Results 11 to 20 of about 2,192 (170)
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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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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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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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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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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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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Tropomyosin-binding properties modulate competition between tropomodulin isoforms [PDF]
Archives of Biochemistry and Biophysics, 2016 The formation and fine-tuning of cytoskeleton in cells are governed by proteins that influence actin filament dynamics. Tropomodulin (Tmod) regulates the length of actin filaments by capping the pointed ends in a tropomyosin (TM)-dependent manner. Tmod1, Tmod2 and Tmod3 are associated with the cytoskeleton of non-muscle cells and their expression has ...
Colpan, Mert +5 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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Blood, 2000 The human erythrocyte membrane skeleton consists of hexagonal lattices with junctional complexes containing F-actin protofilaments of approximately 33-37 nm in length. We hypothesize that complexes formed by tropomodulin, a globular capping protein at the pointed end of actin filaments, and tropomyosin (TM), a rod-like molecule of approximately 33-35 ...
Sung, LA Sung, Lanping Amy +6 more
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