N. Bihoreau

发表

Chronic lymphocytic leukaemia cells are efficiently killed by an anti‐CD20 monoclonal antibody selected for improved engagement of FcγRIIIA/CD16

Bruno Cazin, Charles-Antoine Dutertre, Jean-Luc Teillaud, 2008, British journal of haematology.

Selection of a human anti-RhD monoclonal antibody for therapeutic use: impact of IgG glycosylation on activating and inhibitory Fc gamma R functions.

W. Fridman, M. Hogarth, D. Bourel, 2006, Clinical immunology.

Investigation of monoclonal antibody dimers in a final formulated drug by separation techniques coupled to native mass spectrometry

M. Taverna, N. Bihoreau, N. T. Tran, 2020, mAbs.

Aggregates Dramatically Alter Fibrin Ultrastructure.

B. Polack, Z. Tellier, N. Bihoreau, 2019, Biophysical journal.

Aggregates dramatically alter fibrin ultrastructure

B. Polack, Z. Tellier, N. Bihoreau, 2018, bioRxiv.

Quantification of proteins by data independent acquisition: Performance assessment of the Hi3 methodology.

N. Bihoreau, G. Chevreux, N. Tilly, 2018, Analytical biochemistry.

Combined use of 2,4,6-trihydroxyacetophenone as matrix and enzymatic deglycosylation in organic-aqueous solvent systems for the simultaneous characterization of complex glycoproteins and N-glycans by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

F. Fenaille, L. Siret, N. Bihoreau, 2007, Rapid communications in mass spectrometry : RCM.

C-terminal lysine clipping of IgG1: impact on binding to human FcγRIIIa and neonatal Fc receptors.

Alexander Seifert, N. Bihoreau, G. Chevreux, 2021, European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences.

Igg3 anti rhesus-d in the line yb2/0 having a high phagocytosis activity

D. Bourel, S. Jorieux, N. Bihoreau, 2004 .

Fast analysis of recombinant monoclonal antibodies using IdeS proteolytic digestion and electrospray mass spectrometry.

N. Bihoreau, G. Chevreux, N. Tilly, 2011, Analytical biochemistry.

N-/O-glycosylation analysis of human FVIIa produced in the milk of transgenic rabbits

N. Bihoreau, G. Chevreux, V. Faid, 2013, Glycobiology.

Differential investigations from plasma‐derived and recombinant Factor IX revealed major differences in post‐translational modifications of activation peptides

M-H André, Z. Tellier, N. Bihoreau, 2013, Vox sanguinis.

Site‐specific N‐glycosylation analysis of human factor XI: Identification of a noncanonical NXC glycosite

N. Bihoreau, G. Chevreux, V. Chapuis, 2014, Proteomics.

Glycation of polyclonal IgGs: Effect of sugar excipients during stability studies.

M-H André, Z. Tellier, N. Bihoreau, 2016, European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V.

Human serum albumin presents isoform variants with altered neonatal Fc receptor interactions

Alexander Seifert, N. Bihoreau, G. Chevreux, 2019, Protein science : a publication of the Protein Society.

Characterization of Human Serum Albumin isoforms by ion exchange chromatography coupled on-line to native mass spectrometry.

N. Bihoreau, G. Chevreux, Y. Leblanc, 2018, Journal of chromatography. B, Analytical technologies in the biomedical and life sciences.

Characterization of each isoform of a F(ab')2 by capillary electrophoresis.

R. Vincentelli, N. Bihoreau, 1993, Journal of chromatography.

Biochemical characterization of LR769, a new recombinant factor VIIa bypassing agent produced in the milk of transgenic rabbits

F. Dhainaut, N. Bihoreau, G. Chevreux, 2017, Haemophilia : the official journal of the World Federation of Hemophilia.

Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII

F. Fenaille, S. Chtourou, L. Siret, 2008, Glycoconjugate Journal.

Mass spectrometry based analysis of human plasma‐derived factor X revealed novel post‐translational modifications

N. Bihoreau, G. Chevreux, N. Tilly, 2015, Protein science : a publication of the Protein Society.

Characterization of a recombinant antihaemophilia-A factor (factor VIII-delta II) by matrix-assisted laser desorption/ionization mass spectrometry.

J. Schmitter, N. Bihoreau, J. Scohyers, 1995, Rapid communications in mass spectrometry : RCM.

Charge variants characterization of a monoclonal antibody by ion exchange chromatography coupled on-line to native mass spectrometry: Case study after a long-term storage at +5°C.

N. Bihoreau, Y Leblanc, C Ramon, 2017, Journal of chromatography. B, Analytical technologies in the biomedical and life sciences.

Middle‐up analysis of monoclonal antibodies after combined IgdE and IdeS hinge proteolysis: Investigation of free sulfhydryls

N. Bihoreau, G. Chevreux, Y. Leblanc, 2018, Journal of pharmaceutical and biomedical analysis.

DNA aptamer affinity ligands for highly selective purification of human plasma-related proteins from multiple sources.

Egisto Boschetti, F. Ducongé, E. Boschetti, 2017, Journal of chromatography. A.

Site-specific N-glycan characterization of human complement factor H.

F. Fenaille, L. Siret, N. Bihoreau, 2007, Glycobiology.

A generic method for intact and subunit level characterization of mAb charge variants by native mass spectrometry.

M. Lauber, N. Bihoreau, G. Chevreux, 2019, Journal of chromatography. B, Analytical technologies in the biomedical and life sciences.

Continuous production of large amounts of monoclonal immunoglobulins in hollow fibers using protein-free medium

R. Vincentelli, F. Dhainaut, J. Lirochon, 2004, Cytotechnology.

"Factor composition vii recombinant or transgenic, mostly biantennary glycan having shapes, bisialylated and non fucosylated"

E. Nony, N. Bihoreau, A. Chtourou, 2006 .

LC-MS analysis of polyclonal IgGs using IdeS enzymatic proteolysis for oxidation monitoring.

N. Bihoreau, G. Chevreux, Y. Leblanc, 2014, Journal of chromatography. B, Analytical technologies in the biomedical and life sciences.

DNA aptamer affinity ligands for highly selective purification of human plasma-related proteins from multiple sources.

F. Ducongé, E. Boschetti, S. Chtourou, 2017, Journal of chromatography. A.