Development of "O-Acyl Isopeptide Method"

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概要

• 論文の詳細を見る
• 2007-03-01

著者

• Sohma Youhei

  Department Of Medicinal Chemistry Center For Frontier Research In Medicinal Science 21st Century Coe

• Sohma Youhei

  Department Of Medicinal Chemistry Center For Frontier Research In Medicinal Science And Department O

関連論文

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• Controlled Drug Release : Design and Application of New Water-soluble Prodrugs
• Spontaneously Regenerable Prodrug : Design and Synthesis of Water-soluble Prodrugs of HIV Protease Inhibitors
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• P-262 "O-ACYL ISOPEPTIDE METHOD" FOR THE EFFICIENT SYNTHESIS OF DIFFICULT SEQUENSE-CONTAINING PEPTIDES : UTILIZATION OF "O-ACYL ISODIPEPTIDE UNIT"
• Development of Spontaneously Regenerable Water-Soluble Prodrugs Based on the Peptide Chemistry : Importance of Drug Release Time for the Improvement of Gastrointestinal Absorption
• Structural Analysis of Amyloid-β Protein Fibrils Formed in Raft-Like Model Membranes
• Inhibition of Amyloid β-Protein Aβ-(1-42) Induced Cytotoxicity by Helical Aβ Analog
• O-N Intramolecular Acyloxy Migration Reaction : from the Prodrug Strategy to the Migration of Protective Groups in Amino Acids
• "Click Peptide" Based on the "O-Acyl Isopeptide Method" : an Efficient Preparation of Amyloid β Peptide 1-42 Mutants
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• Click Peptide by Use of the O-Acyl Isopeptide Method : Production of Amyloid β Peptide from Water-Soluble Analogue
• "O-Acyl Isopeptide Method" for the Synthesis of Difficult Sequence-Containing Peptides : Application to the Synthesis of Amyloid β Peptide (Aβ) 1-42
• O-N Intramolecular Acyl and Acyloxy Migration Reaction in the Development of Water-Soluble Prodrugs of Taxoids
• A Novel Method for the Synthesis of Difficult Sequence-Containing Peptides via O-Acyl Isopeptides : The Use of O-N Intramolecular Acyl Migration Reaction
• Development of New Water-Soluble Prodrugs Based on Intramolecular Nucleophilic Reactions in Peptide Chemistry
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• Use of O-Acyl Isopeptides to Identify New Functions of Amyloid β Peptides
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• Synthesis of O-Acyl Isopeptide by Use of Native Chemical Ligation to Efficiently Construct Hydrophobic Polypeptide

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