): “Several unrelated proteins including many IDPs are known to be involved in these protein deposition diseases.(234,235) An illustrative examples of human neurodegenerative diseases associated with IDPs includes Alzheimer’s disease (deposition of amyloid-b, tau-protein, a-synuclein fragment NAC); vari”
Intrinsically disordered proteins in human diseases: introducing the D2 concept. (2008, background): “Although the amyloid fibrils from different diseases are structurally and morphologically similar to each other, the polypeptide constituents of fibrils are diverse and the native conformation may be rich in β-sheet, α-helix, and/or β-helix, or they may be natively unfolded (138).”
Towards an Understanding of the Temperature/ Pressure Configurational and Free-Energy Landscape of Biomolecules (2007, positive): “Some of these diseases result from the simple fact that if proteins do not fold correctly, they will not be able to exercise their proper functions, like insulin, islet amyloid polypeptide (IAPP), b2 microglobulin, and a-lactalbumin [104, 105].”
Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillation (2006, background): “For example, several diseases are associated with protein disorder, either through aggregation (Uversky and Fink 2004) or chromosomal translocations (Dyson and Wright 2005).”
Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature. (2009, methodology): “Fink's empirical equation has been used to analyze numerous data sets thus allowing for comparisons to be made between related data sets [34,35,37,142]; an example is shown in Fig.”