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Registro Completo |
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Biblioteca(s): |
Embrapa Territorial. |
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Data corrente: |
17/04/2012 |
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Data da última atualização: |
20/01/2016 |
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Tipo da produção científica: |
Documentos |
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Autoria: |
BOLFE, E. L.; VICENTE, L. E.; ANDRADE, R. G.; VICTORIA, D. de C.; BATISTELLA, M. |
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Afiliação: |
EDSON LUIS BOLFE, CNPM; LUIZ EDUARDO VICENTE, CNPM; RICARDO GUIMARAES ANDRADE, CNPM; DANIEL DE CASTRO VICTORIA, CNPM; MATEUS BATISTELLA, CNPM. |
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Título: |
A evolução histórica dos Sistemas de Informações Geográficas. |
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Ano de publicação: |
2011 |
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Fonte/Imprenta: |
Campinas: Embrapa Monitoramento por Satélite, 2011. |
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Páginas: |
19 p. |
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Série: |
(Embrapa Monitoramento por Satélite. Documentos, 90) |
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ISSN: |
0103-7811 |
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Idioma: |
Português |
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Palavras-Chave: |
Aspecto histórico. |
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Thesagro: |
Sistema de Informação Geográfica. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/58133/1/025-11.pdf
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Marc: |
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022 $a0103-7811
100 1 $aBOLFE, E. L.
245 $aA evolução histórica dos Sistemas de Informações Geográficas.$h[electronic resource]
260 $aCampinas: Embrapa Monitoramento por Satélite$c2011
300 $a19 p.
490 $a(Embrapa Monitoramento por Satélite. Documentos, 90)
650 $aSistema de Informação Geográfica
653 $aAspecto histórico
700 1 $aVICENTE, L. E.
700 1 $aANDRADE, R. G.
700 1 $aVICTORIA, D. de C.
700 1 $aBATISTELLA, M.
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Registro original: |
Embrapa Territorial (CNPM) |
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Registro Completo
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
20/12/2018 |
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Data da última atualização: |
30/12/2020 |
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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: |
DINIZ, M. R. V.; PAIVA, A. L. B.; GUERRA-DUARTE, C.; NISHIYAMA JÚNIOR, M. Y.; MUDADU, M. de A.; OLIVEIRA, U. de; BORGES, M. H.; YATES, J. R.; JUNQUEIRA-DE-AZEVEDO, I. de. |
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Afiliação: |
MARCELO R. V. DINIZ, Fundação Ezequiel Dias, Belo Horizonte; ANA L. B. PAIVA, Fundação Ezequiel Dias, Belo Horizonte; CLARA GUERRA-DUARTE, Fundação Ezequiel Dias, Belo Horizonte; MILTON Y. NISHIYAMA JÚNIOR, Instituto Butantan, São Paulo; MAURICIO DE ALVARENGA MUDADU, CNPTIA; URSULA DE OLIVEIRA, Instituto Butantan, São Paulo; MÁRCIA H. BORGES, Fundação Ezequiel Dias, Belo Horizonte; JOHN R. YATES, The Scripps Research Institute; INÁCIO DE L. JUNQUEIRA-DE-AZEVEDO, Instituto Butantan, São Paulo. |
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Título: |
An overview of Phoneutria nigriventer spider venom using combined transcriptomic and proteomic approaches. |
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Ano de publicação: |
2018 |
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Fonte/Imprenta: |
Plos One, v. 13, n. 8, p. 1-29, 2018. |
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DOI: |
https://doi.org/10.1371/journal. pone.0200628 |
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Idioma: |
Inglês |
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Notas: |
Artigo e0200628. Na publicação: Mauricio A. Mudadu. |
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Conteúdo: |
Abstract. Phoneutria nigriventer is one of the largest existing true spiders and one of the few considered medically relevant. Its venom contains several neurotoxic peptides that act on different ion channels and chemical receptors of vertebrates and invertebrates. Some of these venom toxins have been shown as promising models for pharmaceutical or biotechnological use. However, the large diversity and the predominance of low molecular weight toxins in this venom have hampered the identification and deep investigation of the less abundant toxins and the proteins with high molecular weight. Here, we combined conventional and next-generation cDNA sequencing with Multidimensional Protein Identification Technology (MudPIT), to obtain an in-depth panorama of the composition of P. nigriventer spider venom. The results from these three approaches showed that cysteine-rich peptide toxins are the most abundant components in this venom and most of them contain the Inhibitor Cysteine Knot (ICK) structural motif. Ninety-eight sequences corresponding to cysteine-rich peptide toxins were identified by the three methodologies and many of them were considered as putative novel toxins, due to the low similarity to previously described toxins. Furthermore, using next-generation sequencing we identified families of several other classes of toxins, including CAPs (Cysteine Rich Secretory ProteinÐCRiSP, antigen 5 and Pathogenesis-Related 1ÐPR-1), serine proteinases, TCTPs (translationally controlled tumor proteins), proteinase inhibitors, metalloproteinases and hyaluronidases, which have been poorly described for this venom. This study provides an overview of the molecular diversity of P. nigriventer venom, revealing several novel components and providing a better basis to understand its toxicity and pharmacological activities. MenosAbstract. Phoneutria nigriventer is one of the largest existing true spiders and one of the few considered medically relevant. Its venom contains several neurotoxic peptides that act on different ion channels and chemical receptors of vertebrates and invertebrates. Some of these venom toxins have been shown as promising models for pharmaceutical or biotechnological use. However, the large diversity and the predominance of low molecular weight toxins in this venom have hampered the identification and deep investigation of the less abundant toxins and the proteins with high molecular weight. Here, we combined conventional and next-generation cDNA sequencing with Multidimensional Protein Identification Technology (MudPIT), to obtain an in-depth panorama of the composition of P. nigriventer spider venom. The results from these three approaches showed that cysteine-rich peptide toxins are the most abundant components in this venom and most of them contain the Inhibitor Cysteine Knot (ICK) structural motif. Ninety-eight sequences corresponding to cysteine-rich peptide toxins were identified by the three methodologies and many of them were considered as putative novel toxins, due to the low similarity to previously described toxins. Furthermore, using next-generation sequencing we identified families of several other classes of toxins, including CAPs (Cysteine Rich Secretory ProteinÐCRiSP, antigen 5 and Pathogenesis-Related 1ÐPR-1), serine proteinases, TCTPs (translationally contro... Mostrar Tudo |
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Palavras-Chave: |
Proteômica; Transcriptoma. |
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Thesaurus NAL: |
Phoneutria nigriventer; Proteomics; Transcriptomics. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/189100/1/AP-Overview-Mudadu.pdf
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Marc: |
LEADER 02800naa a2200301 a 4500
001 2102272
005 2020-12-30
008 2018 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1371/journal. pone.0200628$2DOI
100 1 $aDINIZ, M. R. V.
245 $aAn overview of Phoneutria nigriventer spider venom using combined transcriptomic and proteomic approaches.$h[electronic resource]
260 $c2018
500 $aArtigo e0200628. Na publicação: Mauricio A. Mudadu.
520 $aAbstract. Phoneutria nigriventer is one of the largest existing true spiders and one of the few considered medically relevant. Its venom contains several neurotoxic peptides that act on different ion channels and chemical receptors of vertebrates and invertebrates. Some of these venom toxins have been shown as promising models for pharmaceutical or biotechnological use. However, the large diversity and the predominance of low molecular weight toxins in this venom have hampered the identification and deep investigation of the less abundant toxins and the proteins with high molecular weight. Here, we combined conventional and next-generation cDNA sequencing with Multidimensional Protein Identification Technology (MudPIT), to obtain an in-depth panorama of the composition of P. nigriventer spider venom. The results from these three approaches showed that cysteine-rich peptide toxins are the most abundant components in this venom and most of them contain the Inhibitor Cysteine Knot (ICK) structural motif. Ninety-eight sequences corresponding to cysteine-rich peptide toxins were identified by the three methodologies and many of them were considered as putative novel toxins, due to the low similarity to previously described toxins. Furthermore, using next-generation sequencing we identified families of several other classes of toxins, including CAPs (Cysteine Rich Secretory ProteinÐCRiSP, antigen 5 and Pathogenesis-Related 1ÐPR-1), serine proteinases, TCTPs (translationally controlled tumor proteins), proteinase inhibitors, metalloproteinases and hyaluronidases, which have been poorly described for this venom. This study provides an overview of the molecular diversity of P. nigriventer venom, revealing several novel components and providing a better basis to understand its toxicity and pharmacological activities.
650 $aPhoneutria nigriventer
650 $aProteomics
650 $aTranscriptomics
653 $aProteômica
653 $aTranscriptoma
700 1 $aPAIVA, A. L. B.
700 1 $aGUERRA-DUARTE, C.
700 1 $aNISHIYAMA JÚNIOR, M. Y.
700 1 $aMUDADU, M. de A.
700 1 $aOLIVEIRA, U. de
700 1 $aBORGES, M. H.
700 1 $aYATES, J. R.
700 1 $aJUNQUEIRA-DE-AZEVEDO, I. de
773 $tPlos One$gv. 13, n. 8, p. 1-29, 2018.
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