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RelB, a new Rel family transcription activator that can interact with p50-NF-kappa B
TLDR
A serum-inducible gene, relB, is identified, which encodes a protein of 558 amino acids containing a region with high similarity to c-Rel and other members of the Rel family, which transactivate transcription of a promoter containing a kappa B-binding site.
The xylanolytic enzyme system from the genus Penicillium.
Dissecting the Facilitator and Inhibitor Allosteric Metal Sites of the P2X4 Receptor Channel
TLDR
It is concluded that this region of the P2X4 receptor has a pocket for trace metal coordination with two distinct and separate facilitator and inhibitor metal allosteric sites highlighting the role of trace metals in neuronal excitability.
Differential role of extracellular histidines in copper, zinc, magnesium and proton modulation of the P2X7 purinergic receptor
TLDR
While His‐267 is critically involved in the copper or zinc allosteric modulation, the magnesium inhibitory effects is related to His‐130 and His‐201, his‐130 is involved in proton sensing, highlighting the role of defined extracellular histidines in rat P2X7 receptor allosterIC modulation.
Histidine 140 Plays a Key Role in the Inhibitory Modulation of the P2X4 Nucleotide Receptor by Copper but Not Zinc*
TLDR
It is concluded that His-140 is critical for the action of copper, indicating that this histidine residue forms part of the inhibitory allosteric metal-binding site of the P2X4 receptor, which is distinct from the putative zinc facilitator binding site.
Extracellular histidine residues identify common structural determinants in the copper/zinc P2X2 receptor modulation
TLDR
It is proposed that His120, His192, His213 and His245 form part of a common allosteric metal‐binding site of the P2X2 receptor, which for the specific coordination of copper, but not zinc, additionally involves His319.
4‐Bromo‐2,5‐dimethoxyphenethylamine (2C‐B) and structurally related phenylethylamines are potent 5‐HT2A receptor antagonists in Xenopus laevis oocytes
TLDR
The present results demonstrate that in X. laevis oocytes, a series of 2,5‐dimethoxy‐4‐substituted PEAs blocked the 5‐HT2A but not the 5-HT2C receptor‐mediated responses, revealing 5‐ HT2 receptor subtype selectivity.
The mouse c-rel protein has an N-terminal regulatory domain and a C-terminal transcriptional transactivation domain
TLDR
It is proposed that c-rel protein has an N-terminal regulatory domain and a C-Terminal transactivation domain which together modulate its function as a transcriptional transactivator.
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