Zobrazeno 1 - 7 of 7 pro vyhledávání: '"Yoshiyuki Kayano"'
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Data from Crosstalk to Stromal Fibroblasts Induces Resistance of Lung Cancer to Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitors
Autor: Seiji Yano, Saburo Sone, Yasuhiko Nishioka, Yoshiyuki Kayano, Go Watanabe, Makoto Oda, Isao Matsumoto, Kunio Matsumoto, Tadaaki Yamada, Qi Li, Wei Wang
Purpose: Lung cancers with epidermal growth factor receptor (EGFR)–activating mutations show good clinical response to gefitinib and erlotinib, selective tyrosine kinase inhibitors (TKI) to EGFR, but these tumors invariably develop drug resistance.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a896a11577759bbe6b2c596ff0bdffb
https://doi.org/10.1158/1078-0432.c.6517861
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3
Crosstalk to Stromal Fibroblasts Induces Resistance of Lung Cancer to Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitors
Autor: Makoto Oda, Saburo Sone, Wei Wang, Qi Li, Seiji Yano, Go Watanabe, Tadaaki Yamada, Kunio Matsumoto, Isao Matsumoto, Yasuhiko Nishioka, Yoshiyuki Kayano
Publikováno v: Clinical Cancer Research. 15:6630-6638
Purpose: Lung cancers with epidermal growth factor receptor (EGFR)–activating mutations show good clinical response to gefitinib and erlotinib, selective tyrosine kinase inhibitors (TKI) to EGFR, but these tumors invariably develop drug resistance.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b23a533361d249d6287e4bb426b4f98
https://doi.org/10.1158/1078-0432.ccr-09-1001
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4
The N-terminus of B96Bom, a Bombyx mori G-protein-coupled receptor, is N-myristoylated and translocated across the membrane
Autor: Hiroto Ohta, Toshihiko Utsumi, Yoshiyuki Kayano, Nagisa Sakurai, Yoshihisa Ozoe
Publikováno v: FEBS Journal. 272:472-481
In eukaryotic cellular proteins, protein N-myristoylation has been recognized as a protein modification that occurs mainly on cytoplasmic or nucleoplasmic proteins. In this study, to search for a eukaryotic N-myristoylated transmembrane protein, the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b78576785b29e985afb4269260ffd297
https://doi.org/10.1111/j.1742-4658.2004.04487.x
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5
Vertical-scanning mutagenesis of amino acids in a model N-myristoylation motif reveals the major amino-terminal sequence requirements for protein N-myristoylation
Autor: Rumi Ishisaka, Hiroyuki Iwata, Kengo Nakano, Toshihiko Utsumi, Takeshi Funakoshi, Sayaka Nakao, Nagisa Sakurai, Yoshiyuki Kayano
Publikováno v: European Journal of Biochemistry. 271:863-874
In order to determine the amino-terminal sequence requirements for protein N-myristoylation, site-directed mutagenesis of the N-terminal region was performed using tumor necrosis factor (TNF) mutants as model substrate proteins. Subsequently, the sus
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5894672f6d16f921fcf56a688f23a17f
https://doi.org/10.1111/j.1432-1033.2004.03991.x
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6
The N-terminus of B96Bom, a Bombyx mori G-protein-coupled receptor, is N-myristoylated and translocated across the membrane
Autor: Toshihiko, Utsumi, Hiroto, Ohta, Yoshiyuki, Kayano, Nagisa, Sakurai, Yoshihisa, Ozoe
Publikováno v: The FEBS journal. 272(2)
In eukaryotic cellular proteins, protein N-myristoylation has been recognized as a protein modification that occurs mainly on cytoplasmic or nucleoplasmic proteins. In this study, to search for a eukaryotic N-myristoylated transmembrane protein, the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2884caa4df29324ad685b363a2547328
https://pubmed.ncbi.nlm.nih.gov/15654885
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7
Vertical-scanning mutagenesis of amino acids in a model N-myristoylation motif reveals the major amino-terminal sequence requirements for protein N-myristoylation
Autor: Toshihiko, Utsumi, Kengo, Nakano, Takeshi, Funakoshi, Yoshiyuki, Kayano, Sayaka, Nakao, Nagisa, Sakurai, Hiroyuki, Iwata, Rumi, Ishisaka
Publikováno v: European journal of biochemistry. 271(4)
In order to determine the amino-terminal sequence requirements for protein N-myristoylation, site-directed mutagenesis of the N-terminal region was performed using tumor necrosis factor (TNF) mutants as model substrate proteins. Subsequently, the sus
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::674686d4637803c84656dc6c0a1d87d3
https://pubmed.ncbi.nlm.nih.gov/14764103
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