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Your search keyword '"Severino, B."' showing total 10 results
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10 results on '"Severino, B."'

1. Molecular pathology quality control in Southeast Asia: Results of a multiregional quality assurance study from MASTER KEY Asia

Author

Okuma, Hitomi Sumiyoshi, primary, Yoshida, Hiroshi, additional, Kobayashi, Yoshihisa, additional, Arakaki, Motoko, additional, Mizoguchi, Chiharu, additional, Inagaki, Lina, additional, Voon, Pei Jye, additional, Malik Bin Ismail, Adam, additional, Fen Soo Hoo, Hwoei, additional, Yusak, Suhana, additional, Severino B. Imasa, Marcelo, additional, Nguyen Huy, Thinh, additional, Thai Anh, Tu, additional, Kohsaka, Shinji, additional, Mano, Hiroyuki, additional, Yonemori, Kan, additional, Nakamura, Kenichi, additional, and Yatabe, Yasushi, additional

Published
2023
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2. Molecular pathology quality control in Southeast Asia: Results of a multiregional quality assurance study from MASTER KEY Asia

Author

Hitomi Sumiyoshi Okuma, Hiroshi Yoshida, Yoshihisa Kobayashi, Motoko Arakaki, Chiharu Mizoguchi, Lina Inagaki, Pei Jye Voon, Adam Malik Bin Ismail, Hwoei Fen Soo Hoo, Suhana Yusak, Marcelo Severino B. Imasa, Thinh Nguyen Huy, Tu Thai Anh, Shinji Kohsaka, Hiroyuki Mano, Kan Yonemori, Kenichi Nakamura, and Yasushi Yatabe

Subjects
Cancer Research, Oncology, General Medicine
Published
2023
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9. Synthesis, docking studies, and pharmacological evaluation of 2‐hydroxypropyl‐4‐arylpiperazine derivatives as serotoninergic ligands

Author

Anna Bielenica, Raffaele Capasso, Beatrice Severino, Angela Corvino, Ewa Gibula-Tarlowska, Anna Leśniak, Marta Struga, Elisa Magli, Rosa Sparaco, Ewa Kędzierska, Giovanna Esposito, Giuseppe Caliendo, Stefania Albrizio, Ferdinando Fiorino, Vincenzo Santagada, Magdalena Bujalska-Zadrożny, Agnieszka A. Kaczor, Jolanta Kotlinska, Elisa Perissutti, Francesco Frecentese, Magli, E., Kedzierska, E., Kaczor, A. A., Bielenica, A., Severino, B., Gibula-Tarlowska, E., Kotlinska, J. H., Corvino, A., Sparaco, R., Esposito, G., Albrizio, S., Perissutti, E., Frecentese, F., Lesniak, A., Bujalska-Zadrozny, M., Struga, M., Capasso, R., Santagada, V., Caliendo, G., and Fiorino, F.

Subjects
Male, Stereochemistry, 5-HT, Pharmaceutical Science, Ligands, 01 natural sciences, Rats, Sprague-Dawley, Structure-Activity Relationship, chemistry.chemical_compound, In vivo, Drug Discovery, Animals, norbornene nucleu, Receptor, Piperazine, exo-N-hydroxy-7-oxabicyclo[2.2.1]hept-5-ene-2,3-dicarboximide, 5-HT receptor, Dose-Response Relationship, Drug, Molecular Structure, 010405 organic chemistry, arylpiperazine derivative, Affinities, Rats, serotonin, 0104 chemical sciences, Molecular Docking Simulation, 010404 medicinal & biomolecular chemistry, receptor ligand, chemistry, Docking (molecular), Receptors, Serotonin, Serotonin, Pharmacophore, 1A
Abstract

A new series of norbornene and exo-N-hydroxy-7-oxabicyclo[2.2.1]hept-5-ene-2,3-dicarboximide derivatives was prepared, and their affinities to the 5-HT1A , 5-HT2A , and 5-HT2C receptors were evaluated and compared with a previously synthesized series of derivatives characterized by the same nuclei, to identify selective ligands for the subtype receptors. Arylpiperazines represent one of the most important classes of 5-HT1A R ligands, and the research of new derivatives has been focused on the modification of one or more portions of this pharmacophore. The combination of structural elements (heterocyclic nucleus, hydroxyalkyl chain, and 4-substituted piperazine), known to be critical for the affinity to 5-HT1A receptors, and the proper selection of substituents resulted in compounds with high specificity and affinity toward serotoninergic receptors. The most active compounds were selected for further in vivo assays to determine their functional activity. Finally, to rationalize the obtained results, molecular docking studies were performed. The results of the pharmacological studies showed that 3e, 4j, and 4n were the most active and promising derivatives for the serotonin receptor considered in this study.

Published
2021
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10. Synthetic peptides as probes for conformational preferences of domains of membrane receptors.

Author

Naider F, Khare S, Arshava B, Severino B, Russo J, and Becker JM

Subjects
Amino Acid Sequence, Circular Dichroism, History, 20th Century, Models, Molecular, Molecular Probes history, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Peptides chemical synthesis, Peptides history, Protein Conformation, Protein Structure, Tertiary, Receptors, Cell Surface history, Receptors, Mating Factor, Receptors, Peptide chemistry, Receptors, Peptide history, Saccharomyces cerevisiae Proteins chemistry, Saccharomyces cerevisiae Proteins history, Transcription Factors chemistry, Transcription Factors history, Receptors, Cell Surface chemistry
Abstract

Peptide models have been widely used to investigate conformational aspects of domains of proteins since the early 1950s. A pioneer in this field was Dr. Murray Goodman, who applied a battery of methodologies to study the onset of structure in homooligopeptides. This article reviews some of Dr. Goodman's contributions, and reports recent studies using linear and constrained peptides corresponding to the first extracellular loop and linear peptides corresponding to the sixth transmembrane domain of a G-protein coupled receptor from the yeast Saccharomyces cerevisiae. Peptides containing 30-40 residues were synthesized using solid-phase methods and purified to near homogeneity by reversed phase high performance liquid chromatography. CD and NMR analyses indicated that the first extracellular loop peptides were mostly flexible in water, and assumed some helical structure near the N-terminus in trifluoroethanol and in the presence of micelles. Comparison of oligolysines with native loop residues revealed that three lysines at each terminus of a peptide corresponding to the sixth transmembrane domain of the alpha-factor receptor resulted in better aqueous solubility and greater helicity than the native loop residues., (Copyright 2005 Wiley Periodicals, Inc)

Published
2005
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