The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution
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TLDR
This study shows that the tendency to form aggregates among the four studied proteins correlates with their known amyloidogenic potential, which could perturb the structure and/or stability of the monomeric species leading initially to the formation of soluble aggregates and at a later stage to insoluble amyloids fibrils.About:
This article is published in FEBS Letters.The article was published on 1997-12-01 and is currently open access. It has received 100 citations till now. The article focuses on the topics: Amyloid & Transthyretin.read more
Citations
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Journal ArticleDOI
Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
TL;DR: The results confirm the model of intermolecular β-sheet formation as a widespread underlying mechanism of protein aggregation and opens the door to a fully automated, sequence-based design strategy to improve the aggregation properties of proteins of scientific or industrial interest.
Journal ArticleDOI
Tabulation of human transthyretin (TTR) variants, 2003.
TL;DR: The list presented here documents all TTR gene mutations reported to date and includes information on a total of 100 separate forms of the protein, including 1 1 nonamyloidogenic TTR proteins.
Journal ArticleDOI
Transthyretin aggregation under partially denaturing conditions is a downhill polymerization.
TL;DR: It is suggested that amyloid formation by M-TTR under partially denaturing conditions is a downhill polymerization, in which the highest energy species is the native monomer.
Journal ArticleDOI
Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants.
TL;DR: It is shown that tetramer dissociation and partial unfolding of the monomer precedes amyloid fibril formation, and that TTR variants with the least thermodynamically stable non-native monomer produce the largest amount of partially unfolded monomeric species and soluble aggregates under conditions that are close to physiological.
Journal ArticleDOI
Transthyretin: a review from a structural perspective.
James A. Hamilton,M.D. Benson +1 more
TL;DR: Progress has been made toward solving the mechanism of amyloid formation and detecting the variant gene in individuals at risk of developing Alzheimer's disease.
References
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Estimation of the molecular weights of proteins by Sephadex gel-filtration.
TL;DR: The results are similar to those of previous studies, where the objective was to establish a cause-and-effect relationship, rather than a straightforward relationship between the number of cells and the content of the molecule.
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A peculiar form of peripheral neuropathy; familiar atypical generalized amyloidosis with special involvement of the peripheral nerves.
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Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
Wilfredo Colón,Jeffery W. Kelly +1 more
TL;DR: Near-UV CD analysis in combination with glutaraldehyde cross-linking studies suggests that a pH-mediated tetramer to monomer transition is operative in the pH range where fibril formation occurs, consistent with denaturation to a monomeric TTR intermediate which has lost its native tertiary structure and capability to form fibrils.
ComponentDOI
The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30→Met variant to 1.7-Å resolution
Jean A. Hamilton,L.K. Steinrauf,Bradford C. Braden,Juris J. Liepnieks,Merrill D. Benson,Gosta Holmgren,Ola Sandgren,Lars Steen +7 more
TL;DR: The x-ray crystal structures of transthyretin (prealbumin) and the amyloidogenic Val-30-Met variant have been refined at 1.7-A resolution to R-values of 0.168 and 0.179.
Journal ArticleDOI
Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease.
TL;DR: This biophysical study demonstrates that Val-30-Met TTR is significantly less stable toward acid denaturation and more amyloidogenic than wild-type TTR, which in turn is less stable and moreAmyloidogenicity than Thr-119-MetTTR, and suggests that the Thr- 119-Met mutation confers decreased amyloidsogenicity by stabilizing tetrameric TTR toward acidDenaturation.
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The Acid-Mediated Denaturation Pathway of Transthyretin Yields a Conformational Intermediate That Can Self-Assemble into Amyloid†
Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
Wilfredo Colón,Jeffery W. Kelly +1 more