Zobrazeno 1 - 10 of 36 pro vyhledávání: '"Oscar Hernandez-Alba"'
1
Akademický článek
Denaturing mass photometry for rapid optimization of chemical protein-protein cross-linking reactions
Autor: Hugo Gizardin-Fredon, Paulo E. Santo, Marie-Eve Chagot, Bruno Charpentier, Tiago M. Bandeiras, Xavier Manival, Oscar Hernandez-Alba, Sarah Cianférani
Publikováno v: Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Chemical cross-linking reactions (XL) are an important strategy for studying protein-protein interactions (PPIs), including low abundant sub-complexes, in structural biology. However, choosing XL reagents and conditions is laborious and most
Externí odkaz: https://doaj.org/article/3688e424b082493787ea3c02aaefe808
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2
Akademický článek
Large-Scale Conformational Changes of FhaC Provide Insights Into the Two-Partner Secretion Mechanism
Autor: Giuseppe Sicoli, Albert Konijnenberg, Jérémy Guérin, Steve Hessmann, Elise Del Nero, Oscar Hernandez-Alba, Sophie Lecher, Guillaume Rouaut, Linn Müggenburg, Hervé Vezin, Sarah Cianférani, Frank Sobott, Robert Schneider, Françoise Jacob-Dubuisson
Publikováno v: Frontiers in Molecular Biosciences, Vol 9 (2022)
The Two-Partner secretion pathway mediates protein transport across the outer membrane of Gram-negative bacteria. TpsB transporters belong to the Omp85 superfamily, whose members catalyze protein insertion into, or translocation across membranes with
Externí odkaz: https://doaj.org/article/1d8c2f861f3343c89ad6ee96c59c21e2
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3
Akademický článek
A Combination of Native LC-MS Approaches for the Comprehensive Characterization of the Antibody-Drug Conjugate Trastuzumab Deruxtecan
Autor: Evolène Deslignière, Hélène Diemer, Stéphane Erb, Pierre Coliat, Xavier Pivot, Alexandre Detappe, Oscar Hernandez-Alba, Sarah Cianférani
Publikováno v: Frontiers in Bioscience-Landmark, Vol 27, Iss 10, p 290 (2022)
Background: Native mass spectrometry (nMS) approaches appear attractive to complement bottom-up strategies traditionally used in biopharmaceutical industries thanks to their quite straightforward and rapid workflows, especially through online hyphena
Externí odkaz: https://doaj.org/article/2eb3b84cdb244237b1b7bfa03505ee71
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4
Akademický článek
State-of-the-Art Native Mass Spectrometry and Ion Mobility Methods to Monitor Homogeneous Site-Specific Antibody-Drug Conjugates Synthesis
Autor: Evolène Deslignière, Anthony Ehkirch, Bastiaan L. Duivelshof, Hanna Toftevall, Jonathan Sjögren, Davy Guillarme, Valentina D’Atri, Alain Beck, Oscar Hernandez-Alba, Sarah Cianférani
Publikováno v: Pharmaceuticals, Vol 14, Iss 6, p 498 (2021)
Antibody-drug conjugates (ADCs) are biotherapeutics consisting of a tumor-targeting monoclonal antibody (mAb) linked covalently to a cytotoxic drug. Early generation ADCs were predominantly obtained through non-selective conjugation methods based on
Externí odkaz: https://doaj.org/article/ca5a96c401214bd8a596a8f7067e6039
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5
A Novel Family of Acid-Cleavable Linker Based on Cyclic Acetal Motifs for the Production of Antibody-Drug Conjugates with High Potency and Selectivity
Autor: Tony Rady, Lorenzo Turelli, Marc Nothisen, Elisabetta Tobaldi, Stéphane Erb, Fabien Thoreau, Oscar Hernandez-Alba, Sarah Cianferani, François Daubeuf, Alain Wagner, Guilhem Chaubet
Publikováno v: Bioconjugate Chemistry. 33:1860-1866
Cleavable linkers have become the subject of intense study in the field of chemical biology, particularly because of their applications in the construction of antibody-drug conjugates (ADC), where they facilitate lysosomal cleavage and liberation of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29227329a543ded2df288b4c9d817ee7
https://doi.org/10.1021/acs.bioconjchem.2c00314
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7
Denaturing mass photometry for straightforward optimization of protein-protein cross-linking reactions at single-molecule level
Autor: Hugo Gizardin-Fredon, Paulo E. Santo, Marie-Eve Chagot, Bruno Charpentier, Tiago M. Bandeiras, Xavier Manival, Oscar Hernandez-Alba, Sarah Cianferani
Mass photometry (MP) is a versatile, fast and low sample-consuming biophysical technique that gained interest in structural biology to study noncovalent assemblies in native conditions. We report here on a novel method to perform MP analysis in denat
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a43f2d9b19edbe06ae6afc9f00af2130
https://doi.org/10.1101/2023.05.30.542861
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9
Online collision-induced unfolding of therapeutic monoclonal antibody glyco-variants through direct hyphenation of cation exchange chromatography with native ion mobility-mass spectrometry
Autor: Guusje van Schaick, Elena Domínguez-Vega, Jérôme Castel, Manfred Wuhrer, Oscar Hernandez-Alba, Sarah Cianférani
Publikováno v: Analytical Chemistry, 95(8), 3932-3939. AMER CHEMICAL SOC
Post-translational modifications (PTMs) not only substantially increase structural heterogeneity of proteins but can also alter the conformation or even biological functions. Monitoring of these PTMs is particularly important for therapeutic products
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8cc99c0e3a33cccb97c75bf74c54b05
https://hdl.handle.net/1887/3590832
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10
High-Resolution IMS–MS to Assign Additional Disulfide Bridge Pairing in Complementarity-Determining Regions of an IgG4 Monoclonal Antibody
Autor: Elsa Wagner-Rousset, Olivier Colas, Kevin Giles, Sarah Cianférani, Thomas Botzanowski, Evolène Deslignière, Oscar Hernandez-Alba, Alain Beck, Dale Cooper-Shepherd, Hélène Diemer, Guillaume Béchade
Publikováno v: Journal of The American Society for Mass Spectrometry
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), In press, ⟨10.1021/jasms.1c00151⟩
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), In press
International audience; Monoclonal antibodies (mAbs) have taken on an increasing importance for the treatment of various diseases, including cancers and immunological disorders. Disulfide bonds play a pivotal role in therapeutic antibody structure an
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d8d2127da7e4623cbd97d46b87317e4
https://doi.org/10.1021/jasms.1c00151
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