Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Mayra Quemé-Peña"'
Autor:
Kamal el Battioui, Sohini Chakraborty, András Wacha, Dániel Molnár, Mayra Quemé-Peña, Imola Cs. Szigyártó, Csenge Lilla Szabó, Andrea Bodor, Kata Horváti, Gergő Gyulai, Szilvia Bősze, Judith Mihály, Bálint Jezsó, Loránd Románszki, Judit Tóth, Zoltán Varga, István Mándity, Tünde Juhász, Tamás Beke-Somfai
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract Developing unique mechanisms of action are essential to combat the growing issue of antimicrobial resistance. Supramolecular assemblies combining the improved biostability of non-natural compounds with the complex membrane-attacking mechanis
Externí odkaz:
https://doaj.org/article/19140e0f599745b188faaf71f8024c6a
Autor:
Tünde Juhász, Mayra Quemé-Peña, Bence Kővágó, Judith Mihály, Maria Ricci, Kata Horváti, Szilvia Bősze, Ferenc Zsila, Tamás Beke-Somfai
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
Abstract In the emerging era of antimicrobial resistance, the susceptibility to co-infections of patients suffering from either acquired or inherited hemolytic disorders can lead to dramatic increase in mortality rates. Closely related, heme liberate
Externí odkaz:
https://doaj.org/article/303dc353fe50461882ecf5f2211cc1c0
Publikováno v:
ACS Omega, Vol 6, Iss 24, Pp 15756-15769 (2021)
Externí odkaz:
https://doaj.org/article/44c2bb526a4c46db98f574f88ae93038
Autor:
Vignesh Udyavara Nagaraj, Tünde Juhász, Mayra Quemé-Peña, Imola Cs. Szigyártó, Dóra Bogdán, András Wacha, Judith Mihály, Loránd Románszki, Zoltán Varga, Joakim Andréasson, István Mándity, Tamás Beke-Somfai
Publikováno v:
ACS applied materialsinterfaces. 14(50)
Self-assembled peptide nanostructures with stimuli-responsive features are promising as functional materials. Despite extensive research efforts, water-soluble supramolecular constructs that can interact with lipid membranes in a controllable way are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::126ce169bf2db4535f093c9918f2b51b
https://pubmed.ncbi.nlm.nih.gov/36473125
https://pubmed.ncbi.nlm.nih.gov/36473125
Autor:
Szilvia Bősze, Tamás Beke-Somfai, Tünde Juhász, Bálint Szeder, Ferenc Zsila, Beáta Biri-Kovács, Mayra Quemé-Peña, Maria Ricci, Kata Horváti
Publikováno v:
ACS Pharmacol Transl Sci
[Image: see text] The host defense peptide LL-37 is the only human cathelicidin, characterized by pleiotropic activity ranging from immunological to anti-neoplastic functions. However, its overexpression has been associated with harmful inflammatory
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83d48ec80b5d9dfb8d468a152ccbd9fd
https://doi.org/10.1021/acsptsci.0c00155
https://doi.org/10.1021/acsptsci.0c00155
Autor:
Maria Ricci, Bence Kővágó, Ferenc Zsila, Tamás Beke-Somfai, Judith Mihály, Tünde Juhász, Mayra Quemé-Peña, Szilvia Bősze, Kata Horváti
Publikováno v:
Scientific Reports
Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
In the emerging era of antimicrobial resistance, the susceptibility to co-infections of patients suffering from either acquired or inherited hemolytic disorders can lead to dramatic increase in mortality rates. Closely related, heme liberated during
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::929d884f1423c738936faec3463fba66
http://europepmc.org/articles/PMC8443738
http://europepmc.org/articles/PMC8443738
Autor:
Priyanka Singh, Lívia Fülöp, Mayra Quemé-Peña, Gergely Kohut, Tünde Juhász, Imola Cs. Szigyártó, Tamás Beke-Somfai, Zita I. Papp, Maria Ricci
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 22, Iss 8613, p 8613 (2021)
Volume 22
Issue 16
International Journal of Molecular Sciences, Vol 22, Iss 8613, p 8613 (2021)
Volume 22
Issue 16
Anticancer peptides (ACPs) could potentially offer many advantages over other cancer therapies. ACPs often target cell membranes, where their surface mechanism is coupled to a conformational change into helical structures. However, details on their b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6eacf797a33d15cfd37b5ef9016a800b
https://pubmed.ncbi.nlm.nih.gov/34445319
https://pubmed.ncbi.nlm.nih.gov/34445319
Autor:
Judit Henczkó, Ferenc Zsila, Tünde Juhász, Tamás Beke-Somfai, Kata Horváti, Szilvia Bősze, Mayra Quemé-Peña, Zoltán Varga, Csaba Németh, Bernadett Pályi, Judith Mihály, Imola Cs. Szigyártó
Publikováno v:
Chembiochem
Antimicrobial peptides (AMPs) kill bacteria by targeting their membranes through various mechanisms involving peptide assembly, often coupled with disorder‐to‐order structural transition. However, for several AMPs, similar conformational changes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22961f82cc9e8e95848bd986cb67677f
https://doi.org/10.1002/cbic.201800801
https://doi.org/10.1002/cbic.201800801
Publikováno v:
ACS Omega
ACS Omega, Vol 6, Iss 24, Pp 15756-15769 (2021)
ACS Omega, Vol 6, Iss 24, Pp 15756-15769 (2021)
Owing to their potential applicability against multidrug-resistant bacteria, antimicrobial peptides (AMPs) or host defense peptides (HDPs) gain increased attention. Besides diverse immunomodulatory roles, their classical mechanism of action mostly in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7417b2f02c2f399fe0ff86e3e4f5328
https://pubmed.ncbi.nlm.nih.gov/34179620
https://pubmed.ncbi.nlm.nih.gov/34179620
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