Talk:Antipain

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Wiki Education Foundation-supported course assignment

This article was the subject of a Wiki Education Foundation-supported course assignment, between 27 January 2020 and 8 May 2020. Further details are available on the course page. Student editor(s): Wendtiga.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 17:26, 17 January 2022 (UTC)[reply]

Wiki Education Foundation-supported course assignment

This article was the subject of a Wiki Education Foundation-supported course assignment, between 1 September 2021 and 6 December 2021. Further details are available on the course page. Student editor(s): Quokkaz.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 17:26, 17 January 2022 (UTC)[reply]

Ovid

Publius Ovidius Naso published a paper about Nelfinavir?? What an hoax ...

Radix--2003:F5:EF0C:8456:4893:76EF:33B8:5EF4 (talk) 16:27, 25 June 2021 (UTC)[reply]

Sections removed

I removed a couple of sections from the article and placed them here (below). Much of this content is inconsistent, contradictory, confusing, and/or just plain wrong. The probelm is probably related to the school assignment described above. A few examples:

"Protease inhibitors or antipain are enzymes" - antipain is not an enzyme
"a study published by Ovid" - Ovid lived 2000 years ago
"Antipain is a protease inhibitor ... and is well-against to cathepsin A" - what does that even mean?
"DRUG neurons" - what are drug neurons? (why DRUG neurons, not drug neurons?)

If anyone can make sense of it, correct it, and fix the poor writing then it can be added back into the article.

In addition, the remaining content of the article should be checked for accuracy. Marbletan (talk) 19:43, 25 January 2024 (UTC)[reply]

== Antiretroviral and protease inhibitors ==
There are several [[serine proteases]], which are enzymes that cleave the protein bond, in the [[human genome]]. [[Protease|Proteases]] are ubiquitous. Protease function is also affected by [[Endogeny (biology)|endogenous]] inhibitors.<ref>{{Cite book| vauthors = Dhalla NS |title=Role of Proteases in Cellular Dysfunction|publisher=New York, NY : Springer New York : Imprint: Springer|year=2014|pages=3–15}}</ref> The abnormal functioning of these proteases can lead to the development of cancerous tumors.<ref>{{cite journal | vauthors = Quesada V, Ordóñez GR, Sánchez LM, Puente XS, López-Otín C | title = The Degradome database: mammalian proteases and diseases of proteolysis | journal = Nucleic Acids Research | volume = 37 | issue = Database issue | pages = D239–D243 | date = January 2009 | pmid = 18776217 | pmc = 2686449 | doi = 10.1093/nar/gkn570 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Mariño G, Uría JA, Puente XS, Quesada V, Bordallo J, López-Otín C | title = Human autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy | journal = The Journal of Biological Chemistry | volume = 278 | issue = 6 | pages = 3671–3678 | date = February 2003 | pmid = 12446702 | doi = 10.1074/jbc.M208247200 | doi-access = free }}</ref> Protease inhibitors or antipain are enzymes that are used to regulate their performance.
The antiretroviral drug [[Nelfinavir]] is one example of an antipain. It was classified as an antipain after a study published by [[Ovid]] that investigated the in vitro effect of [[Nelfinavir]] using [[proteolytic foot printing]] and found that it selectively inhibited HER2- positive, a growth factor in breast cancer.<ref>{{cite journal | vauthors = Shim JS, Rao R, Beebe K, Neckers L, Han I, Nahta R, Liu JO | title = Selective inhibition of HER2-positive breast cancer cells by the HIV protease inhibitor nelfinavir | journal = Journal of the National Cancer Institute | volume = 104 | issue = 20 | pages = 1576–1590 | date = October 2012 | pmid = 23042933 | pmc = 3472971 | doi = 10.1093/jnci/djs396 }}</ref>
Antipain is a reversible inhibitor of trypsin, papain, and, plasmin, which is isolated from actinomycetes.<ref>{{Citation|title=Antipain|date=2004-07-15|url=http://dx.doi.org/10.1002/0471684228.egp00764|work=Encyclopedic Dictionary of Genetics, Genomics and Proteomics|place=Hoboken, NJ, USA|publisher=John Wiley & Sons, Inc.|doi=10.1002/0471684228.egp00764 |isbn=0-471-68422-8|access-date=2021-03-29}}</ref>
== Protease inhibitors and DRUG neurons ==
Protease-activated receptors (PARs) are a unique class of [[G protein-coupled receptor]]s activated by proteolytic cleavage of the receptor N terminus.<ref>{{cite journal | vauthors = Nakae K, Kojima F, Sawa R, Kubota Y, Igarashi M, Kinoshita N, Adachi H, Nishimura Y, Akamatsu Y | display-authors = 6 | title = Antipain Y, a new antipain analog that inhibits neurotransmitter release from rat dorsal root ganglion neurons | journal = The Journal of Antibiotics | volume = 63 | issue = 1 | pages = 41–44 | date = January 2010 | pmid = 19911027 | doi = 10.1038/ja.2009.109 | doi-access = free }}</ref> PARs are activated by some Serine Proteases and are important for the physiological, psychological,<ref>{{cite journal | vauthors = Nakae K, Saito K, Iino T, Yamamoto N, Wakabayashi M, Yoshikawa S, Matsushima S, Miyashita H, Sugimoto H, Kiba A, Gupta J | display-authors = 6 | title = A prostacyclin receptor antagonist inhibits the sensitized release of substance P from rat sensory neurons | journal = The Journal of Pharmacology and Experimental Therapeutics | volume = 315 | issue = 3 | pages = 1136–1142 | date = December 2005 | pmid = 16109742 | doi = 10.1124/jpet.105.091967 | s2cid = 14841421 }}</ref> and pathological functions of the human body.
During the study, an antipain [[Functional analog (chemistry)|analogue]] Y was developed and studied. It was shown to have properties as a protease inhibitors but it had a low [[IC50]] than a antipain. Antipain analogue Y was able to suppress [[Trypsin]], which inhibits the secretion of an [[Excitatory synapse|excitatory neuropeptide]] that leads to inflammation and other disorders.{{citation needed|date=October 2021}} Antipain is a protease inhibitor, usually 1–2 μg/mL, and is well-against to cathepsin A, cathepsin B, papain and trypsin protease enzymes.<ref>{{Citation|title=Antipain|date=2008|url=http://dx.doi.org/10.1007/978-1-4020-6754-9_957|encyclopedia=Encyclopedia of Genetics, Genomics, Proteomics and Informatics|pages=120|place=Dordrecht|publisher=Springer Netherlands|doi=10.1007/978-1-4020-6754-9_957 |isbn=978-1-4020-6753-2|access-date=2021-03-29 }}</ref>