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Piezos are large transmembrane proteins conserved among various species, all having between 24 and 36 predicted transmembrane domains. Additionally we are shipping PIEZO1 Antibodies (46) and PIEZO1 Kits (11) and many more products for this protein.
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In the absence of extracellular matrix (ECM (show MMRN1 Proteins)) proteins Piezo1 receptors are relatively insensitive to mechanical forces pushing the cellular membrane, whereas they can hardly be activated by mechanically pulling the membrane. Yet, if conjugated with Matrigel, a mix of ECM (show MMRN1 Proteins) proteins, the receptors become sensitized.
present study was designed to evaluate in hereditary xerocytosis the functional link between mutated Piezo1 and KCNN4 (show KCNN4 Proteins)
the knockdown of PIEZO1 significantly reduced the cell-viability of SW982 cells.
analysis of Piezo1 domains by using localized force on magnetic nanoparticles
Piezo1-shRNA could inhibit the invasion of the osteosarcoma cells.
Piezo1 plays an important role in the apoptosis of human osteoarthritis-derived chondrocytes through a caspase-12-dependent pathway.
MiR (show MLXIP Proteins)-103a might be a potential biomarker of myocardium infarction and could be used as an index for the diagnosis of AMI (show CFD Proteins). It may be involved in the development of HBP (show AZU1 Proteins) and onset of AMI (show CFD Proteins) through regulating the Piezo1 expression.
The structural dynamics of the PIEZO1 channel activation and inactivation by coarse-grained modeling has been reported.
Additional alterations in mutant PIEZO1 channel kinetics, differences in response to osmotic stress, and altered membrane protein trafficking, predicting variant alleles that worsen or ameliorate erythrocyte hydration.
differential regulation of PKA and cell stiffness in unconfined versus confined cells is abrogated by dual, but not individual, inhibition of Piezo1 and myosin II.
three-bladed, propeller-like electron cryo-microscopy structure of mouse Piezo1 and functional revelation of its mechanotransduction components
high-resolution cryo-electron microscopy structure of the mouse Piezo1 trimer
Both TRPV4 (show TRPV4 Proteins) and PIEZO1 channels contribute to currents activated by stimuli applied at cell-substrate contacts but only PIEZO1 mediates stretch-activated currents. These data demonstrate that there are separate, but overlapping, mechanoelectrical transduction pathways in chondrocytes.
Piezo1 is a molecular sensor of physical exercise in the endothelium that triggers endothelial communication to mesenteric vessel muscle cells, leading to vasoconstriction.
data demonstrate that PIEZO1 is required for the regulation of NO formation, vascular tone, and blood pressure.
Our results suggest that Piezo1 is unlikely to be a component of the mechanoelectrical transducer channel complex in mammalian cochlear outer hair cells
Smooth muscle Piezo1 is required for stretch-activated cationic channel activity. PIezo1 is involved in the remodeling of small arteries.
This study demonstrated that Piezo1 proteins consist of distinct responsible for ion conduction, mechanical force sensing, and transduction to coordinately fulfill their function as sophisticated MS channels.
Astrocytes in optic nerve head express multiple mechanosensitive channels, in particular Piezo1 and 2. The expression of putative mechanosensitive channels in these cells may contribute to their responsiveness to traumatic or glaucomatous injury.
Piezos are large transmembrane proteins conserved among various species, all having between 24 and 36 predicted transmembrane domains. 'Piezo' comes from the Greek 'piesi,' meaning 'pressure.' The FAM38A gene encodes PIEZO1, a protein that induces mechanically activated (MA) currents in various cell types (Coste et al., 2010
family with sequence similarity 38, member A
, membrane protein induced by beta-amyloid treatment
, protein PIEZO1