PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6517857-8 1984 Together with the "naked" protein segment, the 118 kDa component contained most of the cysteine residues of the native mucin. Cysteine 87-95 LOC100508689 Homo sapiens 119-124 29802217-6 2018 Single MUC5AC and MUC5B apoproteins have molecular masses of >400 kDa, and von Willebrand factor D-like as well as other cysteine-rich domain segments contribute to mucin polymerization and flexibility, thus increasing apoprotein length and complexity. Cysteine 124-132 LOC100508689 Homo sapiens 168-173 30389136-0 2018 Non-C-mannosylable mucin CYS domains hindered proper folding and secretion of mucin. Cysteine 25-28 LOC100508689 Homo sapiens 19-24 30389136-0 2018 Non-C-mannosylable mucin CYS domains hindered proper folding and secretion of mucin. Cysteine 25-28 LOC100508689 Homo sapiens 78-83 30389136-4 2018 We prepared recombinant CYS domains of the human mucin MUC5B with (WXXW AXXW) and without a single amino acid mutation and mini-5B mucins made of a large Ser/Thr/Pro region flanked by two CYS domains with the WXXW motif or with the mutated AXXW motif on the first, second or both CYS domains. Cysteine 24-27 LOC100508689 Homo sapiens 49-54 30389136-5 2018 We found that the single CYS domain and the two CYS domains of mini-5B mucin must be C-mannosylable for the efficient maturation and secretion of the recombinant molecules; otherwise, they are retained in the cell and co-localized with a resident enzyme of the endoplasmic reticulum. Cysteine 25-28 LOC100508689 Homo sapiens 71-76 30389136-5 2018 We found that the single CYS domain and the two CYS domains of mini-5B mucin must be C-mannosylable for the efficient maturation and secretion of the recombinant molecules; otherwise, they are retained in the cell and co-localized with a resident enzyme of the endoplasmic reticulum. Cysteine 48-51 LOC100508689 Homo sapiens 71-76 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. Cysteine 132-141 LOC100508689 Homo sapiens 157-162 22170355-3 2012 Because GSH, skin, hair, mucosal, and mucin proteins are rich in cysteine, we hypothesized that splanchnic extraction and the efficiency of cysteine utilization would be greater in edematous than in nonedematous SAM. Cysteine 65-73 LOC100508689 Homo sapiens 38-43 23359125-4 2013 Using this approach, we have determined that MUC2, the intestinal gel-forming mucin, dimerizes via its C-terminal cysteine-knot domain and also trimerizes via one of the N-terminal von Willebrand D domains. Cysteine 114-122 LOC100508689 Homo sapiens 78-83 22663354-7 2012 All possible peptides from the cysteine-rich regions that interrupt the heavily glycosylated mucin domains were identified. Cysteine 31-39 LOC100508689 Homo sapiens 93-98 30396166-8 2018 Significant pathways including the Mucin type O-glycan biosynthesis pathway, cell cycle pathway and cysteine and methionine metabolism pathway (all P< 0.05) revealed potential roles of the target genes of miR-30d-5p in the oncogenesis of NSCLC. Cysteine 100-108 LOC100508689 Homo sapiens 35-40 21318237-6 2011 The present study was undertaken to determine a detailed structure of the cysteine-rich region within the C-terminal end of human intestinal mucin (MUC2) via homology modeling, and explore possible configurations of a dimer of this cysteine-rich region, which may play an important role in governing mucus gel formation. Cysteine 74-82 LOC100508689 Homo sapiens 141-146 21318237-6 2011 The present study was undertaken to determine a detailed structure of the cysteine-rich region within the C-terminal end of human intestinal mucin (MUC2) via homology modeling, and explore possible configurations of a dimer of this cysteine-rich region, which may play an important role in governing mucus gel formation. Cysteine 232-240 LOC100508689 Homo sapiens 141-146 20332014-9 2010 CONCLUSIONS: Recombinant mucin proteins containing a bivalent display of Cys-rich domains accelerate colon cell migration and inhibit apoptosis, require a full-length intervening Linker-SEA segment for optimal biologic activity, and are functional when synthesized in either E. coli and insect cell systems. Cysteine 73-76 LOC100508689 Homo sapiens 25-30 21112274-5 2010 Model mucins consist of three types of domains: polar (glycosylated central segments), hydrophobic, and cysteine-rich, located at the terminal part of the mucin chains. Cysteine 104-112 LOC100508689 Homo sapiens 6-11 12957634-3 2003 The effect of the disulphide bond breaker cysteine on thiomer-mucin disulphide bonds was monitored by (1) mucoadhesion studies and (2) rheological studies. Cysteine 42-50 LOC100508689 Homo sapiens 62-67 19376250-0 2009 Mucin CYS domains are ancient and highly conserved modules that evolved in concert. Cysteine 6-9 LOC100508689 Homo sapiens 0-5 19376250-1 2009 BACKGROUND: Many large secreted gel-forming mucins contain multiple copies of a "naked" cysteine-enriched domain (CYS domain) that interrupt or are adjacent to mucin domains (Ser/Thr/Pro regions). Cysteine 88-96 LOC100508689 Homo sapiens 44-49 19376250-1 2009 BACKGROUND: Many large secreted gel-forming mucins contain multiple copies of a "naked" cysteine-enriched domain (CYS domain) that interrupt or are adjacent to mucin domains (Ser/Thr/Pro regions). Cysteine 114-117 LOC100508689 Homo sapiens 44-49 19376250-3 2009 These CYS domains are likely implicated in reversible mucin-mucin interactions that play a central role in mucus properties. Cysteine 6-9 LOC100508689 Homo sapiens 54-59 19376250-3 2009 These CYS domains are likely implicated in reversible mucin-mucin interactions that play a central role in mucus properties. Cysteine 6-9 LOC100508689 Homo sapiens 60-65 18167142-0 2008 Mapping of the 45M1 epitope to the C-terminal cysteine-rich part of the human MUC5AC mucin. Cysteine 46-54 LOC100508689 Homo sapiens 85-90 12957634-7 2003 Diffusion studies demonstrated that a 12.8-fold higher concentration of the thiomer (PAA2-Cys) remains in the mucin gel than the corresponding unmodified polymer. Cysteine 90-93 LOC100508689 Homo sapiens 110-115 17910495-3 2007 It has short side chains and low levels of sialic acid residues and includes minute amounts of cysteine residues that, if abundant, can be responsible for the self-polymerization of mucin. Cysteine 95-103 LOC100508689 Homo sapiens 182-187 17101324-0 2006 Cysteine-rich domains of muc3 intestinal mucin promote cell migration, inhibit apoptosis, and accelerate wound healing. Cysteine 0-8 LOC100508689 Homo sapiens 41-46 17101324-1 2006 BACKGROUND & AIMS: Muc3 intestinal mucin contains an extracellular cysteine-rich domain with 2 epidermal growth factor (EGF)-like motifs. Cysteine 71-79 LOC100508689 Homo sapiens 39-44 17101324-16 2006 CONCLUSIONS: The Muc3 mucin cysteine-rich domain plays an active role in epithelial restitution, and represents a potential novel therapeutic agent for intestinal wound healing. Cysteine 28-36 LOC100508689 Homo sapiens 22-27 16787389-0 2006 Cleavage in the GDPH sequence of the C-terminal cysteine-rich part of the human MUC5AC mucin. Cysteine 48-56 LOC100508689 Homo sapiens 87-92 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). Cysteine 28-36 LOC100508689 Homo sapiens 67-72 12957634-5 2003 The addition of cysteine significantly (P<0.01) reduced the adhesion of thiomer tablets to porcine mucosa and G"/G" values of thiomer-mucin mixtures, whereas unthiolated controls were not influenced. Cysteine 16-24 LOC100508689 Homo sapiens 137-142 12554077-6 2003 Evidence for the formation of disulphide bonds between thiolated polymers and mucin could be provided by the addition of free cysteine resulting in strongly decreased mucoadhesion and by viscosity studies showing comparatively higher viscosity of conjugate/mucin mixtures than of unthiolated polymer/mucin mixtures. Cysteine 126-134 LOC100508689 Homo sapiens 78-83 12676567-1 2003 Using degenerate primers designed from conserved cysteine-rich domains of gel-forming mucins, we cloned two new mouse mucin cDNAs. Cysteine 49-57 LOC100508689 Homo sapiens 86-91 9852122-7 1998 Cells with plasmids in which both half-cystines in the motif in the D1- or D3-domain of mucin are replaced by alanine expressed proteins that were poorly secreted, suggesting that these mutations impair normal folding of the expressed proteins. Cysteine 34-47 LOC100508689 Homo sapiens 88-93 12202389-5 2002 Reduction of the native mucin with dithiothreitol, thereby breaking the S==S bonds between cysteine residues, causes a marked reduction in polymer length. Cysteine 91-99 LOC100508689 Homo sapiens 24-29 10463611-7 1999 The MUC12 cDNA composite encoded a putative transmembrane mucin containing two extracellular cysteine-rich, EGF-like domains, a coiled-coil region, and a mucin-like domain consisting of 28 amino acid degenerate tandem repeats. Cysteine 93-101 LOC100508689 Homo sapiens 58-63 10190986-7 1999 These data identified a functional determinant for mucin-bacterial interactions in the N-terminal region where the only two cysteines (Cys45 and Cys50) in the MG2 apomucin occur. Cysteine 124-133 LOC100508689 Homo sapiens 51-56 7826332-0 1995 Characterization of the human mucin gene MUC5AC: a consensus cysteine-rich domain for 11p15 mucin genes? Cysteine 61-69 LOC100508689 Homo sapiens 30-35 9195947-10 1997 The conservation of the 11 cysteine positions in region 2 suggests the importance of this short region to mucin polymerization. Cysteine 27-35 LOC100508689 Homo sapiens 106-111 9163347-8 1997 Finally, the fact that in the presence of cysteine SNP was able to trigger a late, ODQ-inhibitable, mucin exocytotic response demonstrates the ability of NO to shift its intracellular signalling pathway depending on the changes of the redox state of the milieu. Cysteine 42-50 LOC100508689 Homo sapiens 100-105 9083100-12 1997 Each of these domains in the mucin subunit is separated by a trypsin-sensitive region, and the relative abundance of the major peptides derived by proteolysis of these regions and their occurrence in a contiguous sequence suggest that they contain a common cysteine-rich motif. Cysteine 257-265 LOC100508689 Homo sapiens 29-34 7775418-11 1995 A short amino acid sequence is similar to cysteine-rich sequences repeated in tracheobronchial, gastric, and colonic mucin cDNAs. Cysteine 42-50 LOC100508689 Homo sapiens 117-122 9804771-9 1998 The primary amino acid sequence with a high content of cysteine residues demonstrates a high degree of similarity with other members of the 11p15 mucin gene family, particularly MUC5AC. Cysteine 55-63 LOC100508689 Homo sapiens 146-151 9245735-1 1997 The human mucin gene MUC5AC codes for a large mucin which has tandem repeat units and cysteine rich regions characteristic of several members of this class of glycoproteins. Cysteine 86-94 LOC100508689 Homo sapiens 10-15 9245735-1 1997 The human mucin gene MUC5AC codes for a large mucin which has tandem repeat units and cysteine rich regions characteristic of several members of this class of glycoproteins. Cysteine 86-94 LOC100508689 Homo sapiens 46-51 9163347-7 1997 SNP was likely to act through S-nitrosylation of a cellular target, because cysteine, a reductive thiol that provides decoy targets for SNP through the formation of nitrosocysteine, abolished the early stimulatory effect of SNP on mucin exocytosis. Cysteine 76-84 LOC100508689 Homo sapiens 231-236 7826332-0 1995 Characterization of the human mucin gene MUC5AC: a consensus cysteine-rich domain for 11p15 mucin genes? Cysteine 61-69 LOC100508689 Homo sapiens 92-97 7826332-12 1995 The functional significance for secreted mucins of these cysteine-rich subdomains and the modular organization of mucin peptides are discussed. Cysteine 57-65 LOC100508689 Homo sapiens 41-46 1380835-3 1992 The discontinuity of cysteine-rich and S,T,P-rich areas near the C-terminus has not been observed in other mammalian mucin structures reported to date. Cysteine 21-29 LOC100508689 Homo sapiens 117-122 8267796-1 1993 By analogy with epidermal growth factor and EGF-like repeats, the P-domain, or trefoil motif, is a characteristic shuffled module containing six invariant cysteine residues that forms the basic unit for a family of mucin-associated peptides. Cysteine 155-163 LOC100508689 Homo sapiens 215-220 1400449-0 1992 The human MUC2 intestinal mucin has cysteine-rich subdomains located both upstream and downstream of its central repetitive region. Cysteine 36-44 LOC100508689 Homo sapiens 26-31 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. Cysteine 5-13 LOC100508689 Homo sapiens 38-43 1400449-9 1992 This suggests that these cysteine-rich subdomains are important in the catenation of mucin monomers into oligomers, the structures that confer viscoelasticity upon mucus. Cysteine 25-33 LOC100508689 Homo sapiens 85-90 1449803-6 1992 Less is known about the unique sequences that flank the tandem repeat arrays of secretory mucins, but currently available information indicates that these flanking regions contain cysteine-rich stretches that participate in mucin oligomer formation. Cysteine 180-188 LOC100508689 Homo sapiens 90-95