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001-es BibID:	BIBFORM084931
Első szerző:	Szekrényes Ákos (vegyészmérnök)
Cím:	Multi-Site N-glycan mapping study 1: Capillary electrophoresis ? laser induced fluorescence / Szekrényes Ákos, Park SungAe Suhr, Santos Marcia, Lew Clarence, Jones Aled, Haxo Ted, Kimzey Michael, Pourkaveh Shiva, Szabó Zoltán, Sosic Zoran, Feng Peng, Váradi Csaba, de l'Escaille François, Falmagne Jean-Bernard, Sejwal Preeti, Niedringhaus Thomas, Michels David, Freckleton Gordon, Hamm Melissa, Manuilov Anastasiya, Schwartz Melissa, Luo Jiann-Kae, van Dyck Jonathan, Leung Pui-King, Olajos Marcell, Gu Yingmei, Gao Kai, Wang Wenbo, Wegstein Jo, Tep Samnang, Guttman András
Dátum:	2016
ISSN:	1942-0862 1942-0870
Megjegyzések:	An international team that included 20 independent laboratories from biopharmaceutical companies, universities, analytical contract laboratories and national authorities in the United States, Europe and Asia was formed to evaluate the reproducibility of sample preparation and analysis of N-glycans using capillary electrophoresis of 8-aminopyrene1,3,6-trisulfonic acid (APTS)-labeled glycans with laser induced fluorescence (CE-LIF) detection (16 sites) and ultra highperformance liquid chromatography (UHPLC, 12 sites; results to be reported in a subsequent publication). All participants used the same lot of chemicals, samples, reagents, and columns/capillaries to run their assays. Migration time, peak area and peak area percent values were determined for all peaks with >0.1% peak area. Our results demonstrated low variability and high reproducibility, both, within any given site as well across all sites, which indicates that a standard N-glycan analysis platform appropriate for general use (clone selection, process development, lot release, etc.) within the industry can be established.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Biotherapeutics Capillary electrophoresis Intercompany study N-glycans
Megjelenés:	mAbs. - 8 : 1 (2016), p. 56-64. -
További szerzők:	Park, SungAe Suhr Santos, Marcia Lew, Clarence Jones, Aled Haxo, Ted Kimzey, Michael Pourkaveh, Shiva Szabó Zoltán Sosic, Zoran Feng, Peng Váradi Csaba (1988-) (molekuláris biológus) de l'Escaille, François Falmagne, Jean-Bernard Sejwal, Preeti Niedringhaus, Thomas Michels, David Freckleton, Gordon Hamm, Melissa Manuilov, Anastasiya Schwartz, Melissa Luo, Jiann-Kae van Dyck, Jonathan Leung, Pui-King Olajos Marcell Gu, Yingmei Gao, Kai Wang, Wenbo Wegstein, Jo Tep, Samnang Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	K 116263 NKFIH
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM077852
035-os BibID:	(PMID)29330871 (Scopus)85041568961 (WOS)000429417500010
Első szerző:	Szekrényes Ákos (vegyészmérnök)
Cím:	Multi-site N-Glycan mapping study 2 : UHPLC / Ákos Szekrényes, SungAe Suhr Park, Eoin Cosgrave, Aled Jones, Ted Haxo, Michael Kimzey, Shiva Pourkaveh, Zoltán Szabó, Zoran Sosic, Peng Feng, Preeti Sejwal, Kelsey Dent, David Michels, Gordon Freckleton, Jun Qian, Catherine Lancaster, Toni Duffy, Melissa Schwartz, Jiann-Kae Luo, Jonathan van Dyck, Pui-King Leung, Marcell Olajos, Ronald Kowle, Kai Gao, Wenbo Wang, Jo Wegstein, Samnang Tep, Apolka Domokos, Csaba Váradi, András Guttman
Dátum:	2018
ISSN:	0173-0835 1522-2683
Megjegyzések:	In the first part of this publication, the results from an international study evaluating theprecision (i.e., repeatability and reproducibility) of N-glycosylation analysis using capillaryelectrophoresis of APTS-labeled N-glycans were presented. The corresponding resultsfrom ultra-high performance liquid chromatography (UHPLC) with fluorescence detectionare presented here from 12 participating sites. All participants used the same lot of samples,reagents, and columns to perform the assays. Elution time, peak area and peak areapercent values were determined for all peaks 0.1% peak area, and statistical analysis wasperformed following ISO 5725-2 guideline principles. The results demonstrated adequatereproducibility, within any given site as well across all sites, indicating that standardUHPLC-based N-glycan analysis platforms are appropriate for general use
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk 2-AB Biotherapeutics Intercompany study N-glycans UHPLC
Megjelenés:	Electrophoresis. - 39 : 7 (2018), p. 998-1005. -
További szerzők:	Park, SungAe Suhr Cosgrave, Eoin Jones, Aled Haxo, Ted Kimzey, Michael Pourkaveh, Shiva Szabó Zoltán (orvos) Sosic, Zoran Feng, Peng Sejwal, Preeti Dent, Kelsey Michels, David Freckleton, Gordon Qian, Jun Lancaster, Catherine Duffy, Toni Schwartz, Melissa Luo, Jiann-Kae van Dyck, Jonathan Leung, Pui-King Olajos Marcell Kowle, Ronald Gao, Kai Wang, Wenbo Wegstein, Jo Tep, Samnang Domokos Apolka Váradi Csaba (1988-) (molekuláris biológus) Guttman András (1954-) (vegyészmérnök)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM058348
Első szerző:	Szekrényes Ákos (vegyészmérnök)
Cím:	Sample preparation for N-glycosylation analysis of therapeutic monoclonal antibodies by electrophoresis / Ákos Szekrényes, Jan Partyka, Csaba Varadi, Jana Krenkova, Frantisek Foret, András Guttman
Dátum:	2015
Megjegyzések:	There are a considerable number of biopharmaceuticals that have been approved for clinical use in the past decade. Over half of these new generation drugs are glycoproteins, such as monoclonal antibodies or other recombinant glycoproteins, which are mostly produced in mammalian cell lines. The linked carbohydrate moieties affect not only their physicochemical properties and thermal stability but also crucial features like receptor-binding activity, circulating half-life, as well as immunogenicity. The structural diversity of these attached glycans can be manifested in altered monosaccharide composition and linkages/positions among the monosaccharide building blocks. In addition, as more and more biosimilar products hit the market, understanding the effects of their glycosylation modification has become a recent target in efficacy and safety issues. To ensure consistent quality of these products, glycosylation profiles have to be monitored and controlled in all steps of the manufacturing process, i.e., from clone selection to lot release. In this paper, we describe some of the recently introduced and commonly used sample preparation techniques for capillary electrophoresis (CE)-based profiling and structural elucidation of N-glycans. The presented protocols include protein A affinity partitioning of monoclonal antibodies (mAbs), enzymatic release of the N-linked glycans, labeling of the liberated carbohydrates, reaction mixture purification techniques to remove the excess labeling reagent, and high-resolution and rapid capillary electrophoresis-laser-induced fluorescence (CE-LIF)-based profiling of the labeled and purified N-glycans.
ISBN:	978-1-4939-2353-3
Tárgyszavak:	Orvostudományok Elméleti orvostudományok könyvfejezet N-glycosylation analysis
Megjelenés:	Microchip Capillary Electrophoresis Protocols : Methods in Molecular Biology / Ann Van Schepdael. - p. 183-195. -
További szerzők:	Partyka, Jan Váradi Csaba (1988-) (molekuláris biológus) Krenkova, Jana Foret, František Guttman András (1954-) (vegyészmérnök)
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM043657
Első szerző:	Váradi Csaba (molekuláris biológus)
Cím:	Analysis of Haptoglobin N-glycome Alterations in Inflammatory and Malignant Lung Diseases by Capillary Electrophoresis / Cs. Varadi, S. Mittermayr, A. Szekrenyes, J. Kadas, L. Takacs, I. Kurucz, A. Guttman
Dátum:	2013
ISSN:	0173-0835
Megjegyzések:	A capillary electrophoresis based method was introduced to compare the N-glycosylation profile ofhaptoglobin in normal and pathologic conditions. To assess the biomarker potential of glycosylationchanges in various lung diseases, haptoglobin was isolated from plasma samples of healthy, pneumonia,chronic obstructive pulmonary disease (COPD) and lung cancer patients by means of two haptoglobinspecific monoclonal antibodies. Haptoglobin N-glycans were then enzymatically released, fluorescentlylabeled and profiled by capillary electrophoresis. Disease associated changes of core and antennaryfucosylation were identified by targeted exoglycosidase digestions and their levels were compared inthe different patient groups. Terms such as of core- and arm-fucosylation degree, as well as branchingdegreewere introduced for easier characterization of the changes and statistical analysis was used toexamine which structures are responsible for the observed differences. Increased level of ?1-6fucosylated tri-antennary glycans was found in all disease groups compared to the control. Elevatedamounts of core- and arm fucosylation on tetra-antennary glycans were detected in the lung cancergroup compared to the COPD group. A larger scale study is necessary to confirm and validate thesepreliminary findings in the glycosylation changes of haptoglobin, so could then be used as biomarkers inthe diagnosis of malignant and inflammatory lung diseases.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban biomarker capillary electrophoresis
Megjelenés:	Electrophoresis. - 34 : 16 (2013), p. 2287-2294. -
További szerzők:	Mittermayr, Stefan (1983-) (bioinformatikus) Szekrényes Ákos (1983-) (vegyészmérnök) Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Takács László (1955-) Kurucz István Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	K-81839 OTKA
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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