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See detailThe evolutionarily conserved Kruppel-associated box domain defines a subfamily of eukaryotic multifingered proteins
Bellefroid, Eric J.; Poncelet, Dominique A; Lecocq, Pierre J et al

in Proceedings of the National Academy of Sciences of the United States of America (1991), 88(9), 3608-12

We have previously shown that the human genome includes hundreds of genes coding for putative factors related to the Kruppel zinc-finger protein, which regulates Drosophila segmentation. We report herein ... [more ▼]

We have previously shown that the human genome includes hundreds of genes coding for putative factors related to the Kruppel zinc-finger protein, which regulates Drosophila segmentation. We report herein that about one-third of these genes code for proteins that share a very conserved region of about 75 amino acids in their N-terminal nonfinger portion. Homologous regions are found in a number of previously described finger proteins, including mouse Zfp-1 and Xenopus Xfin. We named this region the Kruppel-associated box (KRAB). This domain has the potential to form two amphipathic alpha-helices. Southern blot analysis of "zoo" blots suggests that the Kruppel-associated box is highly conserved during evolution. Northern blot analysis shows that these genes are expressed in most adult tissues and are down-regulated during in vitro terminal differentiation of human myeloid cells. [less ▲]

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See detailEven Transcriptionally Competent Proviruses Are Silent In Bovine Leukemia Virus-Induced Sheep Tumor-Cells
Vandenbroeke, A.; Cleuter, Y.; Chen, G. et al

in Proceedings of the National Academy of Sciences of the United States of America (1988), 85(23),

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See detailTransferrin receptors in rat plasma.
Beguin, Yves ULg; Huebers, H. A.; Josephson, B. et al

in Proceedings of the National Academy of Sciences of the United States of America (1988), 85(2), 637-40

Antigenic material in rat plasma reacting with rat transferrin receptor antibodies was identified as an intact receptor molecule complexed with transferrin. Plasma transferrin receptors were measured by ... [more ▼]

Antigenic material in rat plasma reacting with rat transferrin receptor antibodies was identified as an intact receptor molecule complexed with transferrin. Plasma transferrin receptors were measured by ELISA in rats of different age and sex, of different iron status, with different degrees of erythropoiesis, and with inflammation. An inverse relationship between iron status and receptor number was found, whereas a direct relationship existed between erythropoiesis and receptors. These changes in receptor number can be explained by assuming that the number of tissue receptors determined the number of plasma receptors and that the erythroid cells possessed most of the body's receptors. Increases in plasma receptors lagged behind the appearance of circulating reticulocytes, suggesting that receptors were released to the plasma during the terminal phase of erythrocyte maturation. [less ▲]

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See detailExpression of a synthetic gene encoding human insulin-like growth factor I in cultured mouse fibroblasts.
Bayne, M. L.; Cascieri, M. A.; Kelder, B. et al

in Proceedings of the National Academy of Sciences of the United States of America (1987), 84

A synthetic gene encoding human insulin-like growth factor I (hIGF-I) was assembled and inserted into an expression vector containing the cytomegalovirus immediate early (CMV-IE) transcriptional ... [more ▼]

A synthetic gene encoding human insulin-like growth factor I (hIGF-I) was assembled and inserted into an expression vector containing the cytomegalovirus immediate early (CMV-IE) transcriptional regulatory region and portions of the bovine growth hormone gene. The recombinant plasmid encodes a 97 amino acid fusion protein containing the first 27 amino acids of the bovine growth hormone precursor and the 70 amino acids of hIGF-I. This plasmid, when transiently introduced into cultured mouse fibroblasts, directs synthesis of the fusion protein, subsequent proteolytic removal of the bovine growth hormone signal peptide, and secretion of hIGF-I into the culture medium. Conditioned medium from transfected cells inhibits binding of 125I-labeled IGF-I to type I IGF receptors on human placental membranes and to acid-stable human serum carrier proteins. The recombinant hIGF-I produced is biologically active, as monitored by the stimulation of DNA synthesis in vascular smooth muscle cells. [less ▲]

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See detailThyroid hormone receptors bind to defined regions of the growth hormone and placental lactogen genes
Barlow, John W; Voz, Marianne ULg; Eliard, Pierre H et al

in Proceedings of the National Academy of Sciences of the United States of America (1986), 83(23), 9021-5

The intracellular receptor for thyroid hormone is a protein found in chromatin. Since thyroid hormone stimulates transcription of the growth hormone gene through an unknown mechanism, the hypothesis that ... [more ▼]

The intracellular receptor for thyroid hormone is a protein found in chromatin. Since thyroid hormone stimulates transcription of the growth hormone gene through an unknown mechanism, the hypothesis that the thyroid hormone-receptor complex interacts with defined regions of this gene has been investigated in a cell-free system. Nuclear extracts from human lymphoblastoid IM-9 cells containing thyroid hormone receptors were incubated with L-3,5,3'-tri[125I]iodothyronine and calf thymus DNA-cellulose. Restriction fragments of the human growth hormone gene were added to determine their ability to inhibit labeled receptor binding to DNA-cellulose. These fragments encompassed nucleotide sequences from about three kilobase pairs upstream to about four kilobase pairs downstream from the transcription initiation site. The thyroid hormone-receptor complex bound preferentially to the 5'-flanking sequences of the growth hormone gene in a region between nucleotide coordinates -290 and -129. The receptor also bound to an analogous promoter region in the human placental lactogen gene, which has 92% nucleotide sequence homology with the growth hormone gene. These binding regions appear to be distinct from those that are recognized by the receptor for glucocorticoids, which stimulate growth hormone gene expression synergistically with thyroid hormone. The presence of thyroid hormone was required for binding of its receptor to the growth hormone gene promoter, suggesting that thyroid hormone renders the receptor capable of recognizing specific gene regions. [less ▲]

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See detailConformational analysis of the calcium--A23187 complex at a lipid--water interface.
Brasseur, Robert ULg; Deleers, M.; Malaisse, W. J. et al

in Proceedings of the National Academy of Sciences of the United States of America (1982), 79(9), 2895-7

A possible conformation of the complex formed by one calcium ion and two molecules of the ionophore A23187 at a simulated lipid--water interface was predicted by a variant method for conformational ... [more ▼]

A possible conformation of the complex formed by one calcium ion and two molecules of the ionophore A23187 at a simulated lipid--water interface was predicted by a variant method for conformational analysis. This method takes into account, in addition to the Van der Waals energy, electrostatic interaction, and torsional potential, the alteration of electrostatic forces attributable to changes in dielectric constant at the interface and the transfer energy for each part of the complex as it moves through the lipid-water interface. The most probable conformer was characterized by a two-fold axial symmetry that was maintained during transition to the hydrophobic bulk conformation. Minor changes in the interfacial structure were sufficient to achieve the configuration characteristic of the hydrophobic bulk phase. [less ▲]

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See detailRegulation of growth hormone messenger RNA by thyroid and glucocorticoid hormones
Martial, Joseph ULg; Baxter, John D; Goodman, Howard M et al

in Proceedings of the National Academy of Sciences of the United States of America (1977), 74(5), 1816-20

Thyroid and glucocorticoid hormones stimulate growth hormone synthesis in cultured rat pituitary cells (GC). We have compared changes in growth hormone production and mRNA in these cells. Triiodothyronine ... [more ▼]

Thyroid and glucocorticoid hormones stimulate growth hormone synthesis in cultured rat pituitary cells (GC). We have compared changes in growth hormone production and mRNA in these cells. Triiodothyronine (10 nM) and dexamethasone (1 micron) stimulated increases in growth hormone production by 2.5- and 3.8-fold, respectively. There were corresponding increases in the capacity of RNA from hormone-treated cells to direct synthesis of pregrowth hormone in a wheat germ cell-free translation system, suggesting hormone-regulated increases in growth hormone mRNA. Hormone-induced changes in mRNA were also demonstrated by determining the kinetics of hybridization of a cDNA probe prepared from RNA enriched (about 70%) for growth hormone translational activity with RNA from control and hormone-treated cells. These results suggest that thyroid and glucocorticoid hormones can regulate growth hormone production by influencing the levels of its mRNA. [less ▲]

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See detailRegulation of growth hormone gene expression: synergistic effects of thyroid and glucocorticoid hormones
Martial, Joseph ULg; Seeburg, Peter H; Guenzi, Doris et al

in Proceedings of the National Academy of Sciences of the United States of America (1977), 74(10), 4293-4295

Cultured rat pituitary cells (GC) respond to thyroid and glucocorticoid hormones by increases in growth hormone production and growth hormone mRNA. When these cells are transferred from medium containing ... [more ▼]

Cultured rat pituitary cells (GC) respond to thyroid and glucocorticoid hormones by increases in growth hormone production and growth hormone mRNA. When these cells are transferred from medium containing normal animal serum (with 1.8 mug of thyroxine per dl) to a medium containing serum from a thyroidectomized calf, "hypothyroid medium" (with no detectable thyroid hormone), growth hormone production decreases markedly. In cells maintained for 5 days in hypothyroid medium, triiodothyronine induces within 50 hr a 17-fold increase in growth hormone production whereas glucocorticoids, during the same time, produce a negligible (3-fold or less) stimulation. In combination, the two hormones promote a 45-fold stimulation. In all instances the changes in growth hormone production are paralleled by changes in the levels of growth hormone mRNA as measured by cell-free translation. The transfer to hypothyroid medium and the hormonal induction do not affect the relative activities of other mRNAs whose products are detectable on polyacrylamide gels. These studies indicate that thyroid hormone can be an activator of the expression of the growth hormone gene. The results also show that triiodothyronine controls the magnitude of the effect of glucocorticoids on growth hormone mRNA, and provide a model for "permissive" triiodothyronine action. The synergistic effect of these two classes of hormone suggests that they increase levels of growth hormone mRNA by different mechanisms. [less ▲]

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See detailFrog oocytes synthesize and completely process the precursor polypeptide to virion structural proteins after microinjection of avian myeloblastosis virus
Ghysdael, Jacques; Hubert, E.; Travnicek, M. et al

in Proceedings of the National Academy of Sciences of the United States of America (1977), 74(8), 3230-3234

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See detailBovine leukemia virus, an exogenous RNA oncogenic virus.
Kettmann, Richard ULg; Portetelle, Daniel ULg; Mammerickx, Marc et al

in Proceedings of the National Academy of Sciences of the United States of America (1976), 73

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See detailTranspeptidase activity of Streptomyces D-alanyl-D carboxypeptidases
Pollock, J. J.; Ghuysen, Jean-Marie ULg; Linder, R. et al

in Proceedings of the National Academy of Sciences of the United States of America (1972), 69(3), 662-666

In the presence of N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-D-Ala as donor, and either D-[(14)C]alanine, [(14)C]-glycine, or meso-[(3)H]diaminopimelic acid as acceptor, the DD carboxypeptidases from ... [more ▼]

In the presence of N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-D-Ala as donor, and either D-[(14)C]alanine, [(14)C]-glycine, or meso-[(3)H]diaminopimelic acid as acceptor, the DD carboxypeptidases from Streptomyces R61 and R39 catalyze a transpeptidation reaction with the release of terminal D-alanine from the donor and the formation of either N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-D-[(14)C]Ala, N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-[(14)C] Gly, or N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-D-meso- [(3)H]diaminopimelic acid. The reaction appears to be a true transpeptidation, and is not simply a "reversal of hydrolysis". Transpeptidation is inhibited by pencillin at concentrations that inhibit hydrolysis (carboxypeptidase action) of the donor peptide. There are differences in the specificity profiles of the Streptomyces enzymes for acceptor molecules:only the R61 enzyme used [(14)C]Gly-Gly as acceptor; transfer of N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala to this acceptor resulted in the formation of N(alpha),N(epsilon)-diacetyl-Lys-D-Ala-[(14)C] Gly-Gly, with the synthesis of a (D-Ala-Gly) peptide bond in an endoposition. [less ▲]

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See detailTwo interesting nuclei of planetary nebulae: IC 418 and NGC 40
Swings, Polydore ULg; Struve, Otto

in Proceedings of the National Academy of Sciences of the United States of America (1941), 27

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See detailHD 167362, an object similar to Campbell's Hydrogen Envelope Star
Swings, Polydore ULg; Struve, Otto

in Proceedings of the National Academy of Sciences of the United States of America (1940), 26

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See detailThe spectrum of RW Hydrae
Swings, Polydore ULg; Struve, Otto

in Proceedings of the National Academy of Sciences of the United States of America (1940), 26

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