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  1. #1
    Wanderer
    Join Date
    Jul 2006
    Location
    Rural Central Alberta, Canada
    Posts
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    "? Heres what i mean, all of those individuals, as mature as they are, respect me, and follow me not because i bark orders at them or even because of my position in the group. They follow because they want to, because of the way i treat them with respect and never loss my temper and can even make a heated argument seem controlled. Am i making sense?

    Ok, so, in my D/s relationship i would consider myself a "soft natural Dom" By this i mean that i do not have to whip my sub into submission (except when though thats what she wants) but she submits because of the way i carry myself, the words that i use, and can control her with the softest touch. "

    If you ask me, yes, you're making sense. As far as I'm concerned you just described what a leader (or a Dom) should, in my opinion, be able to do.
    Mit diesem Herz hab ich die Macht
    die Augenlider zu erpressen
    ich singe bis der Tag erwacht
    ein heller Schein am Firmament
    Mein Herz brennt

    - Rammstein

  2. #2
    Uncle_Ed
    Guest
    A Natural Dominant

    Negative P2X1 Receptor Due to Deletion of a Single Amino Acid Residue*
    Cecile Oury, Emese Toth-Zsamboki§, Chris Van Geet¶, Chantal Thys, Lin Wei, Bernd Nilius, Jos Vermylen**, and Marc F. Hoylaerts
    From the Center for Molecular and Vascular Biology and Laboratory of Physiology, University of Leuven, B-3000 Leuven, Belgium

    The P2X1 receptor belongs to a family of oligomeric ATP-gated ion channels with intracellular N and C termini and two transmembrane segments separating a large extracellular domain. Here, we describe a naturally occurring dominant negative P2X1 mutant. This mutant lacks one leucine within a stretch of four leucine residues in its second transmembrane domain (TM2) (amino acids 351-354). Confocal microscopy revealed proper plasma membrane localization of the mutant in stably transfected HEK293 cells. Nevertheless, voltage-clamped HEK293 cells expressing mutated P2X1 channels failed to develop an ATP or ADP-induced current. Furthermore, when co-expressed with the wild type receptor in Xenopus oocytes, the mutated protein exhibited a dose-dependent dominant negative effect on the normal ATP or ADP-induced P2X1 channel activity. These data indicate that deletion of a single apolar amino acid residue at the inner border of the P2X1 TM2 generates a nonfunctional channel. The inactive and dominant negative form of the P2X1 receptor may constitute a new tool for the study of the physiological role of this channel in native cells.


    Good God guys! It's so obvious...

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