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http://acervodigital.unesp.br/handle/11449/19907
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DC Field | Value | Language |
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dc.contributor.author | de Azevedo, W. F. | - |
dc.contributor.author | Canduri, F. | - |
dc.contributor.author | dos Santos, D. M. | - |
dc.contributor.author | Pereira, J. H. | - |
dc.contributor.author | Dias, MVB | - |
dc.contributor.author | Silva, R. G. | - |
dc.contributor.author | Mendes, M. A. | - |
dc.contributor.author | Basso, L. A. | - |
dc.contributor.author | Palma, Mario Sergio | - |
dc.contributor.author | Santosce, D. S. | - |
dc.date.accessioned | 2014-05-20T13:55:37Z | - |
dc.date.accessioned | 2016-10-25T17:05:18Z | - |
dc.date.available | 2014-05-20T13:55:37Z | - |
dc.date.available | 2016-10-25T17:05:18Z | - |
dc.date.issued | 2003-10-03 | - |
dc.identifier | http://dx.doi.org/10.1016/j.bbrc.2003.08.094 | - |
dc.identifier.citation | Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 309, n. 4, p. 917-922, 2003. | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | http://hdl.handle.net/11449/19907 | - |
dc.identifier.uri | http://acervodigital.unesp.br/handle/11449/19907 | - |
dc.description.abstract | Purine nucleoside phosphorylase (PNP) catalyzes the phosphorolysis of the N-ribosidic bonds of purine nucleosides and deoxynucleosides. PNP is a target for inhibitor development aiming at T-cell immune response modulation. This work reports on the crystallographic study of the complex of human PNP-immucillin-H (HsPNP-ImmH) solved at 2.6 Angstrom resolution using synchrotron radiation. Immucillin-H (ImmH) inhibits the growth of malignant T-cell lines in the presence of deoxyguanosine without affecting non-T-cell tumor lines. ImmH inhibits activated normal human T cells after antigenic stimulation in vitro. These biological effects of ImmH suggest that this agent may have utility in the treatment of certain human diseases characterized by abnormal T-cell growth or activation. This is the first structural report of human PNP complexed with immucillin-H. The comparison of the complex HsPNP-ImmH with recent crystallographic structures of human PNP explains the high specificity of immucillin-H for human PNP. (C) 2003 Elsevier B.V. All rights reserved. | en |
dc.format.extent | 917-922 | - |
dc.language.iso | eng | - |
dc.publisher | Elsevier B.V. | - |
dc.source | Web of Science | - |
dc.subject | PNP | pt |
dc.subject | synchrotron radiation | pt |
dc.subject | Structure | pt |
dc.subject | immucillin-H | pt |
dc.subject | drug design | pt |
dc.title | Structural basis for inhibition of human PNP by immucillin-H | en |
dc.type | outro | - |
dc.contributor.institution | Universidade Estadual Paulista (UNESP) | - |
dc.contributor.institution | Instituto Butantan | - |
dc.contributor.institution | Universidade Federal do Rio Grande do Sul (UFRGS) | - |
dc.contributor.institution | Pontificia Univ Catolica Rio Grande Sul | - |
dc.description.affiliation | UNESP, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil | - |
dc.description.affiliation | Inst Butantan, Ctr Appl Toxinol, BR-05503900 São Paulo, Brazil | - |
dc.description.affiliation | UFRGS, Dept Biol Mol & Biotecnol, Rede Brasileira Pesquisas TB, BR-91501970 Porto Alegre, RS, Brazil | - |
dc.description.affiliation | UNESP, Inst Biosci, Dept Biol, CEIS,Lab Struct Biol & Zoochem, BR-13506900 Rio Claro, SP, Brazil | - |
dc.description.affiliation | Pontificia Univ Catolica Rio Grande Sul, Inst Pesquisas Biomed, Fac Farm, Porto Alegre, RS, Brazil | - |
dc.description.affiliationUnesp | UNESP, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil | - |
dc.description.affiliationUnesp | UNESP, Inst Biosci, Dept Biol, CEIS,Lab Struct Biol & Zoochem, BR-13506900 Rio Claro, SP, Brazil | - |
dc.identifier.doi | 10.1016/j.bbrc.2003.08.094 | - |
dc.identifier.wos | WOS:000185774300032 | - |
dc.rights.accessRights | Acesso restrito | - |
dc.relation.ispartof | Biochemical and Biophysical Research Communications | - |
Appears in Collections: | Artigos, TCCs, Teses e Dissertações da Unesp |
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