Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 4 de 4
Filtrar
Más filtros











Base de datos
Tipo de estudio
Intervalo de año de publicación
1.
J Gynecol Obstet Biol Reprod (Paris) ; 40(2): 166-8, 2011 Apr.
Artículo en Francés | MEDLINE | ID: mdl-20926206

RESUMEN

We report a case of pyometra without any related risk factor. This leads to a severe septic shock. Evolution was successful because of quick surgical management. We report literature management of such infection. Although pyometra is an uncommon disease, it should be kept in mind as delayed management may lead to fatal outcome.


Asunto(s)
Endometritis/diagnóstico , Piómetra/diagnóstico , Antibacterianos/uso terapéutico , Infecciones Bacterianas/tratamiento farmacológico , Endometritis/microbiología , Femenino , Gardnerella vaginalis , Infecciones por Bacterias Grampositivas/tratamiento farmacológico , Humanos , Hipotensión , Persona de Mediana Edad , Peptostreptococcus , Piómetra/microbiología , Piómetra/cirugía , Choque Séptico , Taquicardia , Tomografía Computarizada por Rayos X
2.
Toxicon ; 29(4-5): 516-20, 1991.
Artículo en Inglés | MEDLINE | ID: mdl-1862524

RESUMEN

We prepared a cDNA library from venom glands of the green mamba Dendroaspis angusticeps. A cDNA clone was isolated using an appropriate nucleotide probe. The nucleotide sequence codes for a 21 residue signal peptide followed by a 65 residue protein having the amino acid sequence of muscarinic toxin 2, as confirmed in the accompanying paper (Karlsson, E., Risinger, C., Jolkkonen, M., Wernstedt, C. and Adem, A.). The cDNA encoding the muscarinic toxin has been compared with those encoding other snake toxins. There are close similarities with short-chain curaremimetic neurotoxins.


Asunto(s)
Venenos Elapídicos/química , Neurotoxinas/química , Secuencia de Aminoácidos , Secuencia de Bases , ADN/genética , Venenos Elapídicos/genética , Datos de Secuencia Molecular , Neurotoxinas/genética , Proteínas de Reptiles , Homología de Secuencia de Ácido Nucleico
3.
Mol Cell Biol ; 10(9): 4737-43, 1990 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-2201900

RESUMEN

The RPC31 gene encoding the C31 subunit of Saccharomyces cerevisiae RNA polymerase C (III) has been isolated, starting from a C-terminal fragment cloned on a lambda gt11 library. It is unique on the yeast genome and lies on the left arm of chromosome XIV, very close to a NotI site. Its coding sequence perfectly matches the amino acid sequence of two oligopeptides prepared from purified C31. It is also identical to the ACP2 gene previously described as encoding an HMG1-like protein (W. Haggren and D. Kolodrubetz, Mol. Cell. Biol. 8:1282-1289, 1988). Thus, ACP2 and RPC31 are allelic and encode a subunit of RNA polymerase C. The c31 protein has a highly acidic C-terminal tail also found in several other chromatin-interacting proteins, including animal HMG1. Outside this domain, however, there is no appreciable homology to any known protein. The growth phenotypes of a gene deletion, of insertions, and of nonsense mutations indicate that the C31 protein is strictly required for cell growth and that most of the acidic domain is essential for its function. Random mutagenesis failed to yield temperature-sensitive mutants, but a slowly growing mutant was constructed by partial suppression of a UAA nonsense allele of RPC31. Its reduced rate of tRNA synthesis in vivo relative to 5.8S rRNA supports the hypothesis that the C31 protein is a functional subunit of RNA polymerase C.


Asunto(s)
ARN Polimerasas Dirigidas por ADN/genética , Genes Fúngicos , ARN Polimerasa III/genética , Saccharomyces cerevisiae/genética , Secuencia de Aminoácidos , Clonación Molecular , ADN de Hongos/genética , ADN de Hongos/aislamiento & purificación , Genotipo , Sustancias Macromoleculares , Datos de Secuencia Molecular , Mutación , Plásmidos , ARN de Hongos/genética , ARN de Hongos/aislamiento & purificación , Mapeo Restrictivo , Saccharomyces cerevisiae/enzimología
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA