| scholarly article | Q13442814 |
| P50 | author | Salvador Ventura | Q41047849 |
| Ricardo Graña-Montes | Q55117924 | ||
| Débora Foguel | Q57096247 | ||
| Nathalia Varejão | Q84384765 | ||
| P2093 | author name string | Ricardo Sant'Anna | |
| Yraima Cordeiro | |||
| Juliana Cortines | |||
| Aline Alves | |||
| Carolina Braga | |||
| Karinne M Pimenta | |||
| P2860 | cites work | Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation | Q24530946 |
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| Structural insight into pH-induced conformational changes within the native human transthyretin tetramer | Q27651370 | ||
| Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade | Q27679360 | ||
| SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling | Q27860614 | ||
| The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state | Q28118516 | ||
| Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins | Q28281645 | ||
| Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case | Q30164098 | ||
| Amyloid fibril formation by an SH3 domain | Q30176202 | ||
| Protein sequences encode safeguards against aggregation. | Q30374454 | ||
| Structural classification of toxic amyloid oligomers | Q30484255 | ||
| Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins | Q31041572 | ||
| AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides | Q33275645 | ||
| Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin | Q33435248 | ||
| Anomalous pressure dissociation of large protein aggregates. Lack of concentration dependence and irreversibility at extreme degrees of dissociation of extracellular hemoglobin | Q33469083 | ||
| The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid | Q34380911 | ||
| Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril | Q34429753 | ||
| Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation | Q34440874 | ||
| Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity | Q34443897 | ||
| Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways | Q34468169 | ||
| The pathway by which the tetrameric protein transthyretin dissociates. | Q34469219 | ||
| The importance of sequence diversity in the aggregation and evolution of proteins | Q34474861 | ||
| A consensus method for the prediction of 'aggregation-prone' peptides in globular proteins | Q34552231 | ||
| Prevention of amyloid-like aggregation as a driving force of protein evolution. | Q34658253 | ||
| Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily | Q34675827 | ||
| Heparan sulfate/heparin promotes transthyretin fibrillization through selective binding to a basic motif in the protein | Q34805156 | ||
| The role of hydrophobic interactions in initiation and propagation of protein folding | Q35016494 | ||
| Heparan sulphate proteoglycans in Alzheimer's disease and amyloid-related disorders | Q35183966 | ||
| The role of alpha-synuclein in Parkinson's disease: insights from animal models | Q35209957 | ||
| A three-stage kinetic model of amyloid fibrillation | Q35753756 | ||
| High pressure studies on transthyretin. | Q36074704 | ||
| Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity | Q36098093 | ||
| Protein aggregation and amyloidosis: confusion of the kinds? | Q36376624 | ||
| The role of amyloid-beta derived diffusible ligands (ADDLs) in Alzheimer's disease | Q36483106 | ||
| Interactions between heparan sulfate and proteins: the concept of specificity | Q36552851 | ||
| 1H NMR analysis of fibril-forming peptide fragments of transthyretin. | Q36718089 | ||
| Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis | Q36790516 | ||
| Fourier transform infrared spectroscopic analysis of protein secondary structures | Q36905495 | ||
| Biology of Amyloid: Structure, Function, and Regulation | Q37800223 | ||
| A diversity of assembly mechanisms of a generic amyloid fold | Q37897372 | ||
| The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug | Q37975816 | ||
| Transthyretin deposition in familial amyloidotic polyneuropathy | Q37999492 | ||
| Evolutionary selection for protein aggregation | Q38044424 | ||
| Protein aggregation profile of the human kinome | Q41531353 | ||
| Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins | Q41550219 | ||
| The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions | Q41696172 | ||
| Solvent effects on self-assembly of beta-amyloid peptide | Q42122726 | ||
| The conformation of Alzheimer's beta peptide determines the rate of amyloid formation and its resistance to proteolysis | Q42126660 | ||
| Amyloid fibril formation can proceed from different conformations of a partially unfolded protein | Q43203312 | ||
| Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis | Q43753104 | ||
| Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS. | Q44174044 | ||
| Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease | Q44428767 | ||
| Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro | Q44538680 | ||
| Transthyretin aggregation under partially denaturing conditions is a downhill polymerization | Q44925089 | ||
| Circular dichroic analysis of protein conformation: inclusion of the beta-turns. | Q45959377 | ||
| How evolutionary pressure against protein aggregation shaped chaperone specificity | Q46855190 | ||
| Aggregation gatekeepers modulate protein homeostasis of aggregating sequences and affect bacterial fitness | Q50495075 | ||
| Vitreous amyloidosis in two large mainland Chinese kindreds resulting from transthyretin variant Lys35Thr and Leu55Arg | Q50527948 | ||
| Analysis of protein aggregation kinetics. | Q52143609 | ||
| Elucidating the folding problem of helical peptides using empirical parameters | Q52376869 | ||
| Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. | Q52857635 | ||
| Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB | Q54131245 | ||
| Heparin Binding by Murine Recombinant Prion Protein Leads to Transient Aggregation and Formation of RNA-Resistant Species | Q57084698 | ||
| Probing Solvent Accessibility of Transthyretin Amyloid by Solution NMR Spectroscopy | Q57188082 | ||
| Tetramer Dissociation and Monomer Partial Unfolding Precedes Protofibril Formation in Amyloidogenic Transthyretin Variants | Q57665571 | ||
| A chemical approach to elucidate tin mechanism of transthyretin and β-protein amyloid fibril formation | Q58189789 | ||
| A novel transthyretin mutation at position 30 (Leu for Val) associated with familial amyloidotic polyneuropathy | Q68038569 | ||
| Transthyretin gene analysis in European patients with suspected familial amyloid polyneuropathy | Q72012225 | ||
| Structural features of the Abeta amyloid fibril elucidated by limited proteolysis | Q74552318 | ||
| P433 | issue | 41 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 28324-28337 | |
| P577 | publication date | 2014-08-01 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses | |
| P478 | volume | 289 |
| Q28118595 | Amyloid properties of the leader peptide of variant B cystatin C: implications for Alzheimer and macular degeneration |
| Q31036714 | Attraction by repulsion: compounds with like charges undergo self-assembly in water that improves in high salt and persists in real biological fluids. |
| Q39221178 | Force spectroscopy reveals the presence of structurally modified dimers in transthyretin amyloid annular oligomers. |
| Q51478393 | Heparin promotes fibril formation by the N-terminal fragment of amyloidogenic apolipoprotein A-I. |
| Q36012287 | PrP charge structure encodes interdomain interactions |
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