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성해경,박종태,노진수,이강현 조선대학교 에너지.자원신기술연구소 2002 에너지·자원신기술연구소 논문지 Vol.24 No.2
Blowfish is a symmetric block cipher that can be used as a drop-in replacement for DES or IDEA. It takes a variable-length key, from 32bits to 448bits, making it ideal for both domestic and exportable use. In this paper, the Blowfish unit is designed using pipeline architecture and correctly implements the algorithm with a focus on ease-of-design and ease-of-use without sacrificing too much speed or size. For the real time process of Blowfish, it is required that high-speed operation and small size hardware. So, the scheme of new adders designed has all advantages abstracted from other adders. As a result of this new adder designed, area cost increases by 1.05 times but the operation speed increases by 1.2 times.
Jin Rhee, Hae,Nam, Ju-Suk,Sun, Yuanje,Kim, Min-Jung,Choi, Ho-Kyew,Han, Dong-Hun,Kim, Nam-Ho,Huh, Sung-Oh Lippincott Williams Wilkins, Inc. 2006 NEUROREPORT - Vol.17 No.5
cAMP response element-binding protein (CREB) has been known to play a pivotal role in neuronal differentiation and neuronal plasticity. Lysophosphatidic acid (LPA) was reported to activate CREB in Rat2 fibroblast cells. To study the roles of LPA in neuronal differentiation, we determined whether LPA activates CREB in H19-7, hippocampal progenitor cells. LPA induced three-fold increase in cAMP level in a pertussis toxin-independent manner. Moreover, LPA stimulated CREB phosphorylation, which was inhibited by not only H89 but also Rp-cAMP. In H19-7 cells, high-level expression of lpa1 and moderate-level expression of lpa4 were detected, whereas any detectible expression of lpa2 or lpa3 was not detected by reverse transcription polymerase chain reaction. Together, these data suggested that LPA potentiates cAMP accumulation through activating Gs, and thereby, LPA can stimulate cAMP-CREB signaling cascade.
Hae Jin Rhee,Liting Ji,김남호,Sung-Oh Huh 한국분자세포생물학회 2016 Molecules and cells Vol.39 No.6
The corpus callosum is a bundle of nerve fibers that con-nects the two cerebral hemispheres and is essential for coordinated transmission of information between them. Disruption of early stages of callosal development can cause agenesis of the corpus callosum (AgCC), including both complete and partial callosal absence, causing mild to severe cognitive impairment. Despite extensive studies, the etiology of AgCC remains to be clarified due to the complicated mechanism involved in generating AgCC. The biological function of PI3K signaling including phosphatidylinositol-3,4,5-trisphosphate is well established in diverse biochemical processes including axon and dendrite morphogenesis, but the function of the closely related phosphatidylinositol-3,4,-bisphosphate (PI(3,4)P2) signaling, particularly in the nervous system, is largely unknown. Here, we provide the first report on the role of inositol polyphosphate 4-phosphatase II (INPP4B), a PI(3,4)P2 metabolizing 4-phosphatase in the regulation of callosal axon formation. Depleting INPP4B by in utero electroporation suppressed medially directed callosal axon formation. Moreover, depletion of INPP4B significantly attenuated formation of Satb2-positive pyramidal neurons and axon polarization in cortical neurons during cortical development. Taken together, these data suggest that INPP4B plays a role in the regulating callosal axon formation by controlling axon polarization and the Satb2-positive pyramidal neuron population. Dysregulation of INPP4B during cortical development may be implicated in the generation of partial AgCC.
Translocation of Annexin I to the Nucleus by Epidermal Growth Factor in A549 Cells
Rhee, Hae-Jin,Kim, Seung-Wook,Soo-Ok, Lee,Park, Young-Min,Na, Doe-Sun Korean Society for Biochemistry and Molecular Biol 1999 Journal of biochemistry and molecular biology Vol.32 No.1
Annexin I (also called lipocortin 1), a 37-kDa member of the annexin family of proteins, has been implicated in the mitogenic signal transduction by epidermal growth factor (EGF). Annexin I is phosphorylated by the EGF signal, however, the role of annexin I in the EGF signal transduction is still unknown. To transduce extracellular signals into the intracellular targets, selective translocation of the signaling molecules to their targets would be necessary. In this study, we examined the subcellular locations of annexin I during EGF signal transduction. Treatment of A549 cells with EGF resulted in the translocation of cytoplasmic annexin I to the nucleus and perinuclear region as determined by Western blot and immunofluorescent staining. The nuclear translocation of annexin I was inhibited by tyrphostin AG 1478 and genistein, the inhibitors of EGF receptor kinase and downstream tyrosine kineses, respectively. Pretreatment of cells with cyclohexamide did not inhibit the nuclear translocation. The results suggest that nuclear translocation of annexin I is controlled by a series of kinase dependent events in the EGF receptor signaling pathway and may be important in tranducing the signals by EGF.