Base de dados : LILACS
Pesquisa : D03.633.100.759.646.138.124.070.125 [Categoria DeCS]
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Id: lil-491538
Autor: Ergen, K; Bektas, M; Gõkçe, S; Nurten, R.
Título: Endogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment
Fonte: Biocell;31(1):61-66, abr. 2007. ilus.
Idioma: en.
Resumo: Eukaryotic elongation factor 2 (eEF-2) can undergo ADP-ribosylation in the absence of diphtheria toxin. The binding of free ADP-ribose and endogenous transferase-dependent ADP-ribosylation were distinct reactions for eEF-2, as indicated by different findings. Incubation of eEF-2 tryptic fragment 32/33 kDa (32F) with NAD was ADP-ribosylated and gave rise to the covalent binding of ADP-ribose to eEF-2. 32F was revealed to be at the C-terminal by Edman degradation sequence analysis. In our study, the elution of 32F from SDS-PAGE was ADP-ribosylated both in the presence and absence of diphtheria toxin. These results suggest that endogenous ADP-ribosylation of 32F might be related to protein synthesis. This modification appears to be important for the cell function.
Descritores: ADP Ribose Transferases
Adenosina Difosfato Ribose/metabolismo
Glicosilação
Toxinas Bacterianas/metabolismo
-FACTOR TEMEFOS DE ELONGACION PEPTIDICA
Fragmentos de Peptídeos/metabolismo
Limites: Animais
Ratos
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: AR40.1 - Biblioteca de la Facultad de Ciencias Médicas de la UNCuyo


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Id: lil-308280
Autor: Chini, E. N.
Título: Interactions between intracellular Ca2+ stores: Ca2+ released from the NAADP pool potentiates cADPR-induced Ca2+ release
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;35(5):543-547, May 2002. ilus, graf.
Idioma: en.
Resumo: Cells possess multiple intracellular Ca2+-releasing systems. Sea urchin egg homogenates are a well-established model to study intracellular Ca2+ release. In the present study the mechanism of interaction between three intracellular Ca2+ pools, namely the nicotinic acid adenine dinucleotide phosphate (NAADP), the cyclic ADP-ribose (cADPR) and the inositol 1',4',5'-trisphosphate (IP3)-regulated Ca2+ stores, is explored. The data indicate that the NAADP Ca2+ pool could be used to sensitize the cADPR system. In contrast, the IP3 pool was not affected by the Ca2+ released by NAADP. The mechanism of potentiation of the cADPR-induced Ca2+ release, promoted by Ca2+ released from the NAADP pool, is mediated by the mechanism of Ca2+-induced Ca2+ release. These data raise the possibility that the NAADP Ca2+ store may have a role as a regulator of the cellular sensitivity to cADPR
Descritores: Adenosina Difosfato Ribose
Cálcio
NADP
Óvulo
-Inositol 1,4,5-Trifosfato
NADP
Ouriços-do-Mar
Limites: Animais
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


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Id: lil-28421
Autor: Ortega, J. M; Meneghini, R.
Título: Rearrangement of mammalian chromatic structure following excision repair: absence of an effect of inhibitors of poly (ADP-ribose) polymerase and topoisomerase
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;18(4):455-64, Apr. 1985. tab.
Idioma: en.
Descritores: Adenosina Difosfato Ribose/metabolismo
Benzamidas/farmacologia
Cromatina/ultraestrutura
Nuclease do Micrococo/metabolismo
Novobiocina/farmacologia
Reparo do DNA
-Reparo do DNA/efeitos dos fármacos
Reparo do DNA/efeitos da radiação
Fatores de Tempo
Raios Ultravioleta
Limites: Humanos
Responsável: BR1.1 - BIREME



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