Hiroki Akiba

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Antibodies (immunoglobulins) bind specific molecules (i.e. antigens) with high affinity and specificity. In order to understand their mechanisms of recognition, interaction analysis based on thermodynamic and kinetic parameters, as well as structure determination is crucial. In this review, we focus on mutational analysis which gives information about the(More)
A straightforward and visual method to assess inhibitors on protein tyrosine kinases (PTKs) and phosphatases (PTPs) has been developed. These enzymes play critical roles in a number of diseases and, thus, their inhibitors are important for effective therapy. With the use of the long-life luminescence emitted from a binuclear Tb(III) complex, enzymatic(More)
By using the luminescence from binuclear complexes of Tb(III) (Tb(2)-L(1) and Tb(2)-L(2)), phosphorylated Tyr residue in peptides was selectively detected in neutral aqueous solutions. Neither the non-phosphorylated Tyr, pSer, pThr, nor the other phosphate-containing biomolecules tested affected the luminescence intensity to any notable extent. Upon the(More)
Phosphorylation of proteins is closely associated with various diseases, and, therefore, its detection is vitally important in molecular biology and drug discovery. Previously, we developed a binuclear Tb(III) complex, which emits notable luminescence only in the presence of phosphotyrosine. In this study, we conjugated a newly synthesized binuclear Tb(III)(More)
Bispecific antibody targeting of two different antigens is promising, but when fragment-based antibodies are used, homogeneous production is difficult. To overcome this difficulty, we developed a method using the SpyTag/SpyCatcher system in which a covalent bond is formed between the two polypeptides. Using this method, we constructed a bispecific antibody(More)
Phosphorylation of tyrosine residues in proteins, as well as their dephosphorylation, is closely related to various diseases. However, this phosphorylation is usually accompanied by more abundant phosphorylation of serine and threonine residues in the proteins and covers only 0.05% of the total phosphorylation. Accordingly, highly selective detection of(More)
BACKGROUND The ever-increasing number of people living with Alzheimer's disease urges to develop more effective therapies. Despite considerable success, anti-Alzheimer immunotherapy still faces the challenge of intracerebral and intracellular delivery. This work introduces in situ production of anti-amyloid beta (Aβ) antibody after intracerebral injection(More)
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