Crystallographic studies on protein misfolding: Domain swapping and amyloid formation in the SH3 domain

A Cámara-Artigas - Archives of Biochemistry and Biophysics, 2016 - Elsevier
Oligomerization by 3D domain swapping is found in a variety of proteins of diverse size, fold
and function. In the early 1960s this phenomenon was postulated for the oligomers of …

SH3 domains as suitable models to study amyloid aggregation

B Morel, D Ruzafa, F Conejero-Lara - SH Domains: Structure, Mechanisms …, 2015 - Springer
Protein aggregation and amyloid fibril formation are related to a variety of
neurodegenerative diseases for which no effective therapies or prevention methods exists …

Applications for treatment of neurodegenerative diseases

J Ježek, J Hlaváček, J Šebestík, J Ježek… - … Applications of Acridines …, 2017 - Springer
Hallmark of neurodegenerative disorders such as Alzheimer's, Parkinson's, and prion
diseases is aggregation of various proteins, which accumulate in the brain. The early stages …

[PDF][PDF] Proteínas quimera de los dominios sh3 de la c-src y abl tirosina quinasa: un estudio de las bases moleculares del entrecruzamiento tridimensional de dominios

MC Salinas García - 2022 - repositorio.ual.es
This doctoral thesis investigates the molecular principles of protein misfolding, like
threedimensional domain-swapping or amyloid formation. For this purpose, we have used a …

Cloning and characterisation of alternansucrase from Leuconostoc citreum ABK-1 and role of surface aromatic acids on product size

K Wangpaiboon - 2017 - digital.car.chula.ac.th
Abstract The alternansucrase (ALT, EC 2.4. 1.140) catalyses transferring of glucose from
sucrose to produce a polymer with α-1, 6 and α-1, 3 linkages, so-called" alternan". The ALT …