Results 31 to 40 of about 1,295,695 (149)
Sodium Ions Affect GPR17 Conformational States and Functionality
ABSTRACT Sodium is an allosteric modulator of several class‐A GPCR regulating active versus inactive conformation state and may be a critical issue for the optimization of crystallization procedures. Herein, the role of Na+ in the regulation of GPR17 conformational states was studied through MD simulations of GPR17 wild‐type and mutated on two ...
Luca Palazzolo +6 more
wiley +1 more source
P2Y6 receptor inhibition perturbs CCL2-evoked signalling in human monocytic and peripheral blood mononuclear cells [PDF]
This work is supported the British Heart Foundation [grant number PG/13/22/ 30077]. Deposited in PMC for immediate release.The chemokine CCL2 serves to target circulating monocytes and other leukocytes to tissue during innate immune responses, and ...
Campwala, H. +11 more
core +1 more source
The potential for biased signalling in the P2Y receptor family of GPCRs
The purinergic receptor family is primarily activated by nucleotides, and contains members of both the G protein coupled‐receptor (GPCR) superfamily (P1 and P2Y) and ligand‐gated ion channels (P2X). The P2Y receptors are widely expressed in the human body, and given the ubiquitous nature of nucleotides, purinergic signalling is involved with a plethora
Claudia M. Sisk +2 more
wiley +1 more source
P2X receptors: epithelial ion channels and regulators of salt and water transport. [PDF]
When the results from electrophysiological studies of renal epithelial cells are combined with data from in vivo tubule microperfusion experiments and immunohistochemical surveys of the nephron, the accumulated evidence suggests that ATP-gated ion ...
King, Brian F., Wildman, Scott S.P.
core +1 more source
TMEM16A channel signalling microdomains in the regulation of vascular function
Abstract figure legend Schematic representation of TMEM16A channel signalling microdomains. Calcium influx or calcium release from the endoplasmic/sarcoplasmic reticulum (ER/SR) activates TMEM16A channels through interactions with regulatory proteins in vascular smooth muscle cells or endothelial cells. TMEM16A channel activation drives chloride efflux,
Fênix Araujo, Swapnil K. Sonkusare
wiley +1 more source
Purinergic receptors in skeletal muscles in health and in muscular dystrophy [PDF]
The P2 purinergic (nucleotide) receptor super-family comprises of two families of protein. The P2X, which are channel-forming ionotropic receptors and the P2Y metabotropic receptors activating G protein-mediated signalling pathways.
Young, Christopher +10 more
core
Abstract figure legend The capillary–mitochondria–ion channel (CMIC) axis scales structural resources to match functional workload. (Left) In settings of restricted energetic capacity (e.g. cortical neurons), sparse capillary networks and modest mitochondrial pools set a lower energetic ceiling, sufficient to support phasic, low‐workload excitability. (
L. Fernando Santana, Scott Earley
wiley +1 more source
Purines as potential morphogens during embryonic development [PDF]
Components of purinergic signalling are expressed in the early embryo raising the possibility that ATP, ADP and adenosine may contribute to the mechanisms of embryonic development.
Dale, Nicholas +3 more
core +1 more source
High‐altitude hypobaric hypoxia activates multiorgan GPCR signaling networks that regulate ventilatory responses, cerebral endothelial barrier integrity, erythropoiesis and red blood cell metabolism, pulmonary vascular remodeling, and cardiac adaptation. Dysregulated GPCR pathways contribute to acute and chronic high‐altitude diseases, while clinically
Qing Zhao +13 more
wiley +1 more source
ATP Release and Purinergic Signaling Potentiate β‐Adrenergic Effects on Brown Adipocytes
ABSTRACT Aim Brown adipose tissue (BAT) specializes in energy consumption and thermogenesis in response to cold stress. Brown adipocytes (BA) express purinergic receptors, yet little is known about the source of extracellular ATP and the role of purinergic signaling, and the potential interaction with β‐adrenergic signaling.
Marco Tozzi +8 more
wiley +1 more source

