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1.

001-es BibID:BIBFORM002004
Első szerző:Csánky Eszter (tüdőgyógyász, klinikai immunológus, allergológus)
Cím:Monoclonal antibody proteomics : discovery and prevalidation of chronic obstructive pulmonary disease biomarkers in a single step / Eszter Csanky, Petra Olivova, Eva Rajnavolgyi, William Hempel, Nadege Tardieu, Elesne Toth Katalin, Anne Jullien, Carole Malderez-Bloes, Mariana Kuras, Manuel X. Duval, Laszlo Nagy, Beata Scholtz, William Hancock, Barry Karger, András Guttman, Laszlo Takacs
Dátum:2007
Megjegyzések:We define mAb proteomics as the global generation of disease specific antibodies that permit mass screening of biomarkers. An integrated, high-throughput, disease-specific mAb-based biomarker discovery platform has been developed. The approach readily provided new biomarker leads with the focus on large-scale discovery and production of mAb-based, disease-specific clinical assay candidates. The outcome of the biomarker discovery process was a highly specific and sensitive assay, applicable for testing of clinical validation paradigms, like response to treatment or correlation with other clinical parameters. In contrast to MS-based or systems biology-based strategies, our process produced prevalidated clinical assays as the outcome of the discovery process. By re-engineering the biomarker discovery paradigm, the encouraging results presented in this paper clearly demonstrate the efficiency of the mAb proteomics approach, and set the grounds for the next steps of studies, namely, the hunt for candidate biomarkers that respond to drug treatment.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
antibody
biomarker discovery
proteomics
Megjelenés:Electrophoresis 28 : 23 (2007), p. 4401-4406. -
További szerzők:Olivova, Petra Rajnavölgyi Éva (1950-) (immunológus) Hempel, William Tardieu, Nadège Élesné Tóth Katalin Jullien, Anne Malderez-Bloes, Carole Kuras, Mariana Duval, Manuel X. Nagy László Scholtz Beáta (1967-) (biokémikus, molekuláris biológus) Hancock, William Karger, Barry Guttman András (1954-) (vegyészmérnök) Takács László (1955-)
Internet cím:elektronikus változat
DOI
elektronikus változat
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2.

001-es BibID:BIBFORM023718
035-os BibID:(cikkazonosító)M111.010298 (WoS)000298290300017 (Scopus)83055168546
Első szerző:Guergova-Kuras, Mariana
Cím:Discovery of lung cancer biomarkers by profiling the plasma proteome with monoclonal antibody libraries / Mariana Guergova-Kuras, István Kurucz, William Hempel, Nadege Tardieu, János Kádas, Carole Malderez-Bloes, Anne Jullien, Yann Kieffer, Marina Hincapie, András Guttman, Eszter Csánky, Balázs Dezső, Barry L. Karger, László Takács
Dátum:2011
ISSN:1535-9476 1535-9484
Megjegyzések:A challenge in the treatment of lung cancer is the lack of early diagnostics. Here, we describe the application of monoclonal antibody (mAb) proteomics for discovery of a panel of biomarkers for early detection (stage I) of non small cell lung cancer (NSCLC). We produced large monoclonal antibody libraries directed against the natural form of protein antigens present in the plasma of NSCLC patients. Plasma biomarkers associated with the presence of lung cancer were detected via high throughput ELISA. Differential profiling of plasma proteomes of four clinical cohorts, totalling 301 patients with lung cancer and 235 healthy controls, identified 13 lung cancer associated (p<0.05) monoclonal antibodies. The mAbs recognize five different cognate proteins identified using immunoprecipitation followed by mass spectrometry. Four of the five antigens were present in non-small cell lung cancer cells in-situ. The approach is capable of generating independent antibodies against different epitopes of the same proteins, allowing fast translation to multiplexed sandwich assays. Based on these results, we have verified in two independent clinical collections a panel of five biomarkers for classifying patient disease status with a diagnostics performance of 77% sensitivity and 87% specificity. Combining CYFRA, an established cancer marker, with the panel resulted in a performance of 83 % sensitivity at 95 % specificity for stage I NSCLC.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Molecular and Cellular Proteomics. - 10 : 12 (2011), p. 1-14. -
További szerzők:Kurucz István Hempel, William Tardieu, Nadège Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Malderez-Bloes, Carole Jullien, Anne Kieffer, Yann Hincapie, Marina Guttman András (1954-) (vegyészmérnök) Csánky Eszter (1959-) (tüdőgyógyász, klinikai immunológus, allergológus) Karger, Barry Takács László (1955-) Dezső Balázs (1951-) (pathológus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
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3.

001-es BibID:BIBFORM096076
035-os BibID:(WoS)000672115800032 (Scopus)85110405663
Első szerző:Guttman András (vegyészmérnök)
Cím:Fundamentals of Capillary Electrophoretic Migration and Separation of SDS Proteins in Borate Cross-Linked Dextran Gels / András Guttman, Csenge Filep, Barry L. Karger
Dátum:2021
ISSN:0003-2700
Megjegyzések:Abstract Abstract Image Recent progress in the development and production of new, innovative protein therapeutics require rapid and adjustable high-resolution bioseparation techniques. Sodium dodecyl sulfate capillary gel electrophoresis (SDS-CGE) using a borate (B) cross-linked dextran (D) separation matrix is widely employed today for rapid consistency analysis of therapeutic proteins in manufacturing and release testing. Transient borate cross-linking of the semirigid dextran polymer chains leads to a high-resolution separation gel for SDS?protein complexes. To understand the migration and separation basis of the D/B gel, the present work explores various gel formulations of dextran monomer (2, 5, 7.5, and 10%) and borate cross-linker (2 and 4%) concentrations. Ferguson plots were analyzed for a mixture of protein standards with molecular weights ranging from 20 to 225 kDa, and the resulting nonlinear concave curves pointed to nonclassical sieving behavior. While the 2% D/4% B gel resulted in the fastest analysis time, the 10% D/2% B gel was found to produce the greatest separation window, even higher than with the 10% D/4% B gel, due to a significant increase in the electroosmotic flow of the former composition in the direction opposite to SDS?protein complex migration. The study then focused on SDS-CGE separation of a therapeutic monoclonal antibody and its subunits. A combination of molecular weight and shape selectivity as well as, to a lesser extent, surface charge density differences (due to glycosylation on the heavy chain) influenced migration. Greater molecular weight selectivity occurred for the higher monomer concentration gels, while improved glycoselectivity was obtained using a more dilute gel, even as low as 2% D/2% B. This latter gel took advantage of the dextran?borate?glycoprotein complexation. The study revealed that by modulating the dextran (monomer) and borate (cross-linker) concentration ratios of the sieving matrix, one can optimize the separation for specific biopharmaceutical modalities with excellent column-to-column, run-to-run, and gel-to-gel migration time reproducibilities (<0.96% relative standard deviation (RSD)). The widely used 10% dextran/4% borate gel represents a good screening option, which can then be followed by a modified composition, optimized for a specific separation as necessary.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytical Chemistry. - 93 : 26 (2021), p. 9267-9276. -
További szerzők:Filep Csenge Boróka (1993-) (biomérnök) Karger, Barry
Pályázati támogatás:2.3.2- 15-2016-00017
GINOP
NKFIH (NN 127062)
Egyéb
ÚNKP-20-3-II-DE-294
Egyéb
2020-4.1.1-TKP2020
Egyéb
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM069407
Első szerző:Guttman András (vegyészmérnök)
Cím:Biomarker Discovery by Monoclonal Antibody Proteomics / A. Guttman, B. L. Karger, W. S. Hancock, L. Takacs
Dátum:2006
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Molecular & Cellular Proteomics. - 5 : 10 (2006), 86. p. -
További szerzők:Karger, Barry Hancock, William Takács László (1955-)
Internet cím:Intézményi repozitóriumban tárolt változat
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5.

001-es BibID:BIBFORM099567
035-os BibID:(WoS)000292280900044 (Scopus)79959926784
Első szerző:Szabó Zoltán
Cím:Rapid high resolution characterization of functionally important monoclonal antibody N-Glycans by Capillary Electrophoresis / Zoltan Szabo, András Guttman, Jonathan Bones, Barry L. Karger
Dátum:2011
ISSN:0003-2700
Megjegyzések:Characterization of the N-glycosylation present in the Fc region of therapeutic monoclonal antibodies requires rapid, high-resolution separation methods to guarantee product safety and efficacy during all stages of process development. Determination of fucosylated oligosaccharides is particularly important during clone selection, product characterization, and lot release as fucose has been shown to adversely affect the ability of mAbs to induce antibody dependent cellular cytotoxicity (ADCC). Here, we apply a general capillary electrophoresis optimization strategy to separate functionally relevant fucosylated and afucosylated glycans on mononclonal antibody products in the presence of several high mannose oligosaccharides. The N-glycans chosen represent those most commonly reported on CHO cell derived therapeutic antibodies. A rapid (<7 min) high-resolution separation of 12 commonly reported and functionally important IgG glycans was developed by systematically evaluating the effects of selectivity (boric acid) and efficiency (linear polyacrylamide) enhancing additives. The approach can be used to rapidly optimize capillary electrophoresis separation of other glycan mixtures. Following optimization, the method was applied to overnight sample processing for automated 96 well plate-based glycosylation analyses of two nonproprietary therapeutic monoclonal antibodies, demonstrating ruggedness and suitability for high-throughput process and product monitoring applications.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytical Chemistry. - 83 : 13 (2011), p. 5329-5336. -
További szerzők:Guttman András (1954-) (vegyészmérnök) Bones, Jonathan Karger, Barry
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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6.

001-es BibID:BIBFORM069419
Első szerző:Takács László
Cím:Monoclonal antibody based biomarker discovery and development platform / Laszlo Takacs, Andras Guttman, William S. Hancock, Barry L. Karger, Manuel Duval, Patrick Berna
Dátum:2013
Megjelenés:USA, 2013
Terjedelem:19 p.
Tárgyszavak:Orvostudományok Elméleti orvostudományok szabadalom
További szerzők:Guttman András (1954-) (vegyészmérnök) Hancock, William Karger, Barry Duval, Manuel X. Berna, Patrick
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:
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