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	<title>Thioredoxin - Revision history</title>
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	<updated>2026-04-27T00:56:10Z</updated>
	<subtitle>Revision history for this page on the wiki</subtitle>
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		<id>https://wikimd.org/index.php?title=Thioredoxin&amp;diff=5615090&amp;oldid=prev</id>
		<title>Prab: CSV import</title>
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		<updated>2024-04-16T17:59:12Z</updated>

		<summary type="html">&lt;p&gt;CSV import&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;[[File:FigMech.png|FigMech|thumb]] &amp;#039;&amp;#039;&amp;#039;Thioredoxin&amp;#039;&amp;#039;&amp;#039; is a small [[protein]] that plays a crucial role in many [[biological processes]], including [[redox]] signaling, [[protein folding]], and the regulation of various cellular functions. It is found across all [[organisms]], from [[bacteria]] to [[humans]], highlighting its fundamental importance in [[life sciences|life]].&lt;br /&gt;
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== Function ==&lt;br /&gt;
Thioredoxin functions primarily as a [[redox]] protein, facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. This process is vital for maintaining the cellular [[redox balance]] and is involved in the regulation of [[cellular signaling pathways]] that control [[growth]], [[death]], and [[response to stress]]. In humans, thioredoxin also plays a significant role in [[antioxidant]] defense by reducing [[reactive oxygen species]] (ROS) and maintaining the redox state of [[cells]].&lt;br /&gt;
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== Structure ==&lt;br /&gt;
The thioredoxin protein is characterized by a conserved active site with the sequence -Cys-Gly-Pro-Cys-, which is essential for its catalytic activity. The structure of thioredoxin is compact, with a [[beta-sheet]] flanked by [[alpha-helix|alpha-helices]]. This configuration allows thioredoxin to undergo reversible oxidation and reduction, a feature critical for its function in redox reactions.&lt;br /&gt;
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== Thioredoxin System ==&lt;br /&gt;
The thioredoxin system comprises thioredoxin, [[thioredoxin reductase]], and [[NADPH]]. Thioredoxin reductase regenerates reduced thioredoxin using electrons from NADPH, thus maintaining the thioredoxin pool in its reduced state. This system is essential for cellular redox homeostasis and plays a role in the defense against oxidative stress.&lt;br /&gt;
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== Clinical Significance ==&lt;br /&gt;
Thioredoxin has been implicated in various [[diseases]], including [[cancer]], [[cardiovascular diseases]], and [[neurodegenerative diseases]]. Its ability to regulate cell proliferation and apoptosis makes it a target for cancer therapy. Additionally, the antioxidant properties of thioredoxin are of interest in the treatment of diseases associated with oxidative stress.&lt;br /&gt;
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== Research ==&lt;br /&gt;
Research on thioredoxin is focused on understanding its role in cellular processes and its potential as a therapeutic target. Studies are exploring the use of thioredoxin inhibitors in cancer therapy and the development of drugs that can modulate the thioredoxin system to treat diseases related to oxidative stress.&lt;br /&gt;
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[[Category:Proteins]]&lt;br /&gt;
[[Category:Cell biology]]&lt;br /&gt;
[[Category:Biochemistry]]&lt;br /&gt;
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{{biochemistry-stub}}&lt;/div&gt;</summary>
		<author><name>Prab</name></author>
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