Results 141 to 150 of about 2,192 (170)

Comparative Transcriptomics as a Key to Understanding the Adaptation Mechanisms of Baikal Sculpins to the Deep-Water Habitat. [PDF]

open access: yesBiology (Basel)
Sapozhnikova YP   +11 more
europepmc   +1 more source
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Tropomodulins and tropomodulin/tropomyosin interactions

Cellular and Molecular Life Sciences, 2007
The 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
exaly   +3 more sources

Identification of Residues within Tropomodulin-1 Responsible for Its Localization at the Pointed Ends of the Actin Filaments in Cardiac Myocytes

open access: yesJournal of Biological Chemistry, 2011
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
exaly   +2 more sources

Tropomodulins

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
openaire   +2 more sources

Induced expression of the transcription of tropomodulin 1 by Wnt5a and characterization of the tropomodulin 1 promoter

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
exaly   +3 more sources

Domain structure of tropomodulin [PDF]

open access: yesFEBS Journal, 2000
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
exaly   +3 more sources

Lens Tropomodulin: Developmental Expression during Differentiation

Experimental Eye Research, 1996
Lens 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
exaly   +3 more sources

Tropomodulins: life at the slow end

Trends in Cell Biology, 2003
Dynamic 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
openaire   +2 more sources

Neural tropomodulin: developmental expression and effect of seizure activity

Developmental Brain Research, 1994
Tropomodulin 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
exaly   +3 more sources

Tropomodulin

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
openaire   +1 more source

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