The Experts below are selected from a list of 933 Experts worldwide ranked by ideXlab platform
Mark J. Van Raaij - One of the best experts on this subject based on the ideXlab platform.
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Crystallographic structure of porcine adenovirus type 4 fiber head and galectin domains.
Journal of virology, 2010Co-Authors: Pablo Guardado-calvo, Antonio L. Llamas-saiz, Gavin C. Fox, Joel N. Glasgow, Eva Muñoz, Richard Kahn, David T. Curiel, Mark J. Van RaaijAbstract:Adenovirus isolate NADC-1, a strain of porcine adenovirus type 4, has a fiber containing an N-terminal virus attachment region, shaft and head domains, and a C-terminal galectin domain connected to the head by an RGD-containing sequence. The crystal structure of the head domain is similar to previously solved adenovirus fiber head domains, but specific residues for binding the coxsackievirus and adenovirus receptor (CAR), CD46, or sialic acid are not conserved. The structure of the galectin domain reveals an interaction interface between its two carbohydrate recognition domains, locating both sugar binding sites face to face. Sequence evidence suggests other tandem-repeat galectins have the same arrangement. We show that the galectin domain binds carbohydrates containing lactose and N-acetyl-Lactosamine units, and we present structures of the galectin domain with lactose, N-acetyl-Lactosamine, 3-aminopropyl-lacto-N-neotetraose, and 2-aminoethyl-tri(N-acetyl-Lactosamine), confirming the domain as a bona fide galectin domain.
Pablo Guardado-calvo - One of the best experts on this subject based on the ideXlab platform.
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Crystallographic structure of porcine adenovirus type 4 fiber head and galectin domains.
Journal of virology, 2010Co-Authors: Pablo Guardado-calvo, Antonio L. Llamas-saiz, Gavin C. Fox, Joel N. Glasgow, Eva Muñoz, Richard Kahn, David T. Curiel, Mark J. Van RaaijAbstract:Adenovirus isolate NADC-1, a strain of porcine adenovirus type 4, has a fiber containing an N-terminal virus attachment region, shaft and head domains, and a C-terminal galectin domain connected to the head by an RGD-containing sequence. The crystal structure of the head domain is similar to previously solved adenovirus fiber head domains, but specific residues for binding the coxsackievirus and adenovirus receptor (CAR), CD46, or sialic acid are not conserved. The structure of the galectin domain reveals an interaction interface between its two carbohydrate recognition domains, locating both sugar binding sites face to face. Sequence evidence suggests other tandem-repeat galectins have the same arrangement. We show that the galectin domain binds carbohydrates containing lactose and N-acetyl-Lactosamine units, and we present structures of the galectin domain with lactose, N-acetyl-Lactosamine, 3-aminopropyl-lacto-N-neotetraose, and 2-aminoethyl-tri(N-acetyl-Lactosamine), confirming the domain as a bona fide galectin domain.
Cyrille Grandjean - One of the best experts on this subject based on the ideXlab platform.
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biophysical and structural characterization of mono di arylated Lactosamine derivatives interaction with human galectin 3
Biochemical and Biophysical Research Communications, 2017Co-Authors: Cedric Atmanene, Celine Ronin, Stephane Teletchea, Francoismoana Gautier, Florence Djedainipilard, Fabrice Ciesielski, Valerie Vivat, Cyrille GrandjeanAbstract:Combination of biophysical and structural techniques allowed characterizing and uncovering the mechanisms underlying increased binding affinity of Lactosamine derivatives for galectin 3. In particular, complementing information gathered from X-ray crystallography, native mass spectrometry and isothermal microcalorimetry showed favorable enthalpic contribution of cation-π interaction between Lactosamine aryl substitutions and arginine residues from the carbohydrate recognition domain, which resulted in two log increase in compound binding affinity. This incrementing strategy allowed individual contribution of galectin inhibitor moieties to be dissected. Altogether, our results suggest that core and substituents of these saccharide-based inhibitors can be optimized separately, providing valuable tools to study the role of galectins in diseases.
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Lactosamine based derivatives as tools to delineate the biological functions of galectins application to skin tissue repair
ChemBioChem, 2017Co-Authors: Johann Dion, Frederique Deshayes, Nataliya Storozhylova, Tamara Advedissian, Annie Lambert, Mireille Viguier, Charles Tellier, Christophe Dussouy, Francoise Poirier, Cyrille GrandjeanAbstract:Galectins have been recognized as potential novel therapeutic targets for the numerous fundamental biological processes in which they are involved. Galectins are key players in homeostasis, and as such their expression and function are finely tuned in vivo. Thus, their modes of action are complex and remain largely unexplored, partly because of the lack of dedicated tools. We thus designed galectin inhibitors from a Lactosamine core, functionalized at key C2 and C3' positions by aromatic substituents to ensure both high affinity and selectivity, and equipped with a spacer that can be modified on demand to further modulate their physico-chemical properties. As a proof-of-concept, galectin-3 was selectively targeted. The efficacy of the synthesized di-aromatic Lactosamine tools was shown in cellular assays to modulate collective epithelial cell migration and to interfere with actin/cortactin localization.
Gavin C. Fox - One of the best experts on this subject based on the ideXlab platform.
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Crystallographic structure of porcine adenovirus type 4 fiber head and galectin domains.
Journal of virology, 2010Co-Authors: Pablo Guardado-calvo, Antonio L. Llamas-saiz, Gavin C. Fox, Joel N. Glasgow, Eva Muñoz, Richard Kahn, David T. Curiel, Mark J. Van RaaijAbstract:Adenovirus isolate NADC-1, a strain of porcine adenovirus type 4, has a fiber containing an N-terminal virus attachment region, shaft and head domains, and a C-terminal galectin domain connected to the head by an RGD-containing sequence. The crystal structure of the head domain is similar to previously solved adenovirus fiber head domains, but specific residues for binding the coxsackievirus and adenovirus receptor (CAR), CD46, or sialic acid are not conserved. The structure of the galectin domain reveals an interaction interface between its two carbohydrate recognition domains, locating both sugar binding sites face to face. Sequence evidence suggests other tandem-repeat galectins have the same arrangement. We show that the galectin domain binds carbohydrates containing lactose and N-acetyl-Lactosamine units, and we present structures of the galectin domain with lactose, N-acetyl-Lactosamine, 3-aminopropyl-lacto-N-neotetraose, and 2-aminoethyl-tri(N-acetyl-Lactosamine), confirming the domain as a bona fide galectin domain.
Joel N. Glasgow - One of the best experts on this subject based on the ideXlab platform.
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Crystallographic structure of porcine adenovirus type 4 fiber head and galectin domains.
Journal of virology, 2010Co-Authors: Pablo Guardado-calvo, Antonio L. Llamas-saiz, Gavin C. Fox, Joel N. Glasgow, Eva Muñoz, Richard Kahn, David T. Curiel, Mark J. Van RaaijAbstract:Adenovirus isolate NADC-1, a strain of porcine adenovirus type 4, has a fiber containing an N-terminal virus attachment region, shaft and head domains, and a C-terminal galectin domain connected to the head by an RGD-containing sequence. The crystal structure of the head domain is similar to previously solved adenovirus fiber head domains, but specific residues for binding the coxsackievirus and adenovirus receptor (CAR), CD46, or sialic acid are not conserved. The structure of the galectin domain reveals an interaction interface between its two carbohydrate recognition domains, locating both sugar binding sites face to face. Sequence evidence suggests other tandem-repeat galectins have the same arrangement. We show that the galectin domain binds carbohydrates containing lactose and N-acetyl-Lactosamine units, and we present structures of the galectin domain with lactose, N-acetyl-Lactosamine, 3-aminopropyl-lacto-N-neotetraose, and 2-aminoethyl-tri(N-acetyl-Lactosamine), confirming the domain as a bona fide galectin domain.
