Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Márta Kotormán"'
Autor:
Andrea Rónavári, Margit Balázs, Árpád Szilágyi, Csaba Molnár, Márta Kotormán, István Ilisz, Mónika Kiricsi, Zoltán Kónya
Publikováno v:
Nanoscale Research Letters, Vol 18, Iss 1, Pp 1-16 (2023)
Abstract Due to the widespread applications of metal nanoparticles (NPs), green synthesis strategies have recently advanced, e.g., methods that utilize extracts made from different plant wastes. A particularly innovative approach to reducing large am
Externí odkaz:
https://doaj.org/article/a2fa132d825f4ede9d2fa59cea5baa48
Publikováno v:
Biologia Futura. 72:257-262
Amyloid fibril formation has been associated with a great variety of human diseases. Fruits contain different important bioactive molecules without causing various undesirable side effects, which are necessary for disease prevention and treatment. He
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e3a7e0a61a5bce66970aac174e89c20
https://doi.org/10.1007/s42977-020-00064-y
https://doi.org/10.1007/s42977-020-00064-y
Autor:
Márta Kotormán, Vanda Andrea Bedő
Publikováno v:
Biologia Futura. 71:147-152
In this study, an in vitro α-chymotrypsin aggregation model was used to demonstrate that certain extracts of commercial coffees effectively inhibit protein aggregation in 55% ethanol at pH 7.0. To detect the anti-amyloidogenic effect of the various
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1f4791699fd4869fb9472cfd9ee80ce
https://doi.org/10.1007/s42977-020-00006-8
https://doi.org/10.1007/s42977-020-00006-8
Publikováno v:
Acta Biologica Hungarica. 69:385-394
During the study of inhibition of amyloid fibril formation, α-chymotrypsin protein was developed in 55% ethanol at pH 7.0. We investigated the inhibitory effect of different spices on amyloid fibril formation using turbidity measurements and Congo r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15d9370e85c52361a7fe04fb56f98527
https://doi.org/10.1556/018.69.2018.4.2
https://doi.org/10.1556/018.69.2018.4.2
Publikováno v:
Biologia futura. 72(3)
The extracts of 7 herbs were screened and compared for their functional ability to inhibit the aggregation of trypsin as an appropriate model protein for in vitro fibrillation in aqueous ethanol at pH 7.0. Turbidity measurements, total phenolic conte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::258c389224d4cba3e67a84fb8db07b22
https://pubmed.ncbi.nlm.nih.gov/34554557
https://pubmed.ncbi.nlm.nih.gov/34554557
Publikováno v:
Acta biologica Hungarica. 69(2)
We tested the amyloid fibril formation inhibitory effect of seven teas diluted in 55% ethanol at pH 7.0 at a protein concentration of 0.15 mg/ml α-chymotrypsin. In the experiments we investigated the formation and inhibition of amyloid fibrils by tu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::359c9516ea2416979714e4e6b6914218
https://pubmed.ncbi.nlm.nih.gov/29888672
https://pubmed.ncbi.nlm.nih.gov/29888672
Autor:
Titanilla Szögi, Márta Kotormán, Kitti Szabo, L. Mária Simon, Lívia Fülöp, Attila Borics, Márton Richárd Szabó
Publikováno v:
Protein & Peptide Letters. 22:1104-1110
The formation of amyloid-like fibrils was studied by using the well-known serine protease trypsin as a model protein in the presence of ethanol as organic solvent. Trypsin forms amyloid-like fibrils in aqueous ethanol at pH = 7.0. The dye Congo red (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec93b97248c485344fd0ee55671da2e1
https://doi.org/10.2174/0929866522666151002154324
https://doi.org/10.2174/0929866522666151002154324
Autor:
Márta Kotormán, Phanindra Babu Kasi
Publikováno v:
Natural Product Communications. 14:1934578X1985912
The formation of amyloid fibrils is associated with many human illnesses, such as Alzheimer’s, Huntington’s, and Parkinson’s diseases, amyotrophic lateral sclerosis, spongiform encephalitis, type 2 diabetes, and primary and secondary systemic a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8210a3328f2ba0ba71cf91ad822bbfa3
https://doi.org/10.1177/1934578x19859127
https://doi.org/10.1177/1934578x19859127
Autor:
Márta Kotormán, Phanindra Babu Kasi
Publikováno v:
Natural Product Communications. 14:1934578X1985141
In this work fruit and vegetable juices were analyzed for their ability to prevent the aggregation of trypsin using turbidity measurement. Fruit and vegetable juices are capable of inhibiting the aggregation of PMS-trypsin in aqueous ethanol. Among t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d8ac1e6674691047db7105dfa0a9f7a0
https://doi.org/10.1177/1934578x19851410
https://doi.org/10.1177/1934578x19851410
Publikováno v:
Protein & Peptide Letters. 19:544-550
The formation of amyloid-like fibrils of α-chymotrypsin was studied in aqueous ethanol, methanol, tertbutanol, dimethylformamide and acetonitrile. Thioflavin T (ThT), Congo red (CR) and 1-anilino-8-naphthalenesulfonic acid (ANS) binding, turbidity,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfad069195a2bf3adef710db4e2510fa
https://doi.org/10.2174/092986612800191071
https://doi.org/10.2174/092986612800191071