Zobrazeno 1 - 10
of 61
pro vyhledávání: '"Katalin Soós"'
Autor:
Zsolt Datki, Rita Papp, Dénes Zádori, Katalin Soós, Lívia Fülöp, Anna Juhász, Gábor Laskay, Csaba Hetényi, Erzsébet Mihalik, Márta Zarándi, Botond Penke
Publikováno v:
Neurobiology of Disease, Vol 17, Iss 3, Pp 507-515 (2004)
The cell biology of Alzheimer's disease (AD) is characterized mainly by the neurodegeneration caused by the β-amyloid (Aβ) peptides and by the formation of neurofibrillary tangles. The initial events of neurodegeneration in the brain tissue include
Externí odkaz:
https://doaj.org/article/7f566f2e0b0240ab8e757a54dc8c3200
Autor:
Miklós S.Z. Kellermayer, Andrea Horváth, Katalin Soós, Emőke Lászlóffi, Botond Penke, Ünige Murvai
Publikováno v:
Biophysical Chemistry
Amyloid β25-35 (Aβ25-35) is a toxic fragment of Alzheimer's beta peptide. We have previously shown that Aβ25-35 fibrils form a trigonally oriented network on mica by epitaxial growth mechanisms. Chemical reactivity can be furnished to the fibril b
Publikováno v:
Journal of Molecular Recognition. 24:453-460
Amyloid fibrils are self-associating filamentous structures deposited in extracellular tissue in various neurodegenerative and protein misfolding disorders. It has been shown that beta-sheet-breaker (BSB) peptides may interfere with amyloid fibril as
Autor:
Hajnalka Tóháti, Lívia Fülöp, Mária Csete, Gábor Juhász, Edit Wéber, Botond Penke, Ágnes Kasza, Dóra Simon, Viktor Szegedi, Marta Zarandi, Anasztázia Hetényi, Katalin Soós, Zsolt Bozsó, Ilona Laczkó
Publikováno v:
Peptides; Vol 31
beta-Amyloid (A beta) peptides play a crucial role in the pathology of the neurodegeneration in Alzheimer's disease (AD). Biological experiments (both in vitro and animal model studies of AD) require synthetic A beta peptides of standard quality, agg
Publikováno v:
Journal of Peptide Science. 13:94-99
It has been proved that the principal component of senile plaques is aggregates of beta-amyloid peptide (Abeta) in cases of one of the most common forms of age-related neurodegenerative disorders, Alzheimer's disease (AD). Although the synthetic meth
Publikováno v:
Nanopages. 1:69-83
Alzheimer's disease (AD) related beta amyloid (Aβ) peptides possess high propensity towards aggregation. Their diffusion-controlled association follows a physico-chemically well-defined kinetics: the fibrillization starts from the monomeric/ dimeric
Autor:
Erzsébet Mihalik, Dénes Zádori, Katalin Soós, Gábor Laskay, Marta Zarandi, Anna Juhász, Rita Papp, Lívia Fülöp, Csaba Hetényi, Zsolt Datki, Botond Penke
Publikováno v:
Neurobiology of Disease, Vol 17, Iss 3, Pp 507-515 (2004)
The cell biology of Alzheimer's disease (AD) is characterized mainly by the neurodegeneration caused by the beta-amyloid (Abeta) peptides and by the formation of neurofibrillary tangles. The initial events of neurodegeneration in the brain tissue inc
Publikováno v:
Biochemical and Biophysical Research Communications. 324:64-69
Pr-IIGL(a), a derivative of the tetrapeptide beta-amyloid 31-34 (Abeta(31-34)), exerts controversial effects: it is toxic in a neuroblastoma culture, but it protects glial cells from the cytotoxic action of Abeta(1-42). For an understanding of this p
Publikováno v:
NeuroReport. 15:1649-1652
The effects of Alzheimer's disease-related beta-amyloid (Abeta) peptides on the N-methyl-D-aspartate (NMDA)-evoked cell firing rate were studied in hippocampal CA1 neurons of the rat. Extracellular single-unit recordings were combined with iontophore
Autor:
Katalin Soós, Imre Lengyel, Marta Zarandi, Zsolt Datki, Botond Penke, Csaba Hetényi, Zoltán Molnár
Publikováno v:
Journal of Molecular Structure: THEOCHEM. :507-513
β-Amyloids are neurotoxic compounds produced in the brain and cause Alzheimer-type senile dementia. Their toxicity is in good correlation with their aggregation properties. Short peptide fragments of β-amyloid prevent Aβ-toxicity, probably by bind