Structural Investigation of the Complex of Filamin A Repeat 21 with Integrin αIIb and β3 Cytoplasmic Tails – A Potential “Transmission” to Regulate Cell Migration

Cell functions in multi-cellular organisms are strongly depend on the dynamic cooperation between cell adhesion and cytoskeleton reorganization. Integrins, the major cell adhesion receptors, bind to extracellular matrix (ECM) and soluble ligands on the cell surface and link to the actin cytoskeleton inside the cell membrane. In this manner, integrins integrate cell adhesion and cytoskeleton reorganization by acting as a mechanical force transducer and a biochemical signaling hub (Zamir and Geiger 2001). Consequently, integrins are vital for development, immune responses, leukocyte traffic and hemostasis, and a variety of other cellular and physiological processes. Integrins are also are the focal point of many human diseases, including genetic, autoimmune, cardiovascular and others. In terms of the cell-ECM adhesion, integrins can exist in two major states, active, where it binds to appropriate extracellular ligands, and inactive, where it disassociates from extracellular ligands. The cellular pathways that modify the integrin extracellular ligand binding states have been called inside-out integrin signaling while the pathways that are mediated by the extracellular binding have been called outside-in integrin signaling. Although the directions of outside-in and inside-out signaling point to each other, they often happen reciprocally. Rather than just integrins alone accomplishing integrin signaling, numerous proteins are recruited around integrins and are limited to the clearly defined range of focal adhesion that are large molecular complexes containing \u3e100 proteins which link integrins to cytoskeleton (Figure 1) (Zaidel-Bar et al. 2004). Proteins that directly interact with integrins are crucial for understanding integrin signaling. More importantly, proteins that link integrins to the cytoskeleton are responsible for both mechanical forces and biochemical signal transduction, as well as reorganizing the cytoskeleton. Moreover, the modification of integrin ligand binding states is dependent on the linkage t

Structural Investigation of the Complex of Filamin A Repeat 21 with Integrin αIIb and β3 Cytoplasmic Tails – A Potential “Transmission” to Regulate Cell Migration

Cell functions in multi-cellular organisms are strongly depend on the dynamic cooperation between cell adhesion and cytoskeleton reorganization. Integrins, the major cell adhesion receptors, bind to extracellular matrix (ECM) and soluble ligands on the cell surface and link to the actin cytoskeleton inside the cell membrane. In this manner, integrins integrate cell adhesion and cytoskeleton reorganization by acting as a mechanical force transducer and a biochemical signaling hub (Zamir and Geiger 2001). Consequently, integrins are vital for development, immune responses, leukocyte traffic and hemostasis, and a variety of other cellular and physiological processes. Integrins are also are the focal point of many human diseases, including genetic, autoimmune, cardiovascular and others. In terms of the cell-ECM adhesion, integrins can exist in two major states, active, where it binds to appropriate extracellular ligands, and inactive, where it disassociates from extracellular ligands. The cellular pathways that modify the integrin extracellular ligand binding states have been called inside-out integrin signaling while the pathways that are mediated by the extracellular binding have been called outside-in integrin signaling. Although the directions of outside-in and inside-out signaling point to each other, they often happen reciprocally. Rather than just integrins alone accomplishing integrin signaling, numerous proteins are recruited around integrins and are limited to the clearly defined range of focal adhesion that are large molecular complexes containing \u3e100 proteins which link integrins to cytoskeleton (Figure 1) (Zaidel-Bar et al. 2004). Proteins that directly interact with integrins are crucial for understanding integrin signaling. More importantly, proteins that link integrins to the cytoskeleton are responsible for both mechanical forces and biochemical signal transduction, as well as reorganizing the cytoskeleton. Moreover, the modification of integrin ligand binding states is dependent on the linkage t

Traffic Signal Timing Optimization for Isolated Intersections Based on Differential Evolution Bacteria Foraging Algorithm

AbstractAiming at that the traffic congestion in urban often appears, the signal timing optimization model and method are researched. The signal control model is proposed considering the max throughput of intersection. The objective function of this model is to minimize the delay vehicles of a cycle time. The model has all kinds of constraint. A differential evolution bacteria foraging optimization algorithm is presented. The velocity of the traditional bacteria foraging optimization algorithm is slow. The bacterium position is revised by differential evolution in chemotaxis process to improve the convergence precision. Based on an intersection in Guangzhou City, the model is calculated and simulated through programming. As it shows, it can improve traffic capacity of intersections and especially works well in high demand

Shattered Rim and Shelling of High-Speed Railway Wheels in The Very-High-Cycle Fatigue Regime Under Rolling Contact Loading

Due to the improvement of the wear property, rolling contact fatigue including shattered rim and shelling are the main failure causes of the high-speed railway wheels. In this paper, shattered rim and shelling occurred on the service wheels of the China Railway High-speed (CRH) trains were systematically investigated. The recorded data of the last ten years CRH operation indicated that all shattered rims and shelling were detected with serving \u3e106 km (corresponding to the fatigue life 107–109 cycles) which is very-high-cycle fatigue (VHCF). The crack initiationregion of shattered rim located at the depth of 10–25 mm from the tread, while that of shelling located at the depthsurfaces, i.e., similar VHCF features in uniaxial loading including the defect, fish-eye, and crack propagation region and unique VHCF features of the three dimensional crack surface feature, beach bands uniformly distributed in the crack propagation region, absence of fine granular area (FGA). The VHCF model considering the stress distribution, defect size and hardness were applied to discuss the failure mechanism of the shattered rim and shelling

Bis(μ-ferrocene­carboxyl­ato)bis­[aqua­­bis(ferrocene­carboxyl­ato)methano­l­erbium(III)] methanol disolvate

In the centrosymmetric title coordination compound, [Er2{Fe(C5H5)(C6H4O2)}6(CH3OH)2(H2O)2]·2CH3OH, the two ErIII ions are bridged by two ferrocene­carboxyl­ate anions as asymmetrically bridging ligands, leading to dimeric cores. The ErIII ion has a distorted dodeca­hedral coordination with six coordinating O atoms derived from the ferrocene­carboxyl­ate ligands and two coordinated O atoms from one water mol­ecule and one methanol mol­ecule. The asymmetric unit comprises a half of the complex mol­ecule and a methanol solvent mol­ecule. Intra­molecular O—H⋯O and C—H⋯O inter­actions occur. In the crystal, mol­ecules are linked by inter­molecular O—H⋯O hydrogen bonds and C—H⋯O as well as C—H⋯π inter­actions