D. Legrand

发表

Lipid nanocapsules functionalized with polyethyleneimine for plasmid DNA and drug co-delivery and cell imaging.

R. Boukherroub, T. Gharbi, Nadia Skandrani, 2014, Nanoscale.

Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety.

C. Cambillau, P. Rougé, D. Legrand, 1994, Structure.

Characterization of human lactoferrin produced in the baculovirus expression system.

V. Salmon, D. Legrand, B. Coddeville, 1997, Protein expression and purification.

Overview of Lactoferrin as a Natural Immune Modulator.

D. Legrand, 2016, The Journal of pediatrics.

Lactoferrin-lipopolysaccharide interaction: involvement of the 28-34 loop region of human lactoferrin in the high-affinity binding to Escherichia coli 055B5 lipopolysaccharide.

V. Salmon, D. Legrand, E. Elass-Rochard, 1995, The Biochemical journal.

Biometals and glycosylation in humans: Congenital disorders of glycosylation shed lights into the crucial role of manganese Golgi homeostasis.

D. Legrand, F. Foulquier, 2020, Biochimica et biophysica acta. General subjects.

A critical review of the roles of host lactoferrin in immunity

D. Legrand, J. Mazurier, 2010, BioMetals.

Differential effects of lobe A and lobe B of the Conserved Oligomeric Golgi complex on the stability of β 1,4-galactosyltransferase 1 and α 2,6-sialyltransferase 1

J. Rohrer, G. Matthijs, A. Mir, 2011 .

Studies of cellular informative transfer by THz BioMEMS

B. Bocquet, D. Legrand, J. Mazurier, 2008, 2008 33rd International Conference on Infrared, Millimeter and Terahertz Waves.

Lactoferrin: A Multifunctional Glycoprotein Involved in the Modulation of the Inflammatory Process

D. Legrand, G. Spik, J. Mazurier, 1999, Clinical chemistry and laboratory medicine.

Lactoferrin and host defence: an overview of its immuno-modulating and anti-inflammatory properties

D. Legrand, A. Pierce, J. Mazurier, 2004, Biometals.

PUGNAc treatment leads to an unusual accumulation of free oligosaccharides in CHO cells.

T. Lefebvre, D. Legrand, F. Foulquier, 2012, Journal of biochemistry.

Differential Effects of D-Galactose Supplementation on Golgi Glycosylation Defects in TMEM165 Deficiency

D. Legrand, F. Foulquier, W. Morelle, 2022, Frontiers in Cell and Developmental Biology.

N‐glycosylation influences the structure and self‐association abilities of recombinant nucleolin

D. Legrand, B. Coddeville, J. Mazurier, 2011, The FEBS journal.

Lactoferrin Inhibits the Endotoxin Interaction with CD14 by Competition with the Lipopolysaccharide-Binding Protein

V. Salmon, P. Tobias, D. Legrand, 1998, Infection and Immunity.

Human Lactoferrin Interacts with Soluble CD14 and Inhibits Expression of Endothelial Adhesion Molecules, E-Selectin and ICAM-1, Induced by the CD14-Lipopolysaccharide Complex

D. Fernig, D. Legrand, C. Blanquart, 2000, Infection and Immunity.

Mycobacterial Lipomannan Induces Matrix Metalloproteinase-9 Expression in Human Macrophagic Cells through a Toll-Like Receptor 1 (TLR1)/TLR2- and CD14-Dependent Mechanism

L. Kremer, L. Aubry, D. Legrand, 2005, Infection and Immunity.

The N‐terminal domain I of human lactotransferrin binds specifically to phytohemagglutinin‐stimulated peripheral blood human lymphocyte receptors

D. Legrand, J. Montreuil, G. Spik, 1989, FEBS letters.

Lactoferrin, a key molecule in immune and inflammatory processes.

D. Legrand, 2012, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Lipomannans, But Not Lipoarabinomannans, Purified from Mycobacterium chelonae and Mycobacterium kansasii Induce TNF-α and IL-8 Secretion by a CD14-Toll-Like Receptor 2-Dependent Mechanism1

L. Kremer, D. Legrand, Y. Guérardel, 2003, The Journal of Immunology.

Secreted lactoferrin and lactoferrin-related peptides: insight into structure and biological functions.

D. Legrand, A. Pierce, J. Mazurier, 2010 .

Interactions of lactoferrin with cells involved in immune function.

D. Legrand, J. Mazurier, M. Carpentier, 2006, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Lactoferrin: a modulator of immune and inflammatory responses.

D. Legrand, M. Carpentier, E. Elass, 2005, Cellular and molecular life sciences : CMLS.

Lactoferrin Inhibits the Lipopolysaccharide-Induced Expression and Proteoglycan-Binding Ability of Interleukin-8 in Human Endothelial Cells

D. Legrand, M. Másson, J. Mazurier, 2002, Infection and Immunity.

Lactoferrin inhibits the binding of lipopolysaccharides to L‐selectin and subsequent production of reactive oxygen species by neutrophils

D. Legrand, J. Mazurier, S. Baveye, 2000, FEBS letters.

Porins OmpC and PhoE of Escherichia coli as Specific Cell-surface Targets of Human Lactoferrin

F. Pattus, V. Salmon, D. Legrand, 1999, The Journal of Biological Chemistry.

Production of human lactoferrin in transgenic tobacco plants.

V. Salmon, D. Legrand, M. Slomianny, 1998, Protein expression and purification.

Difference in Binding and Fate of Lactotransferrin in Jurkat Human Lymphoblastic T-Cells and in T-47D Human Breast Cancer Cells

D. Legrand, G. Spik, J. Mazurier, 1997 .

Processes Underlying Interactions of Human Lactoferrin with the Jurkat Human Lymphoblastic T‐cell Line Receptor. I ‐ Quantitative Structure‐Affinity Relationships Studies

D. Legrand, E. Elass-Rochard, A. Elass, 1996 .

Structural determination of two N‐linked glycans isolated from recombinant human lactoferrin expressed in BHK cells

V. Salmon, D. Legrand, B. Coddeville, 1995, FEBS letters.

Study on the binding of lactotransferrin (lactoferrin) to human PHA-activated lymphocytes and non-activated platelets. Localisation and description of the receptor-binding site.

D. Legrand, J. Montreuil, G. Spik, 1994, Advances in experimental medicine and biology.

Lactotransferrin binding to its platelet receptor inhibits platelet aggregation.

D. Legrand, J. Montreuil, G. Spik, 1993, European journal of biochemistry.

Structure and spatial conformation of the iron-binding sites of transferrins.

D. Legrand, J. Montreuil, G. Spik, 1988, Biochimie.

Role of the first N-terminal basic cluster of human lactoferrin (R2R3R4R5) in the interactions with the Jurkat human lymphoblastic T-cells.

V. Salmon, D. Legrand, M. Slomianny, 1998, Advances in experimental medicine and biology.

Nucleolin undergoes partial N- and O-glycosylations in the extranuclear cell compartment.

D. Legrand, B. Coddeville, M. Másson, 2005, Biochemistry.

Molecular interactions between human lactotransferrin and the phytohemagglutinin-activated human lymphocyte lactotransferrin receptor lie in two loop-containing regions of the N-terminal domain I of human lactotransferrin.

G. Vergoten, D. Legrand, P. Maes, 1992, Biochemistry.

Identification by surface plasmon resonance of the mycobacterial lipomannan and lipoarabinomannan domains involved in binding to CD14 and LPS‐binding protein

L. Kremer, D. Legrand, B. Coddeville, 2007, FEBS letters.

Characterization of two kinds of lactotransferrin (lactoferrin) receptors on different target cells.

D. Legrand, A. Pierce, J. Montreuil, 1994, Advances in experimental medicine and biology.

Iron acquisition by Helicobacter pylori: importance of human lactoferrin

H. Leclerc, D. Legrand, G. Spik, 1993, Infection and immunity.

Internalization of human lactoferrin by the Jurkat human lymphoblastic T-cell line.

M. Capron, A. Roche, D. Legrand, 1996, European journal of cell biology.

The binding of lactoferrin to glycosaminoglycans on enterocyte-like HT29-18-C1 cells is mediated through basic residues located in the N-terminus.

D. Legrand, M. Slomianny, G. Spik, 2001, Biochimica et biophysica acta.

The N-terminal Arg2, Arg3 and Arg4 of human lactoferrin interact with sulphated molecules but not with the receptor present on Jurkat human lymphoblastic T-cells.

V. Salmon, D. Legrand, M. Slomianny, 1997, The Biochemical journal.

Crystallization and preliminary X-ray diffraction study of Lathyrus ochrus isolectin II complexed to the human lactotransferrin N2 fragment.

C. Cambillau, P. Rougé, D. Legrand, 1992, Journal of molecular biology.

Characterization of lactotransferrin receptor in epithelial cell lines from non-malignant human breast, benign mastopathies and breast carcinomas.

R. Hamelin, M. Crépin, D. Legrand, 1992, Anticancer research.

TMEM165 deficiencies in Congenital Disorders of Glycosylation type II (CDG-II): Clues and evidences for roles of the protein in Golgi functions and ion homeostasis.

D. Legrand, F. Foulquier, Eudoxie Dulary, 2017, Tissue & cell.

SLC10A7, an orphan member of the SLC10 family involved in congenital disorders of glycosylation

D. Legrand, V. Cormier-Daire, F. Foulquier, 2022, Human genetics.

SLC10A7, an orphan member of the SLC10 family involved in congenital disorders of glycosylation

D. Legrand, V. Cormier-Daire, F. Foulquier, 2022, Human Genetics.

Lactoferrin

D. Legrand, D Legrand, E Elass, 2005, Cellular and Molecular Life Sciences.

Characterization and localization of an iron-binding 18-kDa glycopeptide isolated from the N-terminal half of humanlactotransferrin

D. Legrand, J. Montreuil, G. Spik, 1984 .

Characterization and localization of an iron-binding 18-kDa glycopeptide isolated from the N-terminal half of human lactotransferrin.

P. Jollès, D. Legrand, J. Montreuil, 1984, Biochimica et Biophysica Acta.

The cell surface expressed nucleolin is a glycoprotein that triggers calcium entry into mammalian cells.

J. Briand, D. Legrand, J. Mazurier, 2009, Experimental cell research.

Identification of a major 72 kilodalton surface antigen in twelve isolates of Leishmania braziliensis braziliensis.

A. Capron, D. Legrand, P. Desjeux, 1987, Molecular and biochemical parasitology.

Lactoferrin structure and functions.

D. Legrand, A. Pierce, J. Mazurier, 2008, Advances in experimental medicine and biology.

Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins.

F. Schoentgen, P. Jollès, D. Legrand, 1984, European journal of biochemistry.

Hepatitis C Virus NS5B and Host Cyclophilin A Share a Common Binding Site on NS5A*

J. Wieruszeski, G. Lippens, D. Legrand, 2012, The Journal of Biological Chemistry.

Surface nucleolin participates in both the binding and endocytosis of lactoferrin in target cells.

Mathieu Carpentier, J. Briand, D. Legrand, 2004, European journal of biochemistry.

Conservation of Epidermal Growth Factor Receptor Function in the Human Parasitic Helminth Schistosoma mansoni*

C. Dissous, K. Cailliau, D. Legrand, 2004, Journal of Biological Chemistry.

Advances in Lactoferrin Research

D. Sullivan, D. Legrand, A. Pierce, 1998, Advances in Experimental Medicine and Biology.

Expression of human lactotransferrin receptors in phytohemagglutinin-stimulated human peripheral blood lymphocytes. Isolation of the receptors by antiligand-affinity chromatography.

D. Legrand, J. Montreuil, G. Spik, 1989, European journal of biochemistry.

Trypanosoma cruzi: expression of antigenic component 5 among 35 laboratory clones obtained from 18 different isozymic variants.

D. Legrand, P. Desjeux, D. Afchain, 1987, Revista do Instituto de Medicina Tropical de São Paulo.

Microsoft Word-Manuscript-NS5B_rev31oct.docx

G. Lippens, D. Legrand, H. Launay, 2012 .

Hepatitis C Virus NS 5 B and Host Cyclophilin A share a common binding site on NS 5 A *

J. Wieruszeski, G. Lippens, D. Legrand, 2012 .

Spectroscopic Studies of GSK3β Phosphorylation of the Neuronal Tau Protein and Its Interaction with the N-terminal Domain of Apolipoprotein E

I. Landrieu, J. Wieruszeski, G. Lippens, 2010, The Journal of Biological Chemistry.

Differential effects of lobe A and lobe B of the Conserved Oligomeric Golgi complex on the stability of {beta}1,4-galactosyltransferase 1 and {alpha}2,6-sialyltransferase 1.

Gert Matthijs, J. Rohrer, G. Matthijs, 2011, Glycobiology.

Newly characterized Golgi-localized family of proteins is involved in calcium and pH homeostasis in yeast and human cells

G. Matthijs, E. Peiter, D. Legrand, 2013, Proceedings of the National Academy of Sciences.

TMEM165 deficiency causes a congenital disorder of glycosylation.

H. Freeze, W. Annaert, M. Vikkula, 2012, American journal of human genetics.

Advances in lactoferrin research.

D. Legrand, A. Pierce, 2009, Biochimie.

Properties of the iron-binding site of the N-terminal lobe of human and bovine lactotransferrins. Importance of the glycan moiety and of the non-covalent interactions between the N- and C-terminal lobes in the stability of the iron-binding site.

D. Colavizza, D. Legrand, J. Montreuil, 1990, The Biochemical journal.

Evidence for interactions between the 30 kDa N- and 50 kDa C-terminal tryptic fragments of human lactotransferrin.

D. Legrand, J. Montreuil, G. Spik, 1986, The Biochemical journal.

Involvement of thapsigargin– and cyclopiazonic acid–sensitive pumps in the rescue of TMEM165‐associated glycosylation defects by Mn2+

D. Legrand, B. Gasnier, F. Foulquier, 2018, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Culture of mammalian cells on patterned superhydrophilic/superhydrophobic silicon nanowire arrays

Y. Coffinier, Gaëlle Piret, R. Boukherroub, 2011 .

Impact of disease-causing mutations on TMEM165 subcellular localization, a recently identified protein involved in CDG-II.

G. Matthijs, D. Legrand, G. de Bettignies, 2013, Human molecular genetics.

Insights into the regulation of cellular Mn2+ homeostasis via TMEM165.

D. Legrand, Dorothée Vicogne, F. Foulquier, 2023, Biochimica et biophysica acta. Molecular basis of disease.

Dissection of TMEM165 function in Golgi glycosylation and its Mn2+ sensitivity.

D. Legrand, G. de Bettignies, F. Foulquier, 2019, Biochimie.

Glycosylation disorders of membrane trafficking

D. Legrand, F. Foulquier, Romain Péanne, 2012, Glycoconjugate Journal.

Metalloglycobiology: The power of metals in regulating glycosylation.

D. Legrand, F. Foulquier, Zoé Durin, 2023, Biochimica et biophysica acta. General subjects.

New insights into the pathogenicity of TMEM165 variants using structural modeling based on AlphaFold 2 predictions

M. Lensink, G. Brysbaert, M. Bardor, 2023, Computational and Structural Biotechnology Journal.