Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Ünige Murvai"'
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 19, p 10460 (2024)
β-amyloid (Aβ) peptides form self-organizing fibrils in Alzheimer’s disease. The biologically active, toxic Aβ25–35 fragment of the full-length Aβ-peptide forms a stable, oriented filament network on the mica surface with an epitaxial mechani
Externí odkaz:
https://doaj.org/article/fd691fc02ee44c889521e90370cad336
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854:327-332
Aβ25-35, the fibril-forming, biologically active toxic fragment of the full-length amyloid β-peptide also forms fibrils on mica by an epitaxial assembly mechanism. Here we investigated, by using atomic force microscopy, nanomechanical manipulation
Autor:
Jasna Brujic, Vesna Svetličić, Galja Pletikapić, Miklós S.Z. Kellermayer, Ünige Murvai, Herbert Lannon
Publikováno v:
Biophysical Journal. 107:355-364
Marine-gel biopolymers were recently visualized at the molecular level using atomic force microscopy (AFM) to reveal fine fibril-forming networks with low to high degrees of cross-linking. In this work, we use force spectroscopy to quantify the intra
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:
Botond Penke, Miklós Palkovits, Ünige Murvai, Gábor M Mórotz, Éva M. Szegö, Tamás Janáky, Miklós S.Z. Kellermayer, József Kardos, Attila Csorba, Katalin A. Kékesi, István M. Ábrahám, Gábor Juhász
Publikováno v:
Neuroendocrinology. 93:90-105
Alzheimer disease is characterized by accumulation of β-amyloid (Aβ) and cognitive dysfunctions linked to early loss of cholinergic neurons. As estrogen-based hormone replacement therapy has beneficial effects on cognition of demented patients, and
Autor:
Ferenczy, György G.1 (AUTHOR) ferenczy.gyorgy@semmelweis.hu, Murvai, Ünige1 (AUTHOR) murvai.unige@semmelweis.hu, Fülöp, Lívia2 (AUTHOR) fulop.livia@med.u-szeged.hu, Kellermayer, Miklós1 (AUTHOR) kellermayer.miklos@semmelweis.hu
Publikováno v:
International Journal of Molecular Sciences. Oct2024, Vol. 25 Issue 19, p10460. 11p.
Autor:
József Kardos, Szilvia Erdélyi-Bótor, Árpád Karsai, Miklós S.Z. Kellermayer, Ricardo H. Pires, Ünige Murvai
Publikováno v:
Single-molecule Studies of Proteins ISBN: 9781461449201
Single-molecule biophysical tools have developed in the past two decades from jaw-dropping attractions to essential laboratory tools. In recent years, these methods have been applied to the exploration of the structure, mechanics, and mechanically dr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c696c83790630405bebc958626ec10c9
https://doi.org/10.1007/978-1-4614-4921-8_7
https://doi.org/10.1007/978-1-4614-4921-8_7
Autor:
Ünige Murvai, Miklós S.Z. Kellermayer
Publikováno v:
Biophysical Journal. 100(3)
Amyloid fibrils are filamentous aggregates deposited in extracellular tissue in various neurodegenerative and protein misfolding disorders. Amyloid s (As) peptides form self-associating fibrillar structures in Alzheimer's disease. The As25-35 peptide
Publikováno v:
European biophysics journal : EBJ. 37(7)
Amyloid fibrils are present in the extracellular space of various tissues in neurodegenerative and protein misfolding diseases. Amyloid fibrils may be used in nanotechnology applications, because of their self-assembly properties and stability, if th