PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25717100-6 2015 Targeting mucin disulfide cross-links using current thiol-amino structures such as N-acetylcysteine (NAC) requires high drug concentrations to have mucolytic effects. Disulfides 16-25 LOC100508689 Homo sapiens 10-15 21338337-1 2011 The colonic human MUC2 mucin forms a polymeric gel by covalent disulfide bonds in its N- and C-termini. Disulfides 63-72 LOC100508689 Homo sapiens 23-28 14749330-11 2004 These data indicate that this oligomeric mucin follows a similar assembly to the von Willebrand factor glycoprotein to yield long linear disulfide-linked chains. Disulfides 137-146 LOC100508689 Homo sapiens 41-46 16787389-2 2006 We expressed the C-terminal cysteine-rich part of the human MUC5AC mucin in CHO-K1 cells (Chinese-hamster ovary K1 cells) where it formed disulfide-linked dimers in the ER (endoplasmic reticulum). Disulfides 138-147 LOC100508689 Homo sapiens 67-72 16029046-8 2005 Alternatively, thiol-decorated (nonderivatized) micelles are prepared and show improved mucoadhesion through the formation of disulfide bonds with mucin. Disulfides 126-135 LOC100508689 Homo sapiens 147-152 10824861-4 1999 The results of our experiments suggest that the released proteins can be a part of mucin molecule, cleaved by proteolysis and reduction of disulfide bridges. Disulfides 139-148 LOC100508689 Homo sapiens 83-88 10713099-1 2000 P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded, homodimeric mucin ( approximately 250 kDa) on leukocytes that binds to P-selectin on platelets and endothelial cells during the initial steps in inflammation. Disulfides 47-56 LOC100508689 Homo sapiens 77-82 10820757-0 2000 Mucin domains to explore disulfide-dependent dimer formation. Disulfides 25-34 LOC100508689 Homo sapiens 0-5 9852122-6 1998 The roles of the half-cystines in the CGLCG motifs in the assembly of disulfide-bonded multimers of mucin were also assessed. Disulfides 70-79 LOC100508689 Homo sapiens 100-105 9852122-13 1998 It is possible that these motifs in mucins are engaged in the thiol-disulfide interchange reactions during the assembly of disulfide-bonded multimers of mucin. Disulfides 68-77 LOC100508689 Homo sapiens 36-41 9852122-13 1998 It is possible that these motifs in mucins are engaged in the thiol-disulfide interchange reactions during the assembly of disulfide-bonded multimers of mucin. Disulfides 123-132 LOC100508689 Homo sapiens 36-41 9603957-0 1998 Porcine submaxillary mucin forms disulfide-linked multimers through its amino-terminal D-domains. Disulfides 33-42 LOC100508689 Homo sapiens 21-26 9668062-10 1998 This insoluble MUC2 mucin was recovered by immunoprecipitation after reduction of disulfide bonds. Disulfides 82-91 LOC100508689 Homo sapiens 20-25 9603957-8 1998 Coexpression in the same cells of the amino-terminal region and the disulfide-rich carboxyl-terminal domain of the mucin showed that these structures were not disulfide-linked with one another. Disulfides 68-77 LOC100508689 Homo sapiens 115-120 9603957-9 1998 Cells expressing a DNA construct encoding a fusion protein between the amino- and carboxyl-terminal regions of the mucin secreted disulfide-linked dimeric and high molecular weight multimeric species of the recombinant mucin. Disulfides 130-139 LOC100508689 Homo sapiens 115-120 9603957-9 1998 Cells expressing a DNA construct encoding a fusion protein between the amino- and carboxyl-terminal regions of the mucin secreted disulfide-linked dimeric and high molecular weight multimeric species of the recombinant mucin. Disulfides 130-139 LOC100508689 Homo sapiens 219-224 9603957-11 1998 These studies suggest that disulfide-linked dimers of mucin are subsequently assembled into disulfide-linked multimers by the amino-terminal regions. Disulfides 27-36 LOC100508689 Homo sapiens 54-59 9603957-11 1998 These studies suggest that disulfide-linked dimers of mucin are subsequently assembled into disulfide-linked multimers by the amino-terminal regions. Disulfides 92-101 LOC100508689 Homo sapiens 54-59 9603957-12 1998 They also suggest that the porcine mucin forms branched disulfide-linked multimers. Disulfides 56-65 LOC100508689 Homo sapiens 35-40 9603957-13 1998 This ability of the amino-terminal region of mucin to aid in the assembly of multimers is consistent with its amino acid identities to the amino-terminal region of human von Willebrand factor, which also serves to form disulfide-linked multimers of this protein. Disulfides 219-228 LOC100508689 Homo sapiens 45-50 8621668-0 1996 Porcine submaxillary mucin forms disulfide-bonded dimers between its carboxyl-terminal domains. Disulfides 33-42 LOC100508689 Homo sapiens 21-26 8621668-1 1996 COS-7 cells transfected with three different expression vectors encoding the 240-amino acid residue, disulfide-rich domain at the carboxyl terminus of porcine submaxillary mucin have been used to determine the possible function of the domain in forming higher oligomers of the mucin polypeptide chain. Disulfides 101-110 LOC100508689 Homo sapiens 172-177 8621668-9 1996 These studies suggest that the disulfide-rich domain acts to form dimers of the polypeptide chain of mucin. Disulfides 31-40 LOC100508689 Homo sapiens 101-106 1400449-8 1992 Both cysteine-rich subdomains of this mucin have sequence similarity with von Willebrand factor, a serum protein that exists as a disulfide-linked polymer. Disulfides 130-139 LOC100508689 Homo sapiens 38-43 7512537-6 1994 Treatment of the mucin antigen by heating, reduction of disulfide bonds, or protease digestion abolished immunoreactivity with PAM4. Disulfides 56-65 LOC100508689 Homo sapiens 17-22 1892325-5 1991 Reduction not only cleaves the mucin molecule but opens, presumably by breaking intramolecular disulfide bonds, cryptic "naked" protein regions. Disulfides 95-104 LOC100508689 Homo sapiens 31-36 1612175-6 1992 The results provide evidence that the 150 kDa glycopeptide so-called salivary mucin "link" component is neither an integral part of the mucin molecule, nor linked to mucin subunits by disulfide bonds, but is a fibronectin fragment which associates with mucin. Disulfides 184-193 LOC100508689 Homo sapiens 78-83 2265202-0 1990 Polymeric structure of human respiratory mucin: studies on two protein components released upon reduction of disulfide bonds. Disulfides 109-118 LOC100508689 Homo sapiens 41-46 2265202-13 1990 These observations suggest that the availability of high-affinity probe binding sites upon reduction of mucin disulfide bonds may be either due to binding of the probe to the released component(s) and/or due to noncovalent interaction of the released component(s) with the mucin causing a conformational change in the mucin structure. Disulfides 110-119 LOC100508689 Homo sapiens 104-109 2265202-13 1990 These observations suggest that the availability of high-affinity probe binding sites upon reduction of mucin disulfide bonds may be either due to binding of the probe to the released component(s) and/or due to noncovalent interaction of the released component(s) with the mucin causing a conformational change in the mucin structure. Disulfides 110-119 LOC100508689 Homo sapiens 273-278 2265202-13 1990 These observations suggest that the availability of high-affinity probe binding sites upon reduction of mucin disulfide bonds may be either due to binding of the probe to the released component(s) and/or due to noncovalent interaction of the released component(s) with the mucin causing a conformational change in the mucin structure. Disulfides 110-119 LOC100508689 Homo sapiens 273-278 2393862-7 1990 Since the Mr 70,000 molecule appears to be associated with the breast mucin by disulfide bonds, its study could help elucidate the structure of this latter complex and how it is organized in the cell membrane, and prove useful in diagnosis and therapy of breast cancer. Disulfides 79-88 LOC100508689 Homo sapiens 70-75 2775758-2 1989 Reduction of disulfide linkages released mucin subunits together with an associated protein(s) of approximately 140 kDa. Disulfides 13-22 LOC100508689 Homo sapiens 41-46 34274401-8 2021 The presence of disulfide linkages and thiol groups were shown to favor improved binding of cross-linked nanogels to mucin. Disulfides 16-25 LOC100508689 Homo sapiens 117-122 2692565-0 1989 Human milk-fat globule membrane derived mucin is a disulfide-linked heteromer. Disulfides 51-60 LOC100508689 Homo sapiens 40-45 2692565-4 1989 Immunoprecipitation of the mucin and analysis of the precipitated material using Western blots and identification of transferred material with monoclonal antibodies demonstrated that the MW 70,000 protein and the mucin were co-precipitated and linked by reducible disulfide bonds. Disulfides 264-273 LOC100508689 Homo sapiens 213-218 6324613-2 1984 The free thiol is a mucolytic compound which acts via the reduction of disulfide bonds of mucin molecules. Disulfides 71-80 LOC100508689 Homo sapiens 90-95 6276531-6 1982 When incubated with whole sputum or with purified mucin solutions in vitro, MDP decreased the viscosity of these solutions by reduction of the accessible disulfide bonds of the mucin molecule and was subsequently found in mixed disulfide association with the mucin molecule. Disulfides 154-163 LOC100508689 Homo sapiens 50-55 6276531-6 1982 When incubated with whole sputum or with purified mucin solutions in vitro, MDP decreased the viscosity of these solutions by reduction of the accessible disulfide bonds of the mucin molecule and was subsequently found in mixed disulfide association with the mucin molecule. Disulfides 154-163 LOC100508689 Homo sapiens 177-182 6276531-6 1982 When incubated with whole sputum or with purified mucin solutions in vitro, MDP decreased the viscosity of these solutions by reduction of the accessible disulfide bonds of the mucin molecule and was subsequently found in mixed disulfide association with the mucin molecule. Disulfides 154-163 LOC100508689 Homo sapiens 177-182 4857118-0 1974 Direct spectrophotometric determination of mucin disulfide linkages. Disulfides 49-58 LOC100508689 Homo sapiens 43-48 7251591-4 1981 Disulfide reducing agents reduce the viscosity of concentrated mucin solutions by dissociation of soluble mucin aggregates without affecting the insoluble aggregates. Disulfides 0-9 LOC100508689 Homo sapiens 63-68 7251591-4 1981 Disulfide reducing agents reduce the viscosity of concentrated mucin solutions by dissociation of soluble mucin aggregates without affecting the insoluble aggregates. Disulfides 0-9 LOC100508689 Homo sapiens 106-111 7251591-5 1981 Detailed chemical analyses of the mucins have been carried out and indicate that the reduction of interchain disulfides is accompanied, not only by a reduction in mucin viscosity, but by the liberation of two small proteins from the large mucin molecule. Disulfides 109-119 LOC100508689 Homo sapiens 34-39 7251591-5 1981 Detailed chemical analyses of the mucins have been carried out and indicate that the reduction of interchain disulfides is accompanied, not only by a reduction in mucin viscosity, but by the liberation of two small proteins from the large mucin molecule. Disulfides 109-119 LOC100508689 Homo sapiens 163-168 33431872-3 2021 Biophysical properties of mucus are controlled by mucin glycoproteins that polymerize covalently via disulfide bonds. Disulfides 101-110 LOC100508689 Homo sapiens 50-55 33431872-5 2021 Here we show that reducing mucin disulfide bonds disrupts mucus in human asthmatics and reverses pathological effects of mucus hypersecretion in a mouse allergic asthma model. Disulfides 33-42 LOC100508689 Homo sapiens 27-32 31651920-0 2019 A rational approach to form disulfide linked mucin hydrogels. Disulfides 28-37 LOC100508689 Homo sapiens 45-50 31651920-2 2019 By using a cross-linking reagent capable of forming hydrogen bonds and disulfide linkages within the gel network, we were able to produce mucin-based hydrogels with viscoelastic properties similar to natural mucus as measured by bulk rheology. Disulfides 71-80 LOC100508689 Homo sapiens 138-143 31651920-3 2019 We confirmed disulfide cross-links strongly contribute to gel formation in our system using chemical treatments to block and reduce cysteines where we found mucin hydrogel network formation was inhibited and disrupted, respectively. Disulfides 13-22 LOC100508689 Homo sapiens 157-162 29643478-0 2018 Mucin gel assembly is controlled by a collective action of non-mucin proteins, disulfide bridges, Ca2+-mediated links, and hydrogen bonding. Disulfides 79-88 LOC100508689 Homo sapiens 0-5