PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19331391-3 2009 Increasing size of the substituents at C-1 and C-5 of the diene favors kinetic products arising from oxygen addition at the nonconjugated position, C-3, of the pentadienyl radical intermediate. Oxygen 101-107 complement C3 Homo sapiens 148-151 26041127-2 2016 In this work, we present a 3D microreactor capable of maintaining metabolically active HepG2/C3A spheroids for over 28 days in vitro under stable oxygen gradients mimicking the in vivo microenvironment. Oxygen 146-152 complement C3 Homo sapiens 93-96 21254897-3 2012 Activation of the classical, alternative, and lectin complement pathways and the generation of the anaphylatoxins C3a and C5a lead to recruitment of polymorphonuclear leukocytes, generation of radical oxygen species, up-regulation of adhesion molecules on the endothelium and platelets, and induction of cytokine release. Oxygen 201-207 complement C3 Homo sapiens 114-117 19697924-4 2009 In silico P450 3A4 active site docking of Cmpd A exhibited a low energy pose that orientated the pyrazole ring proximate to the heme iron atom, in which the distance between the C-3 and potential activated oxygen species was shown to be 3.4 A. Quantum molecular calculations showed that the electron density on C-3 was relatively higher than those on C-4 and C-5. Oxygen 206-212 complement C3 Homo sapiens 178-181 19697924-4 2009 In silico P450 3A4 active site docking of Cmpd A exhibited a low energy pose that orientated the pyrazole ring proximate to the heme iron atom, in which the distance between the C-3 and potential activated oxygen species was shown to be 3.4 A. Quantum molecular calculations showed that the electron density on C-3 was relatively higher than those on C-4 and C-5. Oxygen 206-212 complement C3 Homo sapiens 311-314 27404666-2 2016 The C-3 stereogenic center is subsequently exploited to create the C-1 stereocenter by coordination of the nucleophilic reagent to the oxygen atom of oxazolidine. Oxygen 135-141 complement C3 Homo sapiens 4-7 19331391-6 2009 Groups at C-1 and C-5 of the diene can influence product distribution based upon (a) steric demand in the oxygen-radical reaction and (b) the influence of substituents on the rearrangement of the C-3 peroxyl radical to give conjugated diene products. Oxygen 106-112 complement C3 Homo sapiens 196-199 17924615-2 2007 The structures of two representative nonpolar metabolites were identified earlier as dimers of 17beta-estradiol linked through a diaryl ether bond between the C-3 phenolic oxygen of one molecule and the C-2 or C-4 aromatic carbon of another. Oxygen 172-178 complement C3 Homo sapiens 159-162 18236095-4 2004 The diffusion capacities for the[Formula: see text] (between C3 and C9) are arbitrarily assigned.The Fick method gives incorrect results depending on the total arteriovenous diffusive shunt of oxygen[Formula: see text]. Oxygen 193-199 complement C3 Homo sapiens 61-70 17004712-7 2006 The hypotheses are as follows: (1) it is the carboxamide oxygen of the C-3 substituent of 1 that interacts directly with K3.28(192) and (2) the interaction with K3.28(192) is crucial for the production of inverse agonism for biarylpyrazoles such as 1. Oxygen 57-63 complement C3 Homo sapiens 71-74 17004712-14 2006 Taken together, these results support the hypothesis that it is the carboxamide oxygen of the C-3 substituent of 1 that engages in a hydrogen bond with K3.28(192) in WT CB1. Oxygen 80-86 complement C3 Homo sapiens 94-97 16462017-7 2006 All naturally occurring citrus limonoids contain a furan ring attached to the D-ring, at C-17, as well as oxygen containing functional groups at C-3, C-4, C-7, C-16 and C-17. Oxygen 106-112 complement C3 Homo sapiens 145-148 14570878-7 2004 In the case of products formed by oxidation of flavonoid substrates with a C-3 hydroxyl group (e.g. (2R,3R)-trans-dihydroquercetin), the results imply that oxygen exchange can occur at a stage subsequent to initial oxidation of the C-ring, probably via an enzyme-bound C-3 ketone/3,3-gem-diol intermediate. Oxygen 156-162 complement C3 Homo sapiens 75-78 15287594-6 2004 Competition studies with eight different inositol isomers revealed that proton bonds between the C-2, C-3 and C-5 hydroxyl groups of myo-inositol and the transporter protein played a critical role for substrate recognition, and the C-3 hydroxyl oxygen appears to act as an electron donor to form an H-bond with a positive charge of the MIT permease. Oxygen 245-251 complement C3 Homo sapiens 102-105 14570878-7 2004 In the case of products formed by oxidation of flavonoid substrates with a C-3 hydroxyl group (e.g. (2R,3R)-trans-dihydroquercetin), the results imply that oxygen exchange can occur at a stage subsequent to initial oxidation of the C-ring, probably via an enzyme-bound C-3 ketone/3,3-gem-diol intermediate. Oxygen 156-162 complement C3 Homo sapiens 269-272 10420575-2 1999 Infrared and solid state NMR 13C analysis of MA and the ligand strongly suggests that antimony binds to N-methyl glucamine through the oxygen of C-3 carbon. Oxygen 135-141 complement C3 Homo sapiens 145-148 11230564-1 2001 Brassinosteroids (BRs) are plant steroids essential for normal growth and development and can be defined as steroids that carry an oxygen moiety at C-3 and additional ones at one or more of the C-2, C-6, C-22 and C-23 carbon atoms. Oxygen 131-137 complement C3 Homo sapiens 148-151 11032742-8 2000 Using a human thioredoxin in which the structural cysteines were mutated to alanine, Trx-C3A, we show that structural cysteines that do not take part in the catalytic functions of the protein are also important for its reactive oxygen scavenging properties. Oxygen 228-234 complement C3 Homo sapiens 89-92 10810708-0 2000 Unexpected products via singlet oxygen oxygenation of functionalized 5,6-dihydro-1,4-oxathiins [formula: see text] Single oxygen oxygenation of 5,6-dihydro-1,4-oxathiins substituted at C-3 with an electron-withdrawing group leads stereoselectively to ketosulfoxides 5 and 6, instead of the expected dicarbonyl compounds 3. Oxygen 32-38 complement C3 Homo sapiens 185-188 9313864-7 1997 An examination of the SAR of these analogues shows that translocating the napthyl group in AAIs from the C-3 position to C-4 via an oxygen (ether linkage) decreases activity which is in contrast to previous findings that a naphthylcarbonyl at C-4 retains activity. Oxygen 132-138 complement C3 Homo sapiens 105-108 1552891-1 1992 In in-vitro study, human immunoglobulin (Ig) denatured by O2 bubbling markedly produced C4a, C3a, and C5a, whereas human albumin treated identically did not. Oxygen 58-60 complement C3 Homo sapiens 93-96 7850393-0 1994 Mutagenic and carcinogenic risk of oxygen containing chlorinated C-3 hydrocarbons: putative secondary products of C-3 chlorohydrocarbons and chlorination of water. Oxygen 35-41 complement C3 Homo sapiens 65-68 7850393-0 1994 Mutagenic and carcinogenic risk of oxygen containing chlorinated C-3 hydrocarbons: putative secondary products of C-3 chlorohydrocarbons and chlorination of water. Oxygen 35-41 complement C3 Homo sapiens 114-117 7850393-1 1994 Oxygen containing C-3 chlorohydrocarbons are secondary products of C-3 chlorohydrocarbons formed during oxidation at air, in the metabolism of pesticides and by chlorination of drinking water. Oxygen 0-6 complement C3 Homo sapiens 18-21 7850393-1 1994 Oxygen containing C-3 chlorohydrocarbons are secondary products of C-3 chlorohydrocarbons formed during oxidation at air, in the metabolism of pesticides and by chlorination of drinking water. Oxygen 0-6 complement C3 Homo sapiens 67-70 1552891-2 1992 White blood cells (WBC) treated by O2 bubbling significantly increased C3a levels alone, but at a much lesser grade than the Ig. Oxygen 35-37 complement C3 Homo sapiens 71-74 2584778-12 1989 In experimental studies using 20 monkeys (Macaca fascicularis), continuous intraaortic infusion with O2 bubbled autologous blood increased C4a and C3a levels, while autologous blood extracorporeally contacted with nylon increased C3a levels alone. Oxygen 101-103 complement C3 Homo sapiens 147-150 1728718-2 1992 In vitro immunoglobulin fractions denatured by oxygen bubbling produced C4a, C3a, and C5a, but albumin identically treated did not. Oxygen 47-53 complement C3 Homo sapiens 77-80 2584778-12 1989 In experimental studies using 20 monkeys (Macaca fascicularis), continuous intraaortic infusion with O2 bubbled autologous blood increased C4a and C3a levels, while autologous blood extracorporeally contacted with nylon increased C3a levels alone. Oxygen 101-103 complement C3 Homo sapiens 230-233 2584778-14 1989 In vitro studies revealed that human immunoglobulin denatured by O2 bubbling produced C4a, C3a, and C5a in a dose dependent manner, although human albumin treated identically as human immunoglobulin did not produce them. Oxygen 65-67 complement C3 Homo sapiens 91-94 6020561-3 1967 The apparent K(m) for oxygen for thiosulfate oxidation by A-50 was about 223 mum, but, for lactate oxidation by A-50 or thiosulfate oxidation by C-3, the apparent K(m) for oxygen was below 2 mm. Oxygen 172-178 complement C3 Homo sapiens 145-148 3700413-1 1986 Evidence of a requirement for C-3 oxygen in C-19 hydroxylations. Oxygen 34-40 complement C3 Homo sapiens 30-33 3700413-2 1986 Substitution of a methylene group for the C-3 oxygen in androstenedione, testosterone, and the corresponding 19-hydroxy and 19-oxo derivatives results in a new category of inhibitors of estrogen biosynthesis by human placental microsomes. Oxygen 46-52 complement C3 Homo sapiens 42-45 3700413-6 1986 Time-dependent inhibition of aromatization by 10 beta-difluoromethylestr-4-ene-3,17-dione and 10 beta-(2-propynyl)estr-4-ene,3,17-dione was abolished by substitution of a methylene function for the C-3 oxygen, suggesting that the presence of an oxygen at C-3 is required for an oxidative transformation at C-19, an initial step in aromatization. Oxygen 202-208 complement C3 Homo sapiens 198-201 3700413-6 1986 Time-dependent inhibition of aromatization by 10 beta-difluoromethylestr-4-ene-3,17-dione and 10 beta-(2-propynyl)estr-4-ene,3,17-dione was abolished by substitution of a methylene function for the C-3 oxygen, suggesting that the presence of an oxygen at C-3 is required for an oxidative transformation at C-19, an initial step in aromatization. Oxygen 202-208 complement C3 Homo sapiens 255-258 3700413-6 1986 Time-dependent inhibition of aromatization by 10 beta-difluoromethylestr-4-ene-3,17-dione and 10 beta-(2-propynyl)estr-4-ene,3,17-dione was abolished by substitution of a methylene function for the C-3 oxygen, suggesting that the presence of an oxygen at C-3 is required for an oxidative transformation at C-19, an initial step in aromatization. Oxygen 245-251 complement C3 Homo sapiens 198-201 3700413-6 1986 Time-dependent inhibition of aromatization by 10 beta-difluoromethylestr-4-ene-3,17-dione and 10 beta-(2-propynyl)estr-4-ene,3,17-dione was abolished by substitution of a methylene function for the C-3 oxygen, suggesting that the presence of an oxygen at C-3 is required for an oxidative transformation at C-19, an initial step in aromatization. Oxygen 245-251 complement C3 Homo sapiens 255-258 3754548-4 1986 Since a 18OH group was introduced at C-3 on a hydrolytic cleavage of C-2, C-3 epoxy group with alkaline H2(18)O, the original epoxy oxygen should be retained at C-2. Oxygen 132-138 complement C3 Homo sapiens 37-40 2983185-5 1985 Calculated electron and spin densities indicate that the radical formed by H abstraction from the phenol oxygen does not remain localized on the oxygen, but is primarily a semiquinone aryl radical with significant unpaired spin density on the ring carbon atoms, particularly on C-3 and C-5. Oxygen 105-111 complement C3 Homo sapiens 278-281 3382287-8 1988 In vitro studies revealed that human immunoglobulin fractions denatured by oxygen bubbling produced C4a, C3a, and C5a in a dose-dependent manner, although human albumin treated identically as human immunoglobulin did not produce these complements. Oxygen 75-81 complement C3 Homo sapiens 105-108 3079908-3 1986 We propose a stereochemical model in which the oxygens in TPA at C-3, C-4, C-9, and C-20 (O-3, O-4, O-9, and O-20) correspond to the O-11, N-13, N-1, and O-24 positions in teleocidin and the O-27, O-3, O-11, and O-30 oxygens in aplysiatoxin, respectively. Oxygen 47-54 complement C3 Homo sapiens 65-68 3079908-3 1986 We propose a stereochemical model in which the oxygens in TPA at C-3, C-4, C-9, and C-20 (O-3, O-4, O-9, and O-20) correspond to the O-11, N-13, N-1, and O-24 positions in teleocidin and the O-27, O-3, O-11, and O-30 oxygens in aplysiatoxin, respectively. Oxygen 217-224 complement C3 Homo sapiens 65-68 6275773-1 1981 The mannose monosaccharide residue in ristomycin A is bound via C-3 phenolic oxygen of the 1,2,3,5-substituted ring with actinoidinic amino acid. Oxygen 77-83 complement C3 Homo sapiens 64-67 975043-4 1976 The hydrogen atom on C-3 points directly toward the oxygen atom of another molecule. Oxygen 52-58 complement C3 Homo sapiens 21-24 5879171-2 1965 10-Cyanosteroids with an oxygen at C-3. Oxygen 39-45 complement C3 Homo sapiens 49-52 28884388-10 2018 And C3 was associated with AHI, average pulse oxygen saturation (A-spo2), homeostasis model assessment-insulin resistance (HOMA-IR), 2hPG, age, sleep stage (I + II)/TST, and sleep stage (III)/TST, respectively. Oxygen 46-52 complement C3 Homo sapiens 4-6