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