Tipo
Capítulo em Livro
Título
Preparation of Amyloidogenic Aggregates from EF-Hand ?-Parvalbumin and S100 Proteins
Participantes na publicação
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
Resumo
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
Sigurdsson E., Calero M., Gasset M. (eds)
Instituição
BioISI - Biosystems & Integrative Sciences Institute
Suporte
Methods in Molecular Biology - Amyloid Proteins
Identificadores da Publicação
ISSN - 1064-3745
ISBN - 9781493978151,9781493978168
Editora
Humana Press
Coleção
Methods in Molecular Biology
Número de Páginas
12
Página Inicial
167
Página Final
179
Identificadores do Documento
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
Identificadores de Qualidade
SCIMAGO Q3 (2018) - 0.605 - Molecular Biology
Keywords
Amyloids
Calcium
EF-hand
Fish allergens
Gad m 1
S100A6