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protein motifs/domains from interpro member databases  (InterPro Inc)

 
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    InterPro Inc protein motifs/domains from interpro member databases
    Protein Motifs/Domains From Interpro Member Databases, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/protein motifs/domains from interpro member databases/product/InterPro Inc
    Average 90 stars, based on 1 article reviews
    protein motifs/domains from interpro member databases - by Bioz Stars, 2026-04
    90/100 stars

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    Proteome-wide survey unveils distinctively different target proteins in lead-sensitive CD4 + T cells and neutrophils. ( A ) Experimental procedures for detection of Pb-induced proteomic changes (PIPC) in CD4 + T cells and neutrophils, and Pb-binding proteins in HEK293 T cell lysate using Cellular Thermal Shift Assay (CETSA). ( B ) Procedure of data analysis of PIPC and CETSA experiment. There are 113 GOMF and INTERPRO terms outstanding in both CETSA (increased thermostability) and PIPC (decreased expression), in either enrichment or GSEA analysis. There are 682 out of 1306 lead-decreased DEPs that belong to CETSA and PIPC double outstanding terms. ( C ) Protein–protein interaction (PPI) network of the 682 DEPs selected in (B). PPI information is based on String database, only interactions with highest confidence (interaction score > 0.9) were selected, proteins not connected to other protein are not shown. Cell type specificity of all DEPs is annotated with colors

    Journal: Cell Biology and Toxicology

    Article Title: Panoramic lead-immune system interactome reveals diversified mechanisms of immunotoxicity upon chronic lead exposure

    doi: 10.1007/s10565-025-10034-6

    Figure Lengend Snippet: Proteome-wide survey unveils distinctively different target proteins in lead-sensitive CD4 + T cells and neutrophils. ( A ) Experimental procedures for detection of Pb-induced proteomic changes (PIPC) in CD4 + T cells and neutrophils, and Pb-binding proteins in HEK293 T cell lysate using Cellular Thermal Shift Assay (CETSA). ( B ) Procedure of data analysis of PIPC and CETSA experiment. There are 113 GOMF and INTERPRO terms outstanding in both CETSA (increased thermostability) and PIPC (decreased expression), in either enrichment or GSEA analysis. There are 682 out of 1306 lead-decreased DEPs that belong to CETSA and PIPC double outstanding terms. ( C ) Protein–protein interaction (PPI) network of the 682 DEPs selected in (B). PPI information is based on String database, only interactions with highest confidence (interaction score > 0.9) were selected, proteins not connected to other protein are not shown. Cell type specificity of all DEPs is annotated with colors

    Article Snippet: Protein domain database InterPro from https://www.ebi.ac.uk/interpro/ .

    Techniques: Binding Assay, Thermal Shift Assay, Expressing

    PKC-like, PE/DAG-binding proteins are potential targets of immune activation retardation in neutrophils upon lead exposure. ( A ) Schematic diagram showing GSH/MRP-mediated sequestration-aided passive transport (SAPT) model and affinity gradient driven ion transfer. ( B ) Protein structure of the PKC-like, PE/DAG-binding domain from RAF1 (6XBH) and PKCD (2YUU). ( C ) Volcano plot of lead-treatment DEPs of INTERPRO term: PKC-like, PE/DAG-binding domain. ( D ) GSEA results of INTERPRO term: PKC-like, PE/DAG-binding domain showing a significantly increased thermostability upon lead in CETSA experiment. ( E ) DEPs degree centrality in KEGG pathways based on String database ( upper, heatmap ). Protein degree and eigenvector centrality across all KEGG pathways ( right ). ( F ) A subgraph of KEGG pathway (Map04660) of DAG activation in immune cells showing the critical position of RAF1, PKC and their downstream MAPK and phosphatidylinositol signaling. ( G ) GSEA analysis showing significantly reduced MAPK signaling in lead treated dHL-60 cells. ( H ) GSEA analysis showing significantly reduced phosphatidylinositol signaling in lead treated dHL-60 cells, and MK571 further enhanced lead-induced suppression on phosphatidylinositol signaling

    Journal: Cell Biology and Toxicology

    Article Title: Panoramic lead-immune system interactome reveals diversified mechanisms of immunotoxicity upon chronic lead exposure

    doi: 10.1007/s10565-025-10034-6

    Figure Lengend Snippet: PKC-like, PE/DAG-binding proteins are potential targets of immune activation retardation in neutrophils upon lead exposure. ( A ) Schematic diagram showing GSH/MRP-mediated sequestration-aided passive transport (SAPT) model and affinity gradient driven ion transfer. ( B ) Protein structure of the PKC-like, PE/DAG-binding domain from RAF1 (6XBH) and PKCD (2YUU). ( C ) Volcano plot of lead-treatment DEPs of INTERPRO term: PKC-like, PE/DAG-binding domain. ( D ) GSEA results of INTERPRO term: PKC-like, PE/DAG-binding domain showing a significantly increased thermostability upon lead in CETSA experiment. ( E ) DEPs degree centrality in KEGG pathways based on String database ( upper, heatmap ). Protein degree and eigenvector centrality across all KEGG pathways ( right ). ( F ) A subgraph of KEGG pathway (Map04660) of DAG activation in immune cells showing the critical position of RAF1, PKC and their downstream MAPK and phosphatidylinositol signaling. ( G ) GSEA analysis showing significantly reduced MAPK signaling in lead treated dHL-60 cells. ( H ) GSEA analysis showing significantly reduced phosphatidylinositol signaling in lead treated dHL-60 cells, and MK571 further enhanced lead-induced suppression on phosphatidylinositol signaling

    Article Snippet: Protein domain database InterPro from https://www.ebi.ac.uk/interpro/ .

    Techniques: Binding Assay, Activation Assay