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- W3036692344 abstract "Gap junctions are the specialized regions between two adjoining cells responsible for regulated communication. The morphological unit of the gap junction is composed of 12 copies of the connexin molecule. Six connexins form a hexamer in each cell membrane called a connexon and two connexons pair across the two cell membranes of coupled cells to form gated channels. Although other proteins are found in enriched gap junction preparations, it is generally accepted that the gap junction structures are formed from a family of connexin proteins. The connexins are named according to their DNA deduced molecular weights, e.g. Cx32 for the 32kDa liver major connexin and Cx26 for the 26 kDa liver minor connexin. Within a given tissue, several connexins are often found and different connexins are often found within the same junctional plaque. These connexins contain both conserved and variable domains in their primary amino acid sequences, with the major differences occuring in the sequence and size of the cytoplasmic C terminus. The most conserved regions of the compared sequences are in the transmembrane and gap portions of the proteins. Determination of the sequences of the connexin proteins and correlation of information on antibody binding, proteolytic cleavage and chemical reactivity have led to a model where the C- and N- termini are located at the cytoplasmc surface and four α-helical segments of the protein cross the membrane." @default.
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- W3036692344 date "1992-08-01" @default.
- W3036692344 modified "2023-09-25" @default.
- W3036692344 title "Diversity in gap junction structures" @default.
- W3036692344 cites W2020658964 @default.
- W3036692344 doi "https://doi.org/10.1017/s0424820100122617" @default.
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