Creative Commons International The International License Porting Project

When Creative Commons (CC) was founded in 2001, the core Creative Commons licenses were drafted according to United States Copyright Law. Since their first introduction in December 2002, Creative Commons licenses have been enthusiastically adopted by many creators, authors, and other content producers – not only in the United States, but in many other jurisdictions as well. Global interest in the CC licenses prompted a discussion about the need for national versions of the CC licenses. To best address this need, the international license porting project (“Creative Commons International” – formerly known as “International Commons”) was launched in 2003. Creative Commons International works to port the core Creative Commons licenses to different copyright legislations around the world. The porting process includes both linguistically translating the licenses and legally adapting the licenses to a particular jurisdiction such that they are comprehensible in the local jurisdiction and legally enforceable but concurrently retain the same key elements. Since its inception, Creative Commons International has found many supporters all over the world. With Finland, Brazil, and Japan as the first completed jurisdiction projects, experts around the globe have followed their lead and joined the international collaboration with Creative Commons to adapt the licenses to their local copyright. This article aims to present an overview of the international porting process, explain and clarify the international license architecture, its legal and promotional aspects, as well as its most recent challenges

Myokardiale Dysfunktion am Reanimationsmodell bei vorerkrankten Tieren: Auswirkung von milder Hypothermie und Sevoflurane

Tierversuchsmodell. Reanimation von Schweinen und Postreanimationstherapie dieser mit Hypothermie und Sevoflura

SARS-CoV-2 M^pro responds to oxidation by forming disulfide and NOS/SONOS bonds

The main protease (Mpro) of SARS-CoV-2 is critical for viral function and a key drug target. Mpro is only active when reduced; turnover ceases upon oxidation but is restored by re-reduction. This suggests the system has evolved to survive periods in an oxidative environment, but the mechanism of this protection has not been confirmed. Here, we report a crystal structure of oxidized Mpro showing a disulfide bond between the active site cysteine, C145, and a distal cysteine, C117. Previous work proposed this disulfide provides the mechanism of protection from irreversible oxidation. Mpro forms an obligate homodimer, and the C117-C145 structure shows disruption of interactions bridging the dimer interface, implying a correlation between oxidation and dimerization. We confirm dimer stability is weakened in solution upon oxidation. Finally, we observe the protein’s crystallization behavior is linked to its redox state. Oxidized Mpro spontaneously forms a distinct, more loosely packed lattice. Seeding with crystals of this lattice yields a structure with an oxidation pattern incorporating one cysteine-lysine-cysteine (SONOS) and two lysine-cysteine (NOS) bridges. These structures further our understanding of the oxidative regulation of Mpro and the crystallization conditions necessary to study this structurally