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  • Open Access


    Computational and bioinformatics tools for understanding disease mechanisms


    BIOCELL, Vol.48, No.6, pp. 935-944, 2024, DOI:10.32604/biocell.2024.049891

    Abstract Computational methods have significantly transformed biomedical research, offering a comprehensive exploration of disease mechanisms and molecular protein functions. This article reviews a spectrum of computational tools and network analysis databases that play a crucial role in identifying potential interactions and signaling networks contributing to the onset of disease states. The utilization of protein/gene interaction and genetic variation databases, coupled with pathway analysis can facilitate the identification of potential drug targets. By bridging the gap between molecular-level information and disease understanding, this review contributes insights into the impactful utilization of computational methods, paving the way for More >

  • Open Access


    Dephosphorylated mutations affect the protein-protein interactions of ERF in Populus simonii x P. nigra

    Yao SUN, Yao LI, Xin SUN, Qiong WU, Lei WANG*

    BIOCELL, Vol.44, No.1, pp. 117-126, 2020, DOI:10.32604/biocell.2020.08242

    Abstract Phosphorylation is a common type of post-translational modification (PTM). It plays a vital role in many cellular processes. The reversible phosphorylation and dephosphorylation affect protein structures and proteinprotein interactions. Previously, we obtained five proteins that interact with ethylene-responsive factor (ERF) from the cDNA library of Populus simonii x Populus nigra. To further investigate the effect of dephosphorylation of PsnERF on its protein binding ability, we generated different phosphorylation states of PsnERF and demonstrated their protein binding capacity by the yeast two-hybrid assay (Y2H). The secondary structures and 3D structures of PsnERF, ERFm, TrunERF, and psnerf197/198/202a were predicted More >

  • Open Access


    Ultra-stable Biomembrane Force Probe to Characterize Strong Protein-Protein Interactions on a Living Cell

    Chenyi An1, Wei Chen2,*

    Molecular & Cellular Biomechanics, Vol.16, Suppl.2, pp. 109-110, 2019, DOI:10.32604/mcb.2019.07634

    Abstract Biomembrane force probe (BFP) is a single-molecule biomechanical technique that has been widely used to characterize protein dynamics (e.g., protein-protein interactions and protein conformational changes), especially suitable for measuring force-regulated receptor-ligand binding kinetics in situ[1-4]. Integrated with various force spectroscopies, such as lifetime assay, it has become a powerful platform to systematically characterize many force-regulated receptor-ligand dissociation of great biological significance, which cannot be done with traditional solution based assays (e.g., surface plasma resonance) [5].
    Even though the BFP has been quite successful in characterizing binding kinetics of weak and transient molecular interactions, it is… More >

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