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Makoto Fukuda

Researcher at Baylor College of Medicine

Publications -  52
Citations -  6980

Makoto Fukuda is an academic researcher from Baylor College of Medicine. The author has contributed to research in topics: Leptin & Glucose homeostasis. The author has an hindex of 32, co-authored 49 publications receiving 6553 citations. Previous affiliations of Makoto Fukuda include Kyoto University & University of Texas Southwestern Medical Center.

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CRM1 is responsible for intracellular transport mediated by the nuclear export signal

TL;DR: It is shown that p110 is CRM1, which is an evolutionarily conserved protein originally found as an essential nuclear protein in fission yeast and known as a likely target of LMB, which indicates that CRM 1 is an essential mediator of the NES-dependent nuclear export of proteins in eukaryotic cells.
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Direct triggering of the type I interferon system by virus infection: activation of a transcription factor complex containing IRF‐3 and CBP/p300

TL;DR: It is demonstrated that IRF‐3 transmits a virus‐induced signal from the cytoplasm to the nucleus, and it is suggested that IRf‐3 plays an important role in the virus‐inducible primary activation of type I IFN and IFN‐responsive genes.
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Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase

TL;DR: It is shown that introduction of v‐Ras, active STE11 or constitutively active MAPKK can induce nuclear translocation of MAPK in mammalian cultured cells and evidence suggests that MAPK is localized to the cytoplasm through its specific association with MAPKK and that nuclear accumulation is accompanied by dissociation of a complex between MAPK and MAPKK following activation of the MAPK pathway.
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Nuclear export of cyclin B1 and its possible role in the DNA damage‐induced G2 checkpoint

TL;DR: It is shown that expression of the NES‐disrupted cyclin B1 or LMB treatment of the cells is able to override the DNA damage‐induced G2 checkpoint when combined with caffeine treatment, and this results suggest a role of nuclear exclusion ofCytoplasmic localization of cyclIn B1 during interphase is directed by its nuclear export signal (NES)‐dependent transport mechanism.