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Takashi Suzuki
Shimadzu Corp.
28Publications
12H-index
495Citations
Publications 28
Newest
#1Fumiaki ShiratoriH-Index: 2
#2Hideaki ShimadaH-Index: 40
Last.Hironori KanekoH-Index: 23
view all 8 authors...
Purpose Several studies have evaluated the association between ABO blood group and the prognosis of various types of cancer; however, little is known about the relationship between ABO blood group and esophageal squamous cell carcinoma (SCC). We investigated how ABO blood group and clinicopathological characteristics are related to the survival of Japanese patients with esophageal SCC.
#1Koko Moriya (Yamaguchi University)H-Index: 8
#2Kei Nagatoshi (Yamaguchi University)H-Index: 2
Last.Toshihiko Utsumi (Yamaguchi University)H-Index: 27
view all 7 authors...
N-myristoylation of eukaryotic cellular proteins has been recognized as a modification that occurs mainly on cytoplasmic proteins. In this study, we examined the membrane localization, membrane integration, and intracellular localization of four recently identified human N-myristoylated proteins with predicted transmembrane domains. As a result, it was found that protein Lunapark, the human ortholog of yeast protein Lnp1p that has recently been found to be involved in network formation of the en...
#1Koko Moriya (Yamaguchi University)H-Index: 8
#2Takuo Yamamoto (Yamaguchi University)H-Index: 1
Last.Toshihiko Utsumi (Yamaguchi University)H-Index: 27
view all 9 authors...
The subcellular localization of 13 recently identified N-myristoylated proteins and the effects of overexpression of these proteins on cellular morphology were examined with the aim of understanding the physiological roles of the protein N-myristoylation that occurs on these proteins. Immunofluorescence staining of HEK293T cells transfected with cDNAs coding for the proteins revealed that most of them were associated with the plasma membrane or the membranes of intracellular compartments, and di...
#1Toru EzureH-Index: 9
#2Takashi SuzukiH-Index: 12
Last.Susumu TsunasawaH-Index: 38
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Cell-free protein synthesis systems offer production of native proteins with high speed, even for the proteins that are toxic to cells. Among cell-free systems, the system derived from insect cells has the potential to carry out posttranslational modifications that are specific to eukaryotic organisms, as occurs in the rabbit reticulocyte system. In this review, we describe development of this insect cell-free system and its applications.
#1Takashi Suzuki (Shimadzu Corp.)H-Index: 12
#2Koko Moriya (Yamaguchi University)H-Index: 8
Last.Toshihiko Utsumi (Yamaguchi University)H-Index: 27
view all 8 authors...
To establish a strategy for the comprehensive identification of human N-myristoylated proteins, the susceptibility of human cDNA clones to protein N-myristoylation was evaluated by metabolic labeling and MS analyses of proteins expressed in an insect cell-free protein synthesis system. One-hundred-and-forty-one cDNA clones with N-terminal Met-Gly motifs were selected as potential candidates from ∼2000 Kazusa ORFeome project human cDNA clones, and their susceptibility to protein N-myristoylation ...
#1Takashi Suzuki (Shimadzu Corp.)H-Index: 12
#2Toru Ezure (Shimadzu Corp.)H-Index: 9
Last.Susumu Tsunasawa (Osaka University)H-Index: 38
view all 6 authors...
Ubiquitination is one of the most significant posttranslational modifications (PTMs). To evaluate the ability of an insect cell-free protein synthesis system to carry out ubiquitin (Ub) conjugation to in vitro translated proteins, poly-Ub chain formation was studied in an insect cell-free protein synthesis system. Poly-Ub was generated in the presence of Ub aldehyde (UA), a de-ubiquitinating enzyme inhibitor. In vitro ubiquitination of the p53 tumor suppressor protein was also analyzed, and p53 ...
#1Toru Ezure (Shimadzu Corp.)H-Index: 9
#2Takashi Suzuki (Shimadzu Corp.)H-Index: 12
Last.Eiji Ando (Shimadzu Corp.)H-Index: 14
view all 5 authors...
#1Koko MoriyaH-Index: 8
#2T. TsubotaH-Index: 1
Last.Toshihiko UtsumiH-Index: 27
view all 8 authors...
The lipid modifications which occur on Bombyx mori Ras proteins BmRas1, BmRas2 and BmRas3 were studied by metabolic labelling in an insect cell-free protein synthesis system and in a baculovirus expression system, using specific inhibitors of protein prenylation and protein palmitoylation. In addition, the subcellular localization of BmRas proteins was examined using EGFP fusion proteins of constitutively active forms of BmRas proteins transiently expressed in Sf9 cells. As a result, it was reve...
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