T
Tsukasa Osaki
Researcher at Yamagata University
Publications - 41
Citations - 623
Tsukasa Osaki is an academic researcher from Yamagata University. The author has contributed to research in topics: Autoantibody & Factor XIII. The author has an hindex of 13, co-authored 41 publications receiving 480 citations.
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Journal ArticleDOI
Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins, with sequence similarity to spider neurotoxins.
Tsukasa Osaki,Miyuki Omotezako,Ranko Nagayama,Michimasa Hirata,Sadaaki Iwanaga,Jiro Kasahara,Junji Hattori,Isao Ito,Hiroyuki Sugiyama,Shun Ichiro Kawabata +9 more
TL;DR: As horseshoe crab is a close relative of the spider, tachystatins and spider neurotoxins may have evolved from a common ancestral peptide, with adaptive functions.
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Large-scale Identification of Endogenous Secretory Peptides Using Electron Transfer Dissociation Mass Spectrometry
TL;DR: ETD was used, in comparison to collision induced dissociation (CID), to identify endogenous peptides derived from secretory granules of a human endocrine cell line and this advantage was demonstrated in identifying a new antimicrobial peptide from neurosecretory protein VGF, VGF[554–577]-NH2, or in differentiating nearly isobaric peptides that arise from alternatively spliced exons of the gastrin-releasing peptide gene.
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Impaired Recovery of Blood Flow After Hind-Limb Ischemia in Mice Lacking Guanylyl Cyclase-A, a Receptor for Atrial and Brain Natriuretic Peptides
Takeshi Tokudome,Ichiro Kishimoto,Kenichi Yamahara,Tsukasa Osaki,Naoto Minamino,Takeshi Horio,Kazutomo Sawai,Yuhei Kawano,Mikiya Miyazato,Masataka Sata,Masakazu Kohno,Kazuwa Nakao,Kenji Kangawa +12 more
TL;DR: The results suggest that endogenous ANP and BNP play important roles in reparative vascular remodeling in ischemic tissue.
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The Non-catalytic B Subunit of Coagulation Factor XIII Accelerates Fibrin Cross-linking
TL;DR: It is demonstrated that FXIII-B accelerates fibrin cross-linking and plays important roles in the formation of a ternary complex between proenzyme FXIII, prosubstrate fibr inogen, and activator thrombin.
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Peptidomics-based discovery of an antimicrobial peptide derived from insulin-like growth factor-binding protein 5.
TL;DR: This study exemplifies the impact of peptidomics to study naturally occurring peptides and identifies a novel intramolecular disulfide-linked 22-residue amidated peptide, designated AMP-IBP5, which showed antimicrobial activity against six of the eight microorganisms tested at concentrations comparable to or lower than those for well-characterized AMPs cathelicidin and β-defensin-2.