V. Baudin-Creuza

Publications52
h-index16
Citations1,125
Highly Influential Citations30
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Biochemical Characterization and Ligand Binding Properties of Neuroglobin, a Novel Member of the Globin Family*
Neuroglobin is a recently discovered member of the globin superfamily that is suggested to enhance the O2 supply of the vertebrate brain. Spectral measurements with human and mouse recombinant… Expand
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HSP70 sequestration by free α-globin promotes ineffective erythropoiesis in β-thalassaemia
β-Thalassaemia major (β-TM) is an inherited haemoglobinopathy caused by a quantitative defect in the synthesis of β-globin chains of haemoglobin, leading to the accumulation of free α-globin chains… Expand
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α-Hemoglobin Stabilizing Protein (AHSP), a Kinetic Scheme of the Action of a Human Mutant, AHSPV56G*
A kinetic analysis has been made of the interaction of α-Hb chains with a mutant α-hemoglobin stabilizing protein, AHSPV56G, which is the first case of an AHSP mutation associated with clinical… Expand
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Unstable and Thalassemic α Chain Hemoglobin Variants: A Cause of Hb H Disease and Thalassemia Intermedia
We report an update of the α-globin gene point mutations resulting in structural modification associated with an α-thalassemia (α-thal) phenotype. These variants, barely symptomatic in the… Expand
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Neuroglobin Ligand Binding Kinetics
Neuroglobin, cytoglobin, and hemoglobins from Drosophila melanogaster and Arabidopsis thaliana were studied for their ligand binding properties versus temperature. These globins have a common feature… Expand
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High-level production of recombinant sulfide-reactive hemoglobin I from Lucina pectinata in Escherichia coli. High yields of fully functional holoprotein synthesis in the BLi5 E. coli strain.
Hemoglobin I (HbI) from Lucina pectinata is a monomeric protein composed of 143 amino acids with high sulfide affinity. Its unique heme pocket contains three residues not commonly found in vertebrate… Expand
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High-yield expression in Escherichia coli of soluble human alpha-hemoglobin complexed with its molecular chaperone.
The alpha-subunits of human hemoglobin (Hb) have been more difficult to express than beta-chains owing to the high instability of alpha-chains. Here, we describe the production in Escherichia coli of… Expand
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Transfer of Human α- to β-Hemoglobin via Its Chaperone Protein
The α-hemoglobin-stabilizing protein (AHSP), a small protein of 102 amino acids, is synthesized in red blood cell precursors. It binds specifically to α-hemoglobin (α-Hb) subunits acting as a… Expand
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Recombinant hemoglobin βG83C‐F41Y
We have engineered a stable octameric hemoglobin (Hb) of molecular mass 129 kDa, a dimer of recombinant hemoglobin (rHb βG83C‐F41Y) tetramers joined by disulfide bonds at the β83 position. One of the… Expand
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Southeast Asian ovalocytosis in White persons.
We describe two White persons, a girl and her mother, presenting with Southeast Asian ovalocytosis. The child was evaluated for scoliosis. The red cell indices were normal but the cell counter… Expand
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