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mTOR/RAFT1/FRAP is the target of the immunosuppressive drug rapamycin and the central component of a nutrient- and hormone-sensitive signaling pathway that regulates cell growth. We report that mTOR forms a stoichiometric complex with raptor, an evolutionarily conserved protein with at least two roles in the mTOR pathway. Raptor has a positive role in(More)
(2013) Global, 30-m resolution continuous fields of tree cover: Landsat-based rescaling of MODIS vegetation continuous fields with lidar-based estimates of error, Taylor & Francis makes every effort to ensure the accuracy of all the information (the " Content ") contained in the publications on our platform. Taylor & Francis, our agents, and our licensors(More)
The mammalian TOR (mTOR) pathway integrates nutrient- and growth factor-derived signals to regulate growth, the process whereby cells accumulate mass and increase in size. mTOR is a large protein kinase and the target of rapamycin, an immunosuppressant that also blocks vessel restenosis and has potential anticancer applications. mTOR interacts with the(More)
In this paper, we report some important results of design and evaluation of a wheelchair-based robotic arm system, named as KARES II (KAIST Rehabilitation Engineering Service System II), which is newly developed for the disabled. KARES II is designed in consideration of surveyed necessary tasks for the target users (that is, people with spinal cord injury).(More)
The loudness dependence of auditory evoked potentials (LDAEP) has been proposed as a reliable indicator of central serotonin system activity in animal and some human studies. Since low central serotonergic activity is related to suicidality, it is possible that the LDAEP can be used to predict suicidality. The aim of the present study was to determine(More)
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Amino acids stimulate cell growth and suppress autophagy through activation of mTORC1. The activation of mTORC1 by amino acids is mediated by Rag guanosine triphosphatase (GTPase) heterodimers on the lysosome. The molecular mechanism by which amino acids regulate the Rag GTPase heterodimers remains to be elucidated. Here, we identify SH3 domain-binding(More)