PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12543492-1 2002 Stereoselective binding of benzodiazepine and coumarin drugs to serum albumin from human and six mammalian species were studied by chiral chromatographic techniques. coumarin 46-54 albumin Homo sapiens 64-77 14733941-1 2004 The microenvironment of the probe coumarin 153 (C-153) in 1% bovine serum albumin (BSA) is more hydrophobic in nature compared to that in pure micelles or protein-surfactant complexes. coumarin 34-42 albumin Homo sapiens 68-81 567809-0 1978 Binding of coumarin anticoagulants to human and bovine serum albumin. coumarin 11-19 albumin Homo sapiens 55-68 11374572-0 2001 Interaction of coumarin derivatives with human serum albumin: investigation by fluorescence spectroscopic technique and modeling studies. coumarin 15-23 albumin Homo sapiens 47-60 10650717-0 1999 Deconvolution of the fluorescence spectra into its component Gaussians: a method to analyze the binding of coumarin to bovine serum albumin. coumarin 107-115 albumin Homo sapiens 126-139 10650717-1 1999 7-N,N-Diethylamino-4-methylcoumarin, (cou-1), a readily available laser dye binding to bovine serum albumin (BSA), at room temperature has been studied by steady state fluorescence spectroscopy. coumarin 27-30 albumin Homo sapiens 94-107 27494219-0 2017 Biophysical influence of coumarin 35 on bovine serum albumin: Spectroscopic study. coumarin 25-33 albumin Homo sapiens 47-60 30776717-2 2019 It was found that the coumarin-maslinic derivative (MaCo) forms an excellent fluorescence resonance energy transfer (FRET) pair with the tryptophan (Trp) residue of human serum albumin (HSA). coumarin 22-30 albumin Homo sapiens 171-184 30776717-2 2019 It was found that the coumarin-maslinic derivative (MaCo) forms an excellent fluorescence resonance energy transfer (FRET) pair with the tryptophan (Trp) residue of human serum albumin (HSA). coumarin 22-30 albumin Homo sapiens 186-189 27494219-1 2017 The binding mechanism and protein-fluorescence probe interactions between bovine serum albumin (BSA) and coumarin 35 (C35) was investigated by using UV-Vis absorption and fluorescence spectroscopies since they remain major research topics in biophysics. coumarin 105-113 albumin Homo sapiens 81-94 24291035-0 2014 Interaction of anticancer reduced Schiff base coumarin derivatives with human serum albumin investigated by fluorescence quenching and molecular modeling. coumarin 46-54 albumin Homo sapiens 84-91 22947088-0 2012 Spectroscopic interaction of a coumarin derivative with bovine serum albumin. coumarin 31-39 albumin Homo sapiens 63-76