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Yasuyuki Kitaura
Researcher at Nagoya University
Publications - 64
Citations - 2230
Yasuyuki Kitaura is an academic researcher from Nagoya University. The author has contributed to research in topics: Amino acid & Branched-chain amino acid. The author has an hindex of 23, co-authored 60 publications receiving 1950 citations. Previous affiliations of Yasuyuki Kitaura include Columbia University.
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Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK.
Chiaki Takahashi,Zeqi Sheng,Tom Horan,Hitoshi Kitayama,Masatoshi Maki,Kiyotaka Hitomi,Yasuyuki Kitaura,Setsuo Takai,Regina Maki Sasahara,Aki Horimoto,Yoji Ikawa,Barry J. Ratzkin,Tsutomu Arakawa,Makoto Noda +13 more
TL;DR: Restored expression of RECK in malignant cells resulted in suppression of invasive activity with concomitant decrease in the secretion of matrix metalloproteinase-9 (MMP-9), a key enzyme involved in tumor invasion and metastasis.
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Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins.
TL;DR: Penta-EF-hand (PEF) proteins comprise a family of Ca(2+)-binding proteins that have five repetitive EF-hand motifs that have common features: dimerization through unpaired C-terminal EF5s, possession of hydrophobic Gly/Pro-rich N- terminal domains, and Ca( 2+)-dependent translocation to membranes.
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PKA-mediated phosphorylation regulates the function of activation-induced deaminase (AID) in B cells.
TL;DR: It is reported that protein kinase A (PKA) phosphorylates AID and regulates its activity in GC B cells and suggested that the control of T cell-dependent immune responses may be modulated, via AID, by signals that activate PKA.
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Control of the B cell-intrinsic tolerance programs by ubiquitin ligases Cbl and Cbl-b.
Yasuyuki Kitaura,Ihn Kyung Jang,Yan Wang,Yoon-Chi Han,Tetsuya Inazu,Emily J. Cadera,Mark S. Schlissel,Richard R. Hardy,Hua Gu +8 more
TL;DR: Mice with B cell-specific ablation of both Cbl and Cbl-b manifested systemic lupus erythematosus (SLE)-like autoimmune disease and the loss of coordination between these pathways was responsible for the impaired B cell tolerance induction.
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Peflin and ALG-2, Members of the Penta-EF-Hand Protein Family, Form a Heterodimer That Dissociates in a Ca2+-dependent Manner
TL;DR: The results suggest that peflin has features common to those of other PEF proteins (dimerization and translocation to membranes) and may modulate the function of ALG-2 in Ca2+ signaling.