2026-10-13T09:09:03Z https://api.figshare.com/v2/oai

oai:figshare.com:article/34027518 2026-09-29T20:01:59Z category_4 category_13 category_14 category_873 category_46 category_734 category_64 portal_5 item_type_1 month_year_09_2026

<p>Computational and experimental evidence supporting activation of the FABP5–NF-κB signaling axis.</p> Rui An (636731) Shibing Hou (2288815) Min Hong (279203) Jiaorong Zhen (23973891) Zhijuan Wang (1900771) Haoming Huang (12791303) Weixuan Zhao (12058148) Mianmian Liao (10916520) Weiqu Yuan (23973893) Danping Huang (196661) Biochemistry Genetics Molecular Biology Chemical Sciences not elsewhere classified Immunology Biological Sciences not elsewhere classified Cancer xlink "> tcga predicted worse survival independent prognostic factor experimental validation confirmed nf -&# 954 epithelial &# 8211 protein &# 8211 xlink "> fabp5 fabp5 correlated positively immune checkpoint profiles higher tide scores b &# 945 b &# 8211 b pathway genes identify potential fabp5 characterize fabp5 expression duplicate md simulations fabp5 drives pd hcc cell proliferation &# 954 tide scores b pathway therapeutic potential protein docking decreased expression cell rna promising fabp5 fabp5 shapes fabp5 regulates fabp5 knockdown vitro assays targeting compound significantly upregulated seq datasets related pathways regulatory role molecular dynamics molecular docking mesenchymal transition lipid metabolism l1 via l1 upregulation l1 axis immunosuppressive microenvironment <p>(A–C) Representative top-ranked protein–protein docking conformations of FABP5 with IκBα (A), IKKβ (B), and P65 (RelA) (C). (D) RMSD profiles from MD simulations showing that the FABP5–IκBα and FABP5–P65 complexes reached equilibrium after ~80 ns, whereas the FABP5–IKKβ complex exhibited reduced stability. (E) Rg analysis demonstrating stable global compactness of the FABP5–IκBα, FABP5-IKKβ and FABP5–P65 complexes during MD simulations. (F) SASA analysis showing mild fluctuations for the FABP5–IκBα and FABP5-IKKβ complex and minimal variation for the FABP5–P65 complex. (G) Hydrogen bond analysis illustrating persistent intermolecular hydrogen bonding between FABP5 and NF-κB pathway proteins, with a higher average number observed in the FABP5–P65 complex. (H) RMSF analysis indicating limited residue-level flexibility and high structural stability of the FABP5–IκBα and FABP5–P65 complexes. (I) Residue free energy decomposition identifying key amino acid residues contributing to stabilization of the FABP5–IκBα and FABP5–P65 complexes. (J) Western blot analysis showing that FABP5 overexpression increased phosphorylation of IκBα (p-IκBα) and PD-L1 expression in HCC cells, while NF-κB inhibition by Bay 11–7082 abolished these effects.</p> 2026-09-29T20:01:47Z Image Figure 10.1371/journal.pone.0356359.g008 https://figshare.com/articles/figure/_p_Computational_and_experimental_evidence_supporting_activation_of_the_FABP5_NF-_B_signaling_axis_p_/34027518 CC BY 4.0