PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33264978-0 2021 Effects of Fe and Al ions during hydrogen sulphide (H2S)-induced corrosion of tetracalcium aluminoferrite (C4AF) and tricalcium aluminate (C3A). Deuterium 52-55 complement C3 Homo sapiens 139-142 33264978-2 2021 In this study, hydrogen sulphide (H2S)-induced corrosion effects of tetracalcium aluminoferrite (C4AF) and tricalcium aluminate (C3A) phases of cement were evaluated during the initial stages of reaction. Deuterium 34-37 complement C3 Homo sapiens 129-132 21953046-5 2011 This fragmentation pathway was also pronounced in the [M - 2H](2-) ions revealing both the C-6 Z-fragment plus its complementary C-3 C-fragment in addition to glycosidic and cross ring fragmentation. Deuterium 59-61 complement C3 Homo sapiens 129-132 28258193-3 2017 Here, we employed hydrogen-deuterium exchange mass spectrometry to describe the structure and dynamics of iC3b at a peptide resolution level in direct comparison with its parent protein C3b. Deuterium 27-36 complement C3 Homo sapiens 107-110 28258193-5 2017 Several peptides in iC3b showed significantly higher deuterium uptake when compared with C3b, revealing more dynamic, solvent-exposed regions. Deuterium 53-62 complement C3 Homo sapiens 21-24 15954762-3 2005 We demonstrate that when fumarate is the cosubstrate, deuterium is transferred from toluene to the C-3 pro-(R) position of benzylsuccinate, implying a syn addition of toluene to the double bond of fumarate. Deuterium 54-63 complement C3 Homo sapiens 99-102 20836998-2 2010 To install deuterium at C-3 of sphingosine and sphingomyelin, sodium borodeuteride reduction/cerium(III) chloride reduction of an alpha,beta-enone in perdeuteromethanol was used. Deuterium 11-20 complement C3 Homo sapiens 24-27 18456336-0 2008 Dynamic structural changes during complement C3 activation analyzed by hydrogen/deuterium exchange mass spectrometry. Deuterium 80-89 complement C3 Homo sapiens 34-47 15954762-4 2005 However, when maleate is the cosubstrate, the addition of toluene occurs in an anti fashion, so that deuterium transfer to the C-3 pro-(R) position of benzylsuccinate is also observed. Deuterium 101-110 complement C3 Homo sapiens 127-130 10769138-5 2000 Secondary deuterium isotope effects at C-3 were 2.5% at pH 7 and 3.1% at pH 5.5 with the wild-type enzyme, and 4.1% at pH 7 with H97N. Deuterium 10-19 complement C3 Homo sapiens 39-42 11348117-3 2001 In the feeding experiments with [3-(2)H]- and [4-(2)H]-D-glucosamine and [1-(2)H]-D-glucose, deuterium was incorporated into C-3, C-4, and C-1 of 1, respectively. Deuterium 93-102 complement C3 Homo sapiens 125-128 11101483-7 2000 We propose that [(2)H(2)]methionine occurs by remethylation with [(2)H(2)]methyl groups (as 5-methyltetrahydrofolate) formed only from cytosolic processing of [(2)H(3)]serine, whereas [(2)H(1)]methionine is formed with labeled one-carbon units from mitochondrial oxidation of C-3 serine to [(2)H(1)]formate to yield cytosolic [(2)H(1)]methyl groups. Deuterium 17-24 complement C3 Homo sapiens 276-279 11101483-7 2000 We propose that [(2)H(2)]methionine occurs by remethylation with [(2)H(2)]methyl groups (as 5-methyltetrahydrofolate) formed only from cytosolic processing of [(2)H(3)]serine, whereas [(2)H(1)]methionine is formed with labeled one-carbon units from mitochondrial oxidation of C-3 serine to [(2)H(1)]formate to yield cytosolic [(2)H(1)]methyl groups. Deuterium 18-21 complement C3 Homo sapiens 276-279 10400348-14 1999 The deamination reaction displays high reverse reaction commitments and independent evidence from primary deuterium isotope effect data indicates that a thiolate acts as the base for deprotonation at C-3. Deuterium 106-115 complement C3 Homo sapiens 200-203 10400349-0 1999 The 3-methylaspartase reaction probed using 2H- and 15N-isotope effects for three substrates: a flip from a concerted to a carbocationic amino-enzyme elimination mechanism upon changing the C-3 stereochemistry in the substrate from R to S. The mechanisms of the elimination of ammonia from (2S,3S)-3-methylaspartic acid, (2S)-aspartic acid and (2S,3R)-3-methylaspartic acid, catalysed by the enzyme L-threo-3-methylaspartase ammonia-lyase (EC 4.3.1.2) have been probed using 15N-isotope effects. Deuterium 44-46 complement C3 Homo sapiens 190-193 6852253-1 1983 The proton NMR analysis of D-glucosaminate dehydratase reaction in D2O revealed the incorporation of a deuterium atom at C-3 carbon of the product, 2-keto-3-deoxy-D-gluconate. Deuterium 103-112 complement C3 Homo sapiens 121-124 6375666-2 1984 Substitution of deuterium for hydrogen at the terminal carbon atoms (C-3) of Tris-BP significantly decreased both the mutagenic response and the formation rate of 2- bromoacrolein . Deuterium 16-25 complement C3 Homo sapiens 69-72 6426542-3 1984 When the reaction mixture was buffered with phosphate, isolated delta 1-pyrroline contained two deuterium atoms at C-3, indicating that a phosphate-promoted, non-enzymatic isotope exchange had occurred. Deuterium 96-105 complement C3 Homo sapiens 115-118 6852253-2 1983 Based on the chemical shift of C-3 proton of the product and the coupling constant characteristic for the C-3 and C-4 axial-axial coupling in the 2C5 pyranose conformation, the deuterium is in the pro-S position. Deuterium 177-186 complement C3 Homo sapiens 31-34 6852253-2 1983 Based on the chemical shift of C-3 proton of the product and the coupling constant characteristic for the C-3 and C-4 axial-axial coupling in the 2C5 pyranose conformation, the deuterium is in the pro-S position. Deuterium 177-186 complement C3 Homo sapiens 106-109 6658886-2 1983 1H NMR spectra of all four 17 xi-hydroxy/17 xi-methyl C-3 ketones and all eight C-3 alcohols were recorded in chloroform-d and pyridine-d5. Deuterium 35-36 complement C3 Homo sapiens 54-57 6106214-12 1980 This method has also been used to measure isotope exchange (1H-2H) of lactate and of pyruvate at both the C-3 and the C-2 positions, and some of these exchange rates can be interpreted in terms of the activity of specific enzymes in the cells. Deuterium 63-65 complement C3 Homo sapiens 106-109 562233-4 1977 Most of these peripheral sugar chains are linked to two inner D-mannose residues which are substituted at C-3 and C-6, and constitute branching points. Deuterium 62-63 complement C3 Homo sapiens 106-109