View source for User:MonopterusAlbus/sandbox

'''''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]].
{{Italic title}}{{Taxobox
| name = ''Monopterus albus''
| image = Monopterus albus 2.jpg
| regnum = [[Animal]]ia
| phylum = [[Chordate|Chordata]]
| classis = [[Actinopterygii]]
| ordo = [[Synbranchiformes]]
| familia = [[Synbranchidae]]
| genus = ''[[Monopterus]]''
| species = '''''M. albus'''''
| binomial = ''Monopterus albus''
| binomial_authority = ([[Vasily Zuyev|Zuiew]], 1793)
| synonyms = }}

__FORCETOC__
== Practice Editing Wikipedia ==

''The'' [[quick]] [[brown]] [[fox]] [[jumps]] '''OVER''' ''the'' [[lazy]] [[dog]]. <br />
[[User:MonopterusAlbus|MonopterusAlbus]] ([[User talk:MonopterusAlbus|talk]]) 00:25, 9 February 2013 (UTC)

== The Five Pillars of Wikipedia ==

'''1. Wikipedia is an encyclopedia.'''
This means that [[wikipedia|Wikipedia]] exhibits current, factual information from a neutral point of view. It goes beyond defining terms to explaining applications and related concepts.<br />
<br />

'''2. Wikipedia is written from a neutral point of view.'''
Many of the articles on Wikipedia contain controversial topics such as war and political policy. However, bias and opinion are not appropriate on Wikipedia. The purpose of the site is to present information that individual users can interpret. <br />
<br />
'''3. Wikipedia is free content that anyone can edit, use, modify, and distribute.'''
This statement is the reason that moderators exist. If ''everyone'' can edit ''everything'', there is the possibility of inaccuracy and abuse. This also means that Wikipedia periodically places banner ads soliciting users for donations.<br />
<br />
'''4. Editors should interact with each other in a respectful and civil manner.'''
In other words, ''be nice''.<br />
<br />
'''5. Wikipedia does not have firm rules.'''
Wikipedia consists entirely of lawless [[badlands]], like [[The Republic of Texas]].<br />
[[User:MonopterusAlbus|MonopterusAlbus]] ([[User talk:MonopterusAlbus|talk]]) 00:48, 9 February 2013 (UTC)

==Summary of Characteristics of Target Article==

{{ArticlesByQuality|custom1=User}}

Spectrum above from the page, [http://en.wikipedia.org/wiki/Category:Articles_by_quality Articles by quality]. Articles are graded using the [[Wikipedia:Version 1.0 Editorial Team|Version 1.0 Editorial Team]]'s [[WP:WVWP|Work via WikiProjects]] scheme and placed in the categories above. In order to qualify as [[Wikipedia:Version_1.0_Editorial_Team/Assessment/A-Class_criteria|A-Class]] and [[Wikipedia:GA|GA-Class]], the criteria described below must be met. 

===A-Class===

A-Class Articles have the following characteristics in common:
*appropriate length for the subject
*proper formatting
*accurate
*approaching candidacy for Featured Article status

===GA-Class===

Good Articles have the following characteristics in common:
*decent quality that is almost on par with featured articles
*nomination as a good article
*accurate, verifiable information
*well-written without noticeable errors
<br />
''For more information, visit [[Wikipedia:How to write a good article|How to write a good article]].'' <br /> <br />
[[User:MonopterusAlbus|MonopterusAlbus]] ([[User talk:MonopterusAlbus|talk]]) 00:17, 20 February 2013 (UTC)

==Practice Citations==
===Oxidized Low Density Lipoprotein===
[[LDL|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<ref name=Chatterjee>{{cite journal|title=Oxidized low density lipoprotein stimulates aortic smooth muscle cell proliferation.|journal=Glycobiology|date=1996|year=1996|month=April|volume=6|issue=3|pages=303–11|doi=10.1093/glycob/6.3.303|pmid=8724138|url=http://www.ncbi.nlm.nih.gov/pubmed/8724138|accessdate=3 March 2013|last1=Chatterjee|first1=Subroto|last2=Ghosh|first2=Nupur}}</ref>  have shown that the [[oxidized]] form of LDL (oxLDL) stimulates [[Proliferation|cellular proliferation]] in [[Smooth muscle cell|arterial smooth muscle cells]] by promoting the synthesis of the [[glycosphingolipid]] known as [[lactosylceramide]]. Inhibitors of lactosylceramide [[Lipid synthesis|synthesis]] are therefore able to mitigate both oxidized LDL production and atherosclerotic plaque formation<ref name=Chatterjee /> . With the advent of accurate high throughput screening, monoclonal antibody for this biomarker was created<ref name=Witztum>{{cite journal|title=Monoclonal autoantibodies specific for oxidized phospholipids or oxidized phospholipid-protein adducts inhibit macrophage uptake of oxidized low-density lipoproteins.|journal=The Journal of Clinical Investigation|date=1999|year=1999|month=Jan|volume=103|issue=1|pages=117–28|doi=10.1172/JCI4533|pmid=9884341|last1=Hörkkö|first1=Sohvi|last2=Bird|first2=David A.|last3=Miller|first3=Elizabeth|last4=Itabe|first4=Hiroyuki|last5=Leitinger|first5=Norbert|last6=Subbanagounder|first6=Ganesamoorthy|last7=Berliner|first7=Judith A.|last8=Friedman|first8=Peter|last9=Dennis|first9=Edward A.|last10=Curtiss|first10=Linda K.|last11=Palinski|first11=Wulf|last12=Witztum|first12=Joseph L.|pmc=407862}}</ref>  for use on the clinical level to test patients for potential development of atherosclerosis. <br/>
[[User:MonopterusAlbus|MonopterusAlbus]] ([[User talk:MonopterusAlbus|talk]]) 05:34, 3 March 2013 (UTC)

==Practice Adding Images to Wikipedia Articles==
[[File:Pten.jpg|thumb|alt=PTEN, a phosphatase.|Crystallographic structure of [[PTEN (gene)|human phosphatase and tensin homolog]] (PTEN). The [[N-terminus|N-terminal]] phosphatase domain is colored blue while the [[C-terminus|C-terminal]] [[C2 domain]] is colored red. The [[active site]] within the phosphatase is shown in yellow.<ref name="pmid10555148">{{PDB|1d5r}}; {{cite journal | author = Lee JO, Yang H, Georgescu MM, Di Cristofano A, Maehama T, Shi Y, Dixon JE, Pandolfi P, Pavletich NP | title = Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association | journal = Cell | volume = 99 | issue = 3 | pages = 323–34 | year = 1999 | date = October 1999 | pmid = 10555148 | doi = 10.1016/S0092-8674(00)81663-3  | s2cid = 5624414 | url = | issn = }}</ref>]]
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 Article in Sandbox==
'''Dephosphorylation''' is the removal of a [[phosphate]] (PO<sub>4</sub><sup>3-</sup>) group from an [[organic compound]] by [[hydrolysis]]. It is a reversible [[posttranslational modification|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.

==Function==

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. 

=== Posttranslational Modification===
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<ref name="pmid8987393">{{cite journal |author=Barford D |title=Molecular mechanisms of the protein serine/threonine phosphatases |journal=Trends Biochem. Sci. |volume=21 |issue=11 |pages=407–12 |year=1996 |date=November 1996 |pmid=8987393 |doi= 10.1016/s0968-0004(96)10060-8|url=}}</ref>.

===ATP===
''Main article: [[adenosine triphosphate]]''

 ATP<sup>4-</sup> + H<sub>2</sub>O --> ADP<sup>3-</sup> + HPO<sub>4</sub><sup>2-</sup> + H<sup>+</sup>

[[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.<ref>{{cite web|last=Casiday|first=Rachel|title=Energy for the Body: Oxidative Phosphorylation|url=http://www.chemistry.wustl.edu/~edudev/LabTutorials/Cytochromes/cytochromes.html|accessdate=5 April 2013}}</ref>

===Dephosphorylation in other reactions===
Other molecules besides ATP undergo dephosphorylation as part of other biological systems. Different compounds produce different free energy changes as a result of dephosphorylation

{| class="wikitable"
|-
! 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
|}

==Research Applications==
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.<ref name="Cloning manual">{{cite book|last=Sambrook|first=J|title=Molecular Cloning: A Laboratory Manual|year=1989|publisher=Cold Spring Harbor Laboratory Press|edition=2nd|coauthors=Fritsch, E.F., Maniatis, T.}}</ref> These alkaline phosphatases are often sourced naturally, most commonly from calf intestine, and are abbreviated as [[Calf-intestinal alkaline phosphatase|CIP]].<ref name="pmid19838171">{{cite journal |author=Makovets S, Blackburn EH |title=DNA damage signalling prevents deleterious telomere addition at DNA breaks |journal=Nat. Cell Biol. |volume=11 |issue=11 |pages=1383–6 |year=2009 |date=November 2009 |pmid=19838171 |pmc=2806817 |doi=10.1038/ncb1985 |url=}}</ref>


==History==
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.<ref name="pmid38740">{{cite journal |author=Krebs EG, Beavo JA |title=Phosphorylation-dephosphorylation of enzymes |journal=Annu. Rev. Biochem. |volume=48 |issue= |pages=923–59 |year=1979 |pmid=38740 |doi=10.1146/annurev.bi.48.070179.004423 |url=}}</ref> [[Edwin G. Krebs|Edwin Krebs]] and [[Edmond H. Fischer|Edmond Fischer]] won the 1992 [[Nobel Prize in Physiology or Medicine]] for the discovery of reversible protein phosphorylation.<ref name="pmid10859071">{{cite journal |author=Raju TN |title=The Nobel chronicles. 1992: Edmond H Fischer (b 1920) and Edwin G Krebs (b 1918) |journal=Lancet |volume=355 |issue=9219 |pages=2004 |year=2000 |date=June 2000 |pmid=10859071 |doi= 10.1016/s0140-6736(05)72951-2|s2cid=54322974 |url=}}</ref>

== See also ==
[[Phosphatase]]
[[Phosphorylation]]

==References==
 <references />

==External links==
{{Protein posttranslational modification}}

[[:Category:Biochemistry]]
[[:Category:Cell biology]]
[[:Category:Signal transduction]]
[[:Category:Posttranslational modification]]
[[:Category:Phosphorus]]