Results 11 to 20 of about 2,101 (172)
Genomic organization of
BMC Genomics, 2001 Background The tropomodulins (TMODs) are a family of proteins that cap the pointed ends of actin filaments. Four TMODs have been identified in humans, with orthologs in mice.
Zoghbi Huda Y +2 more
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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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Folding Properties of Functional Domains of Tropomodulin [PDF]
Biophysical Journal, 2001 Tropomodulin (Tmod) stabilizes the actin-tropomyosin filament by capping the slow-growing end (P-end). The N- and C-terminal halves play distinct roles; the N-terminal half interacts with the N-terminal region of tropomyosin, whereas the C-terminal half interacts with actin. Our previous study (A. Kostyukova, K. Maeda, E. Yamauchi, I.
Kostyukova, Alla S. +2 more
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Leiomodin and tropomodulin in smooth muscle [PDF]
American Journal of Physiology-Cell Physiology, 2001 Evidence is accumulating to suggest that actin filament remodeling is critical for smooth muscle contraction, which implicates actin filament ends as important sites for regulation of contraction. Tropomodulin (Tmod) and smooth muscle leiomodin (SM-Lmod) have been found in many tissues containing smooth muscle by protein immunoblot and ...
Catharine A. Conley
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Gene Assignment, Expression, and Homology of Human Tropomodulin
Genomics, 1996 Tropomodulin is a newly characterized pointed end capping protein for actin filaments. It binds specifically to the N terminus of tropomyosin and blocks the elongation and depolymerization of tropomyosin-coated actin filaments. A 1.9-kb human tropomodulin cDNA clone was used to map its gene by fluorescence in situ hybridization.
L A, Sung, Y, Fan, C C, Lin
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Tropomodulins and tropomyosins – organizers of cellular microcompartments
Biomolecular Concepts, 2013 Eukaryotic cells show a remarkable compartmentalization into compartments such as the cell nucleus, the Golgi apparatus, the endoplasmic reticulum, and endosomes.
Fath Thomas
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Journal of Cell Science, 1996 ABSTRACT We have identified and characterized two proteins in rat brain that bind to the neuron-specific tropomyosin isoform, TMBr3. The two proteins were identified by blot overlay assay, in which the proteins immobilized on the membrane were probed by epitope-tagged TMBr3, followed by detection with anti-epitope antibody.
Watakabe, A Watakabe, Akiya +2 more
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Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin. [PDF]
PLoS ONE, 2017 Leiomodin proteins are vertebrate homologues of tropomodulin, having a role in the assembly and maintenance of muscle thin filaments. Leiomodin2 contains an N-terminal tropomodulin homolog fragment including tropomyosin-, and actin-binding sites, and a C-
Dávid Szatmári +5 more
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Tropomodulin’s Actin-Binding Abilities Are Required to Modulate Dendrite Development [PDF]
Frontiers in Molecular Neuroscience, 2018 There are many unanswered questions about the roles of the actin pointed end capping and actin nucleation by tropomodulins (Tmod) in regulating neural morphology.
Kevin T. Gray +13 more
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Leiomodin creates a leaky cap at the pointed end of actin-thin filaments.
PLoS Biology, 2020 Improper lengths of actin-thin filaments are associated with altered contractile activity and lethal myopathies. Leiomodin, a member of the tropomodulin family of proteins, is critical in thin filament assembly and maintenance; however, its role is under
Dmitri Tolkatchev +7 more
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