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  • image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/
    Authors: van Chuc Nguyen, ?.; Dandach, A.; Thi Thu Ha Vu, ?.; Fongarland, P.; +1 Authors

    Abstract Tungstated zirconia, ZrW, is reported as an efficient solid acid catalyst in the conversion of cellulose into lactic acid in hydrothermal conditions. The active phase of ZrW is generally ascribed to more or less polymerized WOx domains dispersed on zirconia. In this study, commercial uncalcined and calcined tungstated zirconia were used as catalysts for the conversion of cellulose under hydrothermal conditions at 190 °C. Their activities were also compared with uncalcined zirconium oxyhydroxide, ZrO2-x(OH)2x and calcined zirconia, ZrO2. Contrary to the expected results, it is disclosed that uncalcined ZrW exhibits higher catalytic activity and stability than calcined ZrW. Modifications in the products distribution were observed as glycolic acid formation at the expense of lactic acid formation upon ZrW calcination. Even more surprising, the catalytic activity of W free amorphous zirconium oxyhydroxide ZrO2-x(OH)2x is similar to uncalcined ZrW, with lactic acid as the main product while ZrO2 does not have any catalytic activity. These results suggest that the active phase of these catalysts might combine the couple Zr4+ and OH− species while the role of W species would be of secondary importance.

    image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/ Molecular Catalysisarrow_drop_down
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    image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
    Molecular Catalysis
    Article . 2019
    License: Elsevier TDM
    Data sources: Crossref
    Hal-Diderot
    Article . 2019
    License: CC BY NC
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      image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/ Molecular Catalysisarrow_drop_down
      image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/
      image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
      Molecular Catalysis
      Article . 2019
      License: Elsevier TDM
      Data sources: Crossref
      Hal-Diderot
      Article . 2019
      License: CC BY NC
      Data sources: Hal-Diderot
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  • Authors: Bataille, Sylvaine; Pauchet, Anaïs; Hatchuel, Sarah;

    Entrée sur une série "shakespearienne" dans une encyclopédie à paraître en ligne.

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  • Authors: Borrell, Alexandre; Jadot, Anne; Wojcik, Stéphanie; Lefébure, Pierre;
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  • Authors: Mottier, Hélène; Pascalis, Olivier; Méary, David;

    International audience; Adults (n = 28) were instucted to choose their preferred motion in different pairing. 56 randomized pairs were presented for 5 seconds side-by-side. The aesthetic value of each stimulus was calculated with Elo rating. Data were collected using Matlab 8.2. STIMULI RATING Intercept β0 = 6.09e+1, t(203) = 51.01, p < .001, ŋ²p = .61 Elo score β1 = 1.51e+0, t(200) = 11.95, p < .001, ŋ²p = .08 Age (in days) β2 = 3.86e-0, t(200) = 11.92, p < .001, ŋ²p = .08 Elo ranking x Age β3 = 9.30e-1, t(200) = 2.72, p < .01, ŋ²p = .01 We used Zeki and Stutters' (2012) kinetic patterns. The patterns were initially designed to produce different aesthetic judgment.

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  • image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/
    Authors: Cécile Mons; Thomas Botzanowski; Anton Nikolaev; Petra Hellwig; +4 Authors

    International audience; Human mitoNEET (mNT) is the first identified Fe−S protein of the mammalian outer mitochondrial membrane. Recently, we demonstrated the involvement of mNT in a specific cytosolic pathway dedicated to the reactivation of oxidatively damaged cytosolic aconitase by cluster transfer. In vitro studies using apo-ferredoxin (FDX) reveal that mNT uses an Fe-based redox switch mechanism to regulate the transfer of its cluster. Using the "gold standard" cluster recipient protein, FDX, we show that this transfer is direct and that only one of the two mNT clusters is transferred when the second one is decomposed. Combining complementary biophysical and biochemical approaches, we show that pH affects both the sensitivity of the cluster to O 2 and dimer stability. Around physiological cytosolic pH, the ability of mNT to transfer its cluster is tightly regulated by the pH. Finally, mNT is extremely resistant to H 2 O 2 compared to ISCU and SufB, two other Fe−S cluster transfer proteins, which is consistent with its involvement in a repair pathway of stress-damaged Fe−S proteins. Taken together, our results suggest that the ability of mNT to transfer its cluster to recipient proteins is not only controlled by the redox state of its cluster but also tightly modulated by the pH of the cytosol. We propose that when pathophysiological conditions such as cancer and neurodegenerative diseases dysregulate cellular pH homeostasis, this pH-dependent regulation of mNT is lost, as is the regulation of cellular pathways under the control of mNT. I ron−sulfur (Fe−S) clusters are evolutionarily ancient and highly conserved prosthetic cofactors. Composed of only iron and sulfur, they are involved in many essential biological processes. 1,2 MitoNEET (mNT), also known as CISD1, is the first identified Fe−S protein of the mammalian outer mitochondrial membrane (OMM). 3,4 This is a small homodimeric protein (13 kDa for each monomer) anchored to the OMM by its 32-amino acid N-terminus with the major part of the protein, including the C-terminal Fe−S binding domain, located in the cytosol. 4 Each monomer accommodates one [2Fe-2S] cluster coordinated by three cysteines (C72, C74, and C83) and one histidine (H87) in a CDGSH domain 5−8 as other members of the NEET protein family, 9 which also includes Miner1 (or CISD2) and Miner2 (or CISD3) in mammals. 10 Although the biological activity of mNT is still debated, 11 studies have shown that it is involved in the regulation of iron/reactive oxygen species homeo-stasis, 12−14 in the regulation of lipid and glucose metabolism , 13,15 and in cell proliferation in breast cancer. 16 In vitro studies revealed that holo-mNT (the form of the protein with the cluster) is able to transfer its Fe−S cluster to very diverse apoprotein (an Fe−S protein, which has lost its cluster) recipients assembling either a [2Fe-2S] cluster as ferredoxin from various organisms, 17,18 human anamorsin 19 and CISD2, 20 or a [4Fe-4S] cluster as mammalian iron regulatory protein-1 (IRP-1)/cytosolic aconitase (c-aconi-tase). 14 On the basis of in cellulo experiments, we showed that mNT is able to repair the oxidatively damaged Fe−S cluster of human IRP-1/c-aconitase by transferring its cluster to the damaged protein. 14 Recently, we started to investigate in depth the in vitro cluster transfer reaction, focusing on the transfer from holo-mNT to [2Fe-2S] recipient protein. We unambiguously demonstrated that oxidized mNT ([2Fe-2S] 2+) triggers cluster transfer, whereas reduction of its cluster abrogates this transfer. Moreover, while O 2 significantly affects the lability of the oxidized mNT cluster, it does not interfere with the cluster

    image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/ Biochemistry; Hal-Di...arrow_drop_down
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    Biochemistry
    Article . 2018
    Data sources: Crossref
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  • Authors: van de Velde, Mark, L.O.;

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  • Authors: de Fouchécour, Clotilde;

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  • Authors: Ndamé Ndangué, M.; Stouffs, P;

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  • Authors: Coomber, Charlotte; Benhamou, Laure; Bučar, Dejan-Krešimir; Smith, Peter; +2 Authors

    Herein, we report a silver-free Pd(II)-catalyzed C(sp3)–H arylation of saturated bicyclic and tricyclic amine scaffolds. The reaction provides good yields using a range of aryl iodides and aryl bromides including functionalized examples bearing aldehydes, ketones, esters, free phenols, and heterocycles. The methodology has been applied to medicinally relevant scaffolds. Two of the intermediate palladium complexes in the catalytic cycle have been prepared and characterized, and a mechanism is proposed. Removal of the directing group proceeded with good yield under relatively mild conditions.

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  • Authors: Massei-Chamayou, Marie-Laure;

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3,206,559 Research products
  • image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/
    Authors: van Chuc Nguyen, ?.; Dandach, A.; Thi Thu Ha Vu, ?.; Fongarland, P.; +1 Authors

    Abstract Tungstated zirconia, ZrW, is reported as an efficient solid acid catalyst in the conversion of cellulose into lactic acid in hydrothermal conditions. The active phase of ZrW is generally ascribed to more or less polymerized WOx domains dispersed on zirconia. In this study, commercial uncalcined and calcined tungstated zirconia were used as catalysts for the conversion of cellulose under hydrothermal conditions at 190 °C. Their activities were also compared with uncalcined zirconium oxyhydroxide, ZrO2-x(OH)2x and calcined zirconia, ZrO2. Contrary to the expected results, it is disclosed that uncalcined ZrW exhibits higher catalytic activity and stability than calcined ZrW. Modifications in the products distribution were observed as glycolic acid formation at the expense of lactic acid formation upon ZrW calcination. Even more surprising, the catalytic activity of W free amorphous zirconium oxyhydroxide ZrO2-x(OH)2x is similar to uncalcined ZrW, with lactic acid as the main product while ZrO2 does not have any catalytic activity. These results suggest that the active phase of these catalysts might combine the couple Zr4+ and OH− species while the role of W species would be of secondary importance.

    image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/ Molecular Catalysisarrow_drop_down
    image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/
    image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
    Molecular Catalysis
    Article . 2019
    License: Elsevier TDM
    Data sources: Crossref
    Hal-Diderot
    Article . 2019
    License: CC BY NC
    Data sources: Hal-Diderot
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      image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/ Molecular Catalysisarrow_drop_down
      image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/
      image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
      Molecular Catalysis
      Article . 2019
      License: Elsevier TDM
      Data sources: Crossref
      Hal-Diderot
      Article . 2019
      License: CC BY NC
      Data sources: Hal-Diderot
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  • Authors: Bataille, Sylvaine; Pauchet, Anaïs; Hatchuel, Sarah;

    Entrée sur une série "shakespearienne" dans une encyclopédie à paraître en ligne.

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  • Authors: Borrell, Alexandre; Jadot, Anne; Wojcik, Stéphanie; Lefébure, Pierre;
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  • Authors: Mottier, Hélène; Pascalis, Olivier; Méary, David;

    International audience; Adults (n = 28) were instucted to choose their preferred motion in different pairing. 56 randomized pairs were presented for 5 seconds side-by-side. The aesthetic value of each stimulus was calculated with Elo rating. Data were collected using Matlab 8.2. STIMULI RATING Intercept β0 = 6.09e+1, t(203) = 51.01, p < .001, ŋ²p = .61 Elo score β1 = 1.51e+0, t(200) = 11.95, p < .001, ŋ²p = .08 Age (in days) β2 = 3.86e-0, t(200) = 11.92, p < .001, ŋ²p = .08 Elo ranking x Age β3 = 9.30e-1, t(200) = 2.72, p < .01, ŋ²p = .01 We used Zeki and Stutters' (2012) kinetic patterns. The patterns were initially designed to produce different aesthetic judgment.

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  • image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/
    Authors: Cécile Mons; Thomas Botzanowski; Anton Nikolaev; Petra Hellwig; +4 Authors

    International audience; Human mitoNEET (mNT) is the first identified Fe−S protein of the mammalian outer mitochondrial membrane. Recently, we demonstrated the involvement of mNT in a specific cytosolic pathway dedicated to the reactivation of oxidatively damaged cytosolic aconitase by cluster transfer. In vitro studies using apo-ferredoxin (FDX) reveal that mNT uses an Fe-based redox switch mechanism to regulate the transfer of its cluster. Using the "gold standard" cluster recipient protein, FDX, we show that this transfer is direct and that only one of the two mNT clusters is transferred when the second one is decomposed. Combining complementary biophysical and biochemical approaches, we show that pH affects both the sensitivity of the cluster to O 2 and dimer stability. Around physiological cytosolic pH, the ability of mNT to transfer its cluster is tightly regulated by the pH. Finally, mNT is extremely resistant to H 2 O 2 compared to ISCU and SufB, two other Fe−S cluster transfer proteins, which is consistent with its involvement in a repair pathway of stress-damaged Fe−S proteins. Taken together, our results suggest that the ability of mNT to transfer its cluster to recipient proteins is not only controlled by the redox state of its cluster but also tightly modulated by the pH of the cytosol. We propose that when pathophysiological conditions such as cancer and neurodegenerative diseases dysregulate cellular pH homeostasis, this pH-dependent regulation of mNT is lost, as is the regulation of cellular pathways under the control of mNT. I ron−sulfur (Fe−S) clusters are evolutionarily ancient and highly conserved prosthetic cofactors. Composed of only iron and sulfur, they are involved in many essential biological processes. 1,2 MitoNEET (mNT), also known as CISD1, is the first identified Fe−S protein of the mammalian outer mitochondrial membrane (OMM). 3,4 This is a small homodimeric protein (13 kDa for each monomer) anchored to the OMM by its 32-amino acid N-terminus with the major part of the protein, including the C-terminal Fe−S binding domain, located in the cytosol. 4 Each monomer accommodates one [2Fe-2S] cluster coordinated by three cysteines (C72, C74, and C83) and one histidine (H87) in a CDGSH domain 5−8 as other members of the NEET protein family, 9 which also includes Miner1 (or CISD2) and Miner2 (or CISD3) in mammals. 10 Although the biological activity of mNT is still debated, 11 studies have shown that it is involved in the regulation of iron/reactive oxygen species homeo-stasis, 12−14 in the regulation of lipid and glucose metabolism , 13,15 and in cell proliferation in breast cancer. 16 In vitro studies revealed that holo-mNT (the form of the protein with the cluster) is able to transfer its Fe−S cluster to very diverse apoprotein (an Fe−S protein, which has lost its cluster) recipients assembling either a [2Fe-2S] cluster as ferredoxin from various organisms, 17,18 human anamorsin 19 and CISD2, 20 or a [4Fe-4S] cluster as mammalian iron regulatory protein-1 (IRP-1)/cytosolic aconitase (c-aconi-tase). 14 On the basis of in cellulo experiments, we showed that mNT is able to repair the oxidatively damaged Fe−S cluster of human IRP-1/c-aconitase by transferring its cluster to the damaged protein. 14 Recently, we started to investigate in depth the in vitro cluster transfer reaction, focusing on the transfer from holo-mNT to [2Fe-2S] recipient protein. We unambiguously demonstrated that oxidized mNT ([2Fe-2S] 2+) triggers cluster transfer, whereas reduction of its cluster abrogates this transfer. Moreover, while O 2 significantly affects the lability of the oxidized mNT cluster, it does not interfere with the cluster

    image/svg+xml art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos Open Access logo, converted into svg, designed by PLoS. This version with transparent background. http://commons.wikimedia.org/wiki/File:Open_Access_logo_PLoS_white.svg art designer at PLoS, modified by Wikipedia users Nina, Beao, JakobVoss, and AnonMoos http://www.plos.org/ Biochemistry; Hal-Di...arrow_drop_down
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    Biochemistry
    Article . 2018
    Data sources: Crossref
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  • Authors: van de Velde, Mark, L.O.;

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  • Authors: de Fouchécour, Clotilde;

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  • Authors: Ndamé Ndangué, M.; Stouffs, P;

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  • Authors: Coomber, Charlotte; Benhamou, Laure; Bučar, Dejan-Krešimir; Smith, Peter; +2 Authors

    Herein, we report a silver-free Pd(II)-catalyzed C(sp3)–H arylation of saturated bicyclic and tricyclic amine scaffolds. The reaction provides good yields using a range of aryl iodides and aryl bromides including functionalized examples bearing aldehydes, ketones, esters, free phenols, and heterocycles. The methodology has been applied to medicinally relevant scaffolds. Two of the intermediate palladium complexes in the catalytic cycle have been prepared and characterized, and a mechanism is proposed. Removal of the directing group proceeded with good yield under relatively mild conditions.

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