ArticleBiomolecular NMR assignments2013
¹H, ¹³C, and ¹⁵N backbone resonance assignments of the connexin43 carboxyl terminal domain attached to the 4th transmembrane domain in detergent micelles.
Article in Biomolecular NMR assignments, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Mechanisms of Connexin Regulating Peptides.International journal of molecular sciences · 2021Review
- Connexins: Synthesis, Post-Translational Modifications, and Trafficking in Health and Disease.International journal of molecular sciences · 2018Review
- Atomic structure of the innexin-6 gap junction channel determined by cryo-EM.Nature communications · 2016Article
- Secondary structural analysis of the carboxyl-terminal domain from different connexin isoforms.Biopolymers · 2016Article
- Effects of phosphorylation on the structure and backbone dynamics of the intrinsically disordered connexin43 C-terminal domain.The Journal of biological chemistry · 2013Article
- Proteins and mechanisms regulating gap-junction assembly, internalization, and degradation.Physiology (Bethesda, Md.) · 2013Review
- A history of gap junction structure: hexagonal arrays to atomic resolution.Cell communication & adhesion · 2013Review
- An Escherichia coli strain for expression of the connexin45 carboxyl terminus attached to the 4th transmembrane domain.Frontiers in pharmacology · 2013Article
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3 authors at 1 institution in 1 country.
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Abstract
Gap junctions are specialized membrane channels that enable coordination of cellular functions and whole-organ responses by facilitating both molecular and electrical communication between neighboring cells. Connexin43 (Cx43) is the most widely expressed and well-studied gap junction protein. In the heart, Cx43 is essential for normal cardiac development and function. Studies using a soluble version of the Cx43 carboxyl-terminal domain (Cx43CT; S255-I382) have established the central role it plays in channel regulation. However, in purifying and characterizing a more 'native-like' construct (Cx43CT attached to the fourth transmembrane domain (TM4-Cx43CT; D196-I382)), we have identified that the TM4-Cx43CT is a better model than the soluble Cx43CT to further investigate the mechanisms governing Cx43 channel regulation. Here, we report the backbone (1)H, (15)N, and (13)C assignments and predicted secondary structure of the TM4-Cx43CT. Assignment of the TM4-Cx43CT is a key step towards a better understanding of the structural basis of Cx43 regulation, which will lead to improved strategies for modulation of junctional communication that has been altered due to disease or ischemic injury.
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