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DC Field | Value | Language |
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dc.contributor.author | Park, M. H. | - |
dc.contributor.author | Nishimura, K. | - |
dc.contributor.author | Zanelli, Cleslei Fernando | - |
dc.contributor.author | Valentini, Sandro Roberto | - |
dc.date.accessioned | 2014-05-20T13:24:14Z | - |
dc.date.accessioned | 2016-10-25T16:44:57Z | - |
dc.date.available | 2014-05-20T13:24:14Z | - |
dc.date.available | 2016-10-25T16:44:57Z | - |
dc.date.issued | 2010-02-01 | - |
dc.identifier | http://dx.doi.org/10.1007/s00726-009-0408-7 | - |
dc.identifier.citation | Amino Acids. New York: Springer, v. 38, n. 2, p. 491-500, 2010. | - |
dc.identifier.issn | 0939-4451 | - |
dc.identifier.uri | http://hdl.handle.net/11449/7456 | - |
dc.identifier.uri | http://acervodigital.unesp.br/handle/11449/7456 | - |
dc.description.abstract | The unusual basic amino acid, hypusine [N(epsilon)-(4-amino-2-hydroxybutyl)-lysine], is a modified lysine with the addition of the 4-aminobutyl moiety from the polyamine spermidine. This naturally occurring amino acid is a product of a unique posttranslational modification that occurs in only one cellular protein, eukaryotic translation initiation factor 5A (eIF5A, eIF-5A). Hypusine is synthesized exclusively in this protein by two sequential enzymatic steps involving deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). The deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, and eIF5A, DHS and DOHH are highly conserved suggesting a vital cellular function of eIF5A. Gene disruption and mutation studies in yeast and higher eukaryotes have provided valuable information on the essential nature of eIF5A and the deoxyhypusine/hypusine modification in cell growth and in protein synthesis. In view of the extraordinary specificity and functional significance of hypusine-containing eIF5A in mammalian cell proliferation, eIF5A and the hypusine biosynthetic enzymes are novel potential targets for intervention in aberrant cell proliferation. | en |
dc.description.sponsorship | Intramural Research Program of National Institute of Dental and Craniofacial Research (NIDCR) | - |
dc.description.sponsorship | NIH | - |
dc.description.sponsorship | Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) | - |
dc.description.sponsorship | KANAE Foundation | - |
dc.format.extent | 491-500 | - |
dc.language.iso | eng | - |
dc.publisher | Springer | - |
dc.source | Web of Science | - |
dc.subject | Hypusine | en |
dc.subject | eIF5A | en |
dc.subject | Posttranslational modification | en |
dc.subject | Polyamine | en |
dc.subject | Deoxyhypusine synthase | en |
dc.subject | Deoxyhypusine hydroxylase | en |
dc.subject | Gene inactivation | en |
dc.title | Functional significance of eIF5A and its hypusine modification in eukaryotes | en |
dc.type | outro | - |
dc.contributor.institution | Natl Inst Dent & Craniofacial Res | - |
dc.contributor.institution | Universidade Estadual Paulista (UNESP) | - |
dc.description.affiliation | Natl Inst Dent & Craniofacial Res, Oral & Pharyngeal Canc Branch, NIH, Bethesda, MD 20892 USA | - |
dc.description.affiliation | São Paulo State Univ, Sch Pharmaceut Sci, Dept Biol Sci, Araraquara, Brazil | - |
dc.description.affiliationUnesp | São Paulo State Univ, Sch Pharmaceut Sci, Dept Biol Sci, Araraquara, Brazil | - |
dc.identifier.doi | 10.1007/s00726-009-0408-7 | - |
dc.identifier.wos | WOS:000274384100015 | - |
dc.rights.accessRights | Acesso restrito | - |
dc.relation.ispartof | Amino Acids | - |
Appears in Collections: | Artigos, TCCs, Teses e Dissertações da Unesp |
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