PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20615204-2 2010 This novel in vivo cleavable disulfide linker, based on a dithiocyclopeptide containing a thrombin-sensitive sequence and an intramolecular disulfide bond, was inserted between transferrin and granulocyte colony-stimulating factor (G-CSF) recombinant fusion protein domains. Disulfides 29-38 transferrin Homo sapiens 177-188 20615204-2 2010 This novel in vivo cleavable disulfide linker, based on a dithiocyclopeptide containing a thrombin-sensitive sequence and an intramolecular disulfide bond, was inserted between transferrin and granulocyte colony-stimulating factor (G-CSF) recombinant fusion protein domains. Disulfides 140-149 transferrin Homo sapiens 177-188 20013338-1 2010 Although the fission yeast Schizosaccharomyces pombe has been used for high-level heterologous protein production, the productivity of secreted human serum transferrin (hTF) has been low, presumably, because the protein harbors twenty disulfide bonds and two N-glycosylation sites. Disulfides 235-244 transferrin Homo sapiens 156-167 20219242-2 2010 In this paper, biotinylated transferrin/avidin/biotinylated disulfide containing PEI bioconjugates (TABP-SS) mediated p53 gene delivery system was formed attributed to the "avidin-biotin bridge". Disulfides 60-69 transferrin Homo sapiens 28-39 10945247-2 2000 The transferrin molecule, with a molecular mass of about 80 kDa, is folded into two similarly sized homologous N- and C-lobes that are stabilized by many intrachain disulfides. Disulfides 165-175 transferrin Homo sapiens 4-15 19454248-2 2009 This report describes a process that rapidly and reproducibly precipitates high-abundance disulfide-rich proteins, including albumin and transferrin, from serum and plasma. Disulfides 90-99 transferrin Homo sapiens 137-148 12781465-1 2003 Mass spectrometry, proteomics, and protein chemistry methods are used to characterize the cleavage products of 79 kDa transferrin proteins induced by iron-catalyzed oxidation, including a novel C-terminal polypeptide released upon disulfide reduction. Disulfides 231-240 transferrin Homo sapiens 118-129 12781465-3 2003 Incubation of transferrin with reductants, such as dithiothreitol (DTT) or tris(2-carboxyethyl)-phosphine (TCEP), yields an increase in multiple charging observed by ESI-MS and an increase in molecular weight consistent with disulfide reduction. Disulfides 225-234 transferrin Homo sapiens 14-25 12781465-5 2003 Protein acetylation and MS/MS sequencing demonstrate that the fragment originates from the C-terminus of the protein, and that it is a separate polypeptide linked via three disulfide bonds to the main transferrin chain. Disulfides 173-182 transferrin Homo sapiens 201-212 12651115-2 2003 Obtaining the C-terminal lobe of human transferrin in verified native conformation has been problematic, possibly because its 11 disulfide bonds lead to misfolding when the lobe is expressed without its accompanying N-lobe. Disulfides 129-138 transferrin Homo sapiens 39-50 1632491-1 1992 Polylysine has been covalently bound to human transferrin in a 1:1 molar ratio over a disulfide bond that can be easily split by reducing agents such as dithiothreitol. Disulfides 86-95 transferrin Homo sapiens 46-57 10933939-4 2000 Transferrin (Tf) was conjugated with PNA via a reversible disulfide bond using N-succinimidyl-3-(2-pyridyldithio)propionate. Disulfides 58-67 transferrin Homo sapiens 0-11 10933939-4 2000 Transferrin (Tf) was conjugated with PNA via a reversible disulfide bond using N-succinimidyl-3-(2-pyridyldithio)propionate. Disulfides 58-67 transferrin Homo sapiens 13-15 10411467-4 1999 The obtained thiolated p(DMAEMA-co-AEMA) was conjugated to transferrin (Tf) or the F(ab") fragment of mAb 323/A3 via a disulfide linkage. Disulfides 119-128 transferrin Homo sapiens 59-70 10411467-4 1999 The obtained thiolated p(DMAEMA-co-AEMA) was conjugated to transferrin (Tf) or the F(ab") fragment of mAb 323/A3 via a disulfide linkage. Disulfides 119-128 transferrin Homo sapiens 72-74 9312001-6 1997 When the folding of transferrin in microsomes was analyzed, UDP-glucose enhanced the amount of folded transferrin and reduced the disulfide-linked aggregates. Disulfides 130-139 transferrin Homo sapiens 20-31 8961144-1 1996 Insulin, acylated with dimethylmaleic anhydride, was conjugated to transferrin (Tf) via a disulfide linkage. Disulfides 90-99 transferrin Homo sapiens 67-78 8961144-1 1996 Insulin, acylated with dimethylmaleic anhydride, was conjugated to transferrin (Tf) via a disulfide linkage. Disulfides 90-99 transferrin Homo sapiens 80-82 8824263-2 1996 Transferrin was linked to PE via a disulfide bond. Disulfides 35-44 transferrin Homo sapiens 0-11 2792501-3 1989 The chicken transferrin receptor was shown to be a 190,000 dalton cell surface membrane molecule consisting of two similar disulfide-bonded subunits of approximately 95,000 daltons. Disulfides 123-132 transferrin Homo sapiens 12-23 1721638-4 1991 We coupled [125I]tyrosine to 131I-alpha 2-macroglobulin or [131I] transferrin via a reducible disulfide linker. Disulfides 94-103 transferrin Homo sapiens 66-77 1906465-2 1991 The nascent transferrin receptor containing core-glycosylated asparagine-linked oligosaccharides does not possess complete intersubunit disulfide bonds, sediments predominantly as a monomer in sucrose density gradients, and shows reduced binding to transferrin-agarose. Disulfides 136-145 transferrin Homo sapiens 12-23 2126013-3 1990 Diferric-transferrin was conjugated to biotin via a cleavable disulfide bond and iodinated. Disulfides 62-71 transferrin Homo sapiens 9-20 2333290-3 1990 Human transferrin, as well as the chicken homologue conalbumin, has been covalently linked to the small DNA-binding protein protamine or to polylysines of various sizes through a disulfide linkage. Disulfides 179-188 transferrin Homo sapiens 6-17 2507316-1 1989 The human transferrin receptor is expressed as a disulfide-linked dimer at the cell surface. Disulfides 49-58 transferrin Homo sapiens 10-21 3047122-8 1988 About 30% of human transferrin receptors made in insect cells do not form intermolecular disulfide bonds, but are recognized by the anti-transferrin receptor antibody, B3/25, and bind specifically to a human transferrin-Sepharose column. Disulfides 89-98 transferrin Homo sapiens 19-30 2647146-2 1989 A disulfide derivative of phosphatidylethanolamine containing a reactive N-hydroxysuccinimide ester group is synthesized, and the derivative is reacted with serum transferrin in deoxycholate-containing buffer. Disulfides 2-11 transferrin Homo sapiens 163-174 2647146-3 1989 Disulfide-linked transferrin-phosphatidylethanolamine conjugates containing up to 6 mol phospholipid/mol protein are prepared. Disulfides 0-9 transferrin Homo sapiens 17-28 2647146-7 1989 Using the disulfide linker to release transferrin from the liposomes, evidence is presented for a function of the phosphatidylethanolamine as an anchor-molecule into the liposomal lipid. Disulfides 10-19 transferrin Homo sapiens 38-49 3245844-1 1988 Rabbit serum transferrin is isolated by a procedure designed to preserve its conformation and disulfide linkages. Disulfides 94-103 transferrin Homo sapiens 13-24 3367540-8 1988 The proposed model of circulating transferrin receptor may be the nicked dimers of 55,000 daltons in which inter- and intra-disulfide bridges were present. Disulfides 124-133 transferrin Homo sapiens 34-45 3179277-7 1988 The location of the 19 disulfide bridges is described, and their possible structural roles are discussed in relation to the transferrin family of proteins. Disulfides 23-32 transferrin Homo sapiens 124-135 3276306-0 1988 Monensin is obligatory for the cytotoxic action of a disulfide linked methotrexate-anti-transferrin receptor conjugate. Disulfides 53-62 transferrin Homo sapiens 88-99 3276306-1 1988 Methotrexate (MTX) in the form of a gamma-cysteinylglycine derivative was disulfide linked to a monoclonal antibody reactive with the human transferrin receptor to give an antibody-MTX conjugate (anti-TfR-MTX). Disulfides 74-83 transferrin Homo sapiens 140-151 3500356-1 1987 An immunoconjugate was prepared containing a disulfide linker between a murine monoclonal antibody (5E9), which recognized the human transferrin receptor, and the ribosome-inactivating protein gelonin. Disulfides 45-54 transferrin Homo sapiens 133-144 3327411-1 1987 Ricin A chain, a potent ribosomal poison, was disulfide linked either to the iron transport protein, transferrin, or to anti-transferrin receptor antibodies to produce highly specific derivative toxins, Tf-A and TfR-A, respectively. Disulfides 46-55 transferrin Homo sapiens 101-112 3582362-0 1987 Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid-attachment site. Disulfides 37-46 transferrin Homo sapiens 66-77 3582362-1 1987 Structural studies of the human transferrin receptor have shown that the molecule is a disulfide-bonded dimer consisting of two identical subunits (Mr = 95,000) which are post-translationally modified by the addition of a fatty acyl moiety. Disulfides 87-96 transferrin Homo sapiens 32-43 3534892-6 1986 Preliminary analysis indicated that, unlike the human receptor, the plasmodial transferrin receptor is not a disulfide linked dimer but a single polypeptide acylated via 1,2-diacyl-sn-glycerol. Disulfides 109-118 transferrin Homo sapiens 79-90 2419904-8 1986 Conservation of disulfide bridges and of amino acids thought to compose the iron binding pockets suggests that p97 is also related to transferrin in tertiary structure and function. Disulfides 16-25 transferrin Homo sapiens 134-145 2984291-7 1985 Comparison of the sequence with that of the human transferrin receptor shows a high degree of conservation of the sequences surrounding and penetrating the membrane, including cysteine residues that may be involved in interchain disulfide bonding and/or covalent attachment of lipid. Disulfides 229-238 transferrin Homo sapiens 50-61 6319379-1 1984 The toxic A chain of ricin was linked to human transferrin via a disulfide bond and the resulting conjugate was shown to bind to cell membrane transferrin receptors. Disulfides 65-74 transferrin Homo sapiens 47-58 6086661-4 1984 Transferrin receptors from uninduced and differentiating cells were partially purified by affinity chromatography on transferrin-Sepharose and shown to be disulfide-bridged homodimers of a polypeptide with an apparent molecular weight of approximately 90,000. Disulfides 155-164 transferrin Homo sapiens 0-11 6319379-1 1984 The toxic A chain of ricin was linked to human transferrin via a disulfide bond and the resulting conjugate was shown to bind to cell membrane transferrin receptors. Disulfides 65-74 transferrin Homo sapiens 143-154 28653773-4 2017 Thiol-functionalized transferrin (Tf-SH) is anchored onto the surface of MoS2 nanosheets by the formation of disulfide bonds, which could further enhance the cellular uptake of DOX and MoS2 to HepG2 cells for high-efficiency synergetic therapy. Disulfides 109-118 transferrin Homo sapiens 21-32 32686399-0 2020 Tagging Transferrin Receptor with a Disulfide FRET Probe to Gauge the Redox State in Endosomal Compartments. Disulfides 36-45 transferrin Homo sapiens 8-19 29902373-5 2018 The 4 disulfide bonds of lysozyme and the 19 disulfide bonds of serotransferrin were characterized through LC/UVPD-MS analysis of nonreduced and partially reduced protein digests. Disulfides 45-54 transferrin Homo sapiens 64-79 29649293-4 2018 Cytochrome c and transferrin were cross-linked with a redox sensitive disulfide bond for the intra-cellular release of the protein upon endocytosis by the transferrin receptor. Disulfides 70-79 transferrin Homo sapiens 17-28 29649293-4 2018 Cytochrome c and transferrin were cross-linked with a redox sensitive disulfide bond for the intra-cellular release of the protein upon endocytosis by the transferrin receptor. Disulfides 70-79 transferrin Homo sapiens 155-166 28088015-2 2017 In this system, transferrin (Tf), a naturally existing protein, is grafted on the surfaces of MSNs via redox-cleavable disulfide bonds, serving as both a capping agent and a targeting ligand simultaneously. Disulfides 119-128 transferrin Homo sapiens 16-27 28088015-2 2017 In this system, transferrin (Tf), a naturally existing protein, is grafted on the surfaces of MSNs via redox-cleavable disulfide bonds, serving as both a capping agent and a targeting ligand simultaneously. Disulfides 119-128 transferrin Homo sapiens 29-31 27223606-5 2016 Nanobioconjugates made of low molecular weight polyethylenimine (LMW-PEI) and transferrin (Tf) were synthesized to contain a bioreducible disulfide bond. Disulfides 138-147 transferrin Homo sapiens 78-89 25716754-0 2015 Identification of reduction-susceptible disulfide bonds in transferrin by differential alkylation using O(16)/O(18) labeled iodoacetic acid. Disulfides 40-49 transferrin Homo sapiens 59-70 25716754-7 2015 Application of this method to a cysteine-rich protein transferrin allows the majority of its native disulfide bonds to be measured for their reduction susceptibility, which appears to reflect both solvent accessibility and bond strain energy. Disulfides 100-109 transferrin Homo sapiens 54-65 24820935-4 2014 In this work, the dissociation of disulfide-linked peptide dimers produced by peptic digestion of the 80 kDa glycoprotein transferrin in the course of HDX MS experiments is carried out using electron capture dissociation (ECD). Disulfides 34-43 transferrin Homo sapiens 122-133