Nop18p, an essential nucleolar protein, is involved in the late steps of pre-rRNA processing in Saccharomyces cerevisiae (2005)
- Authors:
- Autor USP: OLIVEIRA, CARLA COLUMBANO DE - IQ
- Unidade: IQ
- Subjects: SACCHAROMYCES; RNA; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Programas e Resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
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ABNT
GRANATO, Daniela C. et al. Nop18p, an essential nucleolar protein, is involved in the late steps of pre-rRNA processing in Saccharomyces cerevisiae. 2005, Anais.. São Paulo: SBBq, 2005. . Acesso em: 18 abr. 2024. -
APA
Granato, D. C., Gonzales, F. A., Luz, J. S. da, & Oliveira, C. C. de. (2005). Nop18p, an essential nucleolar protein, is involved in the late steps of pre-rRNA processing in Saccharomyces cerevisiae. In Programas e Resumos. São Paulo: SBBq. -
NLM
Granato DC, Gonzales FA, Luz JS da, Oliveira CC de. Nop18p, an essential nucleolar protein, is involved in the late steps of pre-rRNA processing in Saccharomyces cerevisiae. Programas e Resumos. 2005 ;[citado 2024 abr. 18 ] -
Vancouver
Granato DC, Gonzales FA, Luz JS da, Oliveira CC de. Nop18p, an essential nucleolar protein, is involved in the late steps of pre-rRNA processing in Saccharomyces cerevisiae. Programas e Resumos. 2005 ;[citado 2024 abr. 18 ] - Characterization of the function of the Saccharomyces cerevisiae exosome subunit RRP43 in mRNA degradation
- Structural and functional analysis of Nip7p, a conserved protein involved in Pre-rRNA processing
- Functional characterization of the S. cerevisiae nucleolar protein Nop8
- Utp25p, a nucleolar Saccharomyces cerevisiae protein, interacts with U3 snoRNP subunits and affects processing of the 35S pre-rRNA
- The essential nucleolar yeast protein NOP8P controls the exosome function during 60S ribosomal subunit maturation
- Identification of proteins co-purifying with the yeast RNA exosome and their effect on the complex stabilization
- Regulation of the expression of the exosome catalytic subunit Rrp6 by a nucleolar protein
- Studies of protein interactions and stability of Sdo1p
- Determination of the functional role of the interaction between the R2TP subunit Nop17 and the Fe/S cluster protein Dre2 in Saccharomyces cerevisiae
- Isolation of Saccharomyces cerevisiae mutants deficient in mRNA 3' end processing
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