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Common core structure of amyloid fibrils by synchrotron X-ray diffraction.
TLDR
Using intense synchrotron sources, it is observed that six different ex vivo amyloid fibrils and two synthetic fibril preparations all gave similar high-resolution X-ray fibre diffraction patterns, consistent with a helical array of beta-sheets parallel to the fibre long axis, with the strands perpendicular to this axis, which confirms that amyloidsfibrils comprise a structural superfamily and share a common protofilament substructure.
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
TLDR
Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.
Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
TLDR
A model for the polypeptide packing as a basis for understanding the structure of amyloid fibrils in general is proposed.
Amyloid fibril formation by an SH3 domain.
TLDR
Results indicate that the A state of PI3-SH3 is partially folded and support the hypothesis that partially folded states formed in solution are precursors of amyloid deposition.
Structural basis for rodlet assembly in fungal hydrophobins.
TLDR
The three-dimensional structure of the monomeric form of the class I hydrophobin EAS, which forms a beta-barrel structure punctuated by several disordered regions and displays a complete segregation of charged and hydrophobic residues on its surface, is described.
Mutations in cardiac T-box factor gene TBX20 are associated with diverse cardiac pathologies, including defects of septation and valvulogenesis and cardiomyopathy.
TLDR
These findings are the first to link TBX20 mutations to human pathology and provide insights into how mutation of different genes in an interactive regulatory circuit lead to diverse clinical phenotypes, with implications for diagnosis, genetic screening, and patient follow-up.
Hydrophobins—Unique Fungal Proteins
TLDR
The self-assembly properties and remarkable structural and physicochemical characteristics of hydrophobin proteins underlie the multiple roles played by these unique proteins in fungal biology.
The protofilament substructure of amyloid fibrils.
TLDR
Cross-correlation techniques are used to average electron microscopy images of multiple cross-sections in order to reconstruct the sub-structure of ex vivo amyloid fibrils composed of amyloids A protein, monoclonal immunoglobulin lambda light chain, Leu60Arg variant apolipoprotein AI, and Asp67His variant lysozyme.
Zinc Fingers‐‐Folds for Many Occasions
TLDR
The similarities and differences in structure and functions of different ZnF classes are reviewed and the versatility of this fold is highlighted.
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