Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Koichi Okamoto"'
Autor:
Takehiro Shiraishi, Koichi Okamoto, Takahiro Einama, Hideki Ueno, Eiji Shinto, Kazuo Hase, Satsuki Mochizuki, Hitoshi Tsuda, Yoshiki Kajiwara
Publikováno v:
Virchows Archiv. 474:297-307
Mesothelin (MSLN) is a cell-surface glycoprotein present on mesothelial cells and in many cancers, where expression is generally associated with an unfavorable prognosis. The clinical significance and pathological characteristics of MSLN expression w
Autor:
Satsuki Mochizuki, Tadakazu Ao, Yoji Kishi, Koichi Okamoto, Hideki Ueno, Eiji Shinto, Keisuke Yonemura, Yoshiki Kajiwara
Publikováno v:
Virchows Archiv : an international journal of pathology. 477(1)
Some preceding studies show that a desmoplastic reaction (DR) at the invasive front of a primary tumor (DRprimary) is a promising prognostic indicator, and its histologic classification is an independent prognostic factor in patients with colorectal
Autor:
Koichi Okamoto, Eiji Shinto, Keisuke Yonemura, Suefumi Aosasa, Yoshiki Kajiwara, Satsuki Mochizuki, Hideki Ueno, Tadakazu Ao
Publikováno v:
Virchows Archiv : an international journal of pathology. 475(3)
Desmoplastic reaction (DR) involves the growth of fibrous or connective tissues around a tumor and has recently attracted attention as an indicator of malignant potential. Previous studies have confirmed that histological categorization of DR in the
Autor:
Yoshio Ikeda, Masamitsu Takatama, Shigeo Murayama, Masaki Ikeda, Tsuneo Yamazaki, Koichi Okamoto, Kouki Makioka
Publikováno v:
Journal of the Neurological Sciences. 365:101-107
Alzheimer's disease (AD) is an age-related neurodegenerative disorder. Its pathological hallmarks are senile plaques (SPs), which contain extracellular deposits of amyloid β (Aβ) protein fibrils and dystrophic neurites (DNs), and neurofibrillary ta
Autor:
Khashayarsha Khazaie, Aziz Zaanan, Hisato Kawakami, Frank A. Sinicrope, Shengbing Huang, Koichi Okamoto
Publikováno v:
Journal of Biological Chemistry. 290:23838-23849
In colorectal cancers with oncogenic GTPase Kras (KRAS) mutations, inhibition of downstream MEK/ERK signaling has shown limited efficacy, in part because of failure to induce a robust apoptotic response. We studied the mechanism of apoptosis resistan
Publikováno v:
Journal of the Neurological Sciences. 336:24-28
The Smad ubiquitination regulatory factor 1 (Smurf1) is one of the E3 ubiquitin ligases and is related to multiple biological processes. Despite the various roles played by this protein, there is no report on the function of Smurf1 in neurodegenerati
Autor:
Masaaki Matsuoka, Koichi Okamoto, Mikiro Nawa, Sadakazu Aiso, Eriko Kage-Nakadai, Shohei Mitani
Publikováno v:
Cell Death & Differentiation. 19:1398-1407
BTBD10, an Akt interactor, activates Akt by decreasing the protein phosphatase 2A-mediated dephosphorylation and inactivation of Akt. Overexpression of BTBD10 suppresses motor neuron death that is induced by a familial amyotrophic lateral sclerosis (
Publikováno v:
Muscle & Nerve. 39:634-641
beta-Synemin was previously identified as an alpha-dystrobrevin-interacting protein in muscle. To better understand its function in neural tissue, in situ and immunohistochemical analyses were performed to identify where the synemin isoforms are expr
Autor:
Yoji Murata, Hideki Okazawa, Jun Okajo, Chie Okuzawa, Yasuyuki Saito, Hiroshi Ohnishi, Takashi Matozaki, Yoriaki Kaneko, Koichi Okamoto, Yoshihisa Nojima, Yuka Kaneko, Takeshi Tomizawa
Publikováno v:
The Kitakanto Medical Journal. 58:133-139
Background & Aims: SHPS-1 is a transmembrane protein that binds the protein tyrosine phosphatases \nSHP-1 and SHP-2 through its cytoplasmic region. It is highly expressed on the surface of CD11c+\ndendritic cells (DCs) and macrophages. We have recent
Autor:
Yuji Mizuno, Jeffrey R. Guyon, Akira Tamaoka, Norio Ohkoshi, Koichi Okamoto, Sachiko Hoshino, Akiko Ishii, Louis M. Kunkel
Publikováno v:
BMC Musculoskeletal Disorders
BMC Musculoskeletal Disorders, Vol 8, Iss 1, p 40 (2007)
BMC Musculoskeletal Disorders, Vol 8, Iss 1, p 40 (2007)
Background β-synemin was originally identified in humans as an α-dystrobrevin-binding protein through a yeast two-hybrid screen using an amino acid sequence derived from exons 1 through 16 of α-dystrobrevin, a region common to both α-dystrobrevin