Relevant bibliographies by topics / Acto-myosin contraction

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  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Acto-myosin contraction'

Author: Grafiati
Published: 2 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Acto-myosin contraction"

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Kelley, Charlotte, and Erin Cram. "Regulation of Actin Dynamics in the C. elegans Somatic Gonad." Journal of Developmental Biology 7, no. 1 (2019): 6. http://dx.doi.org/10.3390/jdb7010006.

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The reproductive system of the hermaphroditic nematode C. elegans consists of a series of contractile cell types—including the gonadal sheath cells, the spermathecal cells and the spermatheca–uterine valve—that contract in a coordinated manner to regulate oocyte entry and exit of the fertilized embryo into the uterus. Contraction is driven by acto-myosin contraction and relies on the development and maintenance of specialized acto-myosin networks in each cell type. Study of this system has revealed insights into the regulation of acto-myosin network assembly and contractility in vivo.
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Giansanti, M. G., S. Bonaccorsi, and M. Gatti. "The role of anillin in meiotic cytokinesis of Drosophila males." Journal of Cell Science 112, no. 14 (1999): 2323–34. http://dx.doi.org/10.1242/jcs.112.14.2323.

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Anillin is a 190 kDa actin-binding protein that concentrates in the leading edges of furrow canals during Drosophila cellularization and in the cleavage furrow of both somatic and meiotic cells. We analyzed anillin behavior during D. melanogaster spermatogenesis, and focused on the relationships between this protein and the F-actin enriched structures. In meiotic anaphases anillin concentrates in a narrow band around the cell equator. Cytological analysis of wild-type meiosis and examination of mutants defective in contractile ring assembly (chickadee and KLP3A), revealed that the formation of
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Lartey, J., and A. López Bernal. "RHO protein regulation of contraction in the human uterus." REPRODUCTION 138, no. 3 (2009): 407–24. http://dx.doi.org/10.1530/rep-09-0160.

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The state of contraction in smooth muscle cells of the human uterus is dependent on the interaction of activated forms of actin and myosin. Ras homology (RHO) proteins are small monomeric GTP-binding proteins that regulate actin polymerisation and myosin phosphorylation in smooth muscle cells. Their action is determined by their level of expression, GTP-bound state, intracellular localisation and phosphorylated status. Agonist activated RHO proteins bind to effector kinases such as RHO kinase (ROCK) and diaphanous proteins (DIAPH) to regulate smooth muscle contraction by two mechanisms: ROCK a
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Moraczewska, Joanna. "Structural determinants of cooperativity in acto-myosin interactions." Acta Biochimica Polonica 49, no. 4 (2002): 805–12. http://dx.doi.org/10.18388/abp.2002_3740.

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Regulation of muscle contraction is a very cooperative process. The presence of tropomyosin on the thin filament is both necessary and sufficient for cooperativity to occur. Data recently obtained with various tropomyosin isoforms and mutants help us to understand better the structural requirements in the thin filament for cooperative protein interactions. Forming an end-to-end overlap between neighboring tropomyosin molecules is not necessary for the cooperativity of the thin filament activation. When direct contacts between tropomyosin molecules are disrupted, the conformational changes in t
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De Pascalis, Chiara, Carlos Pérez-González, Shailaja Seetharaman, et al. "Intermediate filaments control collective migration by restricting traction forces and sustaining cell–cell contacts." Journal of Cell Biology 217, no. 9 (2018): 3031–44. http://dx.doi.org/10.1083/jcb.201801162.

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Mesenchymal cell migration relies on the coordinated regulation of the actin and microtubule networks that participate in polarized cell protrusion, adhesion, and contraction. During collective migration, most of the traction forces are generated by the acto-myosin network linked to focal adhesions at the front of leader cells, which transmit these pulling forces to the followers. Here, using an in vitro wound healing assay to induce polarization and collective directed migration of primary astrocytes, we show that the intermediate filament (IF) network composed of vimentin, glial fibrillary a
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Madan, Aditi, Meera C. Viswanathan, Kathleen C. Woulfe, et al. "TNNT2mutations in the tropomyosin binding region of TNT1 disrupt its role in contractile inhibition and stimulate cardiac dysfunction." Proceedings of the National Academy of Sciences 117, no. 31 (2020): 18822–31. http://dx.doi.org/10.1073/pnas.2001692117.

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Muscle contraction is regulated by the movement of end-to-end-linked troponin−tropomyosin complexes over the thin filament surface, which uncovers or blocks myosin binding sites along F-actin. The N-terminal half of troponin T (TnT), TNT1, independently promotes tropomyosin-based, steric inhibition of acto-myosin associations, in vitro. Recent structural models additionally suggest TNT1 may restrain the uniform, regulatory translocation of tropomyosin. Therefore, TnT potentially contributes to striated muscle relaxation; however, the in vivo functional relevance and molecular basis of this non
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7

Trinickt, John, and Howard White. "CRYO-Electron Microscopy of the Acto-Myosin-ATP Complex." Proceedings, annual meeting, Electron Microscopy Society of America 48, no. 1 (1990): 248–49. http://dx.doi.org/10.1017/s0424820100179993.

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The primary force of muscle contraction is thought to involve a change in the myosin head whilst attached to actin, the energy coming from ATP hydrolysis. This change in attached state could either be a conformational change in the head or an alteration in the binding angle made with actin. A considerable amount is known about one bound state, the so-called strongly attached state, which occurs in the presence of ADP or in the absence of nucleotide. In this state, which probably corresponds to the last attached state of the force-producing cycle, the angle between the long axis myosin head and
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Marcucci, Lorenzo, Hiroki Fukunaga, Toshio Yanagida, and Mitsuhiro Iwaki. "The Synergic Role of Actomyosin Architecture and Biased Detachment in Muscle Energetics: Insights in Cross Bridge Mechanism beyond the Lever-Arm Swing." International Journal of Molecular Sciences 22, no. 13 (2021): 7037. http://dx.doi.org/10.3390/ijms22137037.

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Muscle energetics reflects the ability of myosin motors to convert chemical energy into mechanical energy. How this process takes place remains one of the most elusive questions in the field. Here, we combined experimental measurements of in vitro sliding velocity based on DNA-origami built filaments carrying myosins with different lever arm length and Monte Carlo simulations based on a model which accounts for three basic components: (i) the geometrical hindrance, (ii) the mechano-sensing mechanism, and (iii) the biased kinetics for stretched or compressed motors. The model simulations showed
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Kitayama, Chikako, Asako Sugimoto, and Masayuki Yamamoto. "Type II Myosin Heavy Chain Encoded by the myo2 Gene Composes the Contractile Ring during Cytokinesis in Schizosaccharomyces pombe." Journal of Cell Biology 137, no. 6 (1997): 1309–19. http://dx.doi.org/10.1083/jcb.137.6.1309.

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We cloned the myo2 gene of Schizosaccharomyces pombe, which encodes a type II myosin heavy chain, by virtue of its ability to promote diploidization in fission yeast cells. The myo2 gene encodes 1,526 amino acids in a single open reading frame. Myo2p shows homology to the head domains and the coiledcoil tail of the conventional type II myosin heavy chain and carries putative binding sites for ATP and actin. It also carries the IQ motif, which is a presumed binding site for the myosin light chain. However, Myo2p apparently carries only one IQ motif, while its counterparts in other species have
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Hong, Feng, Richard K. Brizendine, Michael S. Carter, et al. "Diffusion of myosin light chain kinase on actin: A mechanism to enhance myosin phosphorylation rates in smooth muscle." Journal of General Physiology 146, no. 4 (2015): 267–80. http://dx.doi.org/10.1085/jgp.201511483.

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Smooth muscle myosin (SMM) light chain kinase (MLCK) phosphorylates SMM, thereby activating the ATPase activity required for muscle contraction. The abundance of active MLCK, which is tightly associated with the contractile apparatus, is low relative to that of SMM. SMM phosphorylation is rapid despite the low ratio of MLCK to SMM, raising the question of how one MLCK rapidly phosphorylates many SMM molecules. We used total internal reflection fluorescence microscopy to monitor single molecules of streptavidin-coated quantum dot–labeled MLCK interacting with purified actin, actin bundles, and
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Dissertations / Theses on the topic "Acto-myosin contraction"

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Melnyk, Jason Alexander. "Contractile Performance and Energy Utilization of Skeletal Muscle; Creatine Kinase and Acto-myosin ATPase." Diss., Virginia Tech, 2009. http://hdl.handle.net/10919/26116.

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Creatine kinase (CK) primarily serves as an energy buffer assisting in regulating ATP homeostasis through synthesis of ATP from ADP and phosphocreatine (PCr). This enzyme is bound in the sarcomere near sites of ATP consumption via acto-myosin ATPase (A‧M‧ATPase) and research in cardiac muscle has found that PCr can alter contractile performance (maximal isometric force and Ca²⁺ sensitivity). Based on this evidence, CK and A‧M‧ATPase may be coupled in skeletal muscle. Therefore the purpose of this investigation was to determine the influence of the CK system on contractile performance and energ
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Book chapters on the topic "Acto-myosin contraction"

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Onishi, Hirofumi. "Interaction Between Two Myosin Heads in Acto-Smooth Muscle Heavy Meromyosin Rigor Complex." In Mechanism of Myofilament Sliding in Muscle Contraction. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2872-2_20.

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