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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/714
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dc.contributor.authorDelatorre, P.-
dc.contributor.authorOlivieri, JR-
dc.contributor.authorNeto, JR-
dc.contributor.authorLorenzi, CCB-
dc.contributor.authorCanduri, F.-
dc.contributor.authorFadel, V-
dc.contributor.authorKonno, K.-
dc.contributor.authorPalma, Mario Sergio-
dc.contributor.authorYamane, T.-
dc.contributor.authorde Azevedo, W. F.-
dc.date.accessioned2014-05-20T13:12:47Z-
dc.date.accessioned2016-10-25T16:33:23Z-
dc.date.available2014-05-20T13:12:47Z-
dc.date.available2016-10-25T16:33:23Z-
dc.date.issued2001-02-09-
dc.identifierhttp://dx.doi.org/10.1016/S0167-4838(00)00192-8-
dc.identifier.citationBiochimica Et Biophysica Acta-protein Structure and Molecular Enzymology. Amsterdam: Elsevier B.V., v. 1545, n. 1-2, p. 372-376, 2001.-
dc.identifier.issn0167-4838-
dc.identifier.urihttp://hdl.handle.net/11449/714-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/714-
dc.description.abstractMastoparans are tetradecapeptides found to be the major component of vespid venoms. These peptides present a wide spectrum of biological activities, such as mast cell degranulation, hemolytic activity and also reveals antimicrobial activity. A mastoparan toxin isolated from the venom of Anterhynchium flavomarginatum micado has been crystallized. At room temperature these crystals diffracted to 2.8 Angstrom resolution. However, upon cooling to cryogenic temperature around 85 K, the original resolution limit could be improved to 2.0 Angstrom. Crystals were determined to belong to the space group P3(1) (P3(2)). This is the first mastoparan to be crystallized and it will provide further insights in the conformational significance of mastoparan toxins, with respect to their potency and activity in G protein regulation. (C) 3001 Elsevier B.V. B.V. All rights reserved.en
dc.format.extent372-376-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectmastoparanpt
dc.subjectcryocrystallographypt
dc.subjectsynchrotronpt
dc.subjectwasppt
dc.titlePreliminary cryocrystallography analysis of an eumenine mastoparan toxin isolated from the venom of the wasp Anterhynchium flavomarginatum micadoen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionInstituto Butantan-
dc.contributor.institutionFEB-
dc.contributor.institutionCtr Univ Votuporanga-
dc.description.affiliationUNESP, IBILCE, Dept Fis, BR-15054000 Sao Jose Rio Preto, SP, Brazil-
dc.description.affiliationUNESP, Inst Biosci Rio Claro, CEIS, BR-13506900 Rio Claro, SP, Brazil-
dc.description.affiliationInstituto Butantan, Div Mol Toxinol, São Paulo, Brazil-
dc.description.affiliationFEB, Faciba, Dept Fis, BR-14783226 Barretos, SP, Brazil-
dc.description.affiliationCtr Univ Votuporanga, BR-15500030 Votuporanga, SP, Brazil-
dc.description.affiliationUnespUNESP, IBILCE, Dept Fis, BR-15054000 Sao Jose Rio Preto, SP, Brazil-
dc.description.affiliationUnespUNESP, Inst Biosci Rio Claro, CEIS, BR-13506900 Rio Claro, SP, Brazil-
dc.identifier.doi10.1016/S0167-4838(00)00192-8-
dc.identifier.wosWOS:000167072700038-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofBiochimica Et Biophysica Acta-protein Structure and Molecular Enzymology-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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