Spyro (series)

Spyro is a series of platform games which primarily features the protagonist Spyro the Dragon and his friend, Sparx the Dragonfly. Since its introduction in 1998, there has been a complete reboot to the series called The Legend of Spyro trilogy, making it a total of ten Spyro games and three Legend of Spyro games. The Spyro series has sold more than 20 million units worldwide. After The Legend of Spyro series concluded, a spin-off franchise under the name of Skylanders was made where Spyro and other related characters were included in.

Games

Spyro the Dragon

Spyro the Dragon was first released in North America on 11 September 1998, for the PlayStation. It was released in Europe on 23 October 1998, In Australia on 15 November 1998 and in Japan on 1 April 1999. It is a platform game that placed the player as Spyro, a small, purple dragon set with the task of freeing his fellow dragons from crystal prisons, which are scattered around their world. Each level is accessed through 'portals' from a main world. The game concludes with a fight between Spyro and the primary antagonist, Gnasty Gnorc. The game sold well, most critics giving it favorable reviews. It also received acclaim for its musical score by Stewart Copeland.

Hunter (2015 film)

Hunter is a 2015 film directed by Gregory Hatanaka and starring Ron Becks with Magda Marcella, Kristine DeBell, George Lazenby and Laurene Landon. It follows the exploits of a veteran cop who must hunt down a cop killer as well as a female teenage serial killer.

Cast

External links

Watcher (Highlander)

Watchers is a secret organization that watches the Immortals in Highlander: The Series and all subsequent related series and movies.

They were introduced in the season 1 finale as a cliffhanger for the subsequent season. Since then, they became an integral part of the series and Duncan MacLeod's adventures.

Appearances

In "The Watchers", Joe Dawson explains the purpose of the Watchers to Duncan MacLeod: "For as long as your kind's been around, we've been watching ... We observe, we record, but we never interfere... Too much of man's history has been lost. When you get through all of life's crap, the only thing that matters is the truth. We want the truth about Immortals to survive, not a bunch of old wives' tales... If we had revealed your secret in more superstitious times, you can imagine the witch hunts... And today... You'd probably end up on page three in one of those supermarket rags next to the two-headed monkey and I'd've been in a straight jacket."

The Watchers is a secret society of mortal humans that observes the lives of the Immortals without revealing themselves. While the Watchers seem to have the resources to function independently, there are Watchers like Joe Dawson who run their own businesses to provide a cover as well as income. Each Immortal is assigned a Watcher whose sole job is to monitor and record daily activities. The network of Watchers generally keeps careful tabs on subjects and tracks even the casual movements of the Immortals. Most Immortals are unaware of the Watchers. The organization was created by Ammaletu, the Akkadian, after he saw Gilgamesh coming back to life. In early episodes all Watchers wore a medallion of the symbol of their organization. In later episodes, each Watcher has the symbol tattooed on the inner wrist.

UFM1

Ubiquitin-fold modifier 1, also known as UFM1, is a protein which in humans is encoded by the UFM1 gene.

UFM1 is a ubiquitin-like protein that is conjugated to target proteins by E1-like activating enzyme UBA5 (UBE1DC1) and E2-like conjugating enzyme UFC1 (see UBE2M).

Function

UFM1 shares several common properties with ubiquitin (Ub) and other ubiquitin-like molecules (UBLs). Ufm1 has similar tertiary structure to Ub but lacks any obvious sequence similarity. It is synthesized as an inactive precursor form (pro-Ufm1) which has 2 additional amino acids beyond the conserved glycine. The mechanism of Ufm1 conjugation is similar to that of ubiquitin. Mature Ufm1 has an exposed C-terminal glycine which is essential for subsequent activation by its cognate E1 protein (Uba5). This activation step results in the formation of a high-energy thiolester bond in the presence of ATP. The Ufm1 is subsequently transferred to its cognate E2-like enzyme (Ufc1) via a similar thioester linkage with a cysteine at the E2 active site. Ufm1 is conjugated to a variety of target proteins and forms complexes with as yet unidentified proteins. Thus, presumably there exist E3 ligases (none have been identified to date) to perform the final step in Ufm1 conjugation to relevant targets. The modification of proteins with Ufm1 is also reversible. Two novel cysteine proteases have been identified to date (UFSP1 and UFSP2) which cleave Ufm1-peptide C-terminal fusions and also removes Ufm1 from native intracellular conjugates. These proteases have no obvious homology to ubiquitin deconjugating enzymes. The proteins for Ufm1 conjugation (Uba5, Ufc1 and Ufm1) are all conserved in animals and plants (but not yeast) suggesting important roles in multicellular organisms. The exact role of Ufm1 modification in vivo is not yet known.