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Comparative Transcriptomics as a Key to Understanding the Adaptation Mechanisms of Baikal Sculpins to the Deep-Water Habitat. [PDF]
Sapozhnikova YP +11 more
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Tropomodulins and tropomodulin/tropomyosin interactions
Cellular and Molecular Life Sciences, 2007The tropomodulins are a family of proteins that cap the slow-growing (pointed) end of actin filaments and require tropomyosin for optimal function. Tropomodulin is an elongated molecule with a molecular mass of about 40 kDa. The C-terminal half of tropomodulin contains one compact cooperatively melting domain, whereas the N-terminal half has no ...
Alla Kostyukova
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Tropomodulin is a tropomyosin-dependent actin filament capping protein involved in the structural formation of thin filaments and in the regulation of their lengths through its localization at the pointed ends of actin filaments.
Carol Gregorio +2 more
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Current Biology, 2021
Arit Ghosh and Velia Fowler introduce the structural features and functions of tropomodulins - actin-binding proteins that cap the slow-growing (pointed) ends of actin filaments.
Arit, Ghosh, Velia M, Fowler
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Arit Ghosh and Velia Fowler introduce the structural features and functions of tropomodulins - actin-binding proteins that cap the slow-growing (pointed) ends of actin filaments.
Arit, Ghosh, Velia M, Fowler
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Biochemical and Biophysical Research Communications, 2007
Microarray analysis was carried out to identify novel downstream target genes regulated by non-canonical Wnt signaling. We found that Tmod1, known as an actin-capping protein, is up-regulated by Wnt5a, while gelsolin, known as an actin-severing protein, is down-regulated by Wnt5a.
Eek-Hoon Jho
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Microarray analysis was carried out to identify novel downstream target genes regulated by non-canonical Wnt signaling. We found that Tmod1, known as an actin-capping protein, is up-regulated by Wnt5a, while gelsolin, known as an actin-severing protein, is down-regulated by Wnt5a.
Eek-Hoon Jho
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Domain structure of tropomodulin [PDF]
The structure of tropomodulin, the unique capping protein for the pointed end (the slow‐growing end) of an actin filament, was studied. An improved Escherichia coli expression system for chicken E‐tropomodulin was established and tropomodulin was prepared, Tmod (N39), in which 15 amino acid residues from the original C‐terminus are deleted at the DNA ...
Inna Krieger, Alla Kostyukova
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Lens Tropomodulin: Developmental Expression during Differentiation
Experimental Eye Research, 1996Lens epithelial cells undergo a dramatic transformation during the process of differentiation into elongated fiber cells. The membrane-associated actin cytoskeleton is likely to play a critical role in the stabilization and maintenance of the highly elongated fiber cell shape.
Mark Sussman, Larry Kedes, J W McAvoy
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Tropomodulins: life at the slow end
Trends in Cell Biology, 2003Dynamic exchange of actin monomers at filament ends is crucial for the functional architecture of many cytoskeletal-dependent processes. Recent evidence indicates that tropomodulins (Tmods), a conserved family of actin-capping proteins that bind to the pointed (slow-growing) end of actin filaments, regulate a variety of actin structures, including ...
Robert S, Fischer, Velia M, Fowler
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Neural tropomodulin: developmental expression and effect of seizure activity
Developmental Brain Research, 1994Tropomodulin is a 40.6 kDa tropomyosin-binding protein associated with actin filaments in muscle and the membrane cytoskeleton in erythrocytes. We have detected tropomodulin mRNA and protein in brains of rats by northern and western blot analyses.
Imad Najm +2 more
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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
openaire +1 more source

