Results 251 to 260 of about 59,695 (281)
Tryptic Digestion of Tropomyosin A, Tropomyosin B and Myosin [PDF]
Nature, 1966 Two types of tropomyosins co-exist in lamellibranch adductors and in cephalopod muscle1: TMA and TMB, TMA being the protein referred to as invertebrate tropomyosin, or water-insoluble tropomyosin, by Bailey, and TMB the water-soluble variety.
openaire +2 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
β‐Tropomyosin mutations alter tropomyosin isoform composition
European Journal of Neurology, 2008Background and purpose: Tropomyosin (TM) is an actin‐binding protein, which is localized head to tail along the length of the actin filament. There are three major TM isoforms in human striated muscle. Mutations in β‐tropomyosin (TPM2) have recently been identified as an important cause of neuromuscular disorders.
Homa Tajsharghi, J. Nilsson
openaire +3 more sources
Vertebrate and Invertebrate Tropomyosins
Nature, 1957AS a first step toward generalizing the relationship between tropomyosin, actin and myosin found for rabbit skeletal muscle1, we have prepared and examined tropomyosins from the different types of mammalian muscle (cardiac, uterine and smooth), from lower classes within the vertebrate phylum (amphibian, fish and cyclostome) and from representatives of ...
F. Saad, K. Laki, D. R. Kominz
openaire +3 more sources
Journal of Muscle Research and Cell Motility, 2014
Tropomyosin is a two chained α-helical coiled coil protein that binds actin filaments and interacts with various actin binding proteins. Tropomyosin function depends on its ability to move to distinct locations on the surface of actin in response to the binding of different thin filament effectors.
openaire +3 more sources
Tropomyosin is a two chained α-helical coiled coil protein that binds actin filaments and interacts with various actin binding proteins. Tropomyosin function depends on its ability to move to distinct locations on the surface of actin in response to the binding of different thin filament effectors.
openaire +3 more sources
Cold Adaptation of Tropomyosin
Biochemistry, 2011The conformational stability of unphosphorylated and phosphorylated α,α-striated tropomyosins from rabbit and shark (95% identical sequences) has been investigated. Three additional core positions are occupied by atypical amino acids in the protein from shark: Thr179(d), Ser190(a), and Ser211(a).
Tatiana Chevaldina +2 more
openaire +3 more sources
Proceedings of the Royal Society of London. Series B - Biological Sciences, 1953
In all muscles so far examined there is present an unusual protein to which no function has yet been assigned. It occurs side by side with actin and myosin in the myofibril, and because of its similarity to myosin was named tropomyosin (Bailey 1948). Though soluble in water, it is not extracted from coarsely minced muscle by aqueous media;
openaire +3 more sources
In all muscles so far examined there is present an unusual protein to which no function has yet been assigned. It occurs side by side with actin and myosin in the myofibril, and because of its similarity to myosin was named tropomyosin (Bailey 1948). Though soluble in water, it is not extracted from coarsely minced muscle by aqueous media;
openaire +3 more sources
2008
Tropomyosins consist of nearly 100% alpha-helix and assemble into paralleldimeric coiled-coils. Nonmusde as well as muscle tropomyosins can form homodimers, however, expression of both muscle alpha and beta tropomyosin subunits results in the preferential formation of stable alpha/beta heterodimers in native muscle.
openaire +3 more sources
Tropomyosins consist of nearly 100% alpha-helix and assemble into paralleldimeric coiled-coils. Nonmusde as well as muscle tropomyosins can form homodimers, however, expression of both muscle alpha and beta tropomyosin subunits results in the preferential formation of stable alpha/beta heterodimers in native muscle.
openaire +3 more sources
Isoform Sorting of Tropomyosins
2008Cytoskeletal tropomyosin (Tm) isoforms show extensive intracellular sorting, resulting in spatially distinct actin-filament populations. Sorting of Tm isoforms has been observed in a number of cell types, including fibroblasts, epithelial cells, osteoclasts, neurons and muscle cells.
Claire Martin, Peter W. Gunning
openaire +3 more sources
Crystalline sheets of tropomyosin
Journal of Molecular Biology, 1984In the presence of spermine tropomyosin forms sheets having two-dimensional crystallinity and tactoids. The most common form of sheet has cmm symmetry with a = 80 nm and b = 5 nm. The structure of this sheet has been solved in projection to a nominal resolution of 1.5 nm by combining data from electron diffraction and electron microscopy.
openaire +2 more sources
Structure of Molluscan Tropomyosin
Nature, 1957CERTAIN molluscan smooth muscles contain protein filaments with a regular and characteristic fine structure1–3 to which the name paramyosin has been given4. Neither the chemical nature nor the function of these filaments is understood, and attention is once more drawn to these problems by the recent discovery in the same muscles of an asymmetric ...
J. Lowy +7 more
openaire +3 more sources