Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Koji Ebisuno"'
Autor:
Masaya Denda, Chiaki Komiya, Aiko Yamauchi, Hirokazu Tamamura, Koji Ebisuno, Nami Maeda, Wataru Nomura, Jun Yamamoto, Tomohiro Tanaka, Akira Shigenaga, Akira Otaka, Youichi Sato
Publikováno v:
Tetrahedron. 70:5122-5127
A fluoride-responsive (FR) amino acid that induces amide bond cleavage upon the addition of a fluoride was developed, and it was applied to an FR traceable linker. By the use of an alkyne-containing peptide as a model of an alkynylated target protein
Publikováno v:
Tetrahedron Letters. 53:3429-3432
Phosphodiester-type adenylylated (AMPylated) Ser, Thr, and Tyr derivatives were developed for Fmoc solid phase peptide synthesis of AMPylated peptides. One-pot/sequential reaction consisting of condensation of an N-nonprotected adenosine derivative a
Development of a Reduction‐Responsive Amino Acid that Induces Peptide Bond Cleavage in Hypoxic Cells
Autor:
Koichiro Tsuchiya, Licht Miyamoto, Jun Yamamoto, Keiji Ogura, Keisuke Ishizawa, Hiroko Hirakawa, Koji Ebisuno, Akira Shigenaga, Akira Otaka
Publikováno v:
ChemBioChem. 13(7):968-971
Utilization of a hypoxia-responsive amino acid is indispensable in the preparation of hypoxic tumor-specific peptidyl prodrugs. Bioreduction of a nitro group is among the most attractive triggering reactions in the hypoxia-responsive prodrugs. In thi
Autor:
Hao Ding, Kohei Sato, Keiko Yamaguchi, Koji Ebisuno, Akira Shigenaga, Jun Yamamoto, Akira Otaka, Kenichi Akaji, Ko Morishita
Publikováno v:
Tetrahedron. 67:8879-8886
Cysteine proteases are attractive drug targets due to their involvement in a wide variety of diseases. To evaluate the potential of a particular protease as a drug target, use of a reagent that controls activity of the protease is indispensable. In t