PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9461574-12 1998 Intrasubunit disulfide-bridged S100B monomer and disulfide-bonded S100B dimer are phosphorylated by the catalytic CKII-alpha subunit on Ser-62 with a Km of 0.5 microM and a Vmax of 10 pmol/min/100 pmol of S100B. Disulfides 13-22 S100 calcium binding protein B Homo sapiens 31-36 10666291-0 2000 Copper-dependent formation of disulfide-linked dimer of S100B protein. Disulfides 30-39 S100 calcium binding protein B Homo sapiens 56-61 9461574-15 1998 In addition, the phosphorylated intrasubunit disulfide-bridged S100B monomer retains apparent mitogenic activity toward C6 glial cells, and hence, 32P-labeled S100B should be a useful probe for characterizing the mechanisms by which extracellular oxidized S100B functions. Disulfides 45-54 S100 calcium binding protein B Homo sapiens 63-68 9461574-15 1998 In addition, the phosphorylated intrasubunit disulfide-bridged S100B monomer retains apparent mitogenic activity toward C6 glial cells, and hence, 32P-labeled S100B should be a useful probe for characterizing the mechanisms by which extracellular oxidized S100B functions. Disulfides 45-54 S100 calcium binding protein B Homo sapiens 159-164 9461574-15 1998 In addition, the phosphorylated intrasubunit disulfide-bridged S100B monomer retains apparent mitogenic activity toward C6 glial cells, and hence, 32P-labeled S100B should be a useful probe for characterizing the mechanisms by which extracellular oxidized S100B functions. Disulfides 45-54 S100 calcium binding protein B Homo sapiens 159-164 9461574-16 1998 Finally, we show that formation of intrasubunit disulfide-bridged S100B monomer is stimulated by peroxynitrite anion, suggesting that production of mitogenic S100B species could be enhanced in neuropathology associated with peroxynitrite anion production. Disulfides 48-57 S100 calcium binding protein B Homo sapiens 66-71 9461574-16 1998 Finally, we show that formation of intrasubunit disulfide-bridged S100B monomer is stimulated by peroxynitrite anion, suggesting that production of mitogenic S100B species could be enhanced in neuropathology associated with peroxynitrite anion production. Disulfides 48-57 S100 calcium binding protein B Homo sapiens 158-163 9490014-1 1998 Interaction of S100a and S100b with duck gizzard caldesmon was investigated by means of native gel electrophoresis, fluorescent spectroscopy and disulfide crosslinking. Disulfides 145-154 S100 calcium binding protein B Homo sapiens 25-30 2087556-4 1990 The neurotrophic activity is sensitive to reduction of disulfide bonds, and appears to be a disulfide dimer of S100 beta. Disulfides 92-101 S100 calcium binding protein B Homo sapiens 111-120 9055015-6 1996 In the light of recent evidence on the role of nef gene defects/attenuations in long-term survival of HIV-1 infected patients, it may be that the nef gene defect created by gene duplication, which eliminated the cysteine-206 crucial in disulfide bond formation, may play a role in chronic HIV-1 infection in this patient. Disulfides 236-245 S100 calcium binding protein B Homo sapiens 146-149 1420327-0 1992 Disulfide-linked S100 beta dimers and signal transduction. Disulfides 0-9 S100 calcium binding protein B Homo sapiens 17-26 1420327-2 1992 These extracellular trophic activities of S100 beta require a disulfide-linked, dimeric form of the protein. Disulfides 62-71 S100 calcium binding protein B Homo sapiens 42-51 1420327-4 1992 We also report a simplified procedure for preparation of pharmacological amounts of biologically active S100 beta dimers, based on the finding that formation of disulfide-linked S100 beta dimers can be stimulated by the presence of calcium or lipid. Disulfides 161-170 S100 calcium binding protein B Homo sapiens 104-113 1420327-4 1992 We also report a simplified procedure for preparation of pharmacological amounts of biologically active S100 beta dimers, based on the finding that formation of disulfide-linked S100 beta dimers can be stimulated by the presence of calcium or lipid. Disulfides 161-170 S100 calcium binding protein B Homo sapiens 178-187 7734198-6 1995 In addition, because significantly higher levels of the Nef oligomers were consistently observed under the nonreducing SDS-PAGE condition, site-specific mutagenesis was also used to examine the role of cysteine residues in generating disulfide-linked Nef dimers in vitro. Disulfides 234-243 S100 calcium binding protein B Homo sapiens 56-59 7734198-6 1995 In addition, because significantly higher levels of the Nef oligomers were consistently observed under the nonreducing SDS-PAGE condition, site-specific mutagenesis was also used to examine the role of cysteine residues in generating disulfide-linked Nef dimers in vitro. Disulfides 234-243 S100 calcium binding protein B Homo sapiens 251-254 7734198-8 1995 Therefore, these results demonstrate that the leucine zipper-type motif in the HIV-2 Nef protein mediates stable homooligomer formation in vitro, and also establish a role for covalent disulfide bonds in the formation of linked Nef dimers and thermal stability of the monomer Nef in vitro. Disulfides 185-194 S100 calcium binding protein B Homo sapiens 85-88 7734198-8 1995 Therefore, these results demonstrate that the leucine zipper-type motif in the HIV-2 Nef protein mediates stable homooligomer formation in vitro, and also establish a role for covalent disulfide bonds in the formation of linked Nef dimers and thermal stability of the monomer Nef in vitro. Disulfides 185-194 S100 calcium binding protein B Homo sapiens 228-231 7734198-8 1995 Therefore, these results demonstrate that the leucine zipper-type motif in the HIV-2 Nef protein mediates stable homooligomer formation in vitro, and also establish a role for covalent disulfide bonds in the formation of linked Nef dimers and thermal stability of the monomer Nef in vitro. Disulfides 185-194 S100 calcium binding protein B Homo sapiens 228-231 2398350-0 1990 Intra- and interchain disulfide bond generation in S100b protein. Disulfides 22-31 S100 calcium binding protein B Homo sapiens 51-56 2398350-1 1990 Disulfide-bridged S100b protein formation, aircatalyzed and induced by thiol/disulfide exchange, was studied under various ionic conditions. Disulfides 0-9 S100 calcium binding protein B Homo sapiens 18-23 2398350-1 1990 Disulfide-bridged S100b protein formation, aircatalyzed and induced by thiol/disulfide exchange, was studied under various ionic conditions. Disulfides 77-86 S100 calcium binding protein B Homo sapiens 18-23 2398350-2 1990 As native, physiological disulfide-bridged proteins are obtained easily from their reduced counterparts under appropriate redox conditions, this work was performed to determine whether this was the case for disulfide-bridged S100b proteins, reported to have neurite extension activity. Disulfides 207-216 S100 calcium binding protein B Homo sapiens 225-230 2398350-7 1990 Taken together, these data question the physiological relevance of these disulfide-bridged S100b protein species. Disulfides 73-82 S100 calcium binding protein B Homo sapiens 91-96 2337349-0 1990 Structural and ion-binding properties of an S100b protein mixed disulfide: comparison with the reappraised native S100b protein properties. Disulfides 64-73 S100 calcium binding protein B Homo sapiens 44-49 2337349-1 1990 S100b protein, chemically modified by thioethanol groups (linked via disulfide bonds to two out of four Cys per dimer) was largely similar to reduced native S100b protein in its overall structure and differed only by small modifications extending, however, to the whole protein structure. Disulfides 69-78 S100 calcium binding protein B Homo sapiens 0-5 1009954-0 1976 Ca2+, K+-regulated intramolecular crosslinking of S-100 protein via disulfide bond formation. Disulfides 68-77 S100 calcium binding protein B Homo sapiens 50-55 1009954-1 1976 Reaction of the thiol reagent 5,5"-dithio-bis(2-nitrobenzoic acid) (Nbs2) with the brain-specific protein S-100 favours stabilization of the quaternary structure of the protein via disulfide bond formation. Disulfides 181-190 S100 calcium binding protein B Homo sapiens 106-111 1009954-3 1976 Ca2+ markedly favours the reaction of S-100 with Nbs2 but inhibits subsequent disulfide bond formation; K+, on the contrary, is much less effective in promoting interaction with Nbs2 but strongly stimulates disulfide bond formation. Disulfides 207-216 S100 calcium binding protein B Homo sapiens 38-43 1009954-4 1976 These findings are interpreted assuming that in presence of Ca2+ the three subunits forming the native S-100 protein have two cysteine residues exposed to the solvent but mismatched to form disulfides while in presence of K+ the sulphydryl groups are in a less accessible position to Nbs2 but suitable for S-S bond formation. Disulfides 190-200 S100 calcium binding protein B Homo sapiens 103-108 1009954-6 1976 This finding, and the demonstration that both the crosslinked and native S-100 proteins have identical profiles when analyzed by sucrose density centrifugation or gel chromatography indicate that disulfide bond formation occurs among subunits of the same molecule. Disulfides 196-205 S100 calcium binding protein B Homo sapiens 73-78 33326534-0 2021 Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-beta aggregation. Disulfides 49-58 S100 calcium binding protein B Homo sapiens 16-21