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pro vyhledávání: '"János, Gera"'
Autor:
János Gera, Gábor Paragi
Publikováno v:
Molecules, Vol 25, Iss 15, p 3524 (2020)
The aggregation process of the Amyloidβ (Aβ) peptide is one of the central questions in Alzheimers’s research. Fluorescence-labeled single-molecule detection is a novel technique concerning the early stage investigation of Aβ aggregation, where
Externí odkaz:
https://doaj.org/article/a1fc8f9c177245b099cda94eccf747dc
Autor:
Titanilla Szögi, Ildikó Schuster, Emőke Borbély, Andrea Gyebrovszki, Zsolt Bozsó, János Gera, Róbert Rajkó, Miklós Sántha, Botond Penke, Lívia Fülöp
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 12, p 3050 (2019)
Regulated intramembrane proteolysis (RIP) of the amyloid precursor protein (APP) leads to the formation of fragments, among which the intracellular domain of APP (AICD) was also identified to be a causative of early pathological events. AICD-countera
Externí odkaz:
https://doaj.org/article/cfa48ebc3d724cd9be101640c956a9a2
Autor:
Rita Padányi, János Gera, Tamás Hegedűs, Attila Tordai, Gábor Paragi, Hedvig Tordai, Bianka Farkas
Publikováno v:
Cellular and Molecular Life Sciences
Cystic fibrosis (CF), a lethal monogenic disease, is caused by pathogenic variants of the CFTR chloride channel. The majority of CF mutations affect protein folding and stability leading overall to diminished apical anion conductance of epithelial ce
Publikováno v:
Current Protein & Peptide Science. 20:577-599
Alzheimer’s Disease (AD) is a form of progressive dementia involving cognitive impairment, loss of learning and memory. Different proteins (such as amyloid precursor protein (APP), β- amyloid (Aβ) and tau protein) play a key role in the initiatio
Autor:
Zsolt Bozsó, Lívia Fülöp, Ernesto G. Mata, Titanilla Szögi, Ana M. Rodríguez, Luciana Méndez, Federica Cioffi, Kerensa Broersen, János Gera, Gábor Paragi, Carina M. L. Delpiccolo, Exequiel Barrera, Ricardo D. Enriz
Publikováno v:
Bioorganic Chemistry, 81, 211-221. Academic Press
A series of novel mimetic peptides were designed, synthesised and biologically evaluated as inhibitors of Aβ 42 aggregation. One of the synthesised peptidic compounds, termed compound 7 modulated Aβ 42 aggregation as demonstrated by thioflavin T fl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9567179e76932f90539aa2c94effaf53
https://www.sciencedirect.com/science/article/pii/S004520681830573X
https://www.sciencedirect.com/science/article/pii/S004520681830573X
Searching for improved mimetic peptides inhibitors preventing conformational transition of amyloid-β
Autor:
János, Gera, Titanilla, Szögi, Zsolt, Bozsó, Livia, Fülöp, Exequiel E, Barrera, Ana M, Rodriguez, Luciana, Méndez, Carina M L, Delpiccolo, Ernesto G, Mata, Federica, Cioffi, Kerensa, Broersen, Gabor, Paragi, Ricardo D, Enriz
Publikováno v:
Bioorganic chemistry. 81
A series of novel mimetic peptides were designed, synthesised and biologically evaluated as inhibitors of Aβ
Publikováno v:
Current Alzheimer research. 15(13)
Lipids participate in Amyloid Precursor Protein (APP) trafficking and processing - important factors in the initiation of Alzheimer’s disease (AD) pathogenesis and influence the formation of neurotoxic β-amyloid (Aβ) peptides. An important risk f