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N-acetylcysteine-functionalized coating avoids bacterial adhesion and biofilm formation
Average protein density is a molecular-weight-dependent function. Protein Sci.
Chick, H. The Viscosity of Some Protein Solutions.
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Download references. All authors reviewed and agreed the manuscript. Correspondence to M. Cristina L. To view a copy of this license, visit http: Reprints and Permissions.
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Subjects Biomedical materials Drug delivery. Full size table. While molecular mechanism remains unclear, actin depolymerization ACTION ACTINA COSTA 300S we report here are certainly dissimilar from the ACTION ACTINA COSTA 300S responses observed in reconstituted actin-myosin networks, which are attributed to disruption of myosin crosslinks [17,30,31]. Similarly, we have reported that the perturbation of myosin crosslinks by stretch is a major factor in the fluidization of isolated airway smooth muscle cells and integrated tissues [32,33]. However, disruption of myosin crosslinks alone fails to explain the underlying cytoskeletal plasticity [18,34], its scale-free rheology [12,35] or its universality in living cells .
Neither can myosin dynamics alone account for our previously reported differences between fluidization versus reinforcement observed in response to a homogenous versus an inhomogeneous stretch , or account for our current findings of rapid F-actin disassociation followed by a gradual recovery Figure 3 and 4.
As such, we conclude that fluidization is caused not just by agitation or by relative motion, but rather by increased tensile forces that, upon sufficient ACTION ACTINA COSTA 300S, or perhaps upon release of that loading, can lead to dissociation of weak bonds or drive disassociation of actin with binding partners such as a -actinin or VASP, whose recruitment is facilitated by the force-dependent action of zyxin [36—38]. In that connection, zyxin is a logical candidate to account for the slow resolidification that is observed after unstretch, but could zyxin account for prompt fluidization during stretch?
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Increasing cytoskeletal tension causes the rate constant for zyxin dissociation the off-rate from focal adhesions to decrease  and mobilization of zyxin to stress fibers . On the ACTION ACTINA COSTA 300S hand, during the unstretch phase of the transient maneuver, traction forces fall rapidly to zero . Whether zyxin, during that low-tension phase, might demobilize from stress fibers sufficiently to account for ACTION ACTINA COSTA 300S disassembly is unclear and warrants investigation. Another plausible candidate is the actin severing protein, cofilin [39—41]. In its dephosphorylated form, cofilin binds and remodels actin filaments, increases its torsional and bending flexibility, and significantly lowers filament persistence length [42—44].
Taken together, these effects promote bending and disassociation of in vitro actin networks.
A major component of fluidization is F-actin disassembly: staining Download Scientific Diagram
A particle blue attaches to ACTION ACTINA COSTA 300S moieties orange on the cell surface black horizontal lineand the virus-receptor complex diffuses in the plane of the membrane. The virus particle is captured by the clathrin endocytic machinery AP-2, green; clathrin, red after diffusion into an existing clathrin structure e. Dengue virus or entrapment within a clathrin structure that initiates in close proximity to the virion e. VSV and influenza A virus. Clathrin assembly completes, and the virus-containing pit is severed from the cell surface in a dynamin-dependent process. Internalization of VSV also requires local actin assembly.
Clathrin is rapidly removed from the nascent vesicle, and the vesicle is actively transported further into cell. B Example of a complete DI-T internalization event. A dim spot of AP-2 appears beneath the virion, signifying capture of the particle. Download the latest drivers for your Action COSTA E Series to keep your Computer up-to-date.
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