Citation sources

Updated weekly. Details via Crossref
Crossref Scopus Google Scholar
24 22 Search
2025
Deep learning-based denoising for unbiased analysis of morphology and stiffness in amyloid fibrils
Computers in Biology and Medicine
2025
Unraveling the Molecular Pathways of Protein Fibrillation under Thermal Acid Hydrolysis
Small
2024
Study of Insulin Aggregation and Fibril Structure under Different Environmental Conditions
International Journal of Molecular Sciences
2023
Mechanisms and pathology of protein misfolding and aggregation
Nature Reviews Molecular Cell Biology
2023
Chemical Modification of the Amino Groups of Human Insulin: Investigating Structural Properties and Amorphous Aggregation of Acetylated Species
The Protein Journal
2023
Modulation of Insulin Amyloid Fibrillization in Imidazolium-Based Ionic Liquids with Hofmeister Series Anions
International Journal of Molecular Sciences
2022
Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State
International Journal of Molecular Sciences
2022
Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates
Biochemistry (Moscow)
2022
Exploring Epigallocatechin-3-Gallate Autoxidation Products: Specific Incubation Times Required for Emergence of Anti-Amyloid Properties
Antioxidants
2021
Aggregation Condition–Structure Relationship of Mouse Prion Protein Fibrils
International Journal of Molecular Sciences
2021
Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation
PeerJ
2021
Secondary Nucleation and the Conservation of Structural Characteristics of Amyloid Fibril Strains
Frontiers in Molecular Biosciences
2021
Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils
International Journal of Molecular Sciences
2021
Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation
International Journal of Molecular Sciences
2021
Autoxidation Enhances Anti-Amyloid Potential of Flavone Derivatives
Antioxidants
2021
Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration
International Journal of Molecular Sciences
2021
Exploring the occurrence of thioflavin-T-positive insulin amyloid aggregation intermediates
PeerJ
2020
Identifying Insulin Fibril Conformational Differences by Thioflavin-T Binding Characteristics
Biomacromolecules
2020
The Properties of α-Synuclein Secondary Nuclei Are Dominated by the Solution Conditions Rather than the Seed Fibril Strain
ACS Chemical Neuroscience
2020
Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates
International Journal of Molecular Sciences
2020
Gallic acid oxidation products alter the formation pathway of insulin amyloid fibrils
Scientific Reports
2020
Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity
International Journal of Molecular Sciences
2020
Insulin amyloid polymorphs: implications for iatrogenic cytotoxicity
RSC Advances
Additional cited-by details will be shown when available from Crossref