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Relevant bibliographies by topics / Polymerization force

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Journal articles

Academic literature on the topic 'Polymerization force'

Author: Grafiati

Published: 22 February 2023

Last updated: 23 February 2023

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Journal articles on the topic "Polymerization force"

1

Dmitrieff, Serge, and François Nédélec. "Amplification of actin polymerization forces." Journal of Cell Biology 212, no. 7 (2016): 763–66. http://dx.doi.org/10.1083/jcb.201512019.

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The actin cytoskeleton drives many essential processes in vivo, using molecular motors and actin assembly as force generators. We discuss here the propagation of forces caused by actin polymerization, highlighting simple configurations where the force developed by the network can exceed the sum of the polymerization forces from all filaments.

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Yoo, I.-S., D. Kim, K. Kim, and S.-h. Park. "Change in the Shrinkage Forces of Composite Resins According to Controlled Deflection." Operative Dentistry 46, no. 5 (2021): 577–88. http://dx.doi.org/10.2341/20-196-l.

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SUMMARY The aim of this study was to investigate how the polymerization shrinkage forces of composite resins change with change in deflection. Five composites, SDR (Dentsply Caulk, Milford, DE, USA), EcuSphere-Shape (DMG, Hamburg, Germany), Tetric N-Ceram Bulk Fill (Ivoclar Vivadent, Schaan, Liechtenstein), CLEARFIL AP-X (Kuraray Noritake Dental Inc., Sakazu, Kurashiki, Okayama, Japan), and Filtek Z350 XT (3M Dental Products, St Paul, MN, USA), were tested in this experiment. The polymerization shrinkage forces of the composites were measured using a custom-made tooth-deflection-mimicking devi

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3

Rullo, Jacob, Henry Becker, Sharon J. Hyduk та ін. "Actin polymerization stabilizes α4β1 integrin anchors that mediate monocyte adhesion". Journal of Cell Biology 197, № 1 (2012): 115–29. http://dx.doi.org/10.1083/jcb.201107140.

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Leukocytes arrested on inflamed endothelium via integrins are subjected to force imparted by flowing blood. How leukocytes respond to this force and resist detachment is poorly understood. Live-cell imaging with Lifeact-transfected U937 cells revealed that force triggers actin polymerization at upstream α4β1 integrin adhesion sites and the adjacent cortical cytoskeleton. Scanning electron microscopy revealed that this culminates in the formation of structures that anchor monocyte adhesion. Inhibition of actin polymerization resulted in cell deformation, displacement, and detachment. Transfecti

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4

Kozlov, Michael M., and Alexander D. Bershadsky. "Processive capping by formin suggests a force-driven mechanism of actin polymerization." Journal of Cell Biology 167, no. 6 (2004): 1011–17. http://dx.doi.org/10.1083/jcb.200410017.

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Regulation of actin polymerization is essential for cell functioning. Here, we predict a novel phenomenon—the force-driven polymerization of actin filaments mediated by proteins of the formin family. Formins localize to the barbed ends of actin filaments, but, in contrast to the standard capping proteins, allow for actin polymerization in the barbed direction. First, we show that the mechanism of such “leaky capping” can be understood in terms of the elasticity of the formin molecules. Second, we demonstrate that if a pulling force acts on the filament end via the leaky cap, the elastic stress

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5

Chen, Xuesong, Kristin Pavlish, and Joseph N. Benoit. "Myosin phosphorylation triggers actin polymerization in vascular smooth muscle." American Journal of Physiology-Heart and Circulatory Physiology 295, no. 5 (2008): H2172—H2177. http://dx.doi.org/10.1152/ajpheart.91437.2007.

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A variety of contractile stimuli increases actin polymerization, which is essential for smooth muscle contraction. However, the mechanism(s) of actin polymerization associated with smooth muscle contraction is not fully understood. We tested the hypothesis that phosphorylated myosin triggers actin polymerization. The present study was conducted in isolated intact or β-escin-permeabilized rat small mesenteric arteries. Reductions in the 20-kDa myosin regulatory light chain (MLC20) phosphorylation were achieved by inhibiting MLC kinase with ML-7. Increases in MLC20 phosphorylation were achieved

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Herling, Therese W., Gonzalo A. Garcia, Thomas C. T. Michaels, et al. "Force generation by the growth of amyloid aggregates." Proceedings of the National Academy of Sciences 112, no. 31 (2015): 9524–29. http://dx.doi.org/10.1073/pnas.1417326112.

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The generation of mechanical forces are central to a wide range of vital biological processes, including the function of the cytoskeleton. Although the forces emerging from the polymerization of native proteins have been studied in detail, the potential for force generation by aberrant protein polymerization has not yet been explored. Here, we show that the growth of amyloid fibrils, archetypical aberrant protein polymers, is capable of unleashing mechanical forces on the piconewton scale for individual filaments. We apply microfluidic techniques to measure the forces released by amyloid growt

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7

Tejani, Ankit D., Michael P. Walsh, and Christopher M. Rembold. "Tissue length modulates “stimulated actin polymerization,” force augmentation, and the rate of swine carotid arterial contraction." American Journal of Physiology-Cell Physiology 301, no. 6 (2011): C1470—C1478. http://dx.doi.org/10.1152/ajpcell.00149.2011.

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“Stimulated actin polymerization” has been proposed to be involved in force augmentation, in which prior submaximal activation of vascular smooth muscle increases the force of a subsequent maximal contraction by ∼15%. In this study, we altered stimulated actin polymerization by adjusting tissue length and then measured the effect on force augmentation. At optimal tissue length (1.0 Lo), force augmentation was observed and was associated with increased prior stimulated actin polymerization, as evidenced by increased prior Y118 paxillin phosphorylation without changes in prior S3 cofilin or cros

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8

Tizazu, Getachew. "Investigation of the Effect of Molecular Weight, Density, and Initiator Structure Size on the Repulsive Force between a PNIPAM Polymer Brush and Protein." Advances in Polymer Technology 2022 (October 22, 2022): 1–20. http://dx.doi.org/10.1155/2022/9741080.

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This paper focuses on the effect of degree of polymerization (N), density ( σ ), and pattern size ( x ) on the interaction force between a periodically patterned Poly(N-isopropylacrylamide) (PNIPAM) brush and protein. The hydrophobic interaction, the Van der Waals attractive force, and the steric repulsive force were expressed in terms of N , σ , and x . The osmotic constant (k1) and the entropic constant (k2) were determined from the fit of the steric repulsive force to an experimentally obtained force distance curve. The osmotic constant was 0.105, and the entropic constant was 0.255. Using

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9

Schreiber, Christoph, Behnam Amiri, Johannes C. J. Heyn, Joachim O. Rädler, and Martin Falcke. "On the adhesion–velocity relation and length adaptation of motile cells on stepped fibronectin lanes." Proceedings of the National Academy of Sciences 118, no. 4 (2021): e2009959118. http://dx.doi.org/10.1073/pnas.2009959118.

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The biphasic adhesion–velocity relation is a universal observation in mesenchymal cell motility. It has been explained by adhesion-promoted forces pushing the front and resisting motion at the rear. Yet, there is little quantitative understanding of how these forces control cell velocity. We study motion of MDA-MB-231 cells on microlanes with fields of alternating Fibronectin densities to address this topic and derive a mathematical model from the leading-edge force balance and the force-dependent polymerization rate. It reproduces quantitatively our measured adhesion–velocity relation and res

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10

Fung, David C., and Julie A. Theriot. "Actin Dynamics and Force Generation in the Motility of Listeria Monocytogenes." Microscopy and Microanalysis 3, S2 (1997): 209–10. http://dx.doi.org/10.1017/s1431927600007935.

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The gram-positive bacterium Listeria monocytogenes is one of several intracellular pathogens which can move about within its host's cytoplasm using a form of actin-based motility. This motility plays an important role in the virulence of the microbe, which can cause serious disease in humans. Actin is a host-cell protein whose polymerization is required for the locomotion of animal cells. L. monocytogenes exploits this normal cellular machinery for its own movement by creating a “comet” tail of cross-linked actin filaments behind it. Actin polymerization occurs at the bacterial surface and is

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