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Journal articles on the topic 'Polymerization and depolymerization'

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1

Fukushima, Nobuyuki, Isao Ishii, Yoshiaki Habara, Cara B. Allen та Jerold Chun. "Dual Regulation of Actin Rearrangement through Lysophosphatidic Acid Receptor in Neuroblast Cell Lines: Actin Depolymerization by Ca2+-α-Actinin and Polymerization by Rho". Molecular Biology of the Cell 13, № 8 (2002): 2692–705. http://dx.doi.org/10.1091/mbc.01-09-0465.

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Lysophosphatidic acid (LPA) is a potent lipid mediator with actions on many cell types. Morphological changes involving actin polymerization are mediated by at least two cognate G protein-coupled receptors, LPA1/EDG-2 or LPA2/EDG-4. Herein, we show that LPA can also induce actin depolymerization preceding actin polymerization within single TR mouse immortalized neuroblasts. Actin depolymerization resulted in immediate loss of membrane ruffling, whereas actin polymerization resulted in process retraction. Each pathway was found to be independent: depolymerization mediated by intracellular calci
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2

Hofer, Gregor, Florian Grieder, Martin Kröger, A. Dieter Schlüter, and Thomas Weber. "Unraveling two-dimensional polymerization in the single crystal." Journal of Applied Crystallography 51, no. 2 (2018): 481–97. http://dx.doi.org/10.1107/s1600576718002820.

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Two-dimensional single-crystal-to-single-crystal polymerization and depolymerization are described in detail. The results are based on in-house and synchrotron X-ray diffraction experiments conducted on several samples at 100 K and room temperature. The reactions are associated with considerable molecular motions of all components (monomer, template and incorporated solvent molecules), which can be as large as 1 Å. Continuous polymerization leads to a gradual gap opening between the emerging two-dimensional polymer layers, which allows for increased mobility of the solvent molecules. The posit
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3

Wang, Hyun Suk, and Athina Anastasaki. "Chemical Recycling of Polymethacrylates Synthesized by RAFT Polymerization." CHIMIA 77, no. 4 (2023): 217. http://dx.doi.org/10.2533/chimia.2023.217.

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Reversing controlled radical polymerization and regenerating the monomer has been a long-standing challenge for fundamental research and practical applications. Herein, we report a highly efficient depolymerization method for various polymethacrylates synthesized by reversible addition-fragmentation chain-transfer (RAFT) polymerization. The depolymerization process, which does not require any catalyst, exhibits near-quantitative conversions of up to 92%. The key aspect of our approach is the utilization of the high end-group fidelity of RAFT polymers to generate chain-end radicals at 120 °C. T
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4

WILLIAMS, J., H. SCHULTEN, N. VANDERBORGH, and R. WALKER. "Polymerization-depolymerization of 1,3-dioxolane." Polymer 33, no. 21 (1992): 4630–34. http://dx.doi.org/10.1016/0032-3861(92)90424-u.

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5

Kruus, P., J. A. G. Lawrie, and M. L. O'Neill. "Polymerization and depolymerization by ultrasound." Ultrasonics 26, no. 6 (1988): 352–55. http://dx.doi.org/10.1016/0041-624x(88)90035-2.

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6

Geng, Huawei, Zonggang Mou, Ziyong Liu, Fuli Li, and Cheng Yang. "Biochemical Degradation of Chitosan over Immobilized Cellulase and Supported Fenton Catalysts." Catalysts 10, no. 6 (2020): 604. http://dx.doi.org/10.3390/catal10060604.

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This paper describes the application of Fe-MCM-48 (Mobil Composition of Matter No.48) and cellulase-MCM-48 catalysts for the depolymerization of chitosan. The results show that H2O2 is a good oxidant for the depolymerization of chitosan in the presence of Fe-MCM-48. The average polymerization degree of the product decreased to 6.1, and decreased to 29.2 when cellulase-MCM-48 was used as a catalyst, because the effect of the enzyme was affected by the molecular structure of chitosan. When both materials were used for depolymerization, the average degree of polymerization sharply decreased to 3.
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7

Wang, Hyun Suk, Mikhail Agrachev, Hongsik Kim, et al. "Visible light–triggered depolymerization of commercial polymethacrylates." Science 387, no. 6736 (2025): 874–80. https://doi.org/10.1126/science.adr1637.

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The reversion of vinyl polymers with carbon-carbon backbones to their monomers represents an ideal path to alleviate the growing plastic waste stream. However, depolymerizing such stable materials remains a challenge, with state-of-the-art methods relying on “designer” polymers that are neither commercially produced nor suitable for real-world applications. In this work, we report a main chain–initiated, visible light–triggered depolymerization directly applicable to commercial polymers containing undisclosed impurities (e.g., comonomers, additives, or dyes). By in situ generation of chlorine
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8

Flanders, Michael J., and William M. Gramlich. "Reversible-addition fragmentation chain transfer (RAFT) mediated depolymerization of brush polymers." Polymer Chemistry 9, no. 17 (2018): 2328–35. http://dx.doi.org/10.1039/c8py00446c.

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9

Hirshman, Carol A., Defen Zhu, Reynold A. Panettieri та Charles W. Emala. "Actin depolymerization via the β-adrenoceptor in airway smooth muscle cells: a novel PKA-independent pathway". American Journal of Physiology-Cell Physiology 281, № 5 (2001): C1468—C1476. http://dx.doi.org/10.1152/ajpcell.2001.281.5.c1468.

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Actin is a major functional and structural cytoskeletal protein that mediates such diverse processes as motility, cytokinesis, contraction, and control of cell shape and polarity. While many extracellular signals are known to mediate actin filament polymerization, considerably less is known about signals that mediate depolymerization of the actin cytoskeleton. Human airway smooth muscle cells were briefly exposed to isoproterenol, forskolin, or the cAMP-dependent protein kinase A (PKA) agonist stimulatory diastereoisomer of adenosine 3′,5′-cyclic monophosphate (Sp-cAMPS). Actin polymerization
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10

Tirnauer, Jennifer S., E. D. Salmon, and Timothy J. Mitchison. "Microtubule Plus-End Dynamics in Xenopus Egg Extract Spindles." Molecular Biology of the Cell 15, no. 4 (2004): 1776–84. http://dx.doi.org/10.1091/mbc.e03-11-0824.

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Microtubule dynamics underlie spindle assembly, yet we do not know how the spindle environment affects these dynamics. We developed methods for measuring two key parameters of microtubule plus-end dynamic instability in Xenopus egg extract spindles. To measure plus-end polymerization rates and localize growing plus ends, we used fluorescence confocal imaging of EB1. This revealed plus-end polymerization throughout the spindle at ∼11 μm/min, similar to astral microtubules, suggesting polymerization velocity is not regionally regulated by the spindle. The ratio of EB1 to microtubule fluorescence
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11

Kake, T., S. Kimura, K. Takahashi, and K. Maruyama. "Calponin induces actin polymerization at low ionic strength and inhibits depolymerization of actin filaments." Biochemical Journal 312, no. 2 (1995): 587–92. http://dx.doi.org/10.1042/bj3120587.

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Calponin from chicken gizzard induced polymerization of actin in the presence of 10 mM KCl. Only 2 min after the addition of KCl in the presence of a 0.0625-0.25:1 molar ratio of calponin to actin, a Poisson-type length distribution (with an average length of approx. 0.7 micron) was observed with formed actin filaments. This result suggests that calponin-actin complexes served as nuclei for rapid elongation. Calponin caused a rapid polymerization of actin even in G-buffer (2 mM Tris/HCl, pH 8.0) which is usually used for depolymerization of actin filaments. Binding of calponin at a level of up
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12

Hao, Shengli, and Avery August. "Actin Depolymerization Transduces the Strength of B-Cell Receptor Stimulation." Molecular Biology of the Cell 16, no. 5 (2005): 2275–84. http://dx.doi.org/10.1091/mbc.e04-10-0881.

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Polymerization of the actin cytoskeleton has been found to be essential for B-cell activation. We show here, however, that stimulation of BCR induces a rapid global actin depolymerization in a BCR signal strength-dependent manner, followed by polarized actin repolymerization. Depolymerization of actin enhances and blocking actin depolymerization inhibits BCR signaling, leading to altered BCR and lipid raft clustering, ERK activation, and transcription factor activation. Furthermore actin depolymerization by itself induces altered lipid raft clustering and ERK activation, suggesting that F-acti
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13

Lloyd, Danielle J., Vasiliki Nikolaou, Jennifer Collins, et al. "Controlled aqueous polymerization of acrylamides and acrylates and “in situ” depolymerization in the presence of dissolved CO2." Chemical Communications 52, no. 39 (2016): 6533–36. http://dx.doi.org/10.1039/c6cc03027k.

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14

Howard, T. H., and C. O. Oresajo. "The kinetics of chemotactic peptide-induced change in F-actin content, F-actin distribution, and the shape of neutrophils." Journal of Cell Biology 101, no. 3 (1985): 1078–85. http://dx.doi.org/10.1083/jcb.101.3.1078.

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Formyl-met-leu-phe (fMLP) induces actin assembly in neutrophils; the resultant increase in F-actin content correlates with an increase in the rate of cellular locomotion at fMLP concentrations less than or equal to 10(-8) M (Howard, T.H., and W.H. Meyer, 1984, J. Cell Biol., 98:1265-1271). We studied the time course of change in F-actin content, F-actin distribution, and cell shape after fMLP stimulation. F-actin content was quantified by fluorescence activated cell sorter analysis of nitrobenzoxadiazole-phallacidin-stained cells (Howard, T.H., 1982, J. Cell Biol., 95(2, Pt. 2:327a). F-actin d
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15

Nelson, Zachary, Nathan A. Romero, Jan Tiepelt, Marc Baldo, and Timothy M. Swager. "Polymerization and Depolymerization of Photoluminescent Polyarylene Chalcogenides." Macromolecules 54, no. 14 (2021): 6698–704. http://dx.doi.org/10.1021/acs.macromol.1c00546.

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16

Kumar, Rajeev, Zening Liu, Brad Lokitz, et al. "Harnessing autocatalytic reactions in polymerization and depolymerization." MRS Communications 11, no. 4 (2021): 377–90. http://dx.doi.org/10.1557/s43579-021-00061-9.

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Abstract Autocatalysis and its relevance to various polymeric systems are discussed by taking inspiration from biology. A number of research directions related to synthesis, characterization, and multi-scale modeling are discussed in order to harness autocatalytic reactions in a useful manner for different applications ranging from chemical upcycling of polymers (depolymerization and reconstruction after depolymerization), self-generating micelles and vesicles, and polymer membranes. Overall, a concerted effort involving in situ experiments, multi-scale modeling, and machine learning algorithm
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17

Zaltsman, Inbar, and Moshe Kol. "Camphor the polymerization; stay for the depolymerization." Chem 10, no. 10 (2024): 2950–52. http://dx.doi.org/10.1016/j.chempr.2024.09.023.

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18

Hyver, C. "Generation of oscillations in polymerization–depolymerization systems." Journal of Chemical Physics 83, no. 2 (1985): 850–51. http://dx.doi.org/10.1063/1.449499.

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19

Höcker, Hartwig, and Helmut Keul. "Ring-Opening Polymerization and ring-closing depolymerization." Advanced Materials 6, no. 1 (1994): 21–36. http://dx.doi.org/10.1002/adma.19940060104.

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20

Jung, Hyo Il, Incheol Shin, Young Mok Park, Ke Won Kang, and Kwon-Soo Ha. "Colchicine Activates Actin Polymerization by Microtubule Depolymerization." Molecules and Cells 7, no. 3 (1997): 431–37. http://dx.doi.org/10.1016/s1016-8478(23)13317-6.

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21

Fang, Yue, and Hanyu Gao. "Kinetic modeling for radical polymerization and depolymerization." Current Opinion in Chemical Engineering 49 (September 2025): 101152. https://doi.org/10.1016/j.coche.2025.101152.

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22

Fees, Colby P., and Jeffrey K. Moore. "A unified model for microtubule rescue." Molecular Biology of the Cell 30, no. 6 (2019): 753–65. http://dx.doi.org/10.1091/mbc.e18-08-0541.

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How microtubules transition from depolymerization to polymerization, known as rescue, is poorly understood. Here we examine two models for rescue: 1) an “end-driven” model in which the depolymerizing end stochastically switches to a stable state; and 2) a “lattice-driven” model in which rescue sites are integrated into the microtubule before depolymerization. We test these models using a combination of computational simulations and in vitro experiments with purified tubulin. Our findings support the “lattice-driven” model by identifying repeated rescue sites in microtubules. In addition, we di
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23

Ganeshina, Olga, Jessika Erdmann, Sandra Tiberi, Misha Vorobyev, and Randolf Menzel. "Depolymerization of actin facilitates memory formation in an insect." Biology Letters 8, no. 6 (2012): 1023–27. http://dx.doi.org/10.1098/rsbl.2012.0784.

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In mammals, memory formation and stabilization requires polymerization of actin. Here, we show that, in the honeybee, inhibition of actin polymerization within the brain centres involved in memory formation, the mushroom bodies (MBs), enhances associative olfactory memory. Local application of inhibitors of actin polymerization (Cytochalasin D or Latrunculin A) to the MBs 1 h before induction of long-term memory increased memory retention 2 and 24 h after the onset of training. Post-training application of Cytochalasin D also enhanced retention, indicating that memory consolidation is facilita
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24

Joshi, Anup S., Niloofar Alipourasiabi, Keerthi Vinnakota, Maria R. Coleman, and Joseph G. Lawrence. "Improved polymerization and depolymerization kinetics of poly(ethylene terephthalate) by co-polymerization with 2,5-furandicarboxylic acid." RSC Advances 11, no. 38 (2021): 23506–18. http://dx.doi.org/10.1039/d1ra04359e.

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Incorporation of the bio-based 2,5-furandicarboxylic acid (FDCA) in poly(ethylene terephthalate) as a copolymer (PETF) improves esterification and depolymerization kinetics due to higher solubility and acidity of FDCA in the reaction media.
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25

Murray, J. W., B. T. Edmonds, G. Liu, and J. Condeelis. "Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends." Journal of Cell Biology 135, no. 5 (1996): 1309–21. http://dx.doi.org/10.1083/jcb.135.5.1309.

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Elongation factor 1 alpha (EF1 alpha) is an abundant protein that binds aminoacyl-tRNA and ribosomes in a GTP-dependent manner. EF1 alpha also interacts with the cytoskeleton by binding and bundling actin filaments and microtubules. In this report, the effect of purified EF1 alpha on actin polymerization and depolymerization is examined. At molar ratios present in the cytosol, EF1 alpha significantly blocks both polymerization and depolymerization of actin filaments and increases the final extent of actin polymer, while at high molar ratios to actin, EF1 alpha nucleates actin polymerization. A
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26

Norgauer, J., M. Eberle, H. D. Lemke, and K. Aktories. "Activation of human neutrophils by mastoparan. Reorganization of the cytoskeleton, formation of phosphatidylinositol 3,4,5-trisphosphate, secretion up-regulation of complement receptor type 3 and superoxide anion production are stimulated by mastoparan." Biochemical Journal 282, no. 2 (1992): 393–97. http://dx.doi.org/10.1042/bj2820393.

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In human neutrophils, mastoparan induced rapid F-actin polymerization which was followed by a slow and sustained depolymerization to below the initial F-actin content. Incubation of neutrophils with pertussis toxin inhibited mastoparan-stimulated actin polymerization; however it did not prevent sustained depolymerization of F-actin. Analyses of phospholipids performed in parallel revealed that mastoparan stimulated rapid formation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) and consumption of phosphatidylinositol 4,5-bisphosphate (PIP2). Pertussis toxin treatment blocked mastoparan-indu
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27

Hariadi, Rizal F., Bernard Yurke, and Erik Winfree. "Thermodynamics and kinetics of DNA nanotube polymerization from single-filament measurements." Chemical Science 6, no. 4 (2015): 2252–67. http://dx.doi.org/10.1039/c3sc53331j.

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Single-filament measurement of the thermodynamic and kinetic parameters of DNA nanotube assembly supports a polymerization/depolymerization model sharing common features with cytoskeletal polymer models.
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28

Mitchison, T. J., and E. D. Salmon. "Poleward kinetochore fiber movement occurs during both metaphase and anaphase-A in newt lung cell mitosis." Journal of Cell Biology 119, no. 3 (1992): 569–82. http://dx.doi.org/10.1083/jcb.119.3.569.

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Microtubules in the mitotic spindles of newt lung cells were marked using local photoactivation of fluorescence. The movement of marked segments on kinetochore fibers was tracked by digital fluorescence microscopy in metaphase and anaphase and compared to the rate of chromosome movement. In metaphase, kinetochore oscillations toward and away from the poles were coupled to kinetochore fiber shortening and growth. Marked zones on the kinetochore microtubules, meanwhile, moved slowly polewards at a rate of approximately 0.5 micron/min, which identifies a slow polewards movement, or "flux," of kin
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29

Xu, Guangqiang, and Qinggang Wang. "Chemically recyclable polymer materials: polymerization and depolymerization cycles." Green Chemistry 24, no. 6 (2022): 2321–46. http://dx.doi.org/10.1039/d1gc03901f.

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In this review, we aim to summarize strategies for achieving the polymerization–depolymerization cycle to access chemically recyclable polymers and highlight the current studies in this rapidly growing and promising area.
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30

Platts, Steven H., Jeff C. Falcone, William T. Holton, Michael A. Hill, and Gerald A. Meininger. "Alteration of microtubule polymerization modulates arteriolar vasomotor tone." American Journal of Physiology-Heart and Circulatory Physiology 277, no. 1 (1999): H100—H106. http://dx.doi.org/10.1152/ajpheart.1999.277.1.h100.

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Microtubules are important cytoskeletal elements that have been shown to play a major role in many cellular processes because of their mechanical properties and/or their participation in various cell signaling pathways. We tested the hypothesis that depolymerization of microtubules would alter vascular smooth muscle (VSM) tone and hence contractile function. In our studies, isolated cremaster arterioles exhibited significant vasoconstriction that developed over a 20- to 40-min period when they were treated with microtubule depolymerizing drugs colchicine (10 μM), nocodazole (10 μM), or demecol
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31

Abel, Brooks A., Rachel L. Snyder, and Geoffrey W. Coates. "Chemically recyclable thermoplastics from reversible-deactivation polymerization of cyclic acetals." Science 373, no. 6556 (2021): 783–89. http://dx.doi.org/10.1126/science.abh0626.

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Identifying plastics capable of chemical recycling to monomer (CRM) is the foremost challenge in creating a sustainable circular plastic economy. Polyacetals are promising candidates for CRM but lack useful tensile strengths owing to the low molecular weights produced using current uncontrolled cationic ring-opening polymerization (CROP) methods. Here, we present reversible-deactivation CROP of cyclic acetals using a commercial halomethyl ether initiator and an indium(III) bromide catalyst. Using this method, we synthesize poly(1,3-dioxolane) (PDXL), which demonstrates tensile strength compara
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32

Templeton, Douglas M., and Ying Liu. "Effects of cadmium on the actin cytoskeleton in renal mesangial cells." Canadian Journal of Physiology and Pharmacology 91, no. 1 (2013): 1–7. http://dx.doi.org/10.1139/cjpp-2012-0229.

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We provide an overview of our studies on cadmium and the actin cytoskeleton in mesangial cells, from earlier work on the effects of Cd2+ on actin polymerization in vivo and in vitro, to a role of disruption or stabilization of the cytoskeleton in apoptosis and apoptosis-like death. More recent studies implicate cadmium-dependent association of gelsolin and the Ca2+/calmodulin-dependent protein kinase II (CaMK-II) with actin filaments in cytoskeletal effects. We also present previously unpublished data concerning cadmium and the disruption of focal adhesions. The work encompasses studies on rat
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33

Omann, G. M., R. Rengan, J. F. Hoffman, and J. J. Linderman. "Rapid oscillations of actin polymerization/depolymerization in polymorphonuclear leukocytes stimulated by leukotriene B4 and platelet-activating factor." Journal of Immunology 155, no. 11 (1995): 5375–81. http://dx.doi.org/10.4049/jimmunol.155.11.5375.

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Abstract We previously showed that activation of polymorphonuclear leukocytes by leukotriene B4 (LTB4) and platelet-activating factor produces a rapidly oscillating actin polymerization/depolymerization response. In this study, we show that 1) oscillations are not due to the stimulated cyclic release of autocoids that could bind to cell surface receptors and activate subsequent cycles; 2) oscillations are not related to oscillations of ligand binding; and 3) the particular kinetic pattern is a property of the receptor, not of the binding constants of the ligand. The major conclusion of these s
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34

McCoy, Benjamin J., and Giridhar Madras. "Discrete and continuous models for polymerization and depolymerization." Chemical Engineering Science 56, no. 8 (2001): 2831–36. http://dx.doi.org/10.1016/s0009-2509(00)00516-9.

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Höcker, Hartwig, and Helmut Keul. "Ring-opening polymerization and depolymerization in respective polymers." Macromolecular Symposia 98, no. 1 (1995): 825–34. http://dx.doi.org/10.1002/masy.19950980169.

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36

Levee, M. G., M. I. Dabrowska, J. L. Lelli, and D. B. Hinshaw. "Actin polymerization and depolymerization during apoptosis in HL-60 cells." American Journal of Physiology-Cell Physiology 271, no. 6 (1996): C1981—C1992. http://dx.doi.org/10.1152/ajpcell.1996.271.6.c1981.

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Little is known about the biochemical “machinery” responsible for the morphological features of apoptosis, although the cytoskeleton is presumed to be involved. Using flow cytometry, polyacrylamide gel electrophoresis, and fluorescence microscopy, we show that apoptosis induced by ultraviolet (UV) irradiation or 80 micrograms/ml etoposide correlates with early transient polymerization and later depolymerization of filamentous (F)-actin and dramatic changes in visible microfilament organization. Depolymerization of F-actin began before the formation of apoptotic bodies and was ultimately compos
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37

Gao, Yang, Yichun Shuai, Xuchen Zhang, et al. "Genetic dissection of active forgetting in labile and consolidated memories in Drosophila." Proceedings of the National Academy of Sciences 116, no. 42 (2019): 21191–97. http://dx.doi.org/10.1073/pnas.1903763116.

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Different memory components are forgotten through distinct molecular mechanisms. In Drosophila, the activation of 2 Rho GTPases (Rac1 and Cdc42), respectively, underlies the forgetting of an early labile memory (anesthesia-sensitive memory, ASM) and a form of consolidated memory (anesthesia-resistant memory, ARM). Here, we dissected the molecular mechanisms that tie Rac1 and Cdc42 to the different types of memory forgetting. We found that 2 WASP family proteins, SCAR/WAVE and WASp, act downstream of Rac1 and Cdc42 separately to regulate ASM and ARM forgetting in mushroom body neurons. Arp2/3 c
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Matsuzaki, Mizuki, Ikuko Fujiwara, Sae Kashima, et al. "D-Loop Mutation G42A/G46A Decreases Actin Dynamics." Biomolecules 10, no. 5 (2020): 736. http://dx.doi.org/10.3390/biom10050736.

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Depolymerization and polymerization of the actin filament are indispensable in eukaryotes. The DNase I binding loop (D-loop), which forms part of the interface between the subunits in the actin filament, is an intrinsically disordered loop with a large degree of conformational freedom. Introduction of the double mutation G42A/G46A to the D-loop of the beta cytoskeletal mammalian actin restricted D-loop conformational freedom, whereas changes to the critical concentration were not large, and no major structural changes were observed. Polymerization and depolymerization rates at both ends of the
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39

Kutsuna, Haruo, Kenichi Suzuki, Noriko Kamata, et al. "Actin reorganization and morphological changes in human neutrophils stimulated by TNF, GM-CSF, and G-CSF: the role of MAP kinases." American Journal of Physiology-Cell Physiology 286, no. 1 (2004): C55—C64. http://dx.doi.org/10.1152/ajpcell.00131.2003.

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Stimulation of human neutrophils with tumor necrosis factor-α (TNF), granulocyte-macrophage colony-stimulating factor (GM-CSF), or granulocyte CSF (G-CSF) resulted in decreased fluorescence intensity of FITC-phalloidin (actin depolymerization) and morphological changes. Cytokine-induced actin depolymerization was dependent on the concentration of cytokines used as stimuli. The maximal changes were detected at 10 min after stimulation with TNF or GM-CSF and at 20 min after stimulation with G-CSF. Cytokine-induced actin depolymerization was sustained for at least 30 min after stimulation. In con
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40

Chand, Abhishu, Nhi Le, and Kyoungtae Kim. "CdSe/ZnS Quantum Dots’ Impact on In Vitro Actin Dynamics." International Journal of Molecular Sciences 25, no. 8 (2024): 4179. http://dx.doi.org/10.3390/ijms25084179.

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Quantum dots (QDs) are a novel type of nanomaterial that has unique optical and physical characteristics. As such, QDs are highly desired because of their potential to be used in both biomedical and industrial applications. However, the mass adoption of QDs usage has raised concerns among the scientific community regarding QDs’ toxicity. Although many papers have reported the negative impact of QDs on a cellular level, the exact mechanism of the QDs’ toxicity is still unclear. In this investigation, we study the adverse effects of QDs by focusing on one of the most important cellular processes
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41

Pang, Suh Cem, Lee Ken Voon, and Suk Fun Chin. "Controlled Depolymerization of Cellulose Fibres Isolated from Lignocellulosic Biomass Wastes." International Journal of Polymer Science 2018 (July 19, 2018): 1–11. http://dx.doi.org/10.1155/2018/6872893.

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Various types of lignocellulosic biomass wastes (LBW) had been successfully converted into cello-oligomers with different chain lengths via a controlled depolymerization process. Cellulose fibres isolated from LBW samples were dissolved with room temperature ionic liquid (RTIL) in the presence of an acid catalyst, Amberlyst 15 DRY. The effects of reaction time on the degree of polymerization and yields of water-insoluble cello-oligomers formed were studied. Besides, the yields of water-soluble cello-oligomers such as glucose and xylose were also determined. The depolymerization of cellulose fi
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42

Kim, Jee Woo, and Byung-Kwon Kim. "Electrochemical Monitoring of Super-Engineering Polymer Depolymerization: A Rapid and Simple Approach." ECS Meeting Abstracts MA2023-02, no. 65 (2023): 3189. http://dx.doi.org/10.1149/ma2023-02653189mtgabs.

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The mechanical properties and processability of polymers are strongly influenced by their molecular weight, underscoring the critical importance of controlling depolymerization during storage in polymer synthesis and application. However, conventional methods of determining molecular weight, including viscosity measurements, gel permeation chromatography (GPC), and nuclear magnetic resonance (NMR) spectroscopy, typically necessitate substantial quantities of polymer samples and protracted measurement times. Moreover, certain polymers may undergo continuous degradation post-polymerization, rend
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43

Andersland, J. M., and M. V. Parthasarathy. "Conditions affecting depolymerization of actin in plant homogenates." Journal of Cell Science 104, no. 4 (1993): 1273–79. http://dx.doi.org/10.1242/jcs.104.4.1273.

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The successful isolation of actin depends on the ability to control its polymerization state. Conditions that affect the depolymerization of actin in plant homogenates were determined using a qualitative assay for both polymeric and monomeric forms. In this assay, phalloidin was added to homogenates to stabilize actin polymers, which were separated from monomers by gel electrophoresis and detected by immunoblotting. By this criterion, actin in pea and rice root homogenates was initially in filamentous form, but depolymerized rapidly at pH 8 or above. If the pH was neutral to slightly acidic, s
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44

Herrera, Ana M., Eliana C. Martinez, and Chun Y. Seow. "Electron microscopic study of actin polymerization in airway smooth muscle." American Journal of Physiology-Lung Cellular and Molecular Physiology 286, no. 6 (2004): L1161—L1168. http://dx.doi.org/10.1152/ajplung.00298.2003.

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Actin polymerization as part of the normal smooth muscle response to various stimuli has been reported. The actin dynamics are believed to be necessary for cytoskeletal remodeling in smooth muscle in its adaptation to external stress and strain and for maintenance of optimal contractility. We have shown in our previous studies in airway smooth muscle that myosins polymerized in response to contractile activation as well as to adaptation at longer cell lengths. We postulated that the same response could be elicited from actins under the same conditions. In the present study, actin filament form
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45

Enthaler, Stephen, Angela Köhler-Krützfeldt, Benedict Heyder, and Daniel Woelki. "Iron-catalyzed depolymerizations of end-of-life silicones with fatty alcohols." Resource-Efficient Technologies, no. 2 (December 15, 2015): 73–79. http://dx.doi.org/10.18799/24056529/2015/2/38.

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During the last decades, polymers became one of the major materials in our society and a future without polymers is hardly imaginable. However, as negative issue of this success enormous amount of end-of-life materials are accumulated, which are mainly treated by landfill storage, thermal recycling or down-cycling. On the other hand, feedstock recycling can be an interesting option to convert end-of-life polymers to highquality polymers, via depolymerization reactions to low-molecular weight building blocks and subsequent transformation via polymerization reactions. In this regard, we present
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46

Drubin, D., S. Kobayashi, D. Kellogg, and M. Kirschner. "Regulation of microtubule protein levels during cellular morphogenesis in nerve growth factor-treated PC12 cells." Journal of Cell Biology 106, no. 5 (1988): 1583–91. http://dx.doi.org/10.1083/jcb.106.5.1583.

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Nerve growth factor induces neurite process formation in pheochromacytoma (PC12) cells and causes the parallel increase in levels of the microtubule-associated proteins, tau and MAP1, as well as increases in tubulin levels. Mechanisms to insure balanced accumulation of microtubule proteins and make their levels highly responsive to nerve growth factor were investigated. The effects on tau, MAP1, and tubulin are due to changes in protein synthesis rates, which for tau and tubulin we could show are due in part to changes in the mRNA levels. Whereas tubulin shows feedback regulation to modulate s
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Liu, Xiong, Shi Shu, and Edward D. Korn. "Muscle myosins form folded monomers, dimers, and tetramers during filament polymerization in vitro." Proceedings of the National Academy of Sciences 117, no. 27 (2020): 15666–72. http://dx.doi.org/10.1073/pnas.2001892117.

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Muscle contraction depends on the cyclical interaction of myosin and actin filaments. Therefore, it is important to understand the mechanisms of polymerization and depolymerization of muscle myosins. Muscle myosin 2 monomers exist in two states: one with a folded tail that interacts with the heads (10S) and one with an unfolded tail (6S). It has been thought that only unfolded monomers assemble into bipolar and side-polar (smooth muscle myosin) filaments. We now show by electron microscopy that, after 4 s of polymerization in vitro in both the presence (smooth muscle myosin) and absence of ATP
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48

Maddox, Paul, Aaron Straight, Peg Coughlin, Timothy J. Mitchison, and Edward D. Salmon. "Direct observation of microtubule dynamics at kinetochores in Xenopus extract spindles." Journal of Cell Biology 162, no. 3 (2003): 377–82. http://dx.doi.org/10.1083/jcb.200301088.

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Microtubule plus ends dynamically attach to kinetochores on mitotic chromosomes. We directly imaged this dynamic interface using high resolution fluorescent speckle microscopy and direct labeling of kinetochores in Xenopus extract spindles. During metaphase, kinetochores were stationary and under tension while plus end polymerization and poleward microtubule flux (flux) occurred at velocities varying from 1.5–2.5 μm/min. Because kinetochore microtubules polymerize at metaphase kinetochores, the primary source of kinetochore tension must be the spindle forces that produce flux and not a kinetoc
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Garg, Yatharth. "Transforming silicone waste: Depolymerization and polymerization strategies for recycling." International Journal of Engineering in Computer Science 6, no. 2 (2024): 216–27. https://doi.org/10.33545/26633582.2024.v6.i2c.145.

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Omann, G. M., M. M. Porasik, and L. A. Sklar. "Oscillating actin polymerization/depolymerization responses in human polymorphonuclear leukocytes." Journal of Biological Chemistry 264, no. 28 (1989): 16355–58. http://dx.doi.org/10.1016/s0021-9258(19)84712-9.

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