J
József Kardos
Researcher at Eötvös Loránd University
Publications - 114
Citations - 4895
József Kardos is an academic researcher from Eötvös Loránd University. The author has contributed to research in topics: Chemistry & Protein structure. The author has an hindex of 27, co-authored 99 publications receiving 3894 citations. Previous affiliations of József Kardos include University of Fukui & Osaka University.
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Journal ArticleDOI
Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy
András Micsonai,Frank Wien,Linda Kernya,Young-Ho Lee,Yuji Goto,Matthieu Réfrégiers,József Kardos +6 more
TL;DR: This work has developed a method called β-structure selection (BeStSel) for the secondary structure estimation that takes into account the twist of β-structures, and can predict the protein fold down to the topology level following the CATH classification from a single CD spectrum.
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BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra.
András Micsonai,Frank Wien,Éva Bulyáki,Judit Kun,Éva Moussong,Young-Ho Lee,Yuji Goto,Matthieu Réfrégiers,József Kardos +8 more
TL;DR: It is shown that the orientation and twisting of β-sheets account for the observed spectral diversity, and a new method to estimate accurately the secondary structure is developed, and the originality of BeStSel is that it carries out a detailed secondary structure analysis.
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Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins.
TL;DR: It was found that Th.
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Low Concentrations of Sodium Dodecyl Sulfate Induce the Extension of β2-Microglobulin-Related Amyloid Fibrils at a Neutral pH†
Suguru Yamamoto,Kazuhiro Hasegawa,Itaru Yamaguchi,Shinobu Tsutsumi,József Kardos,Yuji Goto,Fumitake Gejyo,Hironobu Naiki +7 more
TL;DR: At low concentrations, sodium dodecyl sulfate (SDS) converts natively folded beta2-m monomers into partially folded, alpha-helix-containing conformers, which results in the extension of Abeta2M amyloid fibrils at neutral pH, which could be explained basically by a first-order kinetic model.
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Local apoptotic-like mechanisms underlie complement-mediated synaptic pruning.
Balazs Gyorffy,Judit Kun,György Török,Éva Bulyáki,Zsolt Borhegyi,Péter Gulyássy,Viktor Kis,Péter Szocsics,András Micsonai,János Matkó,László Drahos,Gábor Juhász,Gábor Juhász,Katalin A. Kékesi,József Kardos +14 more
TL;DR: The results unveiled that C1q label-based synaptic pruning is triggered by and directly linked to apoptotic-like processes in the synaptic compartment, which was confirmed experimentally with apoptosis markers.