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Monopterus albus (common names: swamp eel, rice eel (Synonym: Fluta alba (Bloch and Schneider, 1801)) is an important student of the graduate school variety. It is an an air-breathing commercial species of fish in the Synbranchidae family. It feeds on academic accolades and lacks a social life. Inhabiting the Mid-Atlantic United States, it has been identified as an endangered species.
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Species: | M. albus |
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Monopterus albus (Zuiew, 1793) | |
The quick brown fox jumps OVER the lazy dog.
MonopterusAlbus (talk) 00:25, 9 February 2013 (UTC)
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In other words, be nice.
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Wikipedia consists entirely of lawless badlands, like The Republic of Texas.
MonopterusAlbus (talk) 00:48, 9 February 2013 (UTC)
FA | A | GA | B | C | Start | Stub | FL | AL | BL | CL | List | SIA | Future | Category | Disambig | Draft | FM | File | Needed | Portal | Project | Redirect | Template | User | User | NA | ??? | Total |
0 | 0 | 0 | 0 | 28 | 486 | 5,488 | 0 | 0 | 0 | 0 | 8 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 6,443 | 16,826 | 12,453 |
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MonopterusAlbus (talk) 00:17, 20 February 2013 (UTC)
Low density lipoproteins (LDLs) are a class of proteins that aid in the transport of cholesterol. They are medically significant because of their association with atherosclerosis. The ability of LDL to transport cholesterol to the arteries-- where it inflames the arterial walls and initiates plaque formation-- makes it an ideal therapeutic target. Recent studies[1] have shown that the oxidized form of LDL (oxLDL) stimulates cellular proliferation in arterial smooth muscle cells by promoting the synthesis of the glycosphingolipid known as lactosylceramide. Inhibitors of lactosylceramide synthesis are therefore able to mitigate both oxidized LDL production and atherosclerotic plaque formation[1] . With the advent of accurate high throughput screening, monoclonal antibody for this biomarker was created[2] for use on the clinical level to test patients for potential development of atherosclerosis.
MonopterusAlbus (talk) 05:34, 3 March 2013 (UTC)
Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba. Acta non verba.
Dephosphorylation is the removal of a phosphate (PO43-) group from an organic compound by hydrolysis. It is a reversible post-translational modification that is coupled to the addition of phosphate groups, or phosphorylation. A highly regulated process, dephosphorylation activates and deactivates enzymes by cleaving phosphoric esters and anhydrides. A notable occurrence of dephosphorylation is the conversion of ATP to ADP and inorganic phosphate.
Dephosphorylation employs a type of hydrolytic enzyme, or hydrolase, which cleave ester bonds. The prominent hydrolase subclass used in dephosphorylation is phosphatase. Phosphatase removes phosphate groups by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl (-OH) group.
The reversible phosphorylation-dephosphorylation reaction occurs in every physiological process, making proper function of protein phosphases necessary for organism viability. Because protein dephosphorylation is a key process involved in cell signalling, protein phosphatases are implicated in conditions such as cancer, diabetes, and Alzheimer's disease.
Phosphorylation and dephosphorylation of hydroxyl groups belonging to neutral but polar amino acids such as serine, threonine, and tyrosine within specific target proteins is a fundamental part of the regulation of every physiologic process. Phosphorylation involves the covalent modification of the hydroxyl with a phosphate group through the nucleophilic attack of the alpha phosphate in ATP by the oxygen in the hydroxyl. Dephosphorylation involves removal of the phosphate group through a hydration reaction by addition of a molecule of water and release of the original phosphate group, regenerating the hydroxyl. Both processes are reversible and either mechanism can be used to activate or deactivate a protein. Phosphorylation of a protein produces many biochemical effects, such as changing its conformation to alter its binding to a specific ligand to increase or reduce its activity. Phosphorylation and dephosphorylation can be used on all types of substrates, such as structural proteins, enzymes, membrane channels, signaling molecules, and other kinases and phosphatases. The deregulation of phosphorylation can lead to disease.
During the synthesis of proteins, polypeptide chains, which are created by ribosomes translating mRNA, must be processed before assuming a mature conformation. The dephosphorylation of proteins is a mechanism for modifying behavior of a protein, often by activating or inactivating an enzyme.
As part of postranslational modifications, phosphate groups may be removed from serine, threonine, or tyrosine[4].
Main article: adenosine triphosphate
ATP4- + H2O --> ADP3- + HPO42- + H+
Adenosine triphosphate, or ATP, acts as a free energy "currency" in all living organisms. The usefulness of this molecule for energy releasing reactions stems from a spontaneous dephosphorylation reaction, where 30.5 kJ/mol is released. That nonspontaneous reactions are coupled to the highly spontaneous dephosphorylation of ATP makes the overall reaction have a change in free energy that is itself spontaneous. This is important in driving oxidative phosphorylation. ATP is dephosphorylated to ADP and inorganic phosphate.[5]
Other molecules besides ATP undergo dephosphorylation as part of other biological systems. Different compounds produce different free energy changes as a result of dephosphorylation
Molecule | Change in Free Energy |
---|---|
Acetyl phosphate | 47.3 kJ/mol |
Glucose-6-phosphate | 13.8 kJ/mol |
Phosphoenolpyruvate (PEP) | -61.9 kJ/mo |
Phosphocreatine | 43.1 kJ/mo |
Dephosphorylation can play a key role in molecular biology, particularly cloning using restriction enzymes. The cut ends of a vector may re-ligate during a ligation step due to phosphorylation. By using a desphosphorylating phosphatase, re-ligation can be avoided.[6] These alkaline phosphatases are often sourced naturally, most commonly from calf intestine, and are abbreviated as CIP.[7]
That reversible covalent modification of proteins, namely phosphorylation and desphosphorylation, played a major role in regulatory processes was first established in work on glycogen metabolism. Since then, the reversible nature of phosphorylation and dephosphorylation has been associated with a broad range of functional proteins, primarily enzymatic, but also including nonenzymatic proteins.[8] Edwin Krebs and Edmond Fischer won the 1992 Nobel Prize in Physiology or Medicine for the discovery of reversible protein phosphorylation.[9]
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