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  2. Opioid receptor - Wikipedia

    en.wikipedia.org/wiki/Opioid_receptor

    All G protein α sub-units contain palmitate, which is a 16-carbon saturated fatty acid, that is attached near the N-terminus through a labile, reversible thioester linkage to a cysteine amino acid. It is this palmitoylation that allows the G protein to interact with membrane phospholipids due to the hydrophobic nature of the alpha sub-units.

  3. craigslist - Wikipedia

    en.wikipedia.org/wiki/Craigslist

    Craigslist headquarters in the Inner Sunset District of San Francisco prior to 2010. The site serves more than 20 billion [17] page views per month, putting it in 72nd place overall among websites worldwide and 11th place overall among websites in the United States (per Alexa.com on June 28, 2016), with more than 49.4 million unique monthly visitors in the United States alone (per Compete.com ...

  4. Endorphins - Wikipedia

    en.wikipedia.org/wiki/Endorphins

    [12] α-endorphin and γ-endorphin result from proteolytic cleavage of β-endorphin between the Thr(16)-Leu(17) residues and Leu(17)-Phe(18) respectively. [24] α-endorphin has the shortest sequence, and β-endorphin has the longest sequence. α-endorphin and γ-endorphin are primarily found in the anterior and intermediate pituitary. [25]

  5. Neoendorphin - Wikipedia

    en.wikipedia.org/wiki/Neoendorphin

    The α-neoendorphin is present in greater amounts in the brain than β-neoendorphin. Both are products of the dynorphin gene, which also expresses dynorphin A, dynorphin A-(1-8), and dynorphin B. [2] These opioid neurotransmitters are especially active in Central Nervous System receptors, whose primary function is pain sensation. [3]

  6. Enkephalin - Wikipedia

    en.wikipedia.org/wiki/Enkephalin

    There are three well-characterized families of opioid peptides produced by the body: enkephalins, β-endorphin, and dynorphins.The met-enkephalin peptide sequence is coded for by the enkephalin gene; the leu-enkephalin peptide sequence is coded for by both the enkephalin gene and the dynorphin gene. [3]

  7. Dynorphin - Wikipedia

    en.wikipedia.org/wiki/Dynorphin

    Based on the results of dynorphin A 2-13, the authors proposed a mechanism in which dynorphin A activates bradykinin receptors and thus stimulates pain response. [ 8 ] According to this mechanism, dynorphin activates bradykinin receptors, which triggers the release of calcium ions into the cell through voltage-sensitive channels in the cell ...

  8. β-Endorphin - Wikipedia

    en.wikipedia.org/wiki/Β-endorphin

    β-Endorphin (beta-endorphin) is an endogenous opioid neuropeptide and peptide hormone that is produced in certain neurons within the central nervous system and peripheral nervous system. [1] It is one of three endorphins that are produced in humans, the others of which include α-endorphin and γ-endorphin .

  9. α-Neoendorphin - Wikipedia

    en.wikipedia.org/wiki/Α-Neoendorphin

    α-Neoendorphin is an endogenous opioid peptide with a decapeptide structure and the amino acid sequence Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro-Lys. [1]α-Neoendorphin is a neuropeptide.