The Experts below are selected from a list of 63 Experts worldwide ranked by ideXlab platform
Ramón J. Estévez - One of the best experts on this subject based on the ideXlab platform.
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Chain-Branched Polyhydroxylated Octahydro-1H-Indoles as Potential Leads against Lysosomal Storage Diseases
MDPI AG, 2019Co-Authors: Juan C. Estévez, Marcos A. González, Carmen M. Villaverde, Yuki Hirokami, Atsushi Kato, Fredy Sussman, David Reza, Ramón J. EstévezAbstract:Here, the synthesis and glycosidase inhibition properties of the two first known 3-ethyloctahydro-1H-indole-4,5,6-triols are reported. This study shows the transformation of d-glucose into polyhydroxylated 1-(2-nitrocyclohexane) acetaldehydes, followed by a protocol involving the formation of the azacyclopentane ring. Results of inhibitory potency assays and docking calculations show that at least one of them could be a lead for optimization in the search for compounds that behave like folding chaperones in lysosomal storage diseases
Estévez Cabanas, Ramón José - One of the best experts on this subject based on the ideXlab platform.
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Chain-branched polyhydroxylated Octahydro-1H-Indoles as potential leads against lysosomal storage diseases
'MDPI AG', 2019Co-Authors: Estévez Cabanas, Juan Carlos, González, Marcos A., Villaverde Cameron-walker, María Del Carmen, Hirokami Yuki, Kato Atsushi, Sussman, Fredy Salomon, Reza Ramos David, Estévez Cabanas, Ramón JoséAbstract:Here, the synthesis and glycosidase inhibition properties of the two first known 3-ethyloctahydro-1H-indole-4,5,6-triols are reported. This study shows the transformation of d-glucose into polyhydroxylated 1-(2-nitrocyclohexane) acetaldehydes, followed by a protocol involving the formation of the azacyclopentane ring. Results of inhibitory potency assays and docking calculations show that at least one of them could be a lead for optimization in the search for compounds that behave like folding chaperones in lysosomal storage diseasesThis work has received financial support from the Spanish Ministry of Science and Innovation (CTQ2009-08490), the Xunta de Galicia (Centro Singular de Investigación de Galicia, accreditation 2016–2019, ED431B 2018/13; Project CN2011/037 and Project GRC2014/040), and the European Union (European Regional Development Fund-ERDF). It has also received a Grant-in-Aid for Scientific Research (C) from the Japanese Society for the Promotion of Science (JSPS KAKENHI Grant Number JP17K08362) (AK)S
Gill Stephens - One of the best experts on this subject based on the ideXlab platform.
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structure based insight into the asymmetric bioreduction of the c c double bond of alpha beta unsaturated nitroalkenes by pentaerythritol tetranitrate reductase
Advanced Synthesis & Catalysis, 2008Co-Authors: Helen S Toogood, Anna Fryszkowska, John M Gardiner, Victoria Hare, Karl Fisher, Anna Roujeinikova, David Leys, Gill StephensAbstract:Biocatalytic reduction of alpha- or beta-alkyl-beta-arylnitroalkenes provides a convenient and efficient method to prepare chiral substituted nitroalkanes. Pentaerythritol tetranitrate reductase (PETN reductase) from Enterobacter cloacae st. PB2 catalyses the reduction of nitroolefins such as 1-Nitrocyclohexene (1) with steady state and rapid reaction kinetics comparable to other old yellow enzyme homologues. Furthermore, it reduces 2-aryl-1-nitropropenes (4a-d) to their equivalent (S)-nitropropanes 9a-d. The enzyme shows a preference for the (Z)-isomer of substrates 4a-d, providing almost pure enantiomeric products 9a-d (ees up to>99%) in quantitative yield, whereas the respective (E)-isomers are reduced with lower enantioselectivity (63-89% ee) and lower product yields. 1-Aryl-2-nitropropenes (5a, b) are also reduced efficiently, but the products (R)-10 have lower optical purities. The structure of the enzyme complex with 1-Nitrocyclohexene (1) was determined by X-ray crystallography, revealing two substrate-binding modes, with only one compatible with hydride transfer. Models of nitropropenes 4 and 5 in the active site of PETN reductase predicted that the enantioselectivity of the reaction was dependent on the orientation of binding of the (E)- and (Z)-substrates. This work provides a structural basis for understanding the mechanism of asymmetric bioreduction of nitroalkenes by PETN reductase.
Juan C. Estévez - One of the best experts on this subject based on the ideXlab platform.
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Chain-Branched Polyhydroxylated Octahydro-1H-Indoles as Potential Leads against Lysosomal Storage Diseases
MDPI AG, 2019Co-Authors: Juan C. Estévez, Marcos A. González, Carmen M. Villaverde, Yuki Hirokami, Atsushi Kato, Fredy Sussman, David Reza, Ramón J. EstévezAbstract:Here, the synthesis and glycosidase inhibition properties of the two first known 3-ethyloctahydro-1H-indole-4,5,6-triols are reported. This study shows the transformation of d-glucose into polyhydroxylated 1-(2-nitrocyclohexane) acetaldehydes, followed by a protocol involving the formation of the azacyclopentane ring. Results of inhibitory potency assays and docking calculations show that at least one of them could be a lead for optimization in the search for compounds that behave like folding chaperones in lysosomal storage diseases
Estévez Cabanas, Juan Carlos - One of the best experts on this subject based on the ideXlab platform.
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Chain-branched polyhydroxylated Octahydro-1H-Indoles as potential leads against lysosomal storage diseases
'MDPI AG', 2019Co-Authors: Estévez Cabanas, Juan Carlos, González, Marcos A., Villaverde Cameron-walker, María Del Carmen, Hirokami Yuki, Kato Atsushi, Sussman, Fredy Salomon, Reza Ramos David, Estévez Cabanas, Ramón JoséAbstract:Here, the synthesis and glycosidase inhibition properties of the two first known 3-ethyloctahydro-1H-indole-4,5,6-triols are reported. This study shows the transformation of d-glucose into polyhydroxylated 1-(2-nitrocyclohexane) acetaldehydes, followed by a protocol involving the formation of the azacyclopentane ring. Results of inhibitory potency assays and docking calculations show that at least one of them could be a lead for optimization in the search for compounds that behave like folding chaperones in lysosomal storage diseasesThis work has received financial support from the Spanish Ministry of Science and Innovation (CTQ2009-08490), the Xunta de Galicia (Centro Singular de Investigación de Galicia, accreditation 2016–2019, ED431B 2018/13; Project CN2011/037 and Project GRC2014/040), and the European Union (European Regional Development Fund-ERDF). It has also received a Grant-in-Aid for Scientific Research (C) from the Japanese Society for the Promotion of Science (JSPS KAKENHI Grant Number JP17K08362) (AK)S
