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Tropomyosin: A panallergen that causes a worldwide allergic problem.

Allergy and Asthma Proceedings, 2021
Background: Panallergens are proteins that take part in key processes of organisms and, therefore, are ubiquitously distributed with highly conserved sequences and structures. One class of these panallergens is composed of the tropomyosins.
Francesco Papia, C. Bellia, C. Uasuf
semanticscholar   +1 more source

β‐Tropomyosin mutations alter tropomyosin isoform composition

European Journal of Neurology, 2008
Background 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.
J, Nilsson, H, Tajsharghi
openaire   +2 more sources

Tropomyosin dynamics

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.
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Vertebrate and Invertebrate Tropomyosins

Nature, 1957
AS 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 ...
D R, KOMINZ, K, LAKI, F, SAAD
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Tryptic Digestion of Tropomyosin A, Tropomyosin B and Myosin

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.
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Cold Adaptation of Tropomyosin

Biochemistry, 2011
The 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).
Michael, Hayley   +2 more
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Dimerization of Tropomyosins

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.
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Smooth muscle tropomyosin paracrystals

Journal of Ultrastructure Research, 1982
Ordered aggregates of chicken gizzard tropomyosin were obtained in solutions containing 50 mM MgCl2, 50 mM Tris—HCl, pH 8.0 (Solution A), 0.1 M Na acetate, 0.05 M (NH4)2SO4, 1 mM dithiothreitol (DTT), 1 mM ethylenediaminetetracetic acid (EDTA), pH 5.6 (Solution B), and 0.2 M KCl, 10 mM Na acetate, pH 5.6 (Solution C).
M, Yamaguchi, R M, Robson, M H, Stromer
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