A spidroin-derived solubility tag enables controlled aggregation of a designed amyloid protein

Alzheimer's disease

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Efficient protein production inspired by how spiders make silk

(2017) Nina Kronqvist et al.   Nature Communications

Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state

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Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines

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Monomeric Aβ1–40 and Aβ1–42 Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil

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The formation, function and regulation of amyloids: insights from structural biology

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Large Soluble Oligomers of Amyloid β-Protein from Alzheimer Brain Are Far Less Neuroactive Than the Smaller Oligomers to Which They Dissociate

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Ionic Strength Modulation of the Free Energy Landscape of Aβ40 Peptide Fibril Formation

(2016) Axel Abelein et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

BRICHOS binds to a designed amyloid-forming  -protein and reduces proteasomal inhibition and aggresome formation

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Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA

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The amyloid state and its association with protein misfolding diseases

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The BRICHOS Domain, Amyloid Fibril Formation, and Their Relationship

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Binding of the Radioligand SIL23 to α-Synuclein Fibrils in Parkinson Disease Brain Tissue Establishes Feasibility and Screening Approaches for Developing a Parkinson Disease Imaging Agent

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Proliferation of amyloid- 42 aggregates occurs through a secondary nucleation mechanism

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The Amyloid State of Proteins in Human Diseases

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Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions

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relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins

(2011) Michael Bieri et al.   JOURNAL OF BIOMOLECULAR NMR

Amyloid-β forms fibrils by nucleated conformational conversion of oligomers

(2011) Jiyong Lee et al.   Nature Chemical Biology

Assays for α-synuclein aggregation

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A facile method for expression and purification of the Alzheimer’s disease-associated amyloid β-peptide

(2009) Dominic M. Walsh et al.   FEBS Journal

The Common Architecture of Cross-β Amyloid

(2009) Thomas R. Jahn et al.   JOURNAL OF MOLECULAR BIOLOGY

Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules

(2009) S. K. Maji et al.   SCIENCE

Calcium(II) selectively induces α-synuclein annular oligomers via interaction with the C-terminal domain

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