974 resultados para Bernardi Claraevallensis
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Manipulus 1: [18] p., 2 leaves of plates; manipulus 2: [16] p., 2 leaves of plates; manipulus 3: 30 p., 4 leaves of plates; manipulus 4: 39 p., 6 leaves of plates.
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Each comedy has special t.p. and separate paging.
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Mode of access: Internet.
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Tasso, Torquato. Aminta.-Ongaro, Antonio. Alceo.--Giraldi Cintio, Giovanni Battista Egle.
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Bibliographical footnotes.
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Title of v. 2 includes dedication of Count Mihály Nadesd to Maria Theresia ; title of v. 3 that of Count Ferencz Zichy de Vasonkeō to Joseph II.
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27. Motette: Unser keiner lebet ihm selber.--28. Dialog: Wer ist der, so von Edom kommet.--29. Ich hab's gewagt.--30. Fürchtet euch nicht.--31. Auf das fest der himmelfahrt.--32. Auf das fest des erzengels Michael.--33. Communion-andacht.--34. Von gnad' und recht. Ps. 101.--35. Cum Maria diluculo.--36. Wir glauben all' an einen Gott.--37. Magnificat.--38. Merk auf mein herz.--39. Zwingt die saiten in cithara.
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Most of the letters were written by Francesco Bernardi and Ugo Fiesco.
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At head of title: Saeculum XII, annus 1153.
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Mode of access: Internet.
Jacobi Gretseri Societatis Jesu ... Opera omnia ... : tomus XVII: mamtissa duplex ad universum opus.
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Mode of access: Internet.
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Tartrate-resistant acid phosphatase (TRAP) is highly expressed in osteoclasts and in a subset of tissue macrophages and dendritic cells. It is expressed at lower levels in the parenchymal cells of the liver, glomerular mesangial cells of the kidney and pancreatic acinar cells. We have identified novel TRAP mRNAs that differ in their 5-untranslated region (5'-UTR) sequence, but align with the known murine TRAP mRNA from the first base of Exon 2. The novel 5'-UTRs represent alternative first exons located upstream of the known 5'-UTR. A similar genomic structure exists for the human TRAP gene with partial conservation of the exon and promoter sequences. Expression of the most distal 5'-UTR (Exon 1A) is restricted to adult bone and spleen tissue. Exon 1B is expressed primarily in tissues containing TRAP-positive nonhaematopoietic cells. The known TRAP 5'-UTR (Exon 1) is expressed in tissues characteristic of myeloid cell expression. In addition the Exon 1C promoter sequence is shown to comprise distinct transcription start regions, with an osteoclast-specific transcription initiation site identified downstream of a TATA-like element. Macrophages are shown to initiate transcription of the Exon 1C transcript from a purine-rich region located upstream of the osteoclast-specific transcription start point. The distinct expression patterns for each of the TRAP 5'-UTRs suggest that TRAP mRNA expression is regulated by the use of four alternative tissue- and cell-restricted promoters. (C) 2003 Elsevier Science B.V. All rights reserved.
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Limited but significant sequence similarity has been observed between an uncharacterized human protein, SIN1, and the S. pombe SIN1, Dictyostelium RIP3 and S. cerevisiae AVO1 proteins. The human Sin1 gene has been automatically predicted (MAPKAP1; GenBank accession number NM_024117); however, this sequence appears to be incomplete. In this study, we have cloned and characterized the full-length human Sin1 mRNA and identified a highly conserved domain that defines the family of SIN1 orthologues, members of which are widely distributed in the fungal and metazoan kingdoms. We demonstrate that Sin1 transcripts can use alternative polyadenylation signals and describe a number of Sin1 splice variants that potentially encode functionally different isoforms. (C) 2004 Elsevier B.V. All rights reserved.
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A full-length cDNA sequence coding for Echinococcus granulosus thioredoxin peroxidase (EgTPx) was isolated from a sheep strain protoscolex cDNA library by immunoscreening using a pool of sera from mice infected with oncospheres. EgTPx expressed as a fusion protein with glutathione S-transferase (GST) exhibited significant thiol-dependent peroxidase activity that protected plasmid DNA from damage by metal-catalyzed oxidation (MCO) in vitro. Furthermore, the suggested antioxidant role for EgTPx was reinforced in an in vivo assay, whereby its expression in BL21 bacterial cells markedly increased the tolerance and survival of the cells to high concentrations of H2O2 compared with controls. Immunolocalization studies revealed that EgTPx was specifically expressed in all tissues of the protoscolex and brood capsules. Higher intensity of labelling was detected in many, but not all, calcareous corpuscle cells in protoscoleces. The purified recombinant EgTPx protein was used to screen sera from heavily infected mice and patients with confirmed hydatid infection. Only a portion of the sera reacted positively with the EgTPx-GST fusion protein in Western blots, suggesting that EgTPx may form antibody-antigen complexes or that responses to the EgTPx antigen may be immunologically regulated. Recombinant EgTPx may prove useful for the screening of specific inhibitors that could serve as new drugs for treatment of hydatid disease. Moreover, given that TPx from different parasitic phyla were phylogenetically distant from host TPx molecules, the development of antiparasite TPx inhibitors that do not react with host TPx might be feasible. (C) 2003 Elsevier B.V. All rights reserved.