Common elements persist throughout the series and its spinoff games: turn-based combat recurring monsters, including the Slime, which became the series' mascot a text-based menu system and random encounters in most of the main series. The basic premise of most Dragon Quest games is to play a hero (actually named "Hero" in spinoff fiction, but in some games, the player is able to name their hero) who is out to save the land from peril at the hands of a powerful evil enemy, with the hero usually accompanied by a group of party members. Square Enix did not register the Dragon Quest trademark for use in the United States until 2002. Early in the series, the Dragon Quest games were released under the title Dragon Warrior in North America to avoid trademark conflict with the unrelated tabletop role-playing game DragonQuest. Installments of the series have appeared on various computers, consoles, handheld devices, and mobile phones. The series introduced a number of features to the genre and has had a significant impact on the development of other role-playing games. In addition, there have been numerous manga, anime and novels published under the franchise, with nearly every game in the main series having a related adaptation. With its first game published in 1986, there are eleven main-series games, along with numerous spin-off games. The games are published by Square Enix (formerly Enix) since its inception, with localized remakes and ports of later installments for the Nintendo DS, Nintendo 3DS, and Nintendo Switch being published by Nintendo outside of Japan. Dragon Quest, previously published as Dragon Warrior in North America until 2005, is a franchise of Japanese role-playing video games created by Armor Project ( Yuji Horii), Bird Studio ( Akira Toriyama) and Sugiyama Kobo ( Koichi Sugiyama) to its publisher Enix, with all of the involved parties co-owning the copyright of the series since then.
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In this study, we hypothesize that free cellular uptake is mediated by binding and activation of the EGFR by boron clusters. Proteomic analysis of proteins pulled-down from various EGFR-overexpressing cancer cells using short oligonucleotide probes, conjugated to 1,2-dicarba- closo-dodecaborane (1,2-DCDDB, ) and (FESAN, −), evidenced that boron cage binds to EGFR subdomains. Moreover, inductively coupled plasma mass spectrometry (ICP MS) and fluorescence microscopy analyses confirmed that FESANs-highly decorated B-ASOs were efficiently delivered and internalized by EGFR-overexpressing cells. 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Anagram Twist - Jumble and Unscramble Text |
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