%0 Journal Article %1 Wage_1997_258 %A Wagenknecht, T. %A Radermacher, M. %D 1997 %J Curr. Opin. Struct. Biol. %K 9094329 Animals, Binding Calcium Calmodulin, Calmodulin-Bindi, Carrier Channel, Channels, Conformation, DNA-Binding Electron, Freezing, Gov't, Heat-Shock Humans, Macromolecular Microscopy, Models, Molecular, Muscle Muscle, Non-U.S. P.H.S., Protei, Protein Proteins, Rabbits, Receptor Release Research Ryanodine Skeletal, Substances, Support, Tacrolimus U.S. ng ns, %N 2 %P 258--265 %T Ryanodine receptors: structure and macromolecular interactions. %U http://dx.doi.org/10.1016/S0959-440X(97)80034-6 %V 7 %X Ryanodine receptors (RyRs), a class of intracellular calcium release channels, are the largest ion channels known. Recently, cryoelectron microscopy and image reconstructions of isolated receptors have shown that most of the protein mass forms a porous, multidomain cytoplasmic assembly. Evidence is mounting that suggests that the cytoplasmic assembly communicates with the transmembrane regions over distances of 100 or greater. RyRs are centrally important in excitation-contraction coupling, which occurs at specialized regions where the sarcoplasmic reticulum, containing the RyRs, and the plasma membrane/transverse-tubule system form junctions. Numerous proteins are present at these junctions, some of which interact directly with the RyR.

@article{Wage_1997_258, abstract = {Ryanodine receptors (RyRs), a class of intracellular calcium release channels, are the largest ion channels known. Recently, cryoelectron microscopy and image reconstructions of isolated receptors have shown that most of the protein mass forms a porous, multidomain cytoplasmic assembly. Evidence is mounting that suggests that the cytoplasmic assembly communicates with the transmembrane regions over distances of 100 or greater. RyRs are centrally important in excitation-contraction coupling, which occurs at specialized regions where the sarcoplasmic reticulum, containing the RyRs, and the plasma membrane/transverse-tubule system form junctions. Numerous proteins are present at these junctions, some of which interact directly with the RyR.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {Wagenknecht, T. and Radermacher, M.}, biburl = {https://www.bibsonomy.org/bibtex/20ded17beb311bd2e166a2b751b11c2f6/hake}, description = {The whole bibliography file I use.}, file = {Wage_1997_258.pdf:Wage_1997_258.pdf:PDF}, interhash = {51756e25c7bbc8e476c94b12e5c244b8}, intrahash = {0ded17beb311bd2e166a2b751b11c2f6}, journal = {Curr. Opin. Struct. Biol.}, key = 224, keywords = {9094329 Animals, Binding Calcium Calmodulin, Calmodulin-Bindi, Carrier Channel, Channels, Conformation, DNA-Binding Electron, Freezing, Gov't, Heat-Shock Humans, Macromolecular Microscopy, Models, Molecular, Muscle Muscle, Non-U.S. P.H.S., Protei, Protein Proteins, Rabbits, Receptor Release Research Ryanodine Skeletal, Substances, Support, Tacrolimus U.S. ng ns,}, month = Apr, number = 2, pages = {258--265}, pmid = {9094329}, timestamp = {2009-06-03T11:21:35.000+0200}, title = {Ryanodine receptors: structure and macromolecular interactions.}, url = {http://dx.doi.org/10.1016/S0959-440X(97)80034-6}, volume = 7, year = 1997 }