Results 151 to 160 of about 2,101 (172)
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1999
Abstract Tropomodulin (Tmod) is a ∼40 kDa tropomyosin- and actin-binding protein that is associated with the slow growing (pointed) ends of stable, tropomyosin-coated actin filaments in muscle and non-muscle cells. In vitro and in vivo data indicate that Tmod functions to cap the pointed ends of tropomyosin-actin filaments and prevent ...
Velia M Fowler, Catharine A Conley
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Abstract Tropomodulin (Tmod) is a ∼40 kDa tropomyosin- and actin-binding protein that is associated with the slow growing (pointed) ends of stable, tropomyosin-coated actin filaments in muscle and non-muscle cells. In vitro and in vivo data indicate that Tmod functions to cap the pointed ends of tropomyosin-actin filaments and prevent ...
Velia M Fowler, Catharine A Conley
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Chicken skeletal muscle tropomodulin: novel localization and characterization
Cell and Tissue Research, 1996Tropomodulin is a 40.6-kDa isoform-specific tropomyosin-binding protein which inhibits actin filament elongation from the slow-growing (pointed) end and localizes at or near the pointed ends of thin filaments in rat skeletal muscle. Immunofluorescent localization using affinity-purified anti-tropomodulin antibodies in avian myofibril preparations ...
Mark A Sussman +2 more
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The Role of Tropomodulin in Cardiac Function and Remodeling
Advances in Bioengineering, 2004Tropomodulin is an actin-capping protein in cardiac muscle, and is associated with both sarcomeric and cytoskeletal actin filaments. Homozygous knockout of erythrocyte tropomodulin (E-Tmod) is embryonically lethal, but heterozygous knockout (+/-) mice survive. Heterozygous E-Tmod knockout resulted in smaller right ventricle (RV) cavities and free walls
Andrea Bryan +3 more
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Targeted disruption of the tropomodulin gene in mice
Proceedings of the First Joint BMES/EMBS Conference. 1999 IEEE Engineering in Medicine and Biology 21st Annual Conference and the 1999 Annual Fall Meeting of the Biomedical Engineering Society (Cat. No.99CH37015), 2003Tropomodulin (Tmod) is a tropomyosin (TM)-binding protein that caps the pointed end of the actin filaments and regulates the length of actin filaments in muscle and non-muscle cells. Mouse embryonic stem (ES) cells which normally express tropomodulin survived the targeted disruption of one and two Tmod alleles.
X. Chu +4 more
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Tropomodulin function and thin filament assembly in cardiac myocytes
Trends in Cardiovascular Medicine, 1996The regulation of thin filament length is a fundamental property of all striated muscles. Tropomodulin is an actin and tropomyosin binding protein that is exclusively associated with the free (pointed) ends of thin filaments. In vitro and in vivo studies reveal that tropomodulin is an actin filament pointed end capping protein, which is required to ...
C C, Gregorio, V M, Fowler
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Identification and characterization of tropomodulin and tropomyosin in the adult rat lens
Journal of Cell Science, 1994ABSTRACT The lens fiber cells express all the major components of the erythrocyte membrane skeleton including spectrin, protein 4.1 and ankyrin. We have used immunoblot and immuno-precipitation analyses, as well as immunofluorescence localization to identify and characterize two additional components of the membrane skeleton in the rat ...
M K, Woo, V M, Fowler
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Making tropomodulin find the right point
Science, 2014Actin Cytoskeleton Actin filaments are a key component of the cell's cytoskeleton. Actin filaments have a characteristic polarized architecture with a so-called barbed end and a pointed end—so described because of how the filaments look under the electron microscope when they are coated ...
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Tropomodulin: An Important Player in Cardiac Myofibrillogenesis
2002Tropomodulin has been studied intensively since it was first reported in 1987 as a tropomyosin binding protein associated with the erythrocyte membrane skeleton (Fowler, 1987). The study of tropomodulin’s role in heart myofibrillogenesis was initiated after the discovery that in mature skeletal muscle tropomodulin was localized to the pointed (slow ...
Catherine McLellan, Carol C. Gregorio
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Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons
Journal of Cell Science, 1994ABSTRACT The human erythrocyte membrane skeleton consists of a network of short actin filaments cross-linked into a hexagonal network by long, flexible spectrin molecules. The lengths of the short actin filaments (33±5 nm) at the central junctions are proposed to be stabilized and limited by asso- ciation with tropomyosin and the ...
J A, Ursitti, V M, Fowler
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Structural Requirements of Tropomodulin for Tropomyosin Binding and Actin Filament Capping
Biochemistry, 2005Regulation of actin filament dynamics underlies many cellular functions. Tropomodulin together with tropomyosin can cap the pointed, slowly polymerizing, filament end, inhibiting addition or loss of actin monomers. Tropomodulin has an unstructured N-terminal region that binds tropomyosin and a folded C-terminal domain with six leucine-rich repeats.
Alla S, Kostyukova +4 more
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