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pro vyhledávání: '"L M, Coluccio"'
Autor:
L M, Coluccio
Publikováno v:
American Journal of Physiology-Cell Physiology. 273:C347-C359
The class I myosins are single-headed, actin-binding, mechanochemical “motor” proteins with heavy chains in the molecular mass range of 110-130 kDa; they do not form filaments. Each myosin I heavy chain is associated with one to six light chains
Autor:
L M, Coluccio
Publikováno v:
Journal of Cell Science. 107:2279-2284
We have previously purified and characterized two myosin-1 isoforms from rat liver (molecular masses 130 kDa and 110 kDa; L. M. Coluccio and C. Conaty (1993) Cell Motil. Cytoskel. 24, 189–199). Here, we describe the purification and characterizatio
Autor:
L M, Coluccio, M A, Geeves
Publikováno v:
The Journal of biological chemistry. 274(31)
The 130-kDa myosin I (MI(130)), product of the myr-1 gene, is one member of the mammalian class I myosins, a group of small, calmodulin-binding mechanochemical molecules of the myosin superfamily that translocate actin filaments. Roles for MI(130) ar
Autor:
L M, Coluccio
Publikováno v:
European journal of cell biology. 56(2)
The epithelial layer lining the proximal convoluted tubule of mammalian kidney contains a brush border of numerous microvilli. These microvilli appear in structure to be very similar to the microvilli on epithelial cells of the small intestine. Micro