Proteomics

Dataset Information

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Entamoeba histolytica nuclear proteome


ABSTRACT: The polyadenylation factor EhCFIm25 has been recently reported as a biochemical target in Entamoeba histolytica. The prediction and experimental characterization of its interactome revealed close relationships between proteins involved in gene expression regulation and enzymes of energy metabolism. Here, the identification of the nuclear proteome of E. histolytica by mass spectrometry analysis showed the presence of typically cytoplasmic proteins in the nuclear compartment, which could have moonlight functions. Prediction of PPI network confirmed the relevance of some metabolic enzymes in the coordination between energy and RNA metabolism, opening new perspectives for human amoebiasis control.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Entamoeba Histolytica Hm-1:imss-a

SUBMITTER: Rodolfo G Avila-Bonilla  

LAB HEAD: Laurence A. Marchat

PROVIDER: PXD056950 | Pride | 2025-06-09

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20211216_810_Nucl_A.raw.zip Raw
20211216_810_Nucl_A_IA_final_peptide.csv Csv
20211216_810_Nucl_A_IA_final_protein.csv Csv
20211216_811_Nucl_B.raw.zip Raw
20211216_811_Nucl_B_IA_final_peptide.csv Csv
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Publications

A network of RNA-binding and metabolic proteins evidenced in the Entamoeba histolytica nuclear proteome.

Avila-Bonilla Rodolfo Gamaliel RG   Velázquez Guzmán Jorge A JA   Ramírez-Moreno Esther E   Marchat Laurence A LA  

Experimental parasitology 20250528


Amoebiasis caused by the protozoan parasite Entamoeba histolytica is a serious leading cause of parasite-related death worldwide and there is a need for developing new safe and efficient control methods. The nuclear polyadenylation factor EhCFIm25 has been recently reported as a biochemical target in E. histolytica, being necessary for proliferation and parasite virulence. Interestingly, the prediction and experimental characterization of EhCFIm25 interactome revealed close relationships between  ...[more]

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