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Off or OFF may refer to:
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Off! is an American hardcore punk supergroup, formed in Los Angeles in 2009.
Off! was formed in Los Angeles, California in late 2009 by Circle Jerks/Black Flag singer Keith Morris, Burning Brides frontman Dimitri Coats, Redd Kross bassist Steven Shane McDonald, and Rocket From The Crypt/Hot Snakes drummer Mario Rubalcaba. The idea to form the band came after Coats had worked as producer on a Circle Jerks album which fell apart. During that time, Coats and Morris had written several songs together which they used to start Off!. The group made its live debut at the 2010 South By Southwest Music Festival in Austin, Texas. Off!'s first Los Angeles show featured an original art installation by Raymond Pettibon at a downtown warehouse space.
The first release by Off! is a 7" vinyl EP called 1st EP, which debuted on October 13, 2010. That EP, along with three more EPs, were later released as a four 7" vinyl box set entitled First Four EPs on December 14, 2010. The collection contains sixteen songs and features artwork by Raymond Pettibon.
Environment variables are a set of dynamic named values that can affect the way running processes will behave on a computer.
They are part of the environment in which a process runs. For example, a running process can query the value of the TEMP environment variable to discover a suitable location to store temporary files, or the HOME or USERPROFILE variable to find the directory structure owned by the user running the process.
They were introduced in their modern form in 1979 with Version 7 Unix, so are included in all Unix operating system flavors and variants from that point onward including Linux and OS X. From PC DOS 2.0 in 1982, all succeeding Microsoft operating systems including Microsoft Windows, and OS/2 also have included them as a feature, although with somewhat different syntax, usage and standard variable names.
In all Unix and Unix-like systems, each process has its own separate set of environment variables. By default, when a process is created, it inherits a duplicate environment of its parent process, except for explicit changes made by the parent when it creates the child. At the API level, these changes must be done between running fork
and exec
. Alternatively, from command shells such as bash, a user can change environment variables for a particular command invocation by indirectly invoking it via env
or using the ENVIRONMENT_VARIABLE=VALUE <command>
notation. All Unix operating system flavors, DOS, and Windows have environment variables; however, they do not all use the same variable names. A running program can access the values of environment variables for configuration purposes.
Superoxide dismutase [Cu-Zn] also known as superoxide dismutase 1 or SOD1 is an enzyme that in humans is encoded by the SOD1 gene, located on chromosome 21. SOD1 is one of three human superoxide dismutases. It is implicated in apoptosis and amyotrophic lateral sclerosis.
SOD1 is a 32 kDa homodimer which forms a β-barrel and contains an intramolecular disulfide bond and a binuclear Cu/Zn site in each subunit. This Cu/Zn site holds the copper and a zinc ion and is responsible for catalyzing the disproportionation of superoxide to hydrogen peroxide and dioxygen. The maturation process of this protein is complex and not fully understood, involving the selective binding of copper and zinc ions, formation of the intra-subunit disulfide bond between Cys-57 and Cys-146, and dimerization of the two subunits. The copper chaperone for Sod1 (CCS) facilitates copper insertion and disulfide oxidation. Though SOD1 is synthesized in the cytosol can mature there, the fraction of expressed, and still immature, SOD1 targeted to the mitochondria must be inserted into the intermembrane space. There, it forms the disulfide bond, though not metallation, required for its maturation. The mature protein is highly stable, but unstable when in its metal-free and disulfide-reduced forms. This manifests in vitro, as the loss of metal ions results in increased SOD1 aggregation, and in disease models, where low metallation is observed for insoluble SOD1. Moreover, the surface-exposed reduced cysteines could participate in disulfide crosslinking and, thus, aggregation.
Superoxide dismutase 2, mitochondrial (SOD2), also known as manganese-dependent superoxide dismutase (MnSOD), is an enzyme which in humans is encoded by the SOD2 gene on chromosome 6.
The SOD2 gene contains five exons interrupted by four introns, an uncharacteristic 5′-proximal promoter that possesses a GC-rich region in place of the TATA or CAAT, and an enhancer in the second intron. The proximal promoter region contains multiple binding sites for transcription factors, including specific-1 (Sp1), activator protein 2 (AP-2), and early growth response 1 (Egr-1). This gene is a the mitochondrial member of the iron/manganese superoxide dismutase family. It encodes a mitochondrial matrix protein that forms a homotetramer and binds one manganese ion per subunit. The manganese site forms a trigonal bipyramidal geometry with four ligands from the protein and a fifth solvent ligand. This solvent ligand is a hydroxide believed to serve as the electron acceptor of the enzyme. The active site cavity consists of a network of side chains of several residues associated by hydrogen bonding, extending from the aqueous ligand of the metal. Of note, the highly conserved residue Tyr34 plays a key role in the hydrogen-bonding network, as nitration of this residue inhibits the protein's catalytic ability. This protein also possesses an N-terminal mitochondrial leader sequence which targets it to the mitochondrial matrix, where it converts mitochondrial-generated reactive oxygen species from the respiratory chain to H2.Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Extracellular superoxide dismutase [Cu-Zn] is an enzyme that in humans is encoded by the SOD3 gene.
This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.
SMA may refer to:
I know I've been tolerant 'til now,
But here comes a warning,
There's a very clear line that i'm drawing,
And if you cross it.
Sod off
Sod off
If you think I'll let you pull me down to
Your third-class communication,
And bulldoze over all my sensitivities
You've read me all wrong.
Sod off
Sod off
Sod off
Sod off
Things so far,
Have been too perfect
This is the premiere
But, oh, how many dress rehearsals
I've been through
Darling this is far too pure and perfect
I let you corrupt it.
Sod off!
I wont let you ruin this.
Sod off.
Sod off.
Sod off.
Sod off.