Results 61 to 70 of about 108,706 (283)

The envenomation of general physiology throughout the last century. [PDF]

open access: yes, 2017
Toxins are the poisonous products of organisms. Toxins serve vital defensive and offensive functions for those that harbor them: stinging scorpions, pesticidal plants, sanguinary snakes, fearless frogs, sliming snails, noxious newts, and smarting spiders.
Sack, Jon T
core   +1 more source

Endogenous Neuropeptide Nocistatin Is a Direct Agonist of Acid-Sensing Ion Channels (ASIC1, ASIC2 and ASIC3)

open access: yesBiomolecules, 2019
Acid-sensing ion channel (ASIC) channels belong to the family of ligand-gated ion channels known as acid-sensing (proton-gated) ion channels. Only a few activators of ASICs are known.
Dmitry I. Osmakov   +4 more
doaj   +1 more source

The tarantula toxin psalmotoxin 1 inhibits acid-sensing ion channel (ASIC) 1a by increasing its apparent H+ affinity [PDF]

open access: yes, 2005
Acid-sensing ion channels (ASICs) are ion channels activated by extracellular protons. They are involved in higher brain functions and perception of pain, taste, and mechanical stimuli.
Chen, Xuanmao
core   +1 more source

Spatiotemporal and quantitative analyses of phosphoinositides – fluorescent probe—and mass spectrometry‐based approaches

open access: yesFEBS Letters, EarlyView.
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho   +3 more
wiley   +1 more source

Candidate amino acids involved in H+ gating of acid-sensing ion channel 1a [PDF]

open access: yes, 2008
Acid-sensing ion channels are ligand-gated cation channels, gated by extracellular H+. H+ is the simplest ligand possible, and whereas for larger ligands that gate ion channels complex binding sites in the three-dimensional structure of the proteins have
Chen, Xuanmao   +4 more
core   +1 more source

Structural biology of ferritin nanocages

open access: yesFEBS Letters, EarlyView.
Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley   +1 more source

Prokineticin 2 potentiates acid-sensing ion channel activity in rat dorsal root ganglion neurons

open access: yesJournal of Neuroinflammation, 2012
Background Prokineticin 2 (PK2) is a secreted protein and causes potent hyperalgesia in vivo, and is therefore considered to be a new pronociceptive mediator.
Qiu Chun-Yu   +5 more
doaj   +1 more source

Proton Sensing on the Ocular Surface: Implications in Eye Pain

open access: yesFrontiers in Pharmacology, 2021
Protons reaching the eyeball from exogenous acidic substances or released from damaged cells during inflammation, immune cells, after tissue injury or during chronic ophthalmic conditions, activate or modulate ion channels present in sensory nerve fibers
Núria Comes   +5 more
doaj   +1 more source

Zebrafish acid-sensing ion channel (ASIC) 4, characterization of homo- and heteromeric channels, and identification of regions important for activation by H+ [PDF]

open access: yes, 2007
There are four genes for acid-sensing ion channels (ASICs) in the genome of mammalian species. Whereas ASIC1 to ASIC3 form functional H+-gated Na+ channels, ASIC4 is not gated by H+, and its function is unknown. Zebrafish has two ASIC4 paralogs: zASIC4.1
Chen, Xuanmao   +3 more
core   +1 more source

Structure and hydration of membranes embedded with voltage-sensing domains. [PDF]

open access: yes, 2009
Despite the growing number of atomic-resolution membrane protein structures, direct structural information about proteins in their native membrane environment is scarce.
Freites, J Alfredo   +8 more
core   +2 more sources

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