Solution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalk

By Lee Ka-Ming  

Nucleic Acids Research, Vol. 38, Iss. 15, 2010-08 ,pp. : 5206-5216

Oxford University Press

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The ribosomal P-proteins of the medfly Ceratitis capitata form a heterogeneous stalk structure interacting with the endogenous P-proteins, in conditional P0-null strains of the yeast Saccharomyces cerevisiae

By Gagou Mary Elizabeth   Gabriel M. A. Rodriguez   Ballesta Juan P. G.   Kouyanou Sophia  

Nucleic Acids Research, Vol. 28, Iss. 3, 2000-02 ,pp. : 736-743

Oxford University Press

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Interaction among silkworm ribosomal proteins P1, P2 and P0 required for functional protein binding to the GTPase-associated domain of 28S rRNA

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Nucleic Acids Research, Vol. 30, Iss. 12, 2002-06 ,pp. : 2620-2627

Oxford University Press

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The C‐terminal silencing domain of Rap1p is essential for the repression of ribosomal protein genes in response to a defect in the secretory pathway

By Mizuta Keiko  

Nucleic Acids Research, Vol. 26, Iss. 4, 1998-02 ,pp. : 1063-1069

Oxford University Press

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The amino terminal domain from Mrt4 protein can functionally replace the RNA binding domain of the ribosomal P0 protein

By Rodríguez-Mateos María  

Nucleic Acids Research, Vol. 37, Iss. 11, 2009-06 ,pp. : 3514-3521

Oxford University Press

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