(Q41819101)

English

P1 and P2 protein heterodimer binding to the P0 protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity

scientific article published on 24 January 2012

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

P1 and P2 protein heterodimer binding to the P0 protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity (English)

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

Saccharomyces cerevisiae

1 reference

based on heuristic

inferred from title

author name string

David Cárdenas

1

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

Jesús Revuelta-Cervantes

2

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

Antonio Jiménez-Díaz

3

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

Hendricka Camargo

4

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

Miguel Remacha

5

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

Juan P G Ballesta

6

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

publication date

24 January 2012

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

Nucleic Acids Research

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

40

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

10

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

4520-4529

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

copyright license

Creative Commons Attribution-NonCommercial 3.0 Unported

7 November 2016

1 reference

April 2022 Public Data File from Crossref

copyright status

0 references

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1 reference

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The amino terminal end determines the stability and assembling capacity of eukaryotic ribosomal stalk proteins P1 and P2.

1 reference

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

1 reference

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The ribosomal stalk plays a key role in IF2-mediated association of the ribosomal subunits

1 reference

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Biophysical properties of the eukaryotic ribosomal stalk

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Yeast ribosomal stalk heterogeneity in vivo shown by two-photon FCS and molecular brightness analysis

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A mode of assembly of P0, P1, and P2 proteins at the GTPase-associated center in animal ribosome: in vitro analyses with P0 truncation mutants

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Characterization of the 26S rRNA-binding domain in Saccharomyces cerevisiae ribosomal stalk phosphoprotein P0.

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Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation

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The acidic protein binding site is partially hidden in the free Saccharomyces cerevisiae ribosomal stalk protein P0.

1 reference

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Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation

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Characterization of interaction sites in the Saccharomyces cerevisiae ribosomal stalk components

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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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The acidic ribosomal P proteins

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Ribosomal P-protein stalk function is targeted by sordarin antifungals.

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Binding of mammalian ribosomal protein complex P0.P1.P2 and protein L12 to the GTPase-associated domain of 28 S ribosomal RNA and effect on the accessibility to anti-28 S RNA autoantibody

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The large ribosomal subunit stalk as a regulatory element of the eukaryotic translational machinery.

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Ribosomal protein P0, contrary to phosphoproteins P1 and P2, is required for ribosome activity and Saccharomyces cerevisiae viability

1 reference

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Eukaryotic acidic phosphoproteins interact with the ribosome through their amino-terminal domain.

1 reference

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Ribosomal acidic phosphoproteins P1 and P2 are not required for cell viability but regulate the pattern of protein expression in Saccharomyces cerevisiae

1 reference

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[12] One-step gene disruption in yeast

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1 reference

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1 reference

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Identifiers

10.1093/NAR/GKS036

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 October 2017

ResearchGate publication ID

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