To install click the Add extension button. That's it.
The source code for the WIKI 2 extension is being checked by specialists of the Mozilla Foundation, Google, and Apple. You could also do it yourself at any point in time.
How to transfigure the Wikipedia
Would you like Wikipedia to always look as professional and up-to-date? We have created a browser extension. It will enhance any encyclopedic page you visit with the magic of the WIKI 2 technology.
Try it — you can delete it anytime.
Install in 5 seconds
Yep, but later
4,5
Kelly Slayton
Congratulations on this excellent venture… what a great idea!
Alexander Grigorievskiy
I use WIKI 2 every day and almost forgot how the original Wikipedia looks like.
Calcium release-activated calcium channel protein 1 is a calcium selective ion channel that in humans is encoded by the ORAI1gene.[5][6][7] Orai channels play an important role in the activation of T-lymphocytes. The loss of function mutation of Orai1 causes severe combined immunodeficiency (SCID) in humans[5] The mammalian orai family has two additional homologs, Orai2 and Orai3. Orai proteins share no homology with any other ion channel family of any other known proteins. They have 4 transmembrane domains and form hexamers.
YouTube Encyclopedic
1/3
Views:
1 923
866
574
Store Operated Calcium Entry Part 1
Store Operated Calcium Entry Part 2
Store Operated Calcium Entry Part 5
Transcription
Structure and function
ORAI channels are activated upon the depletion of internal calcium stores, which is called the "store-operated" or the "capacitative" mechanism.[8] They are molecular constituents of the "calcium release activated calcium currents" (ICRAC). Upon activation of phospholipase C by various cell surface receptors, inositol trisphosphate is formed that releases calcium from the endoplasmic reticulum. The decreased calcium concentration in the endoplasmic reticulum is sensed by the STIM1 protein. STIM1 clusters upon the depletion of the calcium stores and forms "puncta", and relocates near the plasma membrane, where it activates ORAI1 via protein-protein interaction.[9][10][11][12]
In 2012, a 3.35-angstrom (Å) crystal structure of the Drosophila Orai channel, which shares 73% sequence identity with human Orai1 within its transmembrane region, was published.[13] The structure, thought to show the closed state of the channel, revealed that a single channel is composed of six Orai subunits, with the transmembrane domains arranged in concentric rings around a central aqueous pore formed exclusively by the first transmembrane helix of each subunit. Transmembrane helices 2 and 3 surround TM1 and are hypothesized to shield it from the surrounding lipid bilayer and provide structural support. The fourth transmembrane helix forms the outermost layer.
Clinical relevance
ORAI1 mutations are associated with Immunodeficiency 9 and Tubular aggregate myopathy type 2 (TAM2).[14]