142 results on '"Sulatskaya, Anna I."'
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2. Broken but not beaten: Challenge of reducing the amyloids pathogenicity by degradation
3. Mammalian odorant-binding proteins are prone to form amorphous aggregates and amyloid fibrils
4. Correction: Sulatskaya et al. Structural Features of Amyloid Fibrils Formed from the Full-Length and Truncated Forms of Beta-2-Microglobulin Probed by Fluorescent Dye Thioflavin T. Int. J. Mol. Sci. 2018, 19, 2762
5. Correction: Stepanenko et al. Trypsin Induced Degradation of Amyloid Fibrils. Int. J. Mol. Sci. 2021, 22, 4828
6. Point mutations affecting yeast prion propagation change the structure of its amyloid fibrils
7. OmpC and OmpF Outer Membrane Proteins of Escherichia coli and Salmonella enterica Form Bona Fide Amyloids
8. Trans-2-[4-(dimethylamino)styryl]-3-ethyl-1,3-benzothiazolium perchlorate - New fluorescent dye for testing of amyloid fibrils and study of their structure
9. Prediction of the Feasibility of Using the ≪Gold Standard≫ Thioflavin T to Detect Amyloid Fibril in Acidic Media.
10. Amyloid Fibrils of Pisum sativum L. Vicilin Inhibit Pathological Aggregation of Mammalian Proteins
11. Different conditions of fibrillogenesis cause polymorphism of lysozyme amyloid fibrils
12. RopB protein of Rhizobium leguminosarum bv. viciae adopts amyloid state during symbiotic interactions with pea (Pisum sativum L.)
13. sfGFP throws light on the early stages of β-barrel amyloidogenesis
14. New Evidence on a Distinction between Aβ40 and Aβ42 Amyloids: Thioflavin T Binding Modes, Clustering Tendency, Degradation Resistance, and Cross-Seeding
15. OmpF porins of Enterobacteriaceae possess amyloidogenic properties
16. New findings on GFP-like protein application as fluorescent tags: Fibrillogenesis, oligomerization, and amorphous aggregation
17. β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis
18. Trypsin Induced Degradation of Amyloid Fibrils
19. A New Trend in the Experimental Methodology for the Analysis of the Thioflavin T Binding to Amyloid Fibrils
20. Ans Fluorescent Probe Induces Clustering of Amyloid Fibers
21. Binding Stoichiometry and Affinity of Fluorescent Dyes to Proteins in Different Structural States
22. Accumulation of storage proteins in plant seeds is mediated by amyloid formation
23. Denaturing Effect of Guanidine Hydrohloride on Amyloid Fibrils
24. Interaction of Benzothiazole Dye Thioflavin T with Acidic Protein Prothymosin Alpha
25. Accumulation of storage proteins in plant seeds is mediated by amyloid formation
26. The Effect of Solution pH on the Structure and Stability of Lysozyme Amyloid Fibrils
27. α-Synuclein Amyloid Fibrils Investigation with the Use of Fluorescent Probe Thioflavin T
28. M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils
29. Aggregation of thioflavin T and its new derivative in the presence of anionic polyelectrolyte
30. Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils
31. Photophysical Properties of Fluorescent Probe Thioflavin T in Crowded Milieu
32. Stoichiometry and Affinity of Thioflavin T Binding to Sup35p Amyloid Fibrils
33. Effects of low urea concentrations on protein-water interactions
34. Photophysical Properties of Thioflavin T. Does it form Excimers When Integrated into Amyloid Fibrils?
35. Protein unfolding in crowded milieu: what crowding can do to a protein undergoing unfolding?
36. High Fluorescence Anisotropy of Thioflavin T in Aqueous Solution Resulting from Its Molecular Rotor Nature
37. High stability of trehalose/maltose binding protein from Thermococcus litoralis makes it a good candidate as a sensitive element in biosensor systems for sugar control
38. Effects of low urea concentrations on protein-water interactions.
39. Fluorescence of Dyes in Solutions with High Absorbance. Inner Filter Effect Correction
40. High Fluorescence Anisotropy of Thioflavin T in Aqueous Solution Resulting from Its Molecular Rotor Nature.
41. Reevaluation of ANS Binding to Human and Bovine Serum Albumins: Key Role of Equilibrium Microdialysis in Ligand – Receptor Binding Characterization
42. Analyzing Thioflavin T Binding to Amyloid Fibrils by an Equilibrium Microdialysis-Based Technique
43. Interaction of Thioflavin T with Amyloid Fibrils: Fluorescence Quantum Yield of Bound Dye
44. Interaction of Thioflavin T with Amyloid Fibrils: Stoichiometry and Affinity of Dye Binding, Absorption Spectra of Bound Dye
45. Fluorescence Quantum Yield of Thioflavin T in Rigid Isotropic Solution and Incorporated into the Amyloid Fibrils
46. High stability of trehalose/maltose binding protein fromThermococcus litoralismakes it a good candidate as a sensitive element in biosensor systems for sugar control
47. Interaction of ThioflavinT with Amyloid Fibrils:Fluorescence Quantum Yield of Bound Dye.
48. Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule Bacterium Rhizobium leguminosarum.
49. Structural Features of Amyloid Fibrils Formed from the Full-Length and Truncated Forms of Beta-2-Microglobulin Probed by Fluorescent Dye Thioflavin T.
50. Investigation of α-Synuclein Amyloid Fibrils Using the Fluorescent Probe Thioflavin T.
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