PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23793566-0 2013 Transferrin-conjugated, fluorescein-loaded magnetic nanoparticles for targeted delivery across the blood-brain barrier. Fluorescein 24-35 transferrin Homo sapiens 0-11 23793566-3 2013 In this study, transferrin (Tf) was employed as a brain targeting ligand to functionalize the fluorescein-loaded magnetic nanoparticles (FMNs). Fluorescein 94-105 transferrin Homo sapiens 15-26 7913709-2 1994 Receptors were labeled with fluorescein-conjugated transferrin (FITC-Tf). Fluorescein 28-39 transferrin Homo sapiens 51-62 10962683-3 2000 Fluorescein lumbar puncture is useful in establishing the exact site of a leak and also in confirming the absence of a leak where the clinical suspicion is high but the beta-2-transferrin is negative. Fluorescein 0-11 transferrin Homo sapiens 176-187 9743595-11 1998 Transport experiments involving fluorescein-transferrin also showed that A549 monolayers were polarized, with a greater amount of intracellular transferrin being transported out of the basolateral side of the cells. Fluorescein 32-43 transferrin Homo sapiens 44-55 19441364-4 2009 Since fluorescein-labeled transferrin-Fe3+ complex exhibited fluorescence changes at lower pH, these three protein complexes covered wide pH-responsive ranges. Fluorescein 6-17 transferrin Homo sapiens 26-37 16478976-3 2006 In cultured PTCs, [(125)I]Tyr-labeled ANG II and fluorescein labeled-ANG II were internalized in a time-dependent manner and colocalized with the endosome marker Alexa Fluor 594-transferrin. Fluorescein 49-60 transferrin Homo sapiens 178-189 12473103-10 2002 The Yb3+-transferrin complex inhibited the uptake of the fluorescein labeled ferric-saturated transferrin (Fe2-transferrin) complex into K562 cells. Fluorescein 57-68 transferrin Homo sapiens 9-20 12473103-10 2002 The Yb3+-transferrin complex inhibited the uptake of the fluorescein labeled ferric-saturated transferrin (Fe2-transferrin) complex into K562 cells. Fluorescein 57-68 transferrin Homo sapiens 94-105 12473103-10 2002 The Yb3+-transferrin complex inhibited the uptake of the fluorescein labeled ferric-saturated transferrin (Fe2-transferrin) complex into K562 cells. Fluorescein 57-68 transferrin Homo sapiens 94-105 3019336-1 1986 Flow cytometry was used to follow the uptake and release of fluorescein-conjugated ferro-transferrin by CCRF-CEM human T - leukaemia cells on an individual cell basis. Fluorescein 60-71 transferrin Homo sapiens 89-100 1577771-8 1992 The involvement of TRF receptors was shown by flow cytometry experiments in which native TRF inhibited binding of fluorescein-labeled TRF-ADR conjugates. Fluorescein 114-125 transferrin Homo sapiens 19-22 1577771-8 1992 The involvement of TRF receptors was shown by flow cytometry experiments in which native TRF inhibited binding of fluorescein-labeled TRF-ADR conjugates. Fluorescein 114-125 transferrin Homo sapiens 89-92 1577771-8 1992 The involvement of TRF receptors was shown by flow cytometry experiments in which native TRF inhibited binding of fluorescein-labeled TRF-ADR conjugates. Fluorescein 114-125 transferrin Homo sapiens 89-92 3408816-3 1988 Here we report that radio- and fluorescein-labelled TF binds to a single class of high-affinity binding sites on MO but not on mo. Fluorescein 31-42 transferrin Homo sapiens 52-54 3051285-8 1988 In addition both fluorescein tests are used for the diagnosis depending on the result of the beta 2-transferrin identification and further measures. Fluorescein 17-28 transferrin Homo sapiens 100-111 2894318-4 1988 Fluorescein-labeled transferrin (Tr-FITC) was observed in the same region when added to the cells simultaneously with EGF-Rh. Fluorescein 0-11 transferrin Homo sapiens 20-31 8424669-6 1993 The binding of TRF-ADR conjugates was determined to be saturable, and competition experiments done with both radioiodinated and fluorescein-labeled TRF-ADR conjugates demonstrated dose-dependent inhibition of conjugate binding by unlabeled TRF, indicating that TRF-ADR conjugates were bound by TRF receptors. Fluorescein 128-139 transferrin Homo sapiens 15-18 8424669-6 1993 The binding of TRF-ADR conjugates was determined to be saturable, and competition experiments done with both radioiodinated and fluorescein-labeled TRF-ADR conjugates demonstrated dose-dependent inhibition of conjugate binding by unlabeled TRF, indicating that TRF-ADR conjugates were bound by TRF receptors. Fluorescein 128-139 transferrin Homo sapiens 148-151 8424669-6 1993 The binding of TRF-ADR conjugates was determined to be saturable, and competition experiments done with both radioiodinated and fluorescein-labeled TRF-ADR conjugates demonstrated dose-dependent inhibition of conjugate binding by unlabeled TRF, indicating that TRF-ADR conjugates were bound by TRF receptors. Fluorescein 128-139 transferrin Homo sapiens 148-151 8424669-6 1993 The binding of TRF-ADR conjugates was determined to be saturable, and competition experiments done with both radioiodinated and fluorescein-labeled TRF-ADR conjugates demonstrated dose-dependent inhibition of conjugate binding by unlabeled TRF, indicating that TRF-ADR conjugates were bound by TRF receptors. Fluorescein 128-139 transferrin Homo sapiens 148-151 8424669-6 1993 The binding of TRF-ADR conjugates was determined to be saturable, and competition experiments done with both radioiodinated and fluorescein-labeled TRF-ADR conjugates demonstrated dose-dependent inhibition of conjugate binding by unlabeled TRF, indicating that TRF-ADR conjugates were bound by TRF receptors. Fluorescein 128-139 transferrin Homo sapiens 148-151 2297227-1 1990 Treatment of two human leukemia cell lines with 1.25% dimethyl sulfoxide at 37 degrees C results in a rapid increase in the number of transferrin receptors on the cell surface detected by fluorescein-labeled anti-transferrin receptor antibodies. Fluorescein 188-199 transferrin Homo sapiens 134-145 2297227-1 1990 Treatment of two human leukemia cell lines with 1.25% dimethyl sulfoxide at 37 degrees C results in a rapid increase in the number of transferrin receptors on the cell surface detected by fluorescein-labeled anti-transferrin receptor antibodies. Fluorescein 188-199 transferrin Homo sapiens 213-224 2995416-1 1985 We have studied the process of transferrin endocytosis in human erythromyeloid cell line K562 using fluorescein (FL) and rhodamine (RD) labeled iron-saturated transferrin (FeTF), and a fluorescein labeled monoclonal antibody to the transferrin receptor (FL-mAB). Fluorescein 100-111 transferrin Homo sapiens 31-42 2995416-1 1985 We have studied the process of transferrin endocytosis in human erythromyeloid cell line K562 using fluorescein (FL) and rhodamine (RD) labeled iron-saturated transferrin (FeTF), and a fluorescein labeled monoclonal antibody to the transferrin receptor (FL-mAB). Fluorescein 185-196 transferrin Homo sapiens 31-42 6292894-3 1982 After endocytosis, transferrin becomes transiently lodged within an acidic compartment inside the cell, as judged by the changed spectral characteristics and quantum yield of fluorescein isothiocyanate-labeled transferrin that is cell-associated at 37 degrees C. Upon binding to transferrin, anti-fluorescein antibody strongly quenches the emission of the fluorescein-labeled residues on the protein and is used to assess whether the transferrin is at the cell surface (incubation at 0 degrees C) or mainly internalized into the cell (incubation at 37 degrees C). Fluorescein 175-186 transferrin Homo sapiens 19-30 6292894-3 1982 After endocytosis, transferrin becomes transiently lodged within an acidic compartment inside the cell, as judged by the changed spectral characteristics and quantum yield of fluorescein isothiocyanate-labeled transferrin that is cell-associated at 37 degrees C. Upon binding to transferrin, anti-fluorescein antibody strongly quenches the emission of the fluorescein-labeled residues on the protein and is used to assess whether the transferrin is at the cell surface (incubation at 0 degrees C) or mainly internalized into the cell (incubation at 37 degrees C). Fluorescein 175-186 transferrin Homo sapiens 210-221 6292894-3 1982 After endocytosis, transferrin becomes transiently lodged within an acidic compartment inside the cell, as judged by the changed spectral characteristics and quantum yield of fluorescein isothiocyanate-labeled transferrin that is cell-associated at 37 degrees C. Upon binding to transferrin, anti-fluorescein antibody strongly quenches the emission of the fluorescein-labeled residues on the protein and is used to assess whether the transferrin is at the cell surface (incubation at 0 degrees C) or mainly internalized into the cell (incubation at 37 degrees C). Fluorescein 175-186 transferrin Homo sapiens 210-221 6292894-3 1982 After endocytosis, transferrin becomes transiently lodged within an acidic compartment inside the cell, as judged by the changed spectral characteristics and quantum yield of fluorescein isothiocyanate-labeled transferrin that is cell-associated at 37 degrees C. Upon binding to transferrin, anti-fluorescein antibody strongly quenches the emission of the fluorescein-labeled residues on the protein and is used to assess whether the transferrin is at the cell surface (incubation at 0 degrees C) or mainly internalized into the cell (incubation at 37 degrees C). Fluorescein 175-186 transferrin Homo sapiens 210-221 6292894-3 1982 After endocytosis, transferrin becomes transiently lodged within an acidic compartment inside the cell, as judged by the changed spectral characteristics and quantum yield of fluorescein isothiocyanate-labeled transferrin that is cell-associated at 37 degrees C. Upon binding to transferrin, anti-fluorescein antibody strongly quenches the emission of the fluorescein-labeled residues on the protein and is used to assess whether the transferrin is at the cell surface (incubation at 0 degrees C) or mainly internalized into the cell (incubation at 37 degrees C). Fluorescein 297-308 transferrin Homo sapiens 19-30 6292894-3 1982 After endocytosis, transferrin becomes transiently lodged within an acidic compartment inside the cell, as judged by the changed spectral characteristics and quantum yield of fluorescein isothiocyanate-labeled transferrin that is cell-associated at 37 degrees C. Upon binding to transferrin, anti-fluorescein antibody strongly quenches the emission of the fluorescein-labeled residues on the protein and is used to assess whether the transferrin is at the cell surface (incubation at 0 degrees C) or mainly internalized into the cell (incubation at 37 degrees C). Fluorescein 297-308 transferrin Homo sapiens 210-221 6292894-3 1982 After endocytosis, transferrin becomes transiently lodged within an acidic compartment inside the cell, as judged by the changed spectral characteristics and quantum yield of fluorescein isothiocyanate-labeled transferrin that is cell-associated at 37 degrees C. Upon binding to transferrin, anti-fluorescein antibody strongly quenches the emission of the fluorescein-labeled residues on the protein and is used to assess whether the transferrin is at the cell surface (incubation at 0 degrees C) or mainly internalized into the cell (incubation at 37 degrees C). Fluorescein 297-308 transferrin Homo sapiens 210-221 6292894-3 1982 After endocytosis, transferrin becomes transiently lodged within an acidic compartment inside the cell, as judged by the changed spectral characteristics and quantum yield of fluorescein isothiocyanate-labeled transferrin that is cell-associated at 37 degrees C. Upon binding to transferrin, anti-fluorescein antibody strongly quenches the emission of the fluorescein-labeled residues on the protein and is used to assess whether the transferrin is at the cell surface (incubation at 0 degrees C) or mainly internalized into the cell (incubation at 37 degrees C). Fluorescein 297-308 transferrin Homo sapiens 210-221