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| Registros recuperados : 4 | |
| 1. |  | CASTRO, C. S. de; SILVESTRE. F. G.; ARAUJO, S. C.; YASBECK, G. de M.; MANGILI, O. C.; CRUZ, I.; CHAVEZ-OLORTEGUI, C.; KALAPOTHAKIS, E. Identification and molecular cloning of insecticidal toxins from the venom of the brown spider Laxosceles intermedia. Toxicon, Elmsford, v. 44, p. 273-280, 2004.| Biblioteca(s): Embrapa Milho e Sorgo. |
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| 2. | | DIAS-LOPES, C.; NESHICH, I. A. P.; NESHICH, G.; ORTEGA, J. M.; GRANIER, C.; CHÁVEZ-OLORTEGUI, C.; MOLINA, F.; FELICORI, L. Identification of new Sphingomyelinases D in pathogenic fungi and other pathogenic organisms. PLoS ONE, San Francisco, v. 8, n. 11, p. 1-12, 2013.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 3. | | MACHADO-DE-ÁVILA, R. A.; VELLOSO, M.; OLIVEIRA, D.; STRANSKY, S.; FLOR-SÁ, A.; SCHNEIDER, F. S.; NESHICH, G.; CHÁVEZ-OLÓRTEGUI, C. Induction of neutralizing antibodies against mutalysin-II from Lachesis muta muta Snake Venom Elicited by a conformational B-cell epitope predicted by Blue Star Sting data base. Immunome Research, v. 11, n. 1, Mar. 2015. Não paginado.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 4. | | VIART, B.; DIAS-LOPES, C.; KOZLOVA, E.; OLIVEIRA, C. F. B.; NGUYEN, C.; NESHICH, G.; CHÁVEZ-OLÓRTEGUI, C.; MOLINA, F.; FELICORI, L. F. EPI-peptide designer: a tool for designing peptide ligand libraries based on epitope-paratope interactions. Bioinformatics, v. 32, n. 10, p. 1462-1470, 2016.| Biblioteca(s): Embrapa Agricultura Digital. |
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| Registros recuperados : 4 | |
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Registro Completo
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
02/01/2014 |
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Data da última atualização: |
02/01/2014 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
DIAS-LOPES, C.; NESHICH, I. A. P.; NESHICH, G.; ORTEGA, J. M.; GRANIER, C.; CHÁVEZ-OLORTEGUI, C.; MOLINA, F.; FELICORI, L. |
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Afiliação: |
CAMILA DIAS-LOPES, UFMG; IZABELLA A. P. NESHICH, Unicamp; GORAN NESHICH, CNPTIA; JOSÉ MIGUEL ORTEGA, UFMG; CLAUDE GRANIER, SysDiag UMR 3145 CNRS/BioRad; CARLOS CHÁVEZ-OLORTEGUI, UFMG; FRANCK MOLINA, SysDiag UMR 3145 CNRS/BioRad; LIZA FELICORI, UFMG. |
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Título: |
Identification of new Sphingomyelinases D in pathogenic fungi and other pathogenic organisms. |
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Ano de publicação: |
2013 |
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Fonte/Imprenta: |
PLoS ONE, San Francisco, v. 8, n. 11, p. 1-12, 2013. |
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ISBN: |
10.1371/journal.pone.0079240 |
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Idioma: |
Inglês |
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Conteúdo: |
Sphingomyelinases D (SMases D) or dermonecrotic toxins are well characterized in Loxosceles spider venoms and have been described in some strains of pathogenic microorganisms, such as Corynebacterium sp. After spider bites, the SMase D molecules cause skin necrosis and occasional severe systemic manifestations, such as acute renal failure. In this paper, we identified new SMase D amino acid sequences from various organisms belonging to 24 distinct genera, of which, 19 are new. These SMases D share a conserved active site and a C-terminal motif. We suggest that the C-terminal tail is responsible for stabilizing the entire internal structure of the SMase D Tim barrel and that it can be considered an SMase D hallmark in combination with the amino acid residues from the active site. Most of these enzyme sequences were discovered from fungi and the SMase D activity was experimentally confirmed in the fungus Aspergillus flavus. Because most of these novel SMases D are from organisms that are endowed with pathogenic properties similar to those evoked by these enzymes alone, they might be associated with their pathogenic mechanisms. |
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Palavras-Chave: |
Bioinformática; Enzimas; Esfingomielinas. |
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Thesaurus NAL: |
Bioinformatics; Enzymes; Sphingomyelins. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/94633/1/Sphingomyelinases-D.pdf
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Marc: |
LEADER 01923naa a2200277 a 4500
001 1974829
005 2014-01-02
008 2013 bl uuuu u00u1 u #d
100 1 $aDIAS-LOPES, C.
245 $aIdentification of new Sphingomyelinases D in pathogenic fungi and other pathogenic organisms.$h[electronic resource]
260 $c2013
520 $aSphingomyelinases D (SMases D) or dermonecrotic toxins are well characterized in Loxosceles spider venoms and have been described in some strains of pathogenic microorganisms, such as Corynebacterium sp. After spider bites, the SMase D molecules cause skin necrosis and occasional severe systemic manifestations, such as acute renal failure. In this paper, we identified new SMase D amino acid sequences from various organisms belonging to 24 distinct genera, of which, 19 are new. These SMases D share a conserved active site and a C-terminal motif. We suggest that the C-terminal tail is responsible for stabilizing the entire internal structure of the SMase D Tim barrel and that it can be considered an SMase D hallmark in combination with the amino acid residues from the active site. Most of these enzyme sequences were discovered from fungi and the SMase D activity was experimentally confirmed in the fungus Aspergillus flavus. Because most of these novel SMases D are from organisms that are endowed with pathogenic properties similar to those evoked by these enzymes alone, they might be associated with their pathogenic mechanisms.
650 $aBioinformatics
650 $aEnzymes
650 $aSphingomyelins
653 $aBioinformática
653 $aEnzimas
653 $aEsfingomielinas
700 1 $aNESHICH, I. A. P.
700 1 $aNESHICH, G.
700 1 $aORTEGA, J. M.
700 1 $aGRANIER, C.
700 1 $aCHÁVEZ-OLORTEGUI, C.
700 1 $aMOLINA, F.
700 1 $aFELICORI, L.
773 $tPLoS ONE, San Francisco$gv. 8, n. 11, p. 1-12, 2013.
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Embrapa Agricultura Digital (CNPTIA) |
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