C
Constantin T. Craescu
Researcher at Curie Institute
Publications - 92
Citations - 2133
Constantin T. Craescu is an academic researcher from Curie Institute. The author has contributed to research in topics: Centrin & Protein structure. The author has an hindex of 26, co-authored 92 publications receiving 2016 citations. Previous affiliations of Constantin T. Craescu include École normale supérieure de Cachan & University of Paris-Sud.
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Polyoxometalate binding to human serum albumin: a thermodynamic and spectroscopic approach.
Guangjin Zhang,Bineta Keita,Constantin T. Craescu,Simona Miron,and Pedro de Oliveira,Louis Nadjo +5 more
TL;DR: The present work reveals a protein conformation change upon P5W30 binding, a new feature not explicitly documented in previous studies, which is a simple exothermic process, with several binding sites.
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Molecular interactions between Wells-Dawson type polyoxometalates and human serum albumin.
Guangjin Zhang,Bineta Keita,Constantin T. Craescu,Simona Miron,Pedro de Oliveira,Louis Nadjo +5 more
TL;DR: Comparison of the physical characteristics and HSA interaction parameters for the POMs of the present work and those studied previously showed that the overall charge of the clusters is not the single parameter governing the binding process and its consequences.
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Molecular Interaction and Energy Transfer between Human Serum Albumin and Polyoxometalates
Guangjin Zhang,Bineta Keita,Jean-Claude Brochon,Pedro de Oliveira,Louis Nadjo,Constantin T. Craescu,Simona Miron +6 more
TL;DR: Circular dichroism was used to assess the structural effects of POM binding on HSA and to confirm the interaction revealed by fluorescence studies, which showed that the two POMs have different effects on the secondary structure of the protein.
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Hemoglobin S Antilles: a variant with lower solubility than hemoglobin S and producing sickle cell disease in heterozygotes
Monplaisir N,Guy Merault,Claude Poyart,M.D. Rhoda,Constantin T. Craescu,Michel Vidaud,Frédéric Galactéros,Yves Blouquit,Jean Rosa +8 more
TL;DR: Fiber formation in the erythrocytes of Hb S Antilles carriers is clearly due to its low solubility and oxygen affinity, showing that heterozygosity for this hemoglobin presents another sickle cell syndrome and suggesting that HbS heterozygotes who exhibit symptoms of Sickle cell disease should be carefully screened for double mutations.
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Xeroderma Pigmentosum Group C Protein Possesses a High Affinity Binding Site to Human Centrin 2 and Calmodulin
A. Popescu,Simona Miron,Yves Blouquit,Patricia Duchambon,Petya Christova,Constantin T. Craescu +5 more
TL;DR: Structurally characterize the complex formed by the C-terminal domain of HsCen2 with P1-XPC, a member of the EF-hand superfamily of Ca2+-binding proteins, which interacts with different affinities and mechanisms with calmodulin.