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This inhibitory interaction is expected to be released by binding of active Rho to the RBD [3], [5].
This autoinhibition can be released by binding of GTP-bound Cdc42 to the GBD domain [ 14].
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Here, the cargo is released by binding of RanGTP to importins.
Commonly, transcription of catabolic enzymes is suppressed by a repressor protein that is released by binding with the secondary sugar.
Further, part of the intracellularly generated S1P could be released by an ATP-binding cassette transporter, ABCC1, which may subsequently activate S1PRs in an autocrine or paracrine manner [29].
Retinol-binding protein 4 (RBP4), which is released primarily by the liver, has recently been shown to be released by adipose tissue as well [ 4].
Autoinhibition of the catalytic triad in the absence of substrate is released by the binding of the Met1-linked proximal Ub.
After hard or soft tissue injury, PDGF is released by blood platelets binding to specific cell surface receptors.
In the presence of BR, BKI1 is released by the direct binding of BR to the 70-amino acid island region in the extracellular domain of BRI1 [ 7].
What is the physiological function of LSR? Earlier studies have shown that LSR was involved in lipoprotein clearance., It was reported that fatty acids, which are released by lipolysis activate the binding of lipoproteins to LSR.
Heparin-binding protein is released by neutrophils during inflammation and disrupts the integrity of the alveolar and capillary endothelial barrier implicated in the development of acute lung injury and systemic organ failure.
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