PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34746605-3 2021 Recently, GenX has been shown to have an impact on several disease-related proteins in humans, and just like PFOS, it binds to human protein human serum albumin (HSA). perfluorooctane sulfonic acid 109-113 albumin Homo sapiens 147-160 32423201-0 2020 Interactions of perfluorooctanesulfonate (PFOS) and 6:2 chlorinated polyfluorinated ether sulfonate (6:2 Cl-PFESA) with human serum albumin (HSA): A comparative study. perfluorooctane sulfonic acid 16-40 albumin Homo sapiens 126-139 32423201-0 2020 Interactions of perfluorooctanesulfonate (PFOS) and 6:2 chlorinated polyfluorinated ether sulfonate (6:2 Cl-PFESA) with human serum albumin (HSA): A comparative study. perfluorooctane sulfonic acid 42-46 albumin Homo sapiens 126-139 32423201-3 2020 Here, the binding characteristics of PFOS and 6:2 Cl-PFESA to human serum albumin (HSA) were explored based on in vitro and in silico methods. perfluorooctane sulfonic acid 37-41 albumin Homo sapiens 68-81 19239717-0 2009 Binding of PFOS to serum albumin and DNA: insight into the molecular toxicity of perfluorochemicals. perfluorooctane sulfonic acid 11-15 albumin Homo sapiens 19-32 32066055-6 2020 In silico evaluation of the binding affinity of 1m-PFOS to human serum albumin (HSA) showed that the two 1m-PFOS enantiomers enantioselectively interacted with the HSA. perfluorooctane sulfonic acid 51-55 albumin Homo sapiens 65-78 32066055-6 2020 In silico evaluation of the binding affinity of 1m-PFOS to human serum albumin (HSA) showed that the two 1m-PFOS enantiomers enantioselectively interacted with the HSA. perfluorooctane sulfonic acid 108-112 albumin Homo sapiens 65-78 22482699-0 2012 Structural evidence of perfluorooctane sulfonate transport by human serum albumin. perfluorooctane sulfonic acid 23-48 albumin Homo sapiens 68-81 22482699-3 2012 PFOS was found mainly bound to human serum albumin (HSA) in plasma, the most abundant protein in human blood plasma, which transports a variety of endogenous and exogenous ligands. perfluorooctane sulfonic acid 0-4 albumin Homo sapiens 37-50 21028884-1 2010 Structure and energies of the binding sites of perfluorooctanoic acid (PFOA) and perfluorooctane sulfonate (PFOS) to human serum albumin (HSA) were determined through molecular modeling. perfluorooctane sulfonic acid 81-106 albumin Homo sapiens 123-136 21028884-1 2010 Structure and energies of the binding sites of perfluorooctanoic acid (PFOA) and perfluorooctane sulfonate (PFOS) to human serum albumin (HSA) were determined through molecular modeling. perfluorooctane sulfonic acid 108-112 albumin Homo sapiens 123-136 32109724-0 2020 Albumin is the major carrier protein for PFOS, PFOA, PFHxS, PFNA and PFDA in human plasma. perfluorooctane sulfonic acid 41-45 albumin Homo sapiens 0-7 32109724-7 2020 Although the data are based on a small sample, they clearly show that albumin is the most important carrier protein for PFOS, PFOA, PFHxS, PFNA and PFDA in native human plasma. perfluorooctane sulfonic acid 120-124 albumin Homo sapiens 70-77 21028884-0 2010 Determination of energies and sites of binding of PFOA and PFOS to human serum albumin. perfluorooctane sulfonic acid 59-63 albumin Homo sapiens 73-86 19239717-3 2009 In this work, the non-covalent interactions between perfluorooctane sulfonate (PFOS) and serum albumin (SA) and DNA were investigated under normal physiological conditions, aiming to elucidate the toxigenicity of PFCs. perfluorooctane sulfonic acid 52-77 albumin Homo sapiens 89-102 19239717-3 2009 In this work, the non-covalent interactions between perfluorooctane sulfonate (PFOS) and serum albumin (SA) and DNA were investigated under normal physiological conditions, aiming to elucidate the toxigenicity of PFCs. perfluorooctane sulfonic acid 79-83 albumin Homo sapiens 89-102