Bisphenol A Analogs Induce Cellular Dysfunction in Human Trophoblast Cells in a Thyroid Hormone Receptor-Dependent Manner: In Silico and In Vitro Analyses | Environmental Science & Technology
Advances in the Simulation of Protein Aggregation at the Atomistic Scale | The Journal of Physical Chemistry B
IJMS | Free Full-Text | The Role of Proteolysis in Amyloidosis
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Square channels formed by a peptide derived from transthyretin - Chemical Science (RSC Publishing) DOI:10.1039/C6SC01927G
Amino acid - Wikipedia
Atomic structure and hierarchical assembly of a cross-β amyloid fibril | PNAS
Square channels formed by a peptide derived from transthyretin - Chemical Science (RSC Publishing) DOI:10.1039/C6SC01927G
IJMS | Free Full-Text | Extracellular Vesicles in Regenerative Processes Associated with Muscle Injury Recovery of Professional Athletes Undergoing Sub Maximal Strength Rehabilitation
Atomic structure and hierarchical assembly of a cross-β amyloid fibril | PNAS
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Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids | Chemical Reviews
Frontiers | Aggregation-Prone Structural Ensembles of Transthyretin Collected With Regression Analysis for NMR Chemical Shift
Multi-eGO: an in-silico lens to look into protein aggregation kinetics at atomic resolution | bioRxiv
Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril | PNAS
Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril | PNAS
Square channels formed by a peptide derived from transthyretin - Chemical Science (RSC Publishing) DOI:10.1039/C6SC01927G
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Three-dimensional structure of TTR(105-115) in the amyloid fibril... | Download Scientific Diagram
Multi-eGO: an in-silico lens to look into protein aggregation kinetics at atomic resolution | bioRxiv
Massively parallel interrogation of protein fragment secretability using SECRiFY reveals features influencing secretory system transit | Nature Communications
Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril | PNAS
Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers | Biomacromolecules
