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1.

001-es BibID:BIBFORM083085
035-os BibID:(WoS)000542144300010 (Scopus)85076708163
Első szerző:Abrahams, Jodie L.
Cím:Recent advances in glycoinformatic platforms for glycomics and glycoproteomics / Jodie L. Abrahams, Ghazaleh Taherzadeh, Gabor Jarvas, Andras Guttman, Yaoqi Zhou, Matthew P. Campbell
Dátum:2020
ISSN:0959-440X
Megjegyzések:Protein glycosylation is the most complex and prevalent posttranslation modification in terms of the number of proteins modified and the diversity generated. To understand the functional roles of glycoproteins it is important to gain an insight into the repertoire of oligosaccharides present. The comparison and relative quantitation of glycoforms combined with site-specific identification and occupancy are necessary steps in this direction. Computational platforms have continued to mature assisting researchers with the interpretation of such glycomics and glycoproteomics data sets, but frequently support dedicated workflows and users rely on the manual interpretation of data to gain insights into the glycoproteome. The growth of site-specific knowledge has also led to the implementation of machine-learning algorithms to predict glycosylation which is now being integrated into glycoproteomics pipelines. This short review describes commercial and open-access databases and software with an emphasis on those that are actively maintained and designed to support current analytical workflows.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Current Opinion In Structural Biology. - 62 (2020), p. 56-69. -
További szerzők:Taherzadeh, Ghazaleh Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök) Zhou, Yaoqi Campbell, Matthew P.
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2.

001-es BibID:BIBFORM099680
035-os BibID:(cikkazonosító)122497
Első szerző:Auer, Felicia
Cím:Recent advances in the analysis of human milk oligosaccharides by liquid phase separation methods / Auer Felicia, Jarvas Gabor, Guttman Andras
Dátum:2021
ISSN:1570-0232
Megjegyzések:Human milk is a complex, dynamically changing biological fluid, which contains a large amount of nonconjugated carbohydrates, referred to as human milk oligosaccharides (HMOs). These HMOs are very important for the infants as they play important roles in the formation of the gut microbiome, the immune system and support brain development. HMOs show highly complex structural diversity due to numerous linkage possibilities of the building monosaccharides. In order to elucidate their structure?function relationship and to develop more effective infant formulas, cutting-edge analytical technologies are in great demand. In this paper, we review the current strategies for HMO analysis based on liquid phase separation methods. High performance liquid chromatography, capillary electrophoresis and their hyphenation with mass spectrometry are critically reviewed, emphasizing their advantages and disadvantages from practical point of views. Recent advances of the methods are categorized according to their application fields.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Human milk
Oligosaccharides
Analysis
Chromatography
Electrophoresis
Mass spectrometry
Megjelenés:Journal Of Chromatography B-Analytical Technologies In The Biomedical And Life Sciences. - 1162 (2021), p. 1-9. -
További szerzők:Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:2018-2.1.17-T?ET-KR-2018-00010
Egyéb
BIONANO_GINOP-2.3.2- 15-2016-00017
GINOP
NN127062
OTKA
TKP2020-IKA-07
OTKA
UNKP-20-5
Egyéb
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3.

001-es BibID:BIBFORM084562
035-os BibID:(Scopus)84961282078 (WOS)000379133500002
Első szerző:Bodnár Judit
Cím:Enzymatic removal of N-glycans by PNGase F coated magnetic microparticles / Bodnar Judit, Szekrenyes Akos, Szigeti Marton, Jarvas Gabor, Krenkova Jana, Foret Frantisek, Guttman Andras
Dátum:2016
ISSN:0173-0835 1522-2683
Megjegyzések:Investigation of protein glycosylation is an important area in biomarker discovery and biopharmaceutical research. Alterations in protein N-glycosylation can be an indication of changes in pathological conditions in the medical field or production parameters of biotherapeutics. Rapid development of these disciplines calls for fast, high-throughput, and reproducible methods to analyze protein N-glycosylation. Currently used methods require either long deglycosylation times or large excess of enzymes. In this paper, we report on the use of PNGase F immobilization onto the surface of magnetic microparticles and their use in rapid and efficient removal of N-glycans from glycoproteins. The use of immobilized PNGase F also allowed reusability of the enzyme-coated beads as the magnetic microparticles can be readily partitioned from the sample by a magnet after each deglycosylation reaction. The efficiency and activity of the PNGase F coated magnetic beads was compared with in-solution enzyme reactions using standard glycoproteins possessing the major N-glycan types of neutral, high mannose, and highly sialylated carbohydrates. The PNGase F coated magnetic beads offered comparable deglycosylation level to the conventional in-solution based method in 10-min reaction times for the model glycoproteins of immunoglobulin G (mostly neutral carbohydrates), ribonuclease B (high mannose type sugars), and fetuin (highly sialylated oligosaccharides) with the special features of easy removal of the enzyme from the reaction mixture and reusability.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Deglycosylation
Enzyme immobilization
Magnetic microparticles
PNGase F
Megjelenés:Electrophoresis. - 37 : 10 (2016), p. 1264-1269. -
További szerzők:Szekrényes Ákos (1983-) (vegyészmérnök) Szigeti Márton (1986-) (környezetmérnök) Járvás Gábor (1982-) (vegyészmérnök) Krenkova, Jana Foret, František Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:K116263
NKFIH
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4.

001-es BibID:BIBFORM071246
Első szerző:Döncző Boglárka (biológiatanár-földrajztanár)
Cím:Glikomika a modern orvostudományban : transzlációs aspektusok / Döncző Boglárka, Bodnár Judit, Szigeti Márton, Járvás Gábor, Hajba László, Guttman András
Dátum:2015
Tárgyszavak:Orvostudományok Elméleti orvostudományok ismeretterjesztő, népszerűsítő cikk
Megjelenés:Interdiszciplináris Magyar Egészségügy 14 : 6 (2015), p. 24-28. -
További szerzők:Bodnár Judit Szigeti Márton (1986-) (környezetmérnök) Járvás Gábor (1982-) (vegyészmérnök) Hajba László Guttman András (1954-) (vegyészmérnök)
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5.

001-es BibID:BIBFORM116213
035-os BibID:(WoS)001104988800001 (Scopus)85178183698
Első szerző:Farsang Róbert
Cím:Capillary Zone Electrophoresis of 8-Aminopyrene-1,3,6-trisulfonic Acid Labeled Carbohydrates with Online Electrokinetic Sample Cleanup / Farsang Robert, Hogyor Kinga, Jarvas Gabor, Guttman Andras
Dátum:2023
ISSN:0003-2700
Megjegyzések:Capillary electrophoresis is one of the frequently used separation techniques for the analysis of complex carbohydrates. Since sugars lack chromophore or fluorophore groups, their capillary electrophoresis analysis usually requires tagging by a charged fluorophore. To speed up the derivatization reaction, a large excess of the labeling reagent is typically used; therefore, a purification step is necessary prior to CE analysis using the industry standard low-pH gel-buffer system. In addition to representing an extra sample preparation step with the associated labor and cost, the purification process also holds the risk of losing some of the sample components. In this paper we introduce an online electrokinetic sample cleanup process with electroosmotic flow (EOF)-assisted separation in a bare fused silica capillary using alkaline pH background electrolyte and normal polarity separation voltage. 8-Aminopyrene-1,3,6-trisulfonic acid (APTS)-labeled maltooligosaccharides were analyzed first to understand the complex effect of the downstream EOF and the counter current electromigration of the sample components including the labeling dye. The use of 150 mM caproic acid?253 mM Tris (pH 8.1) running buffer facilitated the entrance of the sample components of interest into the separation capillary, while the excess labeling reagent was excluded and, therefore, did not interfere with the detection. The alkaline caproic acid?Tris running buffer was then applied to the N-glycome analysis of human serum samples, showing excellent separation performance, and more importantly, the extra sample purification step was not required.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Capillary electrophoresis
Carbohydrates
Electroosmosis
Labeling
Polarity
Megjelenés:Analytical Chemistry. - 95 : 45 (2023), p. 16459-16464. -
További szerzők:Hogyor Kinga Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:DE TUDFIN
Egyéb
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6.

001-es BibID:BIBFORM115940
035-os BibID:(cikkazonosító)115812 (scopus)85175539824
Első szerző:Farsang Róbert
Cím:Purification free N-glycan analysis by capillary zone electrophoresis : Hunt for the lost glycans / Farsang Robert, Jarvas Gabor, Guttman Andras
Dátum:2024
ISSN:0731-7085
Megjegyzések:Capillary gel electrophoresis is a widely used method for rapid separation of fluorophore labeled carbohydrates. Even though, many publications conferred about this popular technique, no report yet investigated the possible sample losses during the purification process of the fluorophore labeling reaction mixture. In the present work, normal polarity capillary zone electrophoresis separation mode was applied to take advantage of the opposite migration directions of the electroosmotic flow and the negatively charged sample components using Tris- hexanoic acid running buffer at basic pH. For purification free oligosaccharide analysis, the separation parameters were designed in such a way that the triple charged labeling reagent of aminopyrenetrisulfonate (APTS) could not enter the separation capillary in contrary to the labeled sample components of interest, therefore, the APTS did not have to be removed before analysis. The method was used to show electrophoretic profile differences possibly caused by the cleanup process that was immediately apparent by comparing the electropherograms of the purified and non-purified APTS labeled maltooligosaccharides. Furthermore, qualitative and quantitative N-glycosylation profile alterations were revealed during CZE separation of the fluorophore labeling reaction mixtures before and after purification along with the analysis of the consecutively used washing solutions for the well characterized standard glycoproteins of IgG, ribonuclease B and fetuin.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
N-glycans
Capillary zone electrophoresis
Purification
Sample loss
Megjelenés:Journal Of Pharmaceutical And Biomedical Analysis. - 238 (2024), p. 1-5. -
További szerzők:Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
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7.

001-es BibID:BIBFORM106794
035-os BibID:(cikkazonosító)333 (scopus)85141755492 (wos)000881482500001
Első szerző:Farsang Róbert
Cím:Ultrahigh-Sensitivity Capillary Electrophoresis Analysis of Trace Amounts of Nitrate and Nitrite in Environmental Water Samples / Farsang Robert, Kovacs Zsofia, Jarvas Gabor, Guttman Andras
Dátum:2022
ISSN:2297-8739
Megjegyzések:The role of nitrite (NO2?) and nitrate (NO3?) is essential in the global nitrogen cycle. Monitoring their concentration in environmental and industrial aqueous samples, surface water, soil, food and agricultural products are of high importance. Especially, the effect of anthropogenic emission, i.e., intensified agriculture is essential due to the overuse of nitrogen, phosphorus and potassium fertilizers. The most widely utilized methods for nitrate and nitrite determination are colorimetry, potentiometry, UV absorption and liquid chromatography. Among them, UV spectroscopy is the most frequently used technique due to the fact of its versatility and simplicity. However, there are industrial and academic needs to develop new methods to overcome some drawbacks of the currently used techniques such as an inadequate limit of detection and potential interferences with organic compounds in the sample. In this paper, we report on the development of a new analytical method based on capillary electrophoresis separation with high-sensitivity UV detection, capable of measuring trace concentrations of nitrite and nitrate well below the current limits of UV spectroscopy methods. During the development process special attention was paid to practical aspects, i.e., the method was tested to quantify nitrate and nitrite in various surface water samples.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Separations. - 9 : 11 (2022), p. 1-7. -
További szerzők:Kovács Zsófia Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:RRF 2.3.1-21-2022-00008
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8.

001-es BibID:BIBFORM082495
035-os BibID:(cikkazonosító)112892
Első szerző:Filep Csenge Boróka (biomérnök)
Cím:N-glycosylation analysis of biopharmaceuticals by multicapillary gel electrophoresis : generation and application of a new glucose unit database / Csenge Filep, Beata Borza, Gabor Jarvas, Andras Guttman
Dátum:2020
ISSN:0731-7085
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal of Pharmaceutical and Biomedical Analysis. - 178 (2020), p. 1-5. -
További szerzők:Borza Beáta (1990-) (biomérnök) Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:NN127062
NKFIH
2018-2.1.17-TÉT-KR-2018-00010
Egyéb
GINOP-2.3.2-15-2016-00017
GINOP
EFOP-3.6.3-VEKOP16-2017-00009
EFOP
ÚNKP-19-3-I-DE-356
Egyéb
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9.

001-es BibID:BIBFORM092956
Első szerző:Fonslow, Bryan
Cím:Multilevel Characterization of Antibody-Ligand Conjugates by CESI-MS / Bryan Fonslow, Gábor Jarvas, Marton Szigeti, András Guttman
Dátum:2020
ISSN:1566-5240
Megjegyzések:Aim: To demonstrate the capabilities of our new capillary electrophoresis mass spectrometry method, which facilitates highly accurate relative quantitation of modification site occupancy of antibody-ligand (e.g., antibody-drug) conjugates. Background: Antibody-drug conjugates play important roles in medical discovery for imaging and therapeutic intervention. The localization and stoichiometry of the conjugation can affect the orientation, selectivity, specificity, and strength of molecular interactions, influencing biochemical function. Objective: To demonstrate the option to analyze the localization and stoichiometry of antibody-ligand conjugates by using essentially the same method at all levels including ligand infusion, peptide mapping, as well as reduced and intact protein analysis. Materials and Methods: Capillary electrophoresis coupled with electrospray ionization mass spectrometry was used to analyze the antibody-ligand conjugates. Results: We identified three prevalent ligand conjugation sites with estimated stoichiometries of 73, 14, and 6% and an average ligand-antibody ratio of 1.37, illustrating the capabilities of CE-ESI-MS for rapid and efficient characterization of antibody-drug conjugates. Conclusion: The developed multilevel analytical method offers a comprehensive way to determine the localization and stoichiometry of antibody-drug conjugates for molecular medicinal applications. In addition, a significant advantage of the reported approach is the small, hydrophilic, unmodified peptides well separated from the neutrals, which is not common with other liquid phase separation methods such as LC.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Current Molecular Medicine. - 20 : 10 (2020), p. 789-797. -
További szerzők:Járvás Gábor (1982-) (vegyészmérnök) Szigeti Márton (1986-) (környezetmérnök) Guttman András (1954-) (vegyészmérnök)
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10.

001-es BibID:BIBFORM065042
035-os BibID:(WoS)000365931100006 (Scopus)84948451094
Első szerző:Guttman András (vegyészmérnök)
Cím:Effect of Separation Temperature on Structure Specific Glycan Migration in Capillary Electrophoresis / Andras Guttman, Marta Kerekgyarto, Gabor Jarvas
Dátum:2015
ISSN:0003-2700
Megjegyzések:Temperature dependent differential migration shifts were studied in capillary electrophoresis between linear (maltooligosaccharides) and branched (sialylated, neutral and core fucosylated biantennary IgG glycans) carbohydrates. Background electrolytes without as well as with low and high molecular weight additives (ethylene glycol, linear polyacrylamide and poly(ethylene oxide)) were investigated for this phenomena in the temperature range of 20-50 ?C. Glucose unit (GU) value shifts were observed with increasing temperature for the all IgG glycans both in additive-free and additive-containing background electrolytes, emphasizing the importance of tight temperature control during glycosylation analysis by capillary electrophoresis. The activation energy concept was applied to understand the structure specific electrophoretic migration of the different sugar molecules. Activation energy values were derived from the slopes of the Arrhenius plots of logarithmic mobility vs reciprocal absolute temperature and compared for the linear and branched sugars as well as for the various background electrolyte additives.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
capillary electrophoresis
glycan structure
mobility
temperature
activation energy
Megjelenés:Analytical Chemistry. - 87 : 23 (2015), p. 11630-11634. -
További szerzők:Kerékgyártó Márta (1987-) (molekuláris biológus) Járvás Gábor (1982-) (vegyészmérnök)
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11.

001-es BibID:BIBFORM115154
035-os BibID:(cikkazonosító)4845 (Scopus)85112582716 (WOS)000689890600001
Első szerző:Járvás Gábor (vegyészmérnök)
Cím:Modification of Hemodialysis Membranes for Efficient Circulating Tumor Cell Capture for Cancer Therapy / Jarvas Gabor, Szerenyi Dora, Tovari Jozsef, Takacs Laszlo, Guttman Andras
Dátum:2021
ISSN:1420-3049
Megjegyzések:It is well known that more than 90% of cancer deaths are due to metastases. However, the entire tumorigenesis process is not fully understood, and it is evident that cells spreading from the primary tumor play a key role in initiating the metastatic process. Tumor proliferation and invasion also elevate the concentration of regular and irregular metabolites in the serum, which may alter the normal function of the entire human homeostasis and possibly causes cancer metabolism syndrome, also referred to as cachexia. Methods: We report on the modification of commercially available hemodialysis membranes to selectively capture circulating tumor cells from the blood stream by means of immobilized human anti?EpCAM antibodies on the inner surface of the fibers. All critical steps are described that required in situ addition of the immuno?affinity feature to hemodialyzer cartridges in order to capture EpCAM positive circulating tumor cells, which represents ~80% of cancer cell types. Results: The cell capture efficiency of the suggested technology was demonstrated by spiking HCT116 cancer cells both into buffer solution and whole blood and run through on the modified cartridge. Flow cytometry was used to quantitatively evaluate the cell clearance performance of the approach. Conclusions: The suggested modification has no significant effect on the porous structure of the hemodialysis membranes; it keeps its cytokine removal capability, addressing cachexia simultaneously with CTC removal.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Capture
Circulating tumor cell
Hemodialysis
Therapy
Megjelenés:Molecules. - 26 : 16 (2021), p. 1-11. -
További szerzők:Szerényi Dóra Tóvári József Takács László (1955-) (orvos) Guttman András (1954-) (vegyészmérnök)
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12.

001-es BibID:BIBFORM111408
035-os BibID:(cikkazonosító)95 (scopus)85148518915 (wos)000936836300002
Első szerző:Járvás Gábor (vegyészmérnök)
Cím:Microbead-based extracorporeal immuno-affinity virus capture : a feasibility study to address the SARS-CoV-2 pandemic / Jarvas Gabor, Szerenyi Dora, Jankovics Hajnalka, Vonderviszt Ferenc, Tovari Jozsef, Takacs Laszlo, Foldes Fanni, Somogyi Balazs, Jakab Ferenc, Guttman Andras
Dátum:2023
ISSN:0026-3672
Megjegyzések:In this paper, we report on the utilization of micro-technology based tools to fight viral infections. Inspired by various hemoperfusion and immune-affinity capture systems, a blood virus depletion device has been developed that offers highly efficient capture and removal of the targeted virus from the circulation, thus decreasing virus load. Single-domain antibodies against the Wuhan (VHH-72) virus strain produced by recombinant DNA technology were immobilized on the surface of glass micro-beads, which were then utilized as stationary phase. For feasibility testing, the virus suspension was flown through the prototype immune-affinity device that captured the viruses and the filtered media left the column. The feasibility test of the proposed technology was performed in a Biosafety Level 4 classified laboratory using the Wuhan SARS-CoV-2 strain. The laboratory scale device actually captured 120,000 virus particles from the culture media circulation proving the feasibility of the suggested technology. This performance has an estimated capture ability of 15 million virus particles by using the therapeutic size column design, representing three times over-engineering with the assumption of 5 million genomic virus copies in an average viremic patient. Our results suggested that this new therapeutic virus capture device could significantly lower virus load thus preventing the development of more severe COVID-19 cases and consequently reducing mortality rate.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Microchimica Acta. - 190 : 3 (2023), p. 1-9. -
További szerzők:Szerényi Dóra Jankovics Hajnalka Vonderviszt Ferenc Tóvári József Takács László (1955-) (orvos) Földes Fanni Vivien (virológus) Somogyi Balázs Jakab Ferenc (1977-) (biológus) Guttman András (1954-) (vegyészmérnök)
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