Multistep nucleus formation and a separate subunit contribution of the amyloidgenesis of heat-denatured monellin

Protein Science

Volumn 10, Issue 10, 2001, Pages 2093-2101

  Konno, T ^a  

^a UNIVERSITY OF FUKUI   (Japan)

Author keywords

Amyloid; Monellin; Nucleation; Seeding effect

Indexed keywords

AMYLOID; MONELLIN; VEGETABLE PROTEIN;

ALPHA CHAIN; ARTICLE; BETA CHAIN; CELL MATURATION; CELL NUCLEUS; CONFORMATIONAL TRANSITION; HEATING; KINETICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION;

AMYLOID; AMYLOIDOSIS; HEAT; KINETICS; PLANT PROTEINS; PROTEIN DENATURATION; RECOMBINANT PROTEINS;

EID: 0034813363     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.20201     Document Type: Article

References (35)

1. The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences
2. Designing conditions for in vitro formation of amyloid protofilaments and fibrils
3. Protein folding and misfolding inside and outside the cell
4. The fundamentals of protein folding: Bringing together theory and experiment
5. Structural characterization of monellin in the alcohol-denatured state by NMR: Evidence for β-sheet to α-helix conversion
6. Protein aggregation: Folding aggregates, inclusion bodies and amyloid
7. A nucleated assembly mechanism of Alzheimer paired helical filaments
8. Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of gamma-trace basic protein (cystatin C)
9. Computed circular dichroism spectra for the evaluation of protein conformation
10. Amyloid fibril formation by an SH3 domain
11. Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
12. Seeding "one-dimensional crystallization" of amytoid: A pathogenic mechanism in Alzheimer's disease and scrapie?
13. Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro
14. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
15. Redesigning a sweet protein: Increased stability and renaturabitity
16. Complete amino acid sequence of the sweet protein monellin
17. Solution X-ray scattering analysis of cold- heat-, and urea-denatured states in a protein. Streptomyces subtilisin inhibitor
18. Amyloid-like aggregates of a plant protein: A case of a sweet-tasting protein, monellin
19. Amyloid diseases: Abnormal protein aggregation in neurodegeneration
20. Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain
21. Purification of monellin, the sweet principle of Dioscoreophyllum cumminsii
22. Formation of oligomeric monellin in protein denaturants
23. Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors
24. Kinetic analysis of amyloid fibril formation
25. The solubility of amino acids and related compounds in aqueous urea solutions
26. Prion protein biology
27. Amyloid fibrillogenesis: Themes and variations
28. Fourier transform infrared spectroscopy in analysis of protein deposits
29. Amyloidosis
30. Two crystal structures of a potently sweet protein. Natural monellin at 2.75 A resolution and single-chain monellin at 1.7 A resolution
31. Solution structure of a sweet protein: NMR study of MNEI, a single chain monellin
32. Amyloidosis
33. 1H resonance assignments, secondary structure and general topology of single-chain monellin in solution as determined by 1H 2D-NMR
34. Evidence for a partially folded intermediate in α-synuclein fibril formation
35. α-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease