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        Flow recovery after posterior clinoidectomy for surgical clipping of anterior choroidal aneurysm

        Federico Carlos Gallardo,Juan Santiago Bottan,Clara Martin,Aylen Andrea Targa Carcia,Roman Pablo Arevalo,Pablo Augusto Rubino 대한뇌혈관외과학회 2021 Journal of Cerebrovascular and Endovascular Neuros Vol.23 No.4

        Inadvertent flow alterations in the parent artery during microsurgical clipping might produce postoperative ischemic complications. Intraoperative recognition of such alterations and its correction might improve operative outcomes in these patients. We present the case of a thirty-five-year-old male with an incidental small left anterior choroidal aneurysm. Microsurgical clipping induced an external compression of the anterior choroidal artery against the posterior clinoidal process which was identified in situ through surgical exploration and the loss of arterial doppler signal in the vessel. After failed attempts at clip repositioning, a posterior clinoidectomy was performed to decompress the artery. This resulted in arterial flow recovery. The aneurysm was successfully treated, and a severe ischemic complication was likely avoided. This intraoperative phenomenon has not yet been described in the literature.

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        Ankyrin Repeat-Rich Membrane Spanning/Kidins220 Protein Interacts with Mammalian Septin 5

        Han Jeong Park,박환우,이신재,Juan Carlos Arevalo,박영석,이승표,Ki-Suk Paik,Moses V. Chao,장미숙 한국분자세포생물학회 2010 Molecules and cells Vol.30 No.2

        Neurotrophin receptors utilize specific adaptor proteins to activate signaling pathways involved in various neuronal functions, such as neurite outgrowth and cytoskeletal re-modeling. The Ankyrin-Repeat Rich Membrane Spanning (ARMS)/kinase D-interacting substrate-220 kDa (Kidins220) serves as a unique downstream adaptor protein of Trk receptor tyrosine kinases. To gain insight into the role of ARMS/Kidins220, a yeast two-hybrid screen of a rat dorsal root ganglion library was performed using the C-terminal region of ARMS/Kidins220 as bait. The screen identified a mammalian septin, Septin 5 (Sept5), as an interacting pro-tein. Co-immunoprecipitation using lysates from tran-siently transfected HEK-293 cells revealed the specific interaction between ARMS/Kidins220 and Sept5. Endoge-nous ARMS/Kidins220 and Sept5 proteins were co-localized in primary hippocampal neurons and were also predominantly expressed at the plasma membrane and in the tips of growing neurites in nerve growth factor-treated PC12 cells. Mapping of Sept5 domains important for ARMS/Kidins220 binding revealed a highly conserved N-terminal region of Sept5. The direct interaction between ARMS/Kidins220 and Sept5 suggests a possible role of ARMS/Kidins220 as a functional link between neurotrophin receptors and septins to mediate neurotrophin-induced intracellular signaling events, such as neurite outgrowth and cytoskeletal remodeling.

      • KCI등재

        Ankyrin Repeat-Rich Membrane Spanning/Kidins220 Protein Interacts with Mammalian Septin 5

        Park, Han-Jeong,Park, Hwan-Woo,Lee, Shin-Jae,Arevalo, Juan Carlos,Park, Young-Seok,Lee, Seung-Pyo,Paik, Ki-Suk,Chao, Moses V.,Chang, Mi-Sook Korean Society for Molecular and Cellular Biology 2010 Molecules and cells Vol.30 No.2

        Neurotrophin receptors utilize specific adaptor proteins to activate signaling pathways involved in various neuronal functions, such as neurite outgrowth and cytoskeletal remodeling. The Ankyrin-Repeat Rich Membrane Spanning (ARMS)/kinase D-interacting substrate-220 kDa (Kidins220) serves as a unique downstream adaptor protein of Trk receptor tyrosine kinases. To gain insight into the role of ARMS/Kidins220, a yeast two-hybrid screen of a rat dorsal root ganglion library was performed using the C-terminal region of ARMS/Kidins220 as bait. The screen identified a mammalian septin, Septin 5 (Sept5), as an interacting protein. Co-immunoprecipitation using lysates from transiently transfected HEK-293 cells revealed the specific interaction between ARMS/Kidins220 and Sept5. Endogenous ARMS/Kidins220 and Sept5 proteins were colocalized in primary hippocampal neurons and were also predominantly expressed at the plasma membrane and in the tips of growing neurites in nerve growth factor-treated PC12 cells. Mapping of Sept5 domains important for ARMS/Kidins220 binding revealed a highly conserved N-terminal region of Sept5. The direct interaction between ARMS/Kidins220 and Sept5 suggests a possible role of RMS/Kidins220 as a functional link between neurotrophin receptors and septins to mediate neurotrophin-induced intracellular signaling events, such as neurite outgrowth and cytoskeletal remodeling.

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