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	<id>https://transhumanist.ru/index.php?action=history&amp;feed=atom&amp;title=ANKRD1</id>
	<title>ANKRD1 - История изменений</title>
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	<updated>2026-06-12T13:46:31Z</updated>
	<subtitle>История изменений этой страницы в вики</subtitle>
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		<id>https://transhumanist.ru/index.php?title=ANKRD1&amp;diff=5330&amp;oldid=prev</id>
		<title>OdysseusBot: Новая страница: «Ankyrin repeat domain-containing protein 1 (Cardiac ankyrin repeat protein) (Cytokine-inducible gene C-193 protein) (Cytokine-inducible nuclear protein) [C193] [C...»</title>
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		<updated>2021-05-12T13:39:25Z</updated>

		<summary type="html">&lt;p&gt;Новая страница: «Ankyrin repeat domain-containing protein 1 (Cardiac ankyrin repeat protein) (Cytokine-inducible gene C-193 protein) (Cytokine-inducible nuclear protein) [C193] [C...»&lt;/p&gt;
&lt;p&gt;&lt;b&gt;Новая страница&lt;/b&gt;&lt;/p&gt;&lt;div&gt;Ankyrin repeat domain-containing protein 1 (Cardiac ankyrin repeat protein) (Cytokine-inducible gene C-193 protein) (Cytokine-inducible nuclear protein) [C193] [CARP] [HA1A2]&lt;br /&gt;
&lt;br /&gt;
==Publications==&lt;br /&gt;
&lt;br /&gt;
{{medline-entry&lt;br /&gt;
|title=[[ANKRD1]] specifically binds [[CASQ2]] in heart extracts and both proteins are co-enriched in piglet cardiac Purkinje cells.&lt;br /&gt;
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/15698842&lt;br /&gt;
|abstract=It has been suggested that the cardiac ankyrin repeat domain 1 protein ([[ANKRD1]]), also known as CARP, can play a pathophysiological role in the contractile responsiveness of myocardium. Here, we study the potential functional roles of [[ANKRD1]] by searching for endogenous cardiac proteins that interact preferentially with [[ANKRD1]] in the heart-tissue extract from neonatal piglets, using non-biased pull-down approaches. These approaches identified, for the first time, a selective interaction between [[ANKRD1]] and endogenous cardiac calsequestrin-2 ([[CASQ2]]) that is important for Ca2  release and excitation-contraction coupling. Blot-overlay and co-immunoprecipitation assays provided further confirmation of the direct and specific interaction between the two proteins. Mapping of the peptides involved in the interaction revealed five non-overlapping binding sequences for [[CASQ2]] on [[ANKRD1]], as well as, three binding peptides for [[ANKRD1]] in [[CASQ2]]. For the first time, we show by immunohistochemistry that endogenous [[ANKRD1]] and [[CASQ2]] are co-enriched in piglet cardiac Purkinje cells. Collectively, the results provide the first sing of a possible functional interaction between [[ANKRD1]] and [[CASQ2]] and suggest a potentially novel role for both proteins in cardiac Purkinje fibers.&lt;br /&gt;
|mesh-terms=* Aging&lt;br /&gt;
* Amino Acid Sequence&lt;br /&gt;
* Animals&lt;br /&gt;
* Binding Sites&lt;br /&gt;
* Calcium&lt;br /&gt;
* Calsequestrin&lt;br /&gt;
* Cell Extracts&lt;br /&gt;
* Dogs&lt;br /&gt;
* Heart&lt;br /&gt;
* Humans&lt;br /&gt;
* Immunohistochemistry&lt;br /&gt;
* Molecular Sequence Data&lt;br /&gt;
* Myocardium&lt;br /&gt;
* Nuclear Proteins&lt;br /&gt;
* Protein Binding&lt;br /&gt;
* Purkinje Cells&lt;br /&gt;
* Repressor Proteins&lt;br /&gt;
* Substrate Specificity&lt;br /&gt;
* Swine&lt;br /&gt;
* Tissue Extracts&lt;br /&gt;
&lt;br /&gt;
|full-text-url=https://sci-hub.do/10.1016/j.yjmcc.2004.11.034&lt;br /&gt;
}}&lt;/div&gt;</summary>
		<author><name>OdysseusBot</name></author>
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