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- W2019857777 endingPage "125" @default.
- W2019857777 startingPage "99" @default.
- W2019857777 abstract "Gap junctions were initially described morphologically, and identified as semi-crystalline arrays of channels linking two cells. This suggested that they may represent an amenable target for electron and X-ray crystallographic studies in much the same way that bacteriorhodopsin has. Over 30 years later, however, an atomic resolution structural solution of these unique intercellular pores is still lacking due to many challenges faced in obtaining high expression levels and purification of these structures. A variety of microscopic techniques, as well as NMR structure determination of fragments of the protein, have now provided clearer and correlated views of how these structures are assembled and function as intercellular conduits. As a complement to these structural approaches, a variety of mutagenic studies linking structure and function have now allowed molecular details to be superimposed on these lower resolution structures, so that a clearer image of pore architecture and its modes of regulation are beginning to emerge." @default.
- W2019857777 created "2016-06-24" @default.
- W2019857777 creator A5033530478 @default.
- W2019857777 creator A5035756158 @default.
- W2019857777 date "2005-06-01" @default.
- W2019857777 modified "2023-10-17" @default.
- W2019857777 title "Structural organization of gap junction channels" @default.
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