The Experts below are selected from a list of 264 Experts worldwide ranked by ideXlab platform
Juan A. Hermoso - One of the best experts on this subject based on the ideXlab platform.
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Structural Basis for Selective Recognition of Endogenous and Microbial Polysaccharides by Macrophage Receptor Sign-R1
Structure (London England : 1993), 2014Co-Authors: Noella Silva-martin, Sergio G. Bartual, Erney Ramírez-aportela, Pablo Chacón, Chae Gyu Park, Juan A. HermosoAbstract:SIGN-R1 is a principal receptor for Microbial Polysaccharides uptake and is responsible for C3 fixation via an unusual complement activation pathway on splenic marginal zone macrophages. In these macrophages, SIGN-R1 is also involved in anti-inflammatory activity of intravenous immunoglobulin by direct interaction with sialylated Fcs. The high-resolution crystal structures of SIGN-R1 carbohydrate recognition domain and its complexes with dextran sulfate or sialic acid, and of the sialylated Fc antibody provide insights into SIGN-R1’s selective recognition of a-2,6-sialylated glycoproteins. Unexpectedly, an additional binding site has been found in the SIGNR1 carbohydrate recognition domain, structurally separate from the calcium-dependent carbohydrate-binding site. This secondary binding site could bind repetitive molecular patterns, as observed in Microbial Polysaccharides, in a calcium-independent manner. These two binding sites may allow SIGNR1 to simultaneously bind both immune glycoproteins and Microbial polysaccharide components, accommodating SIGN-R1’s ability to relate the recognition of microbes to the activation of the classical complement pathway.
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crystallization and preliminary x ray diffraction studies of the carbohydrate recognition domain of sign r1 a receptor for Microbial Polysaccharides and sialylated antibody on splenic marginal zone macrophages
Acta Crystallographica Section F-structural Biology and Crystallization Communications, 2009Co-Authors: Noella Silvamartin, Chae Gyu Park, Joseph D Schauer, Juan A. HermosoAbstract:SIGN-R1, or CD209b, is a mouse C-type lectin receptor that is expressed at high levels on macrophages in lymphoid tissues, especially within the marginal zone of the spleen. SIGN-R1 can bind and mediate the uptake of various Microbial Polysaccharides, including dextrans, lipoPolysaccharides and pneumococcal capsular Polysaccharides. It has been shown that SIGN-R1 mediates the clearance of encapsulated pneumococcus, complement fixation via binding C1q independent of antibody and innate resistance to pneumococcal infection. Recently, SIGN-R1 has also been demonstrated to bind sialylated antibody and mediate its activity to suppress autoimmunity. The carbohydrate-recognition domain (CRD) of SIGN-R1 has been cloned and overexpressed in a soluble secretory form in mammalian Chinese hamster ovary (CHO) cells. The CRD protein of SIGN-R1 was purified from CHO cell-culture supernatant and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of 2 M ammonium sulfate in 0.1 M bis-tris pH 5.5. Single crystals, which belonged to the monoclinic space group C2 with unit-cell parameters a = 146.72, b = 92.77, c = 77.06 A, β = 121.66°, allowed the collection of a full X-ray data set to a maximum resolution of 1.87 A.
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Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for Microbial Polysaccharides and sialylated antibody on splenic marginal zone macrophages.
Acta crystallographica. Section F Structural biology and crystallization communications, 2009Co-Authors: Noella Silva-martin, Chae Gyu Park, Joseph D Schauer, Juan A. HermosoAbstract:SIGN-R1, or CD209b, is a mouse C-type lectin receptor that is expressed at high levels on macrophages in lymphoid tissues, especially within the marginal zone of the spleen. SIGN-R1 can bind and mediate the uptake of various Microbial Polysaccharides, including dextrans, lipoPolysaccharides and pneumococcal capsular Polysaccharides. It has been shown that SIGN-R1 mediates the clearance of encapsulated pneumococcus, complement fixation via binding C1q independent of antibody and innate resistance to pneumococcal infection. Recently, SIGN-R1 has also been demonstrated to bind sialylated antibody and mediate its activity to suppress autoimmunity. The carbohydrate-recognition domain (CRD) of SIGN-R1 has been cloned and overexpressed in a soluble secretory form in mammalian Chinese hamster ovary (CHO) cells. The CRD protein of SIGN-R1 was purified from CHO cell-culture supernatant and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of 2 M ammonium sulfate in 0.1 M bis-tris pH 5.5. Single crystals, which belonged to the monoclinic space group C2 with unit-cell parameters a = 146.72, b = 92.77, c = 77.06 A, beta = 121.66 degrees , allowed the collection of a full X-ray data set to a maximum resolution of 1.87 A.
Chae Gyu Park - One of the best experts on this subject based on the ideXlab platform.
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Structural Basis for Selective Recognition of Endogenous and Microbial Polysaccharides by Macrophage Receptor Sign-R1
Structure (London England : 1993), 2014Co-Authors: Noella Silva-martin, Sergio G. Bartual, Erney Ramírez-aportela, Pablo Chacón, Chae Gyu Park, Juan A. HermosoAbstract:SIGN-R1 is a principal receptor for Microbial Polysaccharides uptake and is responsible for C3 fixation via an unusual complement activation pathway on splenic marginal zone macrophages. In these macrophages, SIGN-R1 is also involved in anti-inflammatory activity of intravenous immunoglobulin by direct interaction with sialylated Fcs. The high-resolution crystal structures of SIGN-R1 carbohydrate recognition domain and its complexes with dextran sulfate or sialic acid, and of the sialylated Fc antibody provide insights into SIGN-R1’s selective recognition of a-2,6-sialylated glycoproteins. Unexpectedly, an additional binding site has been found in the SIGNR1 carbohydrate recognition domain, structurally separate from the calcium-dependent carbohydrate-binding site. This secondary binding site could bind repetitive molecular patterns, as observed in Microbial Polysaccharides, in a calcium-independent manner. These two binding sites may allow SIGNR1 to simultaneously bind both immune glycoproteins and Microbial polysaccharide components, accommodating SIGN-R1’s ability to relate the recognition of microbes to the activation of the classical complement pathway.
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crystallization and preliminary x ray diffraction studies of the carbohydrate recognition domain of sign r1 a receptor for Microbial Polysaccharides and sialylated antibody on splenic marginal zone macrophages
Acta Crystallographica Section F-structural Biology and Crystallization Communications, 2009Co-Authors: Noella Silvamartin, Chae Gyu Park, Joseph D Schauer, Juan A. HermosoAbstract:SIGN-R1, or CD209b, is a mouse C-type lectin receptor that is expressed at high levels on macrophages in lymphoid tissues, especially within the marginal zone of the spleen. SIGN-R1 can bind and mediate the uptake of various Microbial Polysaccharides, including dextrans, lipoPolysaccharides and pneumococcal capsular Polysaccharides. It has been shown that SIGN-R1 mediates the clearance of encapsulated pneumococcus, complement fixation via binding C1q independent of antibody and innate resistance to pneumococcal infection. Recently, SIGN-R1 has also been demonstrated to bind sialylated antibody and mediate its activity to suppress autoimmunity. The carbohydrate-recognition domain (CRD) of SIGN-R1 has been cloned and overexpressed in a soluble secretory form in mammalian Chinese hamster ovary (CHO) cells. The CRD protein of SIGN-R1 was purified from CHO cell-culture supernatant and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of 2 M ammonium sulfate in 0.1 M bis-tris pH 5.5. Single crystals, which belonged to the monoclinic space group C2 with unit-cell parameters a = 146.72, b = 92.77, c = 77.06 A, β = 121.66°, allowed the collection of a full X-ray data set to a maximum resolution of 1.87 A.
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Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for Microbial Polysaccharides and sialylated antibody on splenic marginal zone macrophages.
Acta crystallographica. Section F Structural biology and crystallization communications, 2009Co-Authors: Noella Silva-martin, Chae Gyu Park, Joseph D Schauer, Juan A. HermosoAbstract:SIGN-R1, or CD209b, is a mouse C-type lectin receptor that is expressed at high levels on macrophages in lymphoid tissues, especially within the marginal zone of the spleen. SIGN-R1 can bind and mediate the uptake of various Microbial Polysaccharides, including dextrans, lipoPolysaccharides and pneumococcal capsular Polysaccharides. It has been shown that SIGN-R1 mediates the clearance of encapsulated pneumococcus, complement fixation via binding C1q independent of antibody and innate resistance to pneumococcal infection. Recently, SIGN-R1 has also been demonstrated to bind sialylated antibody and mediate its activity to suppress autoimmunity. The carbohydrate-recognition domain (CRD) of SIGN-R1 has been cloned and overexpressed in a soluble secretory form in mammalian Chinese hamster ovary (CHO) cells. The CRD protein of SIGN-R1 was purified from CHO cell-culture supernatant and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of 2 M ammonium sulfate in 0.1 M bis-tris pH 5.5. Single crystals, which belonged to the monoclinic space group C2 with unit-cell parameters a = 146.72, b = 92.77, c = 77.06 A, beta = 121.66 degrees , allowed the collection of a full X-ray data set to a maximum resolution of 1.87 A.
Noella Silva-martin - One of the best experts on this subject based on the ideXlab platform.
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Structural Basis for Selective Recognition of Endogenous and Microbial Polysaccharides by Macrophage Receptor Sign-R1
Structure (London England : 1993), 2014Co-Authors: Noella Silva-martin, Sergio G. Bartual, Erney Ramírez-aportela, Pablo Chacón, Chae Gyu Park, Juan A. HermosoAbstract:SIGN-R1 is a principal receptor for Microbial Polysaccharides uptake and is responsible for C3 fixation via an unusual complement activation pathway on splenic marginal zone macrophages. In these macrophages, SIGN-R1 is also involved in anti-inflammatory activity of intravenous immunoglobulin by direct interaction with sialylated Fcs. The high-resolution crystal structures of SIGN-R1 carbohydrate recognition domain and its complexes with dextran sulfate or sialic acid, and of the sialylated Fc antibody provide insights into SIGN-R1’s selective recognition of a-2,6-sialylated glycoproteins. Unexpectedly, an additional binding site has been found in the SIGNR1 carbohydrate recognition domain, structurally separate from the calcium-dependent carbohydrate-binding site. This secondary binding site could bind repetitive molecular patterns, as observed in Microbial Polysaccharides, in a calcium-independent manner. These two binding sites may allow SIGNR1 to simultaneously bind both immune glycoproteins and Microbial polysaccharide components, accommodating SIGN-R1’s ability to relate the recognition of microbes to the activation of the classical complement pathway.
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Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for Microbial Polysaccharides and sialylated antibody on splenic marginal zone macrophages.
Acta crystallographica. Section F Structural biology and crystallization communications, 2009Co-Authors: Noella Silva-martin, Chae Gyu Park, Joseph D Schauer, Juan A. HermosoAbstract:SIGN-R1, or CD209b, is a mouse C-type lectin receptor that is expressed at high levels on macrophages in lymphoid tissues, especially within the marginal zone of the spleen. SIGN-R1 can bind and mediate the uptake of various Microbial Polysaccharides, including dextrans, lipoPolysaccharides and pneumococcal capsular Polysaccharides. It has been shown that SIGN-R1 mediates the clearance of encapsulated pneumococcus, complement fixation via binding C1q independent of antibody and innate resistance to pneumococcal infection. Recently, SIGN-R1 has also been demonstrated to bind sialylated antibody and mediate its activity to suppress autoimmunity. The carbohydrate-recognition domain (CRD) of SIGN-R1 has been cloned and overexpressed in a soluble secretory form in mammalian Chinese hamster ovary (CHO) cells. The CRD protein of SIGN-R1 was purified from CHO cell-culture supernatant and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of 2 M ammonium sulfate in 0.1 M bis-tris pH 5.5. Single crystals, which belonged to the monoclinic space group C2 with unit-cell parameters a = 146.72, b = 92.77, c = 77.06 A, beta = 121.66 degrees , allowed the collection of a full X-ray data set to a maximum resolution of 1.87 A.
Luciano Navarini - One of the best experts on this subject based on the ideXlab platform.
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Supramolecular structure of Microbial Polysaccharides in solution: from chain conformation to rheological properties☆
Polymer, 2003Co-Authors: Attilio Cesaro, Amelia Gamini, Luciano NavariniAbstract:Abstract Literature data and unpublished results have been used to correlate the primary and secondary structures of gellan, welan, rhamsan, succinoglycan and galactoglucan in solution with their rheological properties. In dilute solution the chain conformation ranges from that of the random coil of galactoglucan to that of the stiffer double helix of gellan, and possibly a similar conformation exists for welan and rhamsan. In semidilute solution the rheological behaviour of the above Microbial Polysaccharides is mainly determined by their conformation in solution. Ordered regions along the polysaccharide chains seem to be the prerequisite to establish intermolecular interactions which lead to non-transient polymer networks. The lack of ordered secondary structure leads to entangled networks in which the topological constraints govern the rheological behaviour. Experimental evidence is reported to support the hypothesis that the chain conformation and rigidity can be qualitatively predicted on the basis of rheological measurements.
Joseph D Schauer - One of the best experts on this subject based on the ideXlab platform.
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crystallization and preliminary x ray diffraction studies of the carbohydrate recognition domain of sign r1 a receptor for Microbial Polysaccharides and sialylated antibody on splenic marginal zone macrophages
Acta Crystallographica Section F-structural Biology and Crystallization Communications, 2009Co-Authors: Noella Silvamartin, Chae Gyu Park, Joseph D Schauer, Juan A. HermosoAbstract:SIGN-R1, or CD209b, is a mouse C-type lectin receptor that is expressed at high levels on macrophages in lymphoid tissues, especially within the marginal zone of the spleen. SIGN-R1 can bind and mediate the uptake of various Microbial Polysaccharides, including dextrans, lipoPolysaccharides and pneumococcal capsular Polysaccharides. It has been shown that SIGN-R1 mediates the clearance of encapsulated pneumococcus, complement fixation via binding C1q independent of antibody and innate resistance to pneumococcal infection. Recently, SIGN-R1 has also been demonstrated to bind sialylated antibody and mediate its activity to suppress autoimmunity. The carbohydrate-recognition domain (CRD) of SIGN-R1 has been cloned and overexpressed in a soluble secretory form in mammalian Chinese hamster ovary (CHO) cells. The CRD protein of SIGN-R1 was purified from CHO cell-culture supernatant and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of 2 M ammonium sulfate in 0.1 M bis-tris pH 5.5. Single crystals, which belonged to the monoclinic space group C2 with unit-cell parameters a = 146.72, b = 92.77, c = 77.06 A, β = 121.66°, allowed the collection of a full X-ray data set to a maximum resolution of 1.87 A.
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Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for Microbial Polysaccharides and sialylated antibody on splenic marginal zone macrophages.
Acta crystallographica. Section F Structural biology and crystallization communications, 2009Co-Authors: Noella Silva-martin, Chae Gyu Park, Joseph D Schauer, Juan A. HermosoAbstract:SIGN-R1, or CD209b, is a mouse C-type lectin receptor that is expressed at high levels on macrophages in lymphoid tissues, especially within the marginal zone of the spleen. SIGN-R1 can bind and mediate the uptake of various Microbial Polysaccharides, including dextrans, lipoPolysaccharides and pneumococcal capsular Polysaccharides. It has been shown that SIGN-R1 mediates the clearance of encapsulated pneumococcus, complement fixation via binding C1q independent of antibody and innate resistance to pneumococcal infection. Recently, SIGN-R1 has also been demonstrated to bind sialylated antibody and mediate its activity to suppress autoimmunity. The carbohydrate-recognition domain (CRD) of SIGN-R1 has been cloned and overexpressed in a soluble secretory form in mammalian Chinese hamster ovary (CHO) cells. The CRD protein of SIGN-R1 was purified from CHO cell-culture supernatant and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of 2 M ammonium sulfate in 0.1 M bis-tris pH 5.5. Single crystals, which belonged to the monoclinic space group C2 with unit-cell parameters a = 146.72, b = 92.77, c = 77.06 A, beta = 121.66 degrees , allowed the collection of a full X-ray data set to a maximum resolution of 1.87 A.