title: Inhibition of polymerase activity by pristine fullerene nanoparticles can be mitigated by abundant proteins.
abstract: Pristine fullerene nanoparticles are capable of adsorbing polymerase and significantly inhibiting its biologically important replication activity; however, the inhibition can be partially mitigated by abundant proteins through competitive binding.
authors.affiliation: State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing, 100085, China.
authors.forename: Song
authors.initials: S
authors.lastname: Maoyong
authors.forename: Jiang
authors.initials: J
authors.lastname: Guibin
authors.forename: Yin
authors.initials: Y
authors.lastname: Junfa
authors.forename: Wang
authors.initials: W
authors.lastname: Hailin
mesh_terms: D001667:Binding, Competitive; D004247:DNA / Q000378:metabolism; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D005456:Fluorescent Dyes / Q000737:chemistry*; D037741:Fullerenes / Q000737:chemistry*; D006801:Humans; D053758:Nanoparticles / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism
chemical_list: D005456:Fluorescent Dyes; D037741:Fullerenes; D011506:Proteins; D012709:Serum Albumin; C530172:pristine (C60); D004247:DNA; D004259:DNA-Directed DNA Polymerase