Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

In vivo analysis of the acidic ribosomal proteins BmP1 and BmP2 of the silkworm Bombyx mori in the yeast Saccharomyces cerevisiae.

Gene - 15 Feb 2007

Koumarianou Petrina, Marcos Alberto Garcia, Ballesta Juan P G, Kouyanou-Koutsoukou Sophia

Abstract excerpt

In the silkworm Bombyx mori the ribosomal stalk P-protein family consists of two low MW acidic proteins, BmP1 and BmP2, and of one higher MW protein, BmP0, as shown by electrophoretical and immunoblotting western blot analysis of purified ribosomes. Treatment of ribosomes with alkaline phosphatase followed by electrofocusing shifted the isoelectric points to higher pH, implying phosphorylation of the proteins....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bombyx
Share to Genetic Complementation Test

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoblotting

Share to Insect Proteins

Share to Ovarian Follicle

Share to Ribosomal Proteins

Share to Ribosomes

Share to Transformation, Genetic

Source

Identifiers

PMID: 17134850
DOI: 10.1016/j.gene.2006.09.017

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

In vivo analysis of the acidic ribosomal proteins BmP1 and BmP2 of the silkworm Bombyx mori in the yeast Saccharomyces cerevisiae.PMID 17134850Read ↗

Protein BmP0 from the silkworm Bombyx mori can be assembled and is functional in the Saccharomyces cerevisiae ribosomal stalk in the absence of the acidic P1 and P2 proteins.Semantic proximity Read ↗

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

High yield exogenous protein HPL production in the Bombyx mori silk gland provides novel insight into recombinant expression systems.Semantic proximity Read ↗

Ras1(CA) overexpression in the posterior silk gland improves silk yield.Semantic proximity Read ↗

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

Proteomic analysis of the phenotype of the scaleless wings mutant in the silkworm, Bombyx mori.Semantic proximity Read ↗

The β4 Integrin Interactor p27BBP/eIF6 Is an Essential Nuclear Matrix Protein Involved in 60S Ribosomal Subunit AssemblySemantic proximity Read ↗

Bmpali, Bmb1 and Bmcap are necessary for uric acid granule formation in Bombyx mori.Semantic proximity Read ↗

Genetic analysis and transcriptome analysis of the mini mutant of the silkworm, Bombyx mori.Semantic proximity Read ↗

Characterization of the carotenoid-binding protein of the Y-gene dominant mutants of Bombyx mori.Semantic proximity Read ↗

Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins.Semantic proximity Read ↗

Expression and identification of mutated osteoprotegerin in culture cells and larvae of silkworm.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.