Kosuke Ohsawa (22 results)

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  • Language: English

    Published by Springer, 2015

    4431554467 / 9784431554462

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    Seller: Ria Christie Collections, Uxbridge, United KingdomRia Christie Collections

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  • Language: English

    Published by Springer Japan, 2016

    4431562877 / 9784431562870

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  • Language: English

    Published by Springer Japan, 2015

    4431554467 / 9784431554462

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  • Language: English

    Published by Springer, 2015

    4431554467 / 9784431554462

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    Condition: New. 109.

  • Language: English

    Published by Springer, 2015

    4431554467 / 9784431554462

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    Seller: AHA-BUCH GmbH, Einbeck, GermanyAHA-BUCH GmbH

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    Buch. Condition: Neu. Druck auf Anfrage Neuware - Printed after ordering - This book focuses on thielocin B1 (TB1), which was found to be an inhibitor of protein-protein interactions (PPIs) of proteasome assembling chaperone (PAC) 3 homodimer, and elucidates the mechanism by nuclear magnetic resonance (NMR) studies. Interfaces of PPIs recently have been expected to be novel therapeutic targets, while it is difficult to apply conventional methodology based on lock and key theory. The author achieved the first total synthesis of TB1 and its spin-labeled derivative to carry out NMR experiments because the supply of TB1 from natural sources was limited. Unique 2,2',6,6'-tetrasubstituted diphenyl ether moiety of TB1 was synthesized from a depsidone skeleton by chemoselective reduction of lactone. In the process of elongating side wings, efficient formylation utilizing dichloromethyl methyl ether-silver trifluoromethanesulfonate was developed for the sterically hindered aromatic compound. NMR titration experiments and paramagnetic relaxation enhancement observation of PAC3 homodimer were performed with synthesized TB1 and its molecular probe, respectively. The results of the above NMR studies and additional in silico docking studies suggested that TB1 promotes the dissociation to monomeric PAC3 after interaction with PAC3 homodimer. The rare mechanism shown in this book indicates a potential novel drug target in the interfaces of PPIs with no cavity or groove.…

  • Language: English

    Published by Springer, 2016

    4431562877 / 9784431562870

    • Softcover

    Seller: AHA-BUCH GmbH, Einbeck, GermanyAHA-BUCH GmbH

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    Taschenbuch. Condition: Neu. Druck auf Anfrage Neuware - Printed after ordering - This book focuses on thielocin B1 (TB1), which was found to be an inhibitor of protein-protein interactions (PPIs) of proteasome assembling chaperone (PAC) 3 homodimer, and elucidates the mechanism by nuclear magnetic resonance (NMR) studies. Interfaces of PPIs recently have been expected to be novel therapeutic targets, while it is difficult to apply conventional methodology based on lock and key theory. The author achieved the first total synthesis of TB1 and its spin-labeled derivative to carry out NMR experiments because the supply of TB1 from natural sources was limited. Unique 2,2',6,6'-tetrasubstituted diphenyl ether moiety of TB1 was synthesized from a depsidone skeleton by chemoselective reduction of lactone. In the process of elongating side wings, efficient formylation utilizing dichloromethyl methyl ether-silver trifluoromethanesulfonate was developed for the sterically hindered aromatic compound. NMR titration experiments and paramagnetic relaxation enhancement observation of PAC3 homodimer were performed with synthesized TB1 and its molecular probe, respectively. The results of the above NMR studies and additional in silico docking studies suggested that TB1 promotes the dissociation to monomeric PAC3 after interaction with PAC3 homodimer. The rare mechanism shown in this book indicates a potential novel drug target in the interfaces of PPIs with no cavity or groove.…

  • Language: English

    Published by Springer, 2015

    4431554467 / 9784431554462

    • Hardcover

    Seller: Revaluation Books, Exeter, United KingdomRevaluation Books

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  • Language: English

    Published by Springer, 2016

    4431562877 / 9784431562870

    • Softcover

    Seller: preigu, Osnabrück, Germanypreigu

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    Taschenbuch. Condition: Neu. Total Synthesis of Thielocin B1 as a Protein-Protein Interaction Inhibitor of PAC3 Homodimer | Kosuke Ohsawa | Taschenbuch | Springer Theses | xiii | Englisch | 2016 | Springer | EAN 9784431562870 | Verantwortliche Person für die EU: Springer Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu. …

  • Language: English

    Published by Springer Japan, 2015

    4431554467 / 9784431554462

    • Hardcover

    Seller: Buchpark, Trebbin, GermanyBuchpark

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    Condition: Sehr gut. Zustand: Sehr gut | Sprache: Englisch | Produktart: Bücher | This book focuses on thielocin B1 (TB1), which was found to be an inhibitor of protein¿protein interactions (PPIs) of proteasome assembling chaperone (PAC) 3 homodimer, and elucidates the mechanism by nuclear magnetic resonance (NMR) studies. Interfaces of PPIs recently have been expected to be novel therapeutic targets, while it is difficult to apply conventional methodology based on lock and key theory. The author achieved the first total synthesis of TB1 and its spin-labeled derivative to carry out NMR experiments because the supply of TB1 from natural sources was limited. Unique 2,2¿,6,6¿-tetrasubstituted diphenyl ether moiety of TB1 was synthesized from a depsidone skeleton by chemoselective reduction of lactone. In the process of elongating side wings, efficient formylation utilizing dichloromethyl methyl ether¿silver trifluoromethanesulfonate was developed for the sterically hindered aromatic compound. NMR titration experiments and paramagnetic relaxation enhancement observation of PAC3 homodimer were performed with synthesized TB1 and its molecular probe, respectively. The results of the above NMR studies and additional in silico docking studies suggested that TB1 promotes the dissociation to monomeric PAC3 after interaction with PAC3 homodimer. The rare mechanism shown in this book indicates a potential novel drug target in the interfaces of PPIs with no cavity or groove.…

  • Language: English

    Published by Springer, 2016

    4431562877 / 9784431562870

    • Softcover

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    Condition: New. pp. 109.

  • Language: English

    Published by Springer, 2016

    4431562877 / 9784431562870

    • Softcover

    Seller: Revaluation Books, Exeter, United KingdomRevaluation Books

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    Paperback. Condition: Brand New. reprint edition. 124 pages. 9.25x6.10x0.30 inches. In Stock.

  • Language: English

    Published by Springer, 2016

    4431562877 / 9784431562870

    • Softcover

    Seller: Mispah books, Redhill, SURRE, United KingdomMispah books

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  • Language: English

    Published by Springer, 2015

    4431554467 / 9784431554462

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    Seller: Brook Bookstore On Demand, Napoli, NA, ItalyBrook Bookstore On Demand

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  • Language: English

    Published by Springer, 2016

    4431562877 / 9784431562870

    • Softcover
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  • Language: English

    Published by Springer Japan Okt 2016, 2016

    4431562877 / 9784431562870

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    Seller: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, GermanyBuchWeltWeit Ludwig Meier e.K.

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    Taschenbuch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -This book focuses on thielocin B1 (TB1), which was found to be an inhibitor of protein-protein interactions (PPIs) of proteasome assembling chaperone (PAC) 3 homodimer, and elucidates the mechanism by nuclear magnetic resonance (NMR) studies. Interfaces of PPIs recently have been expected to be novel therapeutic targets, while it is difficult to apply conventional methodology based on lock and key theory. The author achieved the first total synthesis of TB1 and its spin-labeled derivative to carry out NMR experiments because the supply of TB1 from natural sources was limited. Unique 2,2',6,6'-tetrasubstituted diphenyl ether moiety of TB1 was synthesized from a depsidone skeleton by chemoselective reduction of lactone. In the process of elongating side wings, efficient formylation utilizing dichloromethyl methyl ether-silver trifluoromethanesulfonate was developed for the sterically hindered aromatic compound. NMR titration experiments and paramagnetic relaxation enhancement observation of PAC3 homodimer were performed with synthesized TB1 and its molecular probe, respectively. The results of the above NMR studies and additional in silico docking studies suggested that TB1 promotes the dissociation to monomeric PAC3 after interaction with PAC3 homodimer. The rare mechanism shown in this book indicates a potential novel drug target in the interfaces of PPIs with no cavity or groove. 124 pp. Englisch.…

  • Language: English

    Published by Springer Japan Jan 2015, 2015

    4431554467 / 9784431554462

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    Seller: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, GermanyBuchWeltWeit Ludwig Meier e.K.

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    Buch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -This book focuses on thielocin B1 (TB1), which was found to be an inhibitor of protein-protein interactions (PPIs) of proteasome assembling chaperone (PAC) 3 homodimer, and elucidates the mechanism by nuclear magnetic resonance (NMR) studies. Interfaces of PPIs recently have been expected to be novel therapeutic targets, while it is difficult to apply conventional methodology based on lock and key theory. The author achieved the first total synthesis of TB1 and its spin-labeled derivative to carry out NMR experiments because the supply of TB1 from natural sources was limited. Unique 2,2',6,6'-tetrasubstituted diphenyl ether moiety of TB1 was synthesized from a depsidone skeleton by chemoselective reduction of lactone. In the process of elongating side wings, efficient formylation utilizing dichloromethyl methyl ether-silver trifluoromethanesulfonate was developed for the sterically hindered aromatic compound. NMR titration experiments and paramagnetic relaxation enhancement observation of PAC3 homodimer were performed with synthesized TB1 and its molecular probe, respectively. The results of the above NMR studies and additional in silico docking studies suggested that TB1 promotes the dissociation to monomeric PAC3 after interaction with PAC3 homodimer. The rare mechanism shown in this book indicates a potential novel drug target in the interfaces of PPIs with no cavity or groove. 124 pp. Englisch.…

  • Language: English

    Published by Springer, 2015

    4431554467 / 9784431554462

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    Condition: New. Print on Demand 109.

  • Language: English

    Published by Springer, 2015

    4431554467 / 9784431554462

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    Seller: Biblios, frankfurt am main, HESSE, GermanyBiblios

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    Condition: New. PRINT ON DEMAND 109.

  • Language: English

    Published by Springer, Springer Okt 2016, 2016

    4431562877 / 9784431562870

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    Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand Titel. Neuware -This book focuses on thielocin B1 (TB1), which was found to be an inhibitor of protein¿protein interactions (PPIs) of proteasome assembling chaperone (PAC) 3 homodimer, and elucidates the mechanism by nuclear magnetic resonance (NMR) studies. Interfaces of PPIs recently have been expected to be novel therapeutic targets, while it is difficult to apply conventional methodology based on lock and key theory. The author achieved the first total synthesis of TB1 and its spin-labeled derivative to carry out NMR experiments because the supply of TB1 from natural sources was limited. Unique 2,2¿,6,6¿-tetrasubstituted diphenyl ether moiety of TB1 was synthesized from a depsidone skeleton by chemoselective reduction of lactone. In the process of elongating side wings, efficient formylation utilizing dichloromethyl methyl ether¿silver trifluoromethanesulfonate was developed for the sterically hindered aromatic compound. NMR titration experiments and paramagnetic relaxation enhancement observation of PAC3 homodimer were performed with synthesized TB1 and its molecular probe, respectively. The results of the above NMR studies and additional in silico docking studies suggested that TB1 promotes the dissociation to monomeric PAC3 after interaction with PAC3 homodimer. The rare mechanism shown in this book indicates a potential novel drug target in the interfaces of PPIs with no cavity or groove.Springer-Verlag KG, Sachsenplatz 4-6, 1201 Wien 124 pp. Englisch.…

  • Language: English

    Published by Springer, Springer Jan 2015, 2015

    4431554467 / 9784431554462

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    Buch. Condition: Neu. This item is printed on demand - Print on Demand Titel. Neuware -This book focuses on thielocin B1 (TB1), which was found to be an inhibitor of protein¿protein interactions (PPIs) of proteasome assembling chaperone (PAC) 3 homodimer, and elucidates the mechanism by nuclear magnetic resonance (NMR) studies. Interfaces of PPIs recently have been expected to be novel therapeutic targets, while it is difficult to apply conventional methodology based on lock and key theory. The author achieved the first total synthesis of TB1 and its spin-labeled derivative to carry out NMR experiments because the supply of TB1 from natural sources was limited. Unique 2,2¿,6,6¿-tetrasubstituted diphenyl ether moiety of TB1 was synthesized from a depsidone skeleton by chemoselective reduction of lactone. In the process of elongating side wings, efficient formylation utilizing dichloromethyl methyl ether¿silver trifluoromethanesulfonate was developed for the sterically hindered aromatic compound. NMR titration experiments and paramagnetic relaxation enhancement observation of PAC3 homodimer were performed with synthesized TB1 and its molecular probe, respectively. The results of the above NMR studies and additional in silico docking studies suggested that TB1 promotes the dissociation to monomeric PAC3 after interaction with PAC3 homodimer. The rare mechanism shown in this book indicates a potential novel drug target in the interfaces of PPIs with no cavity or groove.Springer-Verlag KG, Sachsenplatz 4-6, 1201 Wien 124 pp. Englisch.…

  • Language: English

    Published by Springer, 2016

    4431562877 / 9784431562870

    • Softcover
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    Seller: Majestic Books, Hounslow, United KingdomMajestic Books

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    Condition: New. Print on Demand pp. 109.

  • Language: English

    Published by Springer, 2016

    4431562877 / 9784431562870

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    Seller: Biblios, frankfurt am main, HESSE, GermanyBiblios

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    Condition: New. PRINT ON DEMAND pp. 109.