His primary scientific interests are in Cell biology, Guanine nucleotide exchange factor, Molecular biology, Signal transduction and Adapter molecule crk. His Cell biology study combines topics in areas such as Cancer research and Actin cytoskeleton. Michiyuki Matsuda has included themes like GTP-binding protein regulators, G protein, Rap1 and Phagosome maturation in his Guanine nucleotide exchange factor study.
His Molecular biology research includes elements of Cell culture and SH2 domain. In his research on the topic of Signal transduction, Stimulation, COS cells and Endocytosis is strongly related with Epidermal growth factor. His Adapter molecule crk study combines topics from a wide range of disciplines, such as SH3 domain and Peptide sequence.
Michiyuki Matsuda mainly investigates Cell biology, Förster resonance energy transfer, Signal transduction, MAPK/ERK pathway and Kinase. He frequently studies issues relating to Cell and Cell biology. The concepts of his Förster resonance energy transfer study are interwoven with issues in Biophysics, Live cell imaging, Genetically modified mouse and Biosensor.
His work carried out in the field of MAPK/ERK pathway brings together such families of science as Cell cycle, Cancer research and Cell growth. The RAC1 study combines topics in areas such as Actin cytoskeleton, CDC42, Lamellipodium and RHOA. Michiyuki Matsuda combines subjects such as GTP-binding protein regulators, G protein, Rap1, Adapter molecule crk and Molecular biology with his study of Guanine nucleotide exchange factor.
Cell biology, MAPK/ERK pathway, Kinase, Förster resonance energy transfer and Biophysics are his primary areas of study. Michiyuki Matsuda has included themes like Cell, Cell migration and Cell cycle in his Cell biology study. His work deals with themes such as Chondrogenesis, Cell growth, Wound healing, Mesenchyme and Morphogenesis, which intersect with MAPK/ERK pathway.
His studies deal with areas such as Cell culture, Live cell imaging, Extracellular, Carcinogenesis and Phosphorylation as well as Kinase. His Förster resonance energy transfer research is multidisciplinary, incorporating elements of Protein kinase A, Adenylyl cyclase, Signal transduction, Biosensor and Optogenetics. His work carried out in the field of Biophysics brings together such families of science as Two-photon excitation microscopy, Fluorescence correlation spectroscopy, Endogeny, Dissociation constant and In vivo.
The scientist’s investigation covers issues in Cell biology, Kinase, Förster resonance energy transfer, MAPK/ERK pathway and Biosensor. His work on Intracellular as part of general Cell biology research is frequently linked to DNA replication factor CDT1, thereby connecting diverse disciplines of science. He studied Kinase and Cell that intersect with Mechanotransduction, Chromosomal translocation, Crosstalk and Programmed cell death.
His Förster resonance energy transfer study incorporates themes from Biophysics, Optogenetics, Protein kinase A and Bioluminescence. His MAPK/ERK pathway study is associated with Signal transduction. He has researched Signal transduction in several fields, including Thrombus and Live cell imaging.
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A family of cAMP-binding proteins that directly activate Rap1.
Hiroaki Kawasaki;Gregory M. Springett;Naoki Mochizuki;Shinichiro Toki.
Interferon-|[alpha]| induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6
Taro Kawai;Shintaro Sato;Ken J. Ishii;Cevayir Coban.
Nature Immunology (2004)
Spatio-temporal images of growth-factor-induced activation of Ras and Rap1.
Naoki Mochizuki;Shigeko Yamashita;Kazuo Kurokawa;Yusuke Ohba.
Activation of Rac and Cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells
Reina E. Itoh;Kazuo Kurokawa;Yusuke Ohba;Hisayoshi Yoshizaki.
Molecular and Cellular Biology (2002)
Interleukin-1 receptor-associated kinase-1 plays an essential role for Toll-like receptor (TLR)7- and TLR9-mediated interferon-α induction
Satoshi Uematsu;Shintaro Sato;Masahiro Yamamoto;Tomonori Hirotani.
Journal of Experimental Medicine (2005)
Development of an optimized backbone of FRET biosensors for kinases and GTPases
Naoki Komatsu;Kazuhiro Aoki;Masashi Yamada;Hiroko Yukinaga.
Molecular Biology of the Cell (2011)
Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins.
Michiyuki Matsuda;Bruce J. Mayer;Yasuhisa Fukui;Hidesaburo Hanafusa.
Activation of Rac1 by a Crk SH3-binding protein, DOCK180
Etsuko Kiyokawa;Yuko Hashimoto;Shin Kobayashi;Haruhiko Sugimura.
Genes & Development (1998)
Intravital Imaging Reveals How BRAF Inhibition Generates Drug-Tolerant Microenvironments with High Integrin β1/FAK Signaling
Eishu Hirata;Maria Romina Girotti;Amaya Viros;Steven Hooper.
Cancer Cell (2015)
Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G.
Takaya Gotoh;Seisuke Hattori;Shun Nakamura;Hitoshi Kitayama.
Molecular and Cellular Biology (1995)
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