The Experts below are selected from a list of 279 Experts worldwide ranked by ideXlab platform
Y. Blériot - One of the best experts on this subject based on the ideXlab platform.
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Synthesis of branched seven-membered 1-N-iminosugars and their evaluation as glycosidase inhibitors
Carbohydrate Research, 2012Co-Authors: Y.m. Zhang, S. Favre, P. Vogel, M. Sollogoub, Y. BlériotAbstract:Four branched tetra- and pentahydroxylated azepanes have been synthesized from a common azepane precursor through dihydroxylation followed by deoxygenation. They have been assayed as glycosidase inhibitors on a panel of 22 Glycosidases and one methylated azepane displayed selective, competitive, and moderate inhibition toward bovine kidney alpha-L-fucosidase
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Towards a stable noeuromycin analog with a D-manno configuration: Synthesis and glycosidase inhibition of D-manno-like tri- and tetrahydroxylated azepanes
Bioorganic and Medicinal Chemistry, 2012Co-Authors: J. Deschamp, Y.m. Zhang, M. Sollogoub, M. Mondon, S. Nakagawa, S. Kato, D.s. Alonzi, T.d. Butters, Y. BlériotAbstract:Noeuromycin is a highly potent albeit unstable glycosidase inhibitor due to its hemiaminal function. While stable D-gluco-like analogs have been reported, no data are available for D-manno-like structures. A series of tri- and tetrahydroxylated seven-membered iminosugars displaying either a D-manno-or a L-gulo-like configuration, were synthesized from methyl alpha-D-mannopyranoside using a reductive amination-mediated ring expansion as the key step. Screening towards a range of commercial Glycosidases demonstrated their potency as competitive glycosidase inhibitors while cellular assay showed selective albeit weak glycoprotein processing mannosidase inactivation.
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Towards a stable noeuromycin analog with a D-manno configuration: Synthesis and glycosidase inhibition of D-manno-like tri- and tetrahydroxylated azepanes
Bioorganic and Medicinal Chemistry, 2012Co-Authors: J. Deschamp, Y.m. Zhang, M. Sollogoub, M. Mondon, S. Nakagawa, D.s. Alonzi, T.d. Butters, A. Kato, Y. BlériotAbstract:Noeuromycin is a highly potent albeit unstable glycosidase inhibitor due to its hemiaminal function. While stable D-gluco-like analogs have been reported, no data are available for D-manno-like structures. A series of tri- and tetrahydroxylated seven-membered iminosugars displaying either a D-manno-or a L-gulo-like configuration, were synthesized from methyl alpha-D-mannopyranoside using a reductive amination-mediated ring expansion as the key step. Screening towards a range of commercial Glycosidases demonstrated their potency as competitive glycosidase inhibitors while cellular assay showed selective albeit weak glycoprotein processing mannosidase inactivation. (C) 2010 Elsevier Ltd. All rights reserved.
Y.m. Zhang - One of the best experts on this subject based on the ideXlab platform.
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Synthesis of branched seven-membered 1-N-iminosugars and their evaluation as glycosidase inhibitors
Carbohydrate Research, 2012Co-Authors: Y.m. Zhang, S. Favre, P. Vogel, M. Sollogoub, Y. BlériotAbstract:Four branched tetra- and pentahydroxylated azepanes have been synthesized from a common azepane precursor through dihydroxylation followed by deoxygenation. They have been assayed as glycosidase inhibitors on a panel of 22 Glycosidases and one methylated azepane displayed selective, competitive, and moderate inhibition toward bovine kidney alpha-L-fucosidase
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Towards a stable noeuromycin analog with a D-manno configuration: Synthesis and glycosidase inhibition of D-manno-like tri- and tetrahydroxylated azepanes
Bioorganic and Medicinal Chemistry, 2012Co-Authors: J. Deschamp, Y.m. Zhang, M. Sollogoub, M. Mondon, S. Nakagawa, S. Kato, D.s. Alonzi, T.d. Butters, Y. BlériotAbstract:Noeuromycin is a highly potent albeit unstable glycosidase inhibitor due to its hemiaminal function. While stable D-gluco-like analogs have been reported, no data are available for D-manno-like structures. A series of tri- and tetrahydroxylated seven-membered iminosugars displaying either a D-manno-or a L-gulo-like configuration, were synthesized from methyl alpha-D-mannopyranoside using a reductive amination-mediated ring expansion as the key step. Screening towards a range of commercial Glycosidases demonstrated their potency as competitive glycosidase inhibitors while cellular assay showed selective albeit weak glycoprotein processing mannosidase inactivation.
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Towards a stable noeuromycin analog with a D-manno configuration: Synthesis and glycosidase inhibition of D-manno-like tri- and tetrahydroxylated azepanes
Bioorganic and Medicinal Chemistry, 2012Co-Authors: J. Deschamp, Y.m. Zhang, M. Sollogoub, M. Mondon, S. Nakagawa, D.s. Alonzi, T.d. Butters, A. Kato, Y. BlériotAbstract:Noeuromycin is a highly potent albeit unstable glycosidase inhibitor due to its hemiaminal function. While stable D-gluco-like analogs have been reported, no data are available for D-manno-like structures. A series of tri- and tetrahydroxylated seven-membered iminosugars displaying either a D-manno-or a L-gulo-like configuration, were synthesized from methyl alpha-D-mannopyranoside using a reductive amination-mediated ring expansion as the key step. Screening towards a range of commercial Glycosidases demonstrated their potency as competitive glycosidase inhibitors while cellular assay showed selective albeit weak glycoprotein processing mannosidase inactivation. (C) 2010 Elsevier Ltd. All rights reserved.
Reaz Uddin - One of the best experts on this subject based on the ideXlab platform.
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Selective glycosidase inhibitors: A patent review (2012–present)
International Journal of Biological Macromolecules, 2018Co-Authors: Abdul Wadood, Mehreen Ghufran, Musharraf Jelani, Ajmal Khan, Syed Sikander Azam, Reaz UddinAbstract:Abstract In the recent decades, the interest on Glycosidases has dramatically increased, mainly because these enzymes play a vital role in many biological processes. Based on the biological potential associated to these enzymes, several glycosidase inhibitors have been developed. In this review, the most important inhibitors targeting these enzymes, including the disaccharides, iminosugars, monocyclic iminosugars, bicyclic iminosugars, thiosugars and carbasugars will be discussed and special attention will be given to the ones that are currently used clinically. This review summarizes and characterizes the current knowledge regarding the classes of glycosidase inhibitors that have therapeutic potential in a wide range of diseases. It highlights the patents, relevant research and patent applications filed in the past years in the field. Since the glycosidase inhibitors are involved in several chronic diseases and possibly pandemic, the pharmaceutical research towards developing new generations of these molecules is very important to public health. Most of the glycosidase inhibitors mimics the structures of monosaccharides or oligosaccharides and are well accepted by the organisms since they benefit from privileged drug-like properties. Disaccharides, iminosugars, carbasugars and thiosugars derivatives are the most popular inhibitors among the glycosidase inhibitors.
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Selective glycosidase inhibitors: A patent review (2012-present).
International journal of biological macromolecules, 2018Co-Authors: Abdul Wadood, Mehreen Ghufran, Musharraf Jelani, Ajmal Khan, Syed Sikander Azam, Reaz UddinAbstract:In the recent decades, the interest on Glycosidases has dramatically increased, mainly because these enzymes play a vital role in many biological processes. Based on the biological potential associated to these enzymes, several glycosidase inhibitors have been developed. In this review, the most important inhibitors targeting these enzymes, including the disaccharides, iminosugars, monocyclic iminosugars, bicyclic iminosugars, thiosugars and carbasugars will be discussed and special attention will be given to the ones that are currently used clinically. This review summarizes and characterizes the current knowledge regarding the classes of glycosidase inhibitors that have therapeutic potential in a wide range of diseases. It highlights the patents, relevant research and patent applications filed in the past years in the field. Since the glycosidase inhibitors are involved in several chronic diseases and possibly pandemic, the pharmaceutical research towards developing new generations of these molecules is very important to public health. Most of the glycosidase inhibitors mimics the structures of monosaccharides or oligosaccharides and are well accepted by the organisms since they benefit from privileged drug-like properties. Disaccharides, iminosugars, carbasugars and thiosugars derivatives are the most popular inhibitors among the glycosidase inhibitors.
M. Sollogoub - One of the best experts on this subject based on the ideXlab platform.
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Synthesis of branched seven-membered 1-N-iminosugars and their evaluation as glycosidase inhibitors
Carbohydrate Research, 2012Co-Authors: Y.m. Zhang, S. Favre, P. Vogel, M. Sollogoub, Y. BlériotAbstract:Four branched tetra- and pentahydroxylated azepanes have been synthesized from a common azepane precursor through dihydroxylation followed by deoxygenation. They have been assayed as glycosidase inhibitors on a panel of 22 Glycosidases and one methylated azepane displayed selective, competitive, and moderate inhibition toward bovine kidney alpha-L-fucosidase
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Towards a stable noeuromycin analog with a D-manno configuration: Synthesis and glycosidase inhibition of D-manno-like tri- and tetrahydroxylated azepanes
Bioorganic and Medicinal Chemistry, 2012Co-Authors: J. Deschamp, Y.m. Zhang, M. Sollogoub, M. Mondon, S. Nakagawa, S. Kato, D.s. Alonzi, T.d. Butters, Y. BlériotAbstract:Noeuromycin is a highly potent albeit unstable glycosidase inhibitor due to its hemiaminal function. While stable D-gluco-like analogs have been reported, no data are available for D-manno-like structures. A series of tri- and tetrahydroxylated seven-membered iminosugars displaying either a D-manno-or a L-gulo-like configuration, were synthesized from methyl alpha-D-mannopyranoside using a reductive amination-mediated ring expansion as the key step. Screening towards a range of commercial Glycosidases demonstrated their potency as competitive glycosidase inhibitors while cellular assay showed selective albeit weak glycoprotein processing mannosidase inactivation.
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Towards a stable noeuromycin analog with a D-manno configuration: Synthesis and glycosidase inhibition of D-manno-like tri- and tetrahydroxylated azepanes
Bioorganic and Medicinal Chemistry, 2012Co-Authors: J. Deschamp, Y.m. Zhang, M. Sollogoub, M. Mondon, S. Nakagawa, D.s. Alonzi, T.d. Butters, A. Kato, Y. BlériotAbstract:Noeuromycin is a highly potent albeit unstable glycosidase inhibitor due to its hemiaminal function. While stable D-gluco-like analogs have been reported, no data are available for D-manno-like structures. A series of tri- and tetrahydroxylated seven-membered iminosugars displaying either a D-manno-or a L-gulo-like configuration, were synthesized from methyl alpha-D-mannopyranoside using a reductive amination-mediated ring expansion as the key step. Screening towards a range of commercial Glycosidases demonstrated their potency as competitive glycosidase inhibitors while cellular assay showed selective albeit weak glycoprotein processing mannosidase inactivation. (C) 2010 Elsevier Ltd. All rights reserved.
M.e. Perotti - One of the best experts on this subject based on the ideXlab platform.
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Glycosidases are present on the surface of Drosophila melanogaster spermatozoa
Molecular Reproduction and Development, 1997Co-Authors: Fabio Cattaneo, Maria Enrica Pasini, M.e. PerottiAbstract:We investigated the presence of enzymes on the surface of Drosophila melanogaster spermatozoa that might bind to the carbohydrate residues of the egg shell. Spectrophotometric and fluorimetric studies were used on whole spermatozoa to assay galactosyltransferase and glycosidase activities. No galactosyltransferase is present on the sperm surface, whereas two Glycosidases, β-N-acetylglucosaminidase (GlcNAc'ase) and α-annosidase (Man'ase), have been evidenced. They have an optimal pH of 6-6.5 and 4, respectively. The same Glycosidases were detected as soluble forms probably secreted by the seminal vesicle epithelium. We suggest that these enzymes might be involved in the recognition of -mannose and β-N-acetylglucosamine residues present on the egg shell at the site of sperm entry.
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Glycosidases are present on the surface of Drosophila melanogaster spermatozoa.
Molecular reproduction and development, 1997Co-Authors: Fabio Cattaneo, Maria Enrica Pasini, M.e. PerottiAbstract:We investigated the presence of enzymes on the surface of Drosophila melanogaster spermatozoa that might bind the carbohydrate residues of the egg shell. Spectrophotometric and fluorimetric studies were used on whole spermatozoa to assay galactosyltransferase and glycosidase activities. No galactosyltransferase is present on the sperm surface, whereas two Glycosidases, beta-N-acetylglucosaminidase (GlcNAc'ase) and alpha-mannosidase (Man'ase), have been evidenced. They have an optimal pH of 6-6.5 and 4, respectively. The same Glycosidases were detected as soluble forms probably secreted by the seminal vesicle epithelium. We suggest that these enzymes might be involved in the recognition of alpha-mannose and beta-N-acetylglucosamine residues present on the egg shell at the site of sperm entry.