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Pharmacological modulation of the diazepam-insensitive recombinant gamma-aminobutyric acidA receptors alpha 4 beta 2 gamma 2 and alpha 6 beta 2 gamma 2.
TLDR
Although the alpha 4 beta 2 gamma 2 receptors are insensitive to benzodiazepine binding site full agonists, they can be modulated by certain ligands acting as partial and inverse agonists at diazepam-sensitive receptors and thereby contribute to the respective pharmacological profiles.
The RGG domain in hnRNP A2 affects subcellular localization.
TLDR
The data suggest that hnRNP A2 may contain a novel nuclear localization sequence, regulated by arginine methylation, that lies in the R191-G253 region and may function independently of the M9 transportin-1-binding region in hnHnR NP A2.
hnRNP A2 and hnRNP L bind the 3'UTR of glucose transporter 1 mRNA and exist as a complex in vivo.
TLDR
It is concluded that hnRNP A2 and L associate in vivo and independently bind the 3'UTR of Glut1 mRNA.
Lactate Dehydrogenase Is an AU-rich Element-binding Protein That Directly Interacts with AUF1*
TLDR
Data implicate a role for LDH in the post-transcriptional regulation of gene expression as the glycolytic enzyme lactate dehydrogenase (LDH) M and interaction between LDH and AUF1 is direct as it can be demonstrated in vitro with purified proteins.
v-mos oncoproteins affect the nuclear retention and reutilization of glucocorticoid receptors.
TLDR
Indirect immunofluorescence analyses demonstrate that hormone insensitivity in v-mos transformed cells is associated with inefficient nuclear retention of glucocorticoid receptor (GR) protein, which results in the generation of a novel desensitized receptor apparently trapped in the cytoplasm and incapable of being reutilized.
Modulation of AUUUA Response Element Binding by Heterogeneous Nuclear Ribonucleoprotein A1 in Human T Lymphocytes
The heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) shuttles between the cytoplasm and nucleus and plays important roles in RNA metabolism. Whereas nuclear hnRNP A1 has been shown to bind
Selective effects of alcohols on gamma-aminobutyric acid A receptor subunits expressed in human embryonic kidney cells.
TLDR
These experiments indicate that the presence of alpha 6 or gamma 2L subunits, in itself, does not result in the potentiation of GABA-induced currents by ethanol, as described in some reports, however, the existence of either thealpha 6 or alpha 1 subunit may determine whether the desensitization rate of the GABAA current is affected by the alcohol.
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