Results 51 to 60 of about 2,101 (172)
Actin regulation by tropomodulin and tropomyosin in neuronal morphogenesis and function [PDF]
Molecular and Cellular Neuroscience, 2017 Actin is a profoundly influential protein; it impacts, among other processes, membrane morphology, cellular motility, and vesicle transport. Actin can polymerize into long filaments that push on membranes and provide support for intracellular transport.
Kevin T, Gray +2 more
openaire +2 more sources
Tropomodulin 1 directly controls thin filament length in both wild-type and tropomodulin 4-deficient skeletal muscle [PDF]
, 2015 The sarcomeric tropomodulin (Tmod) isoforms Tmod1 and Tmod4 cap thin filament pointed ends and functionally interact with the leiomodin (Lmod) isoforms Lmod2 and Lmod3 to control myofibril organization, thin filament lengths, and actomyosin crossbridge ...
Fowler, Velia M. +3 more
core +1 more source
Effect of the Structure of the N Terminus of Tropomyosin on Tropomodulin Function [PDF]
Journal of Biological Chemistry, 2004 Tropomodulins (Tmod) bind to the N terminus of tropomyosin and cap the pointed end of actin filaments. Tropomyosin alone also inhibits the rate of actin depolymerization at the pointed end of filaments. Here we have defined 1) the structural requirements of the N terminus of tropomyosin important for regulating the pointed end alone and with ...
Kostyukova, Alla S +1 more
openaire +3 more sources
British Journal of Haematology, EarlyView.Summary Diffuse large B‐cell lymphoma (DLBCL) is the most common aggressive non‐Hodgkin lymphoma and is characterized by substantial heterogeneity. This study aimed to develop a liquid–liquid phase separation (LLPS)‐related prognostic model to improve risk stratification.
Zhen‐Zhong Zhou +11 more
wiley +1 more source
Multifunctional roles of tropomodulin-3 in regulating actin dynamics [PDF]
Biophysical Reviews, 2018 Tropomodulins (Tmods) are proteins that cap the slow growing (pointed) ends of actin filaments (F-actin). The basis for our current understanding of Tmod function comes from studies in cells with relatively stable and highly organized F-actin networks, leading to the view that Tmod capping functions principally to preserve F-actin stability.
Parreno, Justin, Fowler, Velia M
openaire +2 more sources
Cytoplasmic Nuclear Transfer of the Actin-capping Protein Tropomodulin [PDF]
Journal of Biological Chemistry, 2004 Tropomodulin (Tmod) is a cytoskeletal actin-capping protein that interacts with tropomyosin at the pointed end of actin filaments. E-Tmod is an isoform that expresses predominantly in cardiac cells and slow skeletal muscle fibers. We unexpectedly discovered significant levels of Tmod in nuclei and then defined peptide domains in Tmod responsible for ...
Kimi Y, Kong, Larry, Kedes
openaire +2 more sources
Tropomodulin binds two tropomyosins: a novel model for actin filament capping
, 2006 Tropomodulin, a tropomyosin-binding protein, caps the slow-growing (pointed) end of the actin filament regulating its dynamics. Tropomodulin, therefore, is important for determining cell morphology, cell movement, and muscle contraction.
Kostyukova, Alla S +2 more
core +1 more source
Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle [PDF]
, 2010 Regulation of actin filament assembly is essential for efficient contractile activity in striated muscle. Leiomodin is an actin-binding protein and homolog of the pointed-end capping protein, tropomodulin. These proteins are structurally similar, sharing
Kostyukova, Alla S +11 more
core +1 more source
Disease Models & Mechanisms, 2014 Nemaline myopathy is an inherited muscle disease that is mainly diagnosed by the presence of nemaline rods in muscle biopsies. Of the nine genes associated with the disease, five encode components of striated muscle sarcomeres.
Joachim Berger +6 more
doaj +1 more source
The FEBS Journal, EarlyView.Trim32 regulates the transition from proliferation to differentiation in C2C12 cells after myogenic induction. We found that, at the onset of differentiation, Trim32 destabilizes c‐Myc mRNA, promotes cell cycle exit, and enables normal myotube formation.
Lu Xiong +6 more
wiley +1 more source