Base de dados : LILACS
Pesquisa : G02.111.570.160 [Categoria DeCS]
Referências encontradas : 13 [refinar]
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  1 / 13 LILACS  
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Fotocópia
Id: lil-321750
Autor: Anon.
Título: Proteoglycans, glycosaminoglycans and sulfated polysaccharides from connective tissues
Fonte: Mem. Inst. Oswaldo Cruz;86(supl.3):13-22, 1991.
Idioma: en.
Descritores: Tecido Conjuntivo
Glicosaminoglicanos
Polissacarídeos
Proteoglicanas
-Sequência de Carboidratos
Glicosaminoglicanos
Conformação Molecular
Dados de Sequência Molecular
Polissacarídeos
Proteoglicanas
Pepinos-do-Mar
Sulfatos
Urocordados
Vertebrados
Limites: Animais
Seres Humanos
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


  2 / 13 LILACS  
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Fotocópia
Id: lil-321733
Autor: Anon.
Título: The xylan-degrading enzyme system
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(5):1093-1109, May 1994.
Idioma: en.
Descritores: Xilanos
-Biotecnologia
Sequência de Carboidratos
Glicosídeo Hidrolases
Hidrólise
Dados de Sequência Molecular
Sistema da Enzima Desramificadora do Glicogênio/metabolismo
Especificidade por Substrato
Trichoderma
Xilosidases
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


  3 / 13 LILACS  
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Fotocópia
Id: lil-320010
Autor: Ross, Susan R; Dzuris, John L; Golovkina, Tatyana V; Clemmons, Wayne C; van den Hoogen, Bernadette.
Título: Mouse mammary tumor virus (MMTV), a retrovirus that exploits the immune system. Genetics of susceptibility to MMTV infection
Fonte: Medicina (B.Aires);57(Supl.2):34-42, Aug. 1997.
Idioma: en.
Resumo: All animals, including humans, show differential susceptibility to infection with viruses. Study of the genetics of susceptibility or resistance to specific pathogens is most easily studied in inbred mice. We have been using mouse mammary tumor virus (MMTV), a retrovirus that causes mammary tumors in mice, to study virus/host interactions. These studies have focused on understanding the mechanisms that determine genetic susceptibility to MMTV-induced mammary tumors, the regulation of virus gene expression in vivo and how the virus is transmitted between different cell types. We have found that some endogenous MMTVs are only expressed in lymphoid tissue and that a single base pair change in the long terminal repeat of MMTV determines whether the virus is expressed in mammary gland. This expression in lymphoid cells is necessary for the infectious cycle of MMTV, and both T and B cells express and shed MMTV. Infected lymphocytes are required not only for the initial introduction of MMTV to the mammary gland, but also for virus spread at later times. Without this virus spread, mammary tumorigenesis is dramatically reduced. Mammary tumor incidence is also affected by the genetic background of the mouse and at least one gene that affects infection of both lymphocytes and mammary cells has not yet been identified. The results obtained from these studies will greatly increase our understanding of the genetic mechanisms that viruses use to infect their hosts and how genetic resistance to such viruses in the hosts occurs.
Descritores: Predisposição Genética para Doença
Infecções por Retroviridae/genética
Infecções Tumorais por Vírus/genética
Nucleotídeos/genética
Vírus do Tumor Mamário do Camundongo/genética
Gammaretrovirus/genética
-Linfócitos B
CAMUNDONGOS ENDOGAMICOS CABDOMENABDOMINAL INJURIESBL
Infecções por Retroviridae/imunologia
Infecções Tumorais por Vírus/imunologia
Integração Viral/genética
Integração Viral/imunologia
Sequência de Carboidratos/genética
Linfócitos T
Vírus do Tumor Mamário do Camundongo/imunologia
Gammaretrovirus/imunologia
Limites: Animais
Camundongos
Responsável: BR1.1 - BIREME


  4 / 13 LILACS  
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Fotocópia
Id: lil-288917
Autor: Elola, María T; Fink, Nilda E.
Título: Galectinas: estructura, especificidad glicídica y ligandos específicos / Galectins: structure, sugar specificity and specific ligands
Fonte: Acta bioquím. clín. latinoam;34(3):293-330, sept. 2000. ilus.
Idioma: es.
Resumo: Las galectinas se definen por dos propiedades: secuencias de aminoácidos características compartidas y afinidad por azúcares ß-galactosídicos. Numerosas galactinas de mamíferos fueron secuenciadas y bien caracterizadas en diferentes especies, siendo clasificadas como galectina-1 a galectina-10, según sus homologías de secuencia. La identidad entre dominios que ligan carbohidratos de distintas galectinas de una especie de mamífero oscila entre 20-40 por ciento, mientras que la identidad de galectina-1, por ejemplo, entre distintas especies es de 80-90 por ciento. En la presente revisión, se describen las principales propiedades distintivas de las galectinas de mamífero en cuanto a estructura proteica, estructura cristalina, especificidad glicídica y ligandos específicos
Descritores: Técnicas In Vitro
Lectinas/química
Biomarcadores/sangue
Selectinas/química
-Sequência de Aminoácidos
Sequência de Carboidratos
Bovinos
Galinhas
Cristalografia
Laminina/química
Laminina/ultraestrutura
Lectinas/classificação
Lectinas/fisiologia
Mamíferos
Dados de Sequência Molecular
Difração de Raios X
Limites: Seres Humanos
Camundongos
Ratos
Animais
Bovinos
Tipo de Publ: Revisão
Responsável: AR144.1 - CIBCHACO - Centro de Información Biomedica del Chaco


  5 / 13 LILACS  
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Fotocópia
Id: lil-204195
Autor: Tersariol, Ivarne Luis Santos.
Título: Sequenciamento de heparam sulfato e mecanismo de açäo da heparitinase I.
Fonte: Säo Paulo; s.n; 1995. 122 p. ilus, tab.
Idioma: pt.
Tese: Apresentada a Universidade Federal de Sao Paulo. Escola Paulista de Medicina para obtenção do grau de Doutor.
Descritores: Sequência de Carboidratos
Glicosaminoglicanos
Heparitina Sulfato
Responsável: BR1.2 - Biblioteca Central
BR1.2; 2069


  6 / 13 LILACS  
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Tersariol, I. L. S
Id: lil-144462
Autor: Tersariol, I. L. S; Ferreira, T. M. P. C; Medeiros, M. G. L; Porcianatto, M. A; Moraes, C. T; Abreu, L. R. D; Nader, H. B; Dietrich, C. P.
Título: Sequencing of heparan sulfate proteoglycans: identification of variable and constant oligosaccharide regions in eight heparan sulfate proteoglycans of different origins
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(9):2097-102, Sept. 1994. ilus.
Idioma: en.
Conferência: Apresentado em: Brazilian Symposium on Extracellular Matrix, 3, Angra dos Reis, Sept. 11-14, 1994.
Resumo: The sequence of the disacharide units of eight heparan sulfate proteoglycans of different origins is described. All heparan sulfates contain 5 variable regions made of oligosaccharide blocks of disaccharides, namely GlcUA(1-4) GlcNAc, GlcUA(1-4)GlcNS, IdoUA (104)GlcNS) and monosaccharides (GlcNS, and GlcNS,65) at the non-reducing terminal. The N-acetylated region of the heparan sulfates is linked to the serine of the protein core through a trisaccharide of Xyl-Gal-Gal. Heparan sulfates differ from one another in terms of the number of disaccharides that compose each block
Descritores: Heparitina Sulfato/química
Oligossacarídeos/química
Proteoglicanas/química
-Acetilação
Sequência de Carboidratos
Fracionamento Químico
Dissacarídeos/química
Dados de Sequência Molecular
Polissacarídeo-Liase/análise
Análise de Sequência
Limites: Bovinos
Cães
Coelhos
Animais
Responsável: BR1.1 - BIREME


  7 / 13 LILACS  
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Id: lil-140258
Autor: Lederkremer, R. M. de.
Título: Free and protein-linked glycoinositolphospholipids in Trypanosoma cruzi
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(2):239-42, Feb. 1994. ilus.
Idioma: en.
Conferência: Apresentado em: GPI-Anchor Proteins : Structure and Function - 1994 Meeting, Angra dos Reis, 20-26 Feb. 1994.
Resumo: Two glycoinositol phospholipids (GIPL A and GIPL B) have been purified from epimastigotes of Trypanosoma cruzi at the logarithmic phase of growth (2 days). The GIPLs differ mainly in the lipid moiety and are similar to the lipopeptidophosphoglycan (LPPG) previously isolated from epimastigotes at the stationary phase (4-5 days). [3H]-palmitic acid was incorporated into 1-O-hexadecyl-2-O-palmitoylglycerol in GIPL A and into a sphinganine ceramide with palmitic acid and lignoceric acid as the fatty acids in GIPL B. The lipids could be released by incubation with phosphatidylinositol-specific phospholipase C (PI-PLC) or glycosylphosphatidylinositol phospholipase D (GPI-PLD) from rat serum. The oligosaccharides share the common core structure of the glycosylphosphatidilinositol (GPI) membrane anchors. Microheterogeneity was demonstrated, as well as substitution by galactose, which is mainly in the furanose configuration as was previously described for the LPPG. However, methylation analysis indicated that 20 percent of the galactose is present as terminal pyranose units. In infective trypomastigotes, [3H]-palmitic acid was incorporated into the anchor of the Tc-85 glycoprotein. The lipid cleaved by phospholipase C digestion was identified as 1-O-hexadecylglycerol and the main oligosaccharide has the structure of the conserved core of all GPI anchors. [3H]-palmitic acid-labelled Tc-85 released into the culture medium as membrane vesicles showed 80 percent resistance to the action of PI-PLC. However, after mild alkaline hydrolysis, part of the radioactivity was released by the enzyme
Descritores: Glicoesfingolipídeos/química
Oligossacarídeos/química
Trypanosoma cruzi/química
-Sequência de Carboidratos
Ácidos Graxos
Glicoesfingolipídeos/isolamento & purificação
Dados de Sequência Molecular
Oligossacarídeos/análise
Oligossacarídeos/isolamento & purificação
Ácidos Palmíticos
Peptidoglicano/química
Peptidoglicano/isolamento & purificação
Fosfolipídeos/química
Fosfolipídeos/isolamento & purificação
Fosfolipases Tipo C
Limites: Animais
Ratos
Responsável: BR26.1 - Biblioteca Central


  8 / 13 LILACS  
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Id: lil-140257
Autor: Heise, N; Raper, J; Cardoso de Almeida, M. L.
Título: Characterization of a phospholipase C-resistant inositol containing glycolipid from Trypanosoma cruzi
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(2):233-8, Feb. 1994. ilus.
Idioma: en.
Conferência: Apresentado em: GPI-Anchor Proteins: Structure and Functions - 1994 Meeting, Angra dos Reis, 20-26 Feb. 1994.
Resumo: Since glycosylphosphatidylinositol is the most common form of attachment of proteins to membranes in T. cruzi, and that this parasite depends on surface-mediated interactions for survival within the vector and mammalian host, it is probable that a drug which interfers with the metabolism of glycosylphosphatidylinositol (GPI) could be successfully employed in chemotherapy. Over the last few years several groups have been characterizing this mode of attachment in T. cruzi and more recently we have been concentrating our efforts on the identification of candidate precursors for protein anchors in metacyclic trypomastigotes. Previously detected GPI heterogeneity regarding solubilization of a major stage-specific antigen (1G7-Ag) by phospholipase C led us to investigate whether biosynthetic precursors with similar properties could also be identified. Two glycolipid species whose migration properties resemble glycolipids A and C of T. brucei were amenable to biosynthetic radiolabelling with palmitic acid, inositol, ethanolamine, glucosamine and mannose. Following purification, these species were submitted to classical GPI diagnostic treatments. In both cases digestion with GPI-specific phospholipase D (GPIPLD) produced phosphatidic acid and treatment with either mild base or phospholipase A2 (PLA2) produced free fatty acid, indicating an acylation at least at position 2 of the glycerol. The glycolipid A-like species proved to be susceptible to solubilization by PIPLC of B. thuriengiensis and by GPIPLC of T. brucei and the glycolipid C-like material proved to be fully resistant to both lipases. Although the glycolipid A-like species indeed presents these and other properties compatible with a precursor for the chemically characterized 1G7-Ag anchor, the PLC-resistant species which is completely insensitive to nitrous acid deamination might be an exception to the general finding of a non-acetylated glucosamine in the GPI moieties so far described
Descritores: Antígenos de Protozoários
Fosfatidilinositóis/química
Glicolipídeos/química
Trypanosoma cruzi/imunologia
Fosfolipases Tipo C/química
-Sequência de Bases
Sequência de Carboidratos
Ácidos Graxos
Dados de Sequência Molecular
Responsável: BR26.1 - Biblioteca Central


  9 / 13 LILACS  
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Colli, W
Id: lil-138289
Autor: Casal, O. L; Zingales, B; Colli, W.
Título: Structural features of LPPG and related compounds isolated from Trypanosoma cruzi trypomastigotes
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(2):227-31, Feb. 1994. ilus.
Idioma: en.
Conferência: Apresentado em: GPI-Anchor Proteins: Structure and function - 1994 Meeting, Angra dos Reis, 20-26 Feb. 1994.
Resumo: A hydrophobic fraction isolated from trypomastigotes of Trypanosoma cruzi is being characterized using immunological and chemical techniques. The lipopeptidophosphoglycan (LPPG) was identified in this fraction since it gave a positive reaction with anti-LPPG rabbit serum and had similar structural features such as the presence of ceramide as the lipid moiety, furanoic galactose, and a glycan moiety consistent with that obtained from an authentic sample of epimastigote LPPG, as judged by thin-layer chromatography. Furthermore, the hydrophobic fraction contained other glycolipids with different structural features. The lipid moiety of these compounds is alkylglycerol rather than a ceramide, the carbohydrate chain appears to be less complex than that in LPPG and no reactivity was observed towards an anti-LPPG serum
Descritores: Glicoconjugados/química
Peptidoglicano/química
Fosfolipídeos/química
Trypanosoma cruzi/química
-Western Blotting
Sequência de Carboidratos
Glicoproteínas/imunologia
Glicoproteínas/química
Glicoconjugados/imunologia
Dados de Sequência Molecular
Peptidoglicano/imunologia
Fosfolipídeos/imunologia
Trypanosoma cruzi/imunologia
Limites: Animais
Coelhos
Responsável: BR26.1 - Biblioteca Central


  10 / 13 LILACS  
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Id: lil-138288
Autor: Jones, C; Previato, J. O; Mendonça-Previato, L; Wait, R.
Título: The use of NMR spectroscopy in the structure determination of a Leptomonas samueli glycosylphosphosphingolipid-derived oligosaccharide
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(2):219-26, Feb. 1994. ilus.
Idioma: en.
Conferência: Apresentado em: GPI-Anchor Proteins: Structure and function - 1994 Meeting, Angra dos Reis, 20-26 Feb. 1994.
Resumo: Nuclear magnetic resonance (NMR) spectroscopy provides an extremely powerful technique to determine the structure of oligosaccharides, particularly when used in conjuction with other physical techniques such as methylation analysis and fast atom bombardment mass spectroscopy (FAB-MS). This brief review describes the application of NMR to the determination of the structure of an oligosaccharide isolated from the glycophosphosphingolipid (GPS) from the monogenetic trypanosomatid Leptomonas samueli. Where ambiguities arise in the NMR interpretation, the use of other data will be discussed
Descritores: Glicoesfingolipídeos/química
Oligossacarídeos/química
Espectroscopia de Ressonância Magnética
Trypanosomatina/química
-Sequência de Carboidratos
Glicoesfingolipídeos/isolamento & purificação
Fosfatos de Inositol/análise
Dados de Sequência Molecular
Oligossacarídeos/isolamento & purificação
Espectrometria de Massas de Bombardeamento Rápido de Átomos
Limites: Animais
Responsável: BR26.1 - Biblioteca Central



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