Tropomyosins, N-terminal acetylation and their impact on yeast cytoskeletal function: A characterisation of novel tropomyosins from N. crassa and the N-terminal acetyltransferase, Nat3p [PDF]
, 2009 PhDWhile the fundamental role of tropomyosins (Tms) in the maintenance of the actin cytoskeleton in yeast is established, details of their exact regulatory functions in lower eukaryotes remains to be deciphered.
Ebrahim, Seham
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Mutations changing tropomodulin affinity for tropomyosin alter neurite formation and extension [PDF]
PeerJ, 2013 Assembly of the actin cytoskeleton is an important part of formation of neurites in developing neurons. Tropomodulin, a tropomyosin-dependent capping protein for the pointed end of the actin filament, is one of the key players in this process ...
Natalia Moroz +3 more
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Foods, 2023 Tropomyosin (TM) is the major allergen of shrimp (Penaeus chinensis). Previous studies showed that separate cold plasma or glycation have their drawback in reducing allergenicity of TM, including effectiveness and reliability. In the current study, a new
Feng-Qi Wang +2 more
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Pathogens, 2023 The immunoprophylactic management of ticks is the most effective option to control tick infestations and counter spread the acaricide resistance problem worldwide.
Balasamudram Chandrasekhar Parthasarathi +13 more
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Altering the stability of the Cdc8 overlap region modulates the ability of this tropomyosin to bind cooperatively to actin and regulate myosin. [PDF]
, 2011 Tropomyosin (Tm) is an evolutionarily conserved ?-helical coiled-coil protein, dimers of which form end-to-end polymers capable of associating with and stabilising actin-filaments and regulate myosin function. The fission yeast, Schizosaccharomyces pombe,
Duncan Sousa +15 more
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The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast. [PDF]
, 2010 Tropomyosin (Tm) is a conserved dimeric coiled-coil protein, which forms polymers that curl around actin filaments in order to regulate actomyosin function.
Mulvihill, Daniel P. +9 more
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Tropomyosin isoforms and reagents [PDF]
BioArchitecture, 2011 Tropomyosins are rod-like dimers which form head-to-tail polymers along the length of actin filaments and regulate the access of actin binding proteins to the filaments.1 The diversity of tropomyosin isoforms, over 40 in mammals, and their role in an increasing number of biological processes presents a challenge both to experienced researchers and ...
Galina, Schevzov +4 more
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Genetic variation among lambs in peripheral IgE activity against the larval stages of Teladorsagia circumcincta [PDF]
, 2010 IgA and IgE activity against Teladorsagia circumcincta was investigated in a flock of Texel lambs following natural, mixed nematode infection among lambs.
Bishop, S. C. +12 more
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Tropomyosin diffusion over actin subunits facilitates thin filament assembly
Structural Dynamics, 2016 Coiled-coil tropomyosin binds to consecutive actin-subunits along actin-containing thin filaments. Tropomyosin molecules then polymerize head-to-tail to form cables that wrap helically around the filaments. Little is known about the assembly process that
Stefan Fischer +3 more
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Hydra tropomyosin TROP1 is expressed in head-specific epithelial cells and is a major component of the cytoskeletal structure that anchors nematocytes [PDF]
, 1994 A cDNA clone encoding a 253 amino acid tropomyosin was isolated from Hydra in a differential screen for headspecific genes. The Hydra tropomyosin gene, designated trop1, is a single copy gene, lacks introns and is strongly expressed in tentacle-specific ...
Lopez de Haro, Maria S. +3 more
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