His primary scientific interests are in Cell biology, Molecular biology, Cyclin-dependent kinase, Cyclin-dependent kinase 2 and Cell cycle. Masatoshi Kitagawa combines subjects such as Geranylgeranyl pyrophosphate, Ubiquitin, NFKB1, Biochemistry and S phase with his study of Cell biology. His Ubiquitin ligase study in the realm of Ubiquitin connects with subjects such as Glomerulosclerosis.
His work investigates the relationship between Molecular biology and topics such as Phosphorylation that intersect with problems in Binding site and DNA damage. His Cyclin-dependent kinase research integrates issues from Cyclin E and E2F. His study in Cell cycle is interdisciplinary in nature, drawing from both Epigenetics and Kinase.
His primary areas of study are Cell biology, Molecular biology, Cancer research, Ubiquitin ligase and Cyclin-dependent kinase. He has researched Cell biology in several fields, including Cell cycle, Retinoblastoma protein and Biochemistry. His research investigates the connection between Molecular biology and topics such as Phosphorylation that intersect with problems in MYB.
His study looks at the relationship between Cancer research and fields such as Metastasis, as well as how they intersect with chemical problems. His Ubiquitin ligase study results in a more complete grasp of Ubiquitin. He has included themes like E2F, Kinase and Cyclin-dependent kinase 2 in his Cyclin-dependent kinase study.
Masatoshi Kitagawa spends much of his time researching Cell biology, Molecular biology, Cancer research, Ubiquitin ligase and Transcription factor. His studies deal with areas such as Chromatin, Retinoblastoma protein, Epigenetics and Long non-coding RNA as well as Cell biology. His Molecular biology study combines topics from a wide range of disciplines, such as Protein degradation, Cell division control protein 4, Mutant, Cyclin B and Phosphorylation.
In the subject of general Cancer research, his work in Angiogenesis is often linked to Progressive disease, thereby combining diverse domains of study. His Ubiquitin ligase study is concerned with the field of Ubiquitin as a whole. His Cyclin-dependent kinase study is focused on Cell cycle in general.
His main research concerns Molecular biology, Cell biology, Transcription factor, Ubiquitin ligase and F-box protein. His biological study spans a wide range of topics, including Cell division control protein 4, Cyclin-dependent kinase 2, HEK 293 cells, Phosphorylation and Kinase. The various areas that Masatoshi Kitagawa examines in his Cell biology study include Cell cycle, Cyclin-dependent kinase inhibitor protein, Cyclin-dependent kinase and Epigenetics.
His Transcription factor research includes elements of Cell cycle checkpoint, DNA damage, Protein degradation, Small interfering RNA and Protein subunit. His Ubiquitin ligase study is concerned with Ubiquitin in general. His F-box protein research incorporates elements of Demethylase, Senescence, Cell aging, Mutant and Ectopic expression.
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Long non-coding RNA ANRIL is required for the PRC2 recruitment to and silencing of p15(INK4B) tumor suppressor gene.
Y Kotake;T Nakagawa;K Kitagawa;S Suzuki.
Targeted disruption of Skp2 results in accumulation of cyclin E and p27 (Kip1), polyploidy and centrosome overduplication
Keiko Nakayama;Hiroyasu Nagahama;Yohji A. Minamishima;Masaki Matsumoto.
The EMBO Journal (2000)
An F-box protein, FWD1, mediates ubiquitin-dependent proteolysis of β-catenin
Masatoshi Kitagawa;Shigetsugu Hatakeyama;Michiko Shirane;Masaki Matsumoto.
The EMBO Journal (1999)
The consensus motif for phosphorylation by cyclin D1-Cdk4 is different from that for phosphorylation by cyclin A/E-Cdk2.
M. Kitagawa;H. Higashi;H.-K. Jung;I. Suzuki-Takahashi.
The EMBO Journal (1996)
Evidence that reactive oxygen species do not mediate NF‐κB activation
Makio Hayakawa;Hiroshi Miyashita;Isao Sakamoto;Masatoshi Kitagawa.
The EMBO Journal (2003)
Skp2-mediated degradation of p27 regulates progression into mitosis.
Keiko Nakayama;Hiroyasu Nagahama;Yohji A. Minamishima;Satoshi Miyake.
Developmental Cell (2004)
Geranylgeranylated Rho Small GTPase(s) Are Essential for the Degradation of p27Kip1 and Facilitate the Progression from G1 to S Phase in Growth-stimulated Rat FRTL-5 Cells
Aizan Hirai;Susumu Nakamura;Yoshihiko Noguchi;Tatsuji Yasuda.
Journal of Biological Chemistry (1997)
Down-regulation of p27 Kip1 by Two Mechanisms, Ubiquitin-mediated Degradation and Proteolytic Processing
Michiko Shirane;Yumiko Harumiya;Noriko Ishida;Aizan Hirai.
Journal of Biological Chemistry (1999)
Butyrolactone I, a selective inhibitor of cdk2 and cdc2 kinase.
Kitagawa M;Okabe T;Ogino H;Matsumoto H.
Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability.
Noriko Ishida;Masatoshi Kitagawa;Shigetsugu Hatakeyama;Kei-ichi Nakayama.
Journal of Biological Chemistry (2000)
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