The Experts below are selected from a list of 261 Experts worldwide ranked by ideXlab platform
Qingmin Wang - One of the best experts on this subject based on the ideXlab platform.
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Design, synthesis, structure, and acaricidal/insecticidal activity of novel spirocyclic tetronic acid derivatives containing an Oxalyl moiety.
Journal of agricultural and food chemistry, 2011Co-Authors: Liu Zhihui, Qiong Lei, Lixia Xiong, Haibin Song, Qingmin WangAbstract:A series of novel spirocyclic tetronic acid derivatives containing an Oxalyl moiety was designed and synthesized via the key intermediate 3-(2,4,6-trimethyl)-2-oxo-1-oxaspiro[4.4]-decyl-3-en-4-ol. The target compounds were identified by (1)H NMR and elemental analysis or high-resolution mass spectrum (HRMS). The results of bioassays indicated that most of the target compounds possessed excellent acaricidal activities against carmine spider mite larvae and eggs. Especially, diisopropylamino Oxalyl compound 7g and piperidine Oxalyl compound 7h were 1.4- and 2.3-fold as high as the activities of commercial Spiromesifen, respectively, against spider mite eggs. Moreover, most of the target compounds exhibited insecticidal activities against Lepidoptera pest. Interestingly, compounds containing alkylamino-substituted Oxalyl moiety showed obvious selectivity between spider mite larvae and eggs because the activities against spider mite eggs of 7g and 7h were 25-fold those against spider mite larvae, whereas Spiromesifen had no significant differences in these activities. This meant that the introduction of an Oxalyl moiety to spirocyclic tetronic acid might lead to novel biological activity characteristics.
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design synthesis structure and acaricidal insecticidal activity of novel spirocyclic tetronic acid derivatives containing an Oxalyl moiety
Journal of Agricultural and Food Chemistry, 2011Co-Authors: Zhihui Liu, Qiong Lei, Lixia Xiong, Haibin Song, Qingmin WangAbstract:A series of novel spirocyclic tetronic acid derivatives containing an Oxalyl moiety was designed and synthesized via the key intermediate 3-(2,4,6-trimethyl)-2-oxo-1-oxaspiro[4.4]-decyl-3-en-4-ol. The target compounds were identified by (1)H NMR and elemental analysis or high-resolution mass spectrum (HRMS). The results of bioassays indicated that most of the target compounds possessed excellent acaricidal activities against carmine spider mite larvae and eggs. Especially, diisopropylamino Oxalyl compound 7g and piperidine Oxalyl compound 7h were 1.4- and 2.3-fold as high as the activities of commercial Spiromesifen, respectively, against spider mite eggs. Moreover, most of the target compounds exhibited insecticidal activities against Lepidoptera pest. Interestingly, compounds containing alkylamino-substituted Oxalyl moiety showed obvious selectivity between spider mite larvae and eggs because the activities against spider mite eggs of 7g and 7h were 25-fold those against spider mite larvae, whereas Spiromesifen had no significant differences in these activities. This meant that the introduction of an Oxalyl moiety to spirocyclic tetronic acid might lead to novel biological activity characteristics.
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Synthesis and insecticidal evaluation of novel N‐Oxalyl derivatives of diacylhydrazines containing methylcarbamate moieties
Heteroatom Chemistry, 2005Co-Authors: Chunhui Mao, Qingmin Wang, Runqiu Huang, Li Chen, Jian ShangAbstract:A series of new N-Oxalyl derivatives of diacylhydrazines containing methylcarbamate moieties were synthesized by the reaction of N-Oxalyl chloride of N-methylcarbmates with N-tert-butyl-N,N′-diacylhydrazines in the presence of sodium hydride. The reaction of Oxalyl chloride with N-tert-butyl-N, N′-diacylhydrazines to yield 1,3,4-oxadiazole and 4-tert-butyl-2-substituted-phenyl-4H-1,3,4-oxadiazine-5,6-dione was found, and the reaction was studied in some detail. The title compounds were evaluated for molting hormone mimicking activity. The results of bioassay showed that the title compounds exhibit moderate larvicidal activities, and toxicity assays indicated that these compounds can induce a premature, abnormal, and lethal larval molt. © 2005 Wiley Periodicals, Inc. Heteroatom Chem 16:472–475, 2005; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/hc.20135
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synthesis and insecticidal evaluation of novel n Oxalyl derivatives of diacylhydrazines containing methylcarbamate moieties
Heteroatom Chemistry, 2005Co-Authors: Chunhui Mao, Qingmin Wang, Runqiu Huang, Li Chen, Jian ShangAbstract:A series of new N-Oxalyl derivatives of diacylhydrazines containing methylcarbamate moieties were synthesized by the reaction of N-Oxalyl chloride of N-methylcarbmates with N-tert-butyl-N,N′-diacylhydrazines in the presence of sodium hydride. The reaction of Oxalyl chloride with N-tert-butyl-N, N′-diacylhydrazines to yield 1,3,4-oxadiazole and 4-tert-butyl-2-substituted-phenyl-4H-1,3,4-oxadiazine-5,6-dione was found, and the reaction was studied in some detail. The title compounds were evaluated for molting hormone mimicking activity. The results of bioassay showed that the title compounds exhibit moderate larvicidal activities, and toxicity assays indicated that these compounds can induce a premature, abnormal, and lethal larval molt. © 2005 Wiley Periodicals, Inc. Heteroatom Chem 16:472–475, 2005; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/hc.20135
Yingsheng Zhao - One of the best experts on this subject based on the ideXlab platform.
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Pd-Catalyzed Coupling of γ-C(sp3)–H Bonds of Oxalyl Amide-Protected Amino Acids with Heteroaryl and Aryl Iodides
The Journal of organic chemistry, 2016Co-Authors: Jian Han, Da Qing Shi, Runsheng Zeng, Yongxiang Zheng, Chao Wang, Yan Zhu, Zhi-bin Huang, Yingsheng ZhaoAbstract:Pd-catalyzed regioselective coupling of γ-C(sp3)–H bonds of Oxalyl amide-protected amino acids with heteroaryl and aryl iodides is reported. A wide variety of iodides are tolerated, giving the corresponding products in moderate to good yields. Various Oxalyl amide-protected amino acids were compatible in this C–H transformation, thus representing a practical method for constructing non-natural amino acid derivatives.
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Palladium‐Catalyzed Oxalyl Amide Directed Silylation and Germanylation of Amine Derivatives.
ChemInform, 2015Co-Authors: Changpeng Chen, Mingyu Guan, Jingyu Zhang, Zhenkang Wen, Yingsheng ZhaoAbstract:Conditions for the ortho-selective trimethylsilylation of Oxalyl amide protected benzylamine and phenylethylamine derivatives are developed which tolerate a diverse range of functional groups.
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Oxalyl amide assisted palladium catalyzed synthesis of pyrrolidones via carbonylation of γ c sp3 h bonds of aliphatic amine substrates
ChemInform, 2015Co-Authors: Chao Wang, Changpeng Chen, Jian Han, Li Zhang, Yingming Yao, Yingsheng ZhaoAbstract:The first Pd-catalyzed regioselective γ-carbonylation of Oxalyl amide protected aliphatic amines with carbon monoxide results in the formation of pyrrolidones.
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palladium catalyzed Oxalyl amide directed silylation and germanylation of amine derivatives
ChemInform, 2015Co-Authors: Changpeng Chen, Mingyu Guan, Jingyu Zhang, Zhenkang Wen, Yingsheng ZhaoAbstract:Conditions for the ortho-selective trimethylsilylation of Oxalyl amide protected benzylamine and phenylethylamine derivatives are developed which tolerate a diverse range of functional groups.
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Palladium-catalyzed Oxalyl amide assisted direct ortho-alkynylation of arylalkylamine derivatives at δ and ε positions
Chemical communications (Cambridge England), 2015Co-Authors: Mingyu Guan, Changpeng Chen, Jingyu Zhang, Runsheng Zeng, Yingsheng ZhaoAbstract:Palladium-catalyzed Oxalyl amide directed ortho-alkynylation of arylalkylamine derivatives is reported for the first time. A wide variety of β-arylethamine and γ-arylpropamine derivatives are compatible with this protocol. This method provides a general means to synthesize substituted alkynylarylalkylamine derivatives, highlighting the ability of Oxalyl amide in promoting C-H functionalization at unique δ and ε positions.
Ylva Lindqvist - One of the best experts on this subject based on the ideXlab platform.
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structural basis for activation of the thiamin diphosphate dependent enzyme Oxalyl coa decarboxylase by adenosine diphosphate
Journal of Biological Chemistry, 2005Co-Authors: Catrine L Berthold, Nigel G J Richards, Patricia Moussatche, Ylva LindqvistAbstract:Abstract Oxalyl-coenzyme A decarboxylase is a thiamin diphosphate-dependent enzyme that plays an important role in the catabolism of the highly toxic compound oxalate. We have determined the crystal structure of the enzyme from Oxalobacter formigenes from a hemihedrally twinned crystal to 1.73 A resolution and characterized the steady-state kinetic behavior of the decarboxylase. The monomer of the tetrameric enzyme consists of three α/β-type domains, commonly seen in this class of enzymes, and the thiamin diphosphate-binding site is located at the expected subunit-subunit interface between two of the domains with the cofactor bound in the conserved V-conformation. Although Oxalyl-CoA decarboxylase is structurally homologous to acetohydroxyacid synthase, a molecule of ADP is bound in a region that is cognate to the FAD-binding site observed in acetohydroxyacid synthase and presumably fulfils a similar role in stabilizing the protein structure. This difference between the two enzymes may have physiological importance since Oxalyl-CoA decarboxylation is an essential step in ATP generation in O. formigenes, and the decarboxylase activity is stimulated by exogenous ADP. Despite the significant degree of structural conservation between the two homologous enzymes and the similarity in catalytic mechanism to other thiamin diphosphate-dependent enzymes, the active site residues of Oxalyl-CoA decarboxylase are unique. A suggestion for the reaction mechanism of the enzyme is presented.
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Structural basis for activation of the thiamin diphosphate-dependent enzyme Oxalyl-CoA decarboxylase by adenosine diphosphate.
The Journal of biological chemistry, 2005Co-Authors: Catrine L Berthold, Nigel G J Richards, Patricia Moussatche, Ylva LindqvistAbstract:Oxalyl-coenzyme A decarboxylase is a thiamin diphosphate-dependent enzyme that plays an important role in the catabolism of the highly toxic compound oxalate. We have determined the crystal structure of the enzyme from Oxalobacter formigenes from a hemihedrally twinned crystal to 1.73 A resolution and characterized the steady-state kinetic behavior of the decarboxylase. The monomer of the tetrameric enzyme consists of three alpha/beta-type domains, commonly seen in this class of enzymes, and the thiamin diphosphate-binding site is located at the expected subunit-subunit interface between two of the domains with the cofactor bound in the conserved V-conformation. Although Oxalyl-CoA decarboxylase is structurally homologous to acetohydroxyacid synthase, a molecule of ADP is bound in a region that is cognate to the FAD-binding site observed in acetohydroxyacid synthase and presumably fulfils a similar role in stabilizing the protein structure. This difference between the two enzymes may have physiological importance since Oxalyl-CoA decarboxylation is an essential step in ATP generation in O. formigenes, and the decarboxylase activity is stimulated by exogenous ADP. Despite the significant degree of structural conservation between the two homologous enzymes and the similarity in catalytic mechanism to other thiamin diphosphate-dependent enzymes, the active site residues of Oxalyl-CoA decarboxylase are unique. A suggestion for the reaction mechanism of the enzyme is presented.
Nadia Soussi-yanicostas - One of the best experts on this subject based on the ideXlab platform.
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Surfen and Oxalyl surfen decrease tau hyperphosphorylation and mitigate neuron deficits in vivo in a zebrafish model of tauopathy
Translational neurodegeneration, 2018Co-Authors: Seyedeh Maryam Alavi Naini, Constantin Yanicostas, Rahma Hassan-abdi, Sébastien Blondeel, Mohamed Bennis, Ryan J. Weiss, Yitzhak Tor, Jeffrey D. Esko, Nadia Soussi-yanicostasAbstract:Tauopathies comprise a family of neurodegenerative disorders including Alzheimer's disease for which there is an urgent and unmet need for disease-modifying treatments. Tauopathies are characterized by pathological tau hyperphosphorylation, which has been shown to correlate tightly with disease progression and memory loss in patients suffering from Alzheimer's disease. We recently demonstrated an essential requirement for 3-O-sulfated heparan sulfate in pathological tau hyperphosphorylation in zebrafish, a prominent model organism for human drug discovery. Here, we investigated whether in vivo treatment with surfen or its derivatives Oxalyl surfen and hemisurfen, small molecules with heparan sulfate antagonist properties, could mitigate tau hyperphosphorylation and neuronal deficits in a zebrafish model of tauopathies. In vivo treatment of Tg[HuC::hTauP301L; DsRed] embryos for 2 days with surfen or Oxalyl surfen significantly reduced the accumulation of the pThr181 tau phospho-epitope measured by ELISA by 30% and 51%, respectively. Western blot analysis also showed a significant decrease of pThr181 and pSer396/pSer404 in embryos treated with surfen or Oxalyl surfen. Immunohistochemical analysis further confirmed that treatment with surfen or Oxalyl surfen significantly decreased the AT8 tau epitope in spinal motoneurons. In addition, in vivo treatment of Tg[HuC::hTauP301L; DsRed] embryos with surfen or Oxalyl surfen significantly rescued spinal motoneuron axon-branching defects and, as a likely consequence, the impaired stereotypical touch-evoked escape response. Importantly, treatment with hemisurfen, a surfen derivative devoid of heparan sulfate antagonist activity, does not affect tau hyperphosphorylation, nor neuronal or behavioural deficits in Tg[HuC::hTauP301L; DsRed] embryos. Our findings demonstrate for the first time that surfen, a well-tolerated molecule in clinical settings, and its derivative, Oxalyl surfen, could mitigate or delay neuronal defects in tauopathies, including Alzheimer's disease.
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Surfen and Oxalyl surfen decrease tau hyperphosphorylation and mitigate neuron deficits in vivo in a zebrafish model of tauopathy
Translational Neurodegeneration, 2018Co-Authors: Seyedeh Maryam Alavi Naini, Constantin Yanicostas, Rahma Hassan-abdi, Sébastien Blondeel, Mohamed Bennis, Ryan J. Weiss, Yitzhak Tor, Jeffrey D. Esko, Nadia Soussi-yanicostasAbstract:Background Tauopathies comprise a family of neurodegenerative disorders including Alzheimer’s disease for which there is an urgent and unmet need for disease-modifying treatments. Tauopathies are characterized by pathological tau hyperphosphorylation, which has been shown to correlate tightly with disease progression and memory loss in patients suffering from Alzheimer’s disease. We recently demonstrated an essential requirement for 3-O-sulfated heparan sulfate in pathological tau hyperphosphorylation in zebrafish, a prominent model organism for human drug discovery. Here, we investigated whether in vivo treatment with surfen or its derivatives Oxalyl surfen and hemisurfen, small molecules with heparan sulfate antagonist properties, could mitigate tau hyperphosphorylation and neuronal deficits in a zebrafish model of tauopathies. Results In vivo treatment of Tg[HuC::hTauP301L; DsRed] embryos for 2 days with surfen or Oxalyl surfen significantly reduced the accumulation of the pThr181 tau phospho-epitope measured by ELISA by 30% and 51%, respectively. Western blot analysis also showed a significant decrease of pThr181 and pSer396/pSer404 in embryos treated with surfen or Oxalyl surfen. Immunohistochemical analysis further confirmed that treatment with surfen or Oxalyl surfen significantly decreased the AT8 tau epitope in spinal motoneurons. In addition, in vivo treatment of Tg[HuC::hTauP301L; DsRed] embryos with surfen or Oxalyl surfen significantly rescued spinal motoneuron axon-branching defects and, as a likely consequence, the impaired stereotypical touch-evoked escape response. Importantly, treatment with hemisurfen, a surfen derivative devoid of heparan sulfate antagonist activity, does not affect tau hyperphosphorylation, nor neuronal or behavioural deficits in Tg[HuC::hTauP301L; DsRed] embryos. Conclusion Our findings demonstrate for the first time that surfen, a well-tolerated molecule in clinical settings, and its derivative, Oxalyl surfen, could mitigate or delay neuronal defects in tauopathies, including Alzheimer’s disease.
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Additional file 1: of Surfen and Oxalyl surfen decrease tau hyperphosphorylation and mitigate neuron deficits in vivo in a zebrafish model of tauopathy
2018Co-Authors: Seyedeh Maryam Alavi Naini, Constantin Yanicostas, Rahma Hassan-abdi, Sébastien Blondeel, Mohamed Bennis, Yitzhak Tor, Jeffrey D. Esko, Ryan Weiss, Nadia Soussi-yanicostasAbstract:Figure S1. Percentage of embryonic survival observed for 72 hpf wild-type (WT) and Tg[HuC::hTauP301L; DsRed] (non-treated) embryos incubated for 2 days in E3 medium containing 1% DMSO or E3 medium containing 1% DMSO with LiCl (10–150 mM) (a), surfen (0.1–10 μM) (b), Oxalyl surfen (0.1–10 μM) (c) or hemisurfen (0.1–10 μM) (d). Note that at the selected concentrations (80 mM LiCl, 3 μM for surfen and hemisurfen and 2 μM for Oxalyl surfen) are the maximal non-toxic concentrations (n = 250, *P
Catrine L Berthold - One of the best experts on this subject based on the ideXlab platform.
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structural basis for activation of the thiamin diphosphate dependent enzyme Oxalyl coa decarboxylase by adenosine diphosphate
Journal of Biological Chemistry, 2005Co-Authors: Catrine L Berthold, Nigel G J Richards, Patricia Moussatche, Ylva LindqvistAbstract:Abstract Oxalyl-coenzyme A decarboxylase is a thiamin diphosphate-dependent enzyme that plays an important role in the catabolism of the highly toxic compound oxalate. We have determined the crystal structure of the enzyme from Oxalobacter formigenes from a hemihedrally twinned crystal to 1.73 A resolution and characterized the steady-state kinetic behavior of the decarboxylase. The monomer of the tetrameric enzyme consists of three α/β-type domains, commonly seen in this class of enzymes, and the thiamin diphosphate-binding site is located at the expected subunit-subunit interface between two of the domains with the cofactor bound in the conserved V-conformation. Although Oxalyl-CoA decarboxylase is structurally homologous to acetohydroxyacid synthase, a molecule of ADP is bound in a region that is cognate to the FAD-binding site observed in acetohydroxyacid synthase and presumably fulfils a similar role in stabilizing the protein structure. This difference between the two enzymes may have physiological importance since Oxalyl-CoA decarboxylation is an essential step in ATP generation in O. formigenes, and the decarboxylase activity is stimulated by exogenous ADP. Despite the significant degree of structural conservation between the two homologous enzymes and the similarity in catalytic mechanism to other thiamin diphosphate-dependent enzymes, the active site residues of Oxalyl-CoA decarboxylase are unique. A suggestion for the reaction mechanism of the enzyme is presented.
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Structural basis for activation of the thiamin diphosphate-dependent enzyme Oxalyl-CoA decarboxylase by adenosine diphosphate.
The Journal of biological chemistry, 2005Co-Authors: Catrine L Berthold, Nigel G J Richards, Patricia Moussatche, Ylva LindqvistAbstract:Oxalyl-coenzyme A decarboxylase is a thiamin diphosphate-dependent enzyme that plays an important role in the catabolism of the highly toxic compound oxalate. We have determined the crystal structure of the enzyme from Oxalobacter formigenes from a hemihedrally twinned crystal to 1.73 A resolution and characterized the steady-state kinetic behavior of the decarboxylase. The monomer of the tetrameric enzyme consists of three alpha/beta-type domains, commonly seen in this class of enzymes, and the thiamin diphosphate-binding site is located at the expected subunit-subunit interface between two of the domains with the cofactor bound in the conserved V-conformation. Although Oxalyl-CoA decarboxylase is structurally homologous to acetohydroxyacid synthase, a molecule of ADP is bound in a region that is cognate to the FAD-binding site observed in acetohydroxyacid synthase and presumably fulfils a similar role in stabilizing the protein structure. This difference between the two enzymes may have physiological importance since Oxalyl-CoA decarboxylation is an essential step in ATP generation in O. formigenes, and the decarboxylase activity is stimulated by exogenous ADP. Despite the significant degree of structural conservation between the two homologous enzymes and the similarity in catalytic mechanism to other thiamin diphosphate-dependent enzymes, the active site residues of Oxalyl-CoA decarboxylase are unique. A suggestion for the reaction mechanism of the enzyme is presented.
