BIBLIOS

Document type
Book chapters


Title
Preparation of Amyloidogenic Aggregates from EF-Hand ?-Parvalbumin and S100 Proteins

Participants in the publication
Javier Martínez (Author)
BioISI - Biosystems & Integrative Sciences Institute
Joana S. Cristóvão (Author)
BioISI - Biosystems & Integrative Sciences Institute
Rosa Sánchez (Author)
Maria Gasset (Author)
Cláudio M. Gomes (Author)
Dep. Química e Bioquímica
BioISI

Summary
Proteins containing EF-hand helix-loop-helix-binding motifs play essential roles in calcium homeostasis and signaling pathways. These proteins have considerable structural and functional diversity by virtue of their cation-binding properties, and occur as either Ca2+-bound or Ca2+-free states with distinct aggregation propensities. That is the case among β-parvalbumins and S100 proteins, which under certain conditions undergo Ca2+-dependent self-assembly reactions with the formation of oligomers, amyloid-type aggregates and fibrils. These phenomena may be particularly relevant in human S100A6 protein and in fish Gad m 1 allergenic protein, which are implicated in human disease processes. Here, we describe detailed methods to generate and monitor the formation of amyloidogenic assemblies and aggregates of these two EF-hand proteins in vitro.

Editor(s)
Sigurdsson E., Calero M., Gasset M. (eds)


Institution
BioISI - Biosystems & Integrative Sciences Institute

Where published
Methods in Molecular Biology - Amyloid Proteins

Publication Identifiers
ISSN - 1064-3745
ISBN - 9781493978151,9781493978168

Publisher
Humana Press

Collection
Methods in Molecular Biology



Document Identifiers
DOI - https://doi.org/10.1007/978-1-4939-7816-8_11
URL - http://dx.doi.org/10.1007/978-1-4939-7816-8_11

Rankings
SCIMAGO Q3 (2018) - 0.605 - Molecular Biology

Keywords
Amyloids Calcium EF-hand Fish allergens Gad m 1 S100A6