Rela Koppel
Tel Aviv University
18 Papers
185 Citations
Rela Koppel is an academic researcher from Tel Aviv University. The author has contributed to research in topics: Monoclonal antibody & Immobilized enzyme. The author has an hindex of 13, co-authored 18 publications.
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Papers
Disaggregation of Alzheimer β-amyloid by site-directed mAb
TL;DR: Findings give hints on how to convert in vivo senile plaques into nontoxic, diffuse components and may have therapeutic interest for those studying Alzheimer disease and other human diseases related to amyloidogenic properties of physiological peptides and proteins.
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Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer beta-amyloid peptide.
TL;DR: It is found that the mAs prevent the aggregation of beta-amyloid peptide and that the inhibitory effect appears to be related to the localization of the antibody-binding sites and the nature of the aggregating agents.
EFRH-phage immunization of Alzheimer’s disease animal model improves behavioral performance in morris water maze trials
Vered Lavie,María Inés Becker,Rachel Cohen-Kupiec,Iftach Yacoby,Rela Koppel,Manuela Wedenig,Birgit Hutter-Paier,Beka Solomon +7 more
TL;DR: It is found that phage displaying high E FRH copy number are effective in eliciting humoral response against the EFRH sequence, which in turn relieves the amyloid burden in the brains of amyloids precursor protein Tg mice and improves their ability to perform cognitive tasks.
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Enzyme immobilization via monoclonal antibodies I. Preparation of a highly active immobilized carboxypeptidase A
TL;DR: A novel method for the preparation of highly active immobilized enzymes is described, based on the binding of enzymes to suitable carriers via monoclonal antibodies, which bind to the enzyme with high affinity without affecting its catalytic activity.
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Immunostaining of calmodulin and aluminium in Alzheimer's disease-affected brains.
TL;DR: The loss of CAM1 immunoreactivity and the occurrence of large amounts of aluminium suggest an alteration of the active conformation of calmodulin in disease-affected brains, which could be involved in the development of Alzheimer's disease pathology.
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