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731.
Marques Daniel Ruivo Gomes Ana Allen Clemente Vanda dos Santos José Moutinho Serra Joana de Azevedo Maria Helena Pinto 《Sleep and biological rhythms》2020,18(3):199-207
Sleep and Biological Rhythms - Insomnia disorder has known striking developments over the last few years. Partly due to advances in neuroimaging techniques and brain sciences, our understanding of... 相似文献
732.
Carla Reale Anna Iervolino Ivan Scudiero Angela Ferravante Luca Egildo D'Andrea Pellegrino Mazzone Tiziana Zotti Antonio Leonardi Luca Roberto Mariastella Zannini Tiziana de Cristofaro Muralitharan Shanmugakonar Giovambattista Capasso Manolis Pasparakis Pasquale Vito Romania Stilo 《The Journal of biological chemistry》2016,291(11):5765-5773
733.
M B Canani F Rea D A Capasso 《Bollettino della Società italiana di biologia sperimentale》1965,41(16):901-904
734.
N di Clemente S Ghaffari R B Pepinsky C Pieau N Josso R L Cate B Vigier 《Development (Cambridge, England)》1992,114(3):721-727
Anti-Müllerian hormone (AMH), also known as Müllerian-inhibiting substance or factor, has previously been shown to sex-reverse the steroidogenic pattern of fetal mammalian ovaries through repression of aromatase biosynthesis. Study of the ontogeny of the response of cyclic AMP-stimulated aromatase activity of rat fetal ovaries to AMH has allowed us to develop a quantitative bioassay for the hormone. Linear responses as a function of the logarithm of AMH concentration were observed over ranges of 0.2-7.5 micrograms/ml for the bovine protein and 0.15-2 micrograms/ml for the human protein, with a maximal decrease in aromatase activity of 90% for both proteins. Under the same in vitro conditions, AMH treatment did not affect cyclic AMP-stimulated fetal rat testicular aromatase activity. Partially purified chick AMH also decreased rat ovarian aromatase activity, allowing us to use this test to study AMH ontogeny in chick gonads. Analysis of the species specificity of AMH repression of ovarian aromatase activity indicated that turtle and rat fetal ovaries responded to AMH of other vertebrate classes, whereas aromatase activity of chick embryo ovaries could be repressed only by the homospecific hormone. 相似文献
735.
736.
The covariances among the populations of distinct compartments are studied for the multi-compartmental birthless death-migration-immigration
process. The important role played by the transition matrix of the deterministic process is underlined. Several examples are
discussed.
Work performed under the auspices of the GNFM-CNR. 相似文献
737.
738.
Domenico Russo Floriana Della Ragione Riccardo Rizzo Eiji Sugiyama Francesco Scalabrì Kei Hori Serena Capasso Lucia Sticco Salvatore Fioriniello Roberto De Gregorio Ilaria Granata Mario R Guarracino Vittorio Maglione Ludger Johannes Gian Carlo Bellenchi Mikio Hoshino Mitsutoshi Setou Maurizio D'Esposito Alberto Luini Giovanni D'Angelo 《The EMBO journal》2018,37(7)
Neural development is accomplished by differentiation events leading to metabolic reprogramming. Glycosphingolipid metabolism is reprogrammed during neural development with a switch from globo‐ to ganglio‐series glycosphingolipid production. Failure to execute this glycosphingolipid switch leads to neurodevelopmental disorders in humans, indicating that glycosphingolipids are key players in this process. Nevertheless, both the molecular mechanisms that control the glycosphingolipid switch and its function in neurodevelopment are poorly understood. Here, we describe a self‐contained circuit that controls glycosphingolipid reprogramming and neural differentiation. We find that globo‐series glycosphingolipids repress the epigenetic regulator of neuronal gene expression AUTS2. AUTS2 in turn binds and activates the promoter of the first and rate‐limiting ganglioside‐producing enzyme GM3 synthase, thus fostering the synthesis of gangliosides. By this mechanism, the globo–AUTS2 axis controls glycosphingolipid reprogramming and neural gene expression during neural differentiation, which involves this circuit in neurodevelopment and its defects in neuropathology. 相似文献
739.
S Capasso L Mazzarella F Sica A Zagari 《International journal of peptide and protein research》1984,24(6):588-596
Boc-L-Asu-L-Ala-Gly-OMe crystallizes in the monoclinic space group P2(1) with cell dimensions a = 14.315 (3) A, b = 9.280 (2) A, c = 14.358(3) A, beta = 103.63(1) A, V= 1853.4 (9) A3, with two molecules in the asymmetric unit. The conformation of the two molecules is characterized by a type II' beta-bend, similar to that predicted earlier by potential energy calculations, stabilized by an intramolecular hydrogen bond. I.r. and 1H-n.m.r. data show that the folded conformation is also stable in chloroform solution. 相似文献
740.
P Galletti D Ingrosso C Manna F Sica S Capasso P Pucci G Marino 《European journal of biochemistry》1988,177(1):233-239
Eukaryotic protein carboxyl methyltransferase catalyzes a two-substrates reaction in which the methyl group of S-adenosylmethionine is transferred to the free carboxyl group of D-aspartyl and L-isoaspartyl-containing peptide or protein substrates. It has been previously shown that at least three binding sites are required for the interaction of adenosylmethionine with the enzyme and/or the protein substrate [Oliva A., Galletti P., Zappia V., Paik W. K. & Kim S. (1980) Eur. J. Biochem. 104, 595-602], while very little is known concerning the structural requirements of the protein substrate. In this study several synthetic tripeptides were selected in order to elucidate the structural requirements of the methyl-accepting substrates. The results obtained with this series of peptides suggested that: (1) three residues appear to be the minimal length, so far identified, required for a productive enzyme-substrate interaction, several dipeptides being ineffective as substrates [McFadden P. N. & Clarke S. (1986) J. Biol. Chem. 261, 11,503-11,511]; (2) the isoaspartyl residue is not recognized unless its alpha-amino group is involved in a carboamide bond; (3) an hydrogen atom on the amide linkage following the isoaspartyl residue is essential for both recognition and catalysis; (4) oligopeptides containing both D-aspartyl and D-isoaspartyl residues are not recognized by this methyltransferase. On the basis of these results, interaction sites between the peptide substrate and the enzyme molecule have been proposed. This paper also reports the first application of fast-atom-bombardment mass spectrometry to the detection of the products of the enzymatic methyl esterification reaction. By this soft ionization technique, the methyl-esterified peptides as well as the corresponding cyclic imides generated during the spontaneous demethylation process have been identified. 相似文献