PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7907470-5 1994 The 1H/13C satellite resonances from glutamate C-4 and lactate C-3 in brain tissue were followed from 4 min onwards in the presence of 5 mM [1-13C]glucose. Hydrogen 4-6 complement C3 Homo sapiens 63-66 8999873-9 1997 The preference of the enzyme for donor substrates with D-threo configuration at the C-3 and C-4 positions and for alpha-hydroxylated acceptor substrates can be understood from the pattern of hydrogen bonds between enzyme and substrate. Hydrogen 191-199 complement C3 Homo sapiens 84-87 8916426-4 1996 Unimolecular loss of hydrogen atom from C-2- and C-3-protonated pyrrole cations is preceded by proton migration in the ring. Hydrogen 21-29 complement C3 Homo sapiens 49-52 7981420-6 1994 An autoxidative pyrrole dimer containing a methylene bridge between C-2 of one pyrrole ring and C-3 of a second ring was characterized by thermospray MS and 1H-NMR spectroscopy. Hydrogen 157-159 complement C3 Homo sapiens 96-99 1939111-6 1991 The hydrogen atom at C-3 of the enzyme product is introduced from solvent water. Hydrogen 4-12 complement C3 Homo sapiens 21-24 8405445-2 1993 Each analog with hydrogen, methyl, ethyl, isopropyl, isobutyl, tert-butyl, and isoamyl group on C-3 functions as a substrate, implying a broad substrate specificity of the enzyme toward alkylmalates. Hydrogen 17-25 complement C3 Homo sapiens 96-99 1531295-0 1992 Mechanism of C-3 hydrogen exchange and the elimination of ammonia in the 3-methylaspartate ammonia-lyase reaction. Hydrogen 17-25 complement C3 Homo sapiens 13-16 1531295-1 1992 The enzyme 3-methylaspartate ammonia-lyase (EC 4.3.1.2) catalyzes the exchange of the C-3 hydrogen of the substrate, (2S,3S)-3-methylaspartic acid, with solvent hydrogen. Hydrogen 90-98 complement C3 Homo sapiens 86-89 1531295-1 1992 The enzyme 3-methylaspartate ammonia-lyase (EC 4.3.1.2) catalyzes the exchange of the C-3 hydrogen of the substrate, (2S,3S)-3-methylaspartic acid, with solvent hydrogen. Hydrogen 161-169 complement C3 Homo sapiens 86-89 3266557-0 1988 1H NMR studies of human C3a anaphylatoxin in solution: sequential resonance assignments, secondary structure, and global fold. Hydrogen 0-2 complement C3 Homo sapiens 24-27 3266557-1 1988 The spin systems that comprise the 1H nuclear magnetic resonance (NMR) spectrum of the complement fragment C3a (Mr 8900) have been completely identified by an approach which integrates data from a wide range of two-dimensional NMR experiments. Hydrogen 35-37 complement C3 Homo sapiens 107-110 7141529-3 1982 All compounds exhibited the (M-OH)+ ion, for which the hydrogen abstraction is non-specific, involving the C-2 and C-3 positions in the methylbutyl homolog. Hydrogen 55-63 complement C3 Homo sapiens 115-118 3260670-1 1988 Two-dimensional 1H NMR investigations were used to locate elements of regular secondary structure in the human complement protein C3a (the des-Arg77 derivative) in solution. Hydrogen 16-18 complement C3 Homo sapiens 130-133 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. Hydrogen 104-106 complement C3 Homo sapiens 37-40 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 . Hydrogen 30-38 complement C3 Homo sapiens 69-72 3416869-8 1988 The lectins are involved in strong hydrogen bonds through charged groups with the C-3 and C-4 hydroxyl groups of galactose, with the latter serving as hydrogen-bond donors. Hydrogen 35-43 complement C3 Homo sapiens 82-85 3416869-8 1988 The lectins are involved in strong hydrogen bonds through charged groups with the C-3 and C-4 hydroxyl groups of galactose, with the latter serving as hydrogen-bond donors. Hydrogen 151-159 complement C3 Homo sapiens 82-85 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. Hydrogen 0-2 complement C3 Homo sapiens 54-57 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. Hydrogen 0-2 complement C3 Homo sapiens 80-83 7141529-4 1982 In the same compound, the M-propene ion required the specific transfer of hydrogen from C-3. Hydrogen 74-82 complement C3 Homo sapiens 88-91 6271696-6 1981 The three other reactions could be conveniently monitored in gamma-irradiated polycrystalline alanine at 110 degrees C. The first of the other three reactions takes place between the methyl hydrogens of the radicals and the C-2 hydrogens of nearby molecules, while the remaining processes involve exchange between the hydrogen atoms of the amino group and those on the C-2 and C-3 carbon atoms of the deamination radical. Hydrogen 190-199 complement C3 Homo sapiens 377-380 6271696-6 1981 The three other reactions could be conveniently monitored in gamma-irradiated polycrystalline alanine at 110 degrees C. The first of the other three reactions takes place between the methyl hydrogens of the radicals and the C-2 hydrogens of nearby molecules, while the remaining processes involve exchange between the hydrogen atoms of the amino group and those on the C-2 and C-3 carbon atoms of the deamination radical. Hydrogen 228-237 complement C3 Homo sapiens 377-380 6271696-6 1981 The three other reactions could be conveniently monitored in gamma-irradiated polycrystalline alanine at 110 degrees C. The first of the other three reactions takes place between the methyl hydrogens of the radicals and the C-2 hydrogens of nearby molecules, while the remaining processes involve exchange between the hydrogen atoms of the amino group and those on the C-2 and C-3 carbon atoms of the deamination radical. Hydrogen 190-198 complement C3 Homo sapiens 377-380 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. Hydrogen 60-62 complement C3 Homo sapiens 106-109 1156576-11 1975 Exhaustive incubation of the tritiated malate (3-H/14-C = 1.95) with fumarase to labilize the pro-R hydrogen at C-3 resulted in release of 65% of the tritium into water. Hydrogen 100-108 complement C3 Homo sapiens 112-115 116677-6 1979 On the basis of these studies, it is suggested that hydrogen bonding occurs between the hydrogen atoms of the C-3 and C-4 hydroxyl groups of alpha-D-GalNAcp and alpha-D-galp units and the A and B subunits, respectively. Hydrogen 52-60 complement C3 Homo sapiens 110-113 116677-6 1979 On the basis of these studies, it is suggested that hydrogen bonding occurs between the hydrogen atoms of the C-3 and C-4 hydroxyl groups of alpha-D-GalNAcp and alpha-D-galp units and the A and B subunits, respectively. Hydrogen 88-96 complement C3 Homo sapiens 110-113 975043-4 1976 The hydrogen atom on C-3 points directly toward the oxygen atom of another molecule. Hydrogen 4-12 complement C3 Homo sapiens 21-24 447726-3 1979 In the reaction of L-tryptophan methyl ester, the enzyme also catalyzes stereospecific removal of the pro-S hydrogen at C-3, but the product 3-hydroxytryptophan methyl ester is racemic at C-3. Hydrogen 108-116 complement C3 Homo sapiens 120-123 447726-3 1979 In the reaction of L-tryptophan methyl ester, the enzyme also catalyzes stereospecific removal of the pro-S hydrogen at C-3, but the product 3-hydroxytryptophan methyl ester is racemic at C-3. Hydrogen 108-116 complement C3 Homo sapiens 188-191 447726-4 1979 The unreacted tryptophan methyl ester is shown to incorporate solvent hydrogen into the pro-S position at C-3 in an at least partially stereospecific manner, suggesting that the reaction of L-tryptophan methyl ester is reversible. Hydrogen 70-78 complement C3 Homo sapiens 106-109 1083847-9 1976 Each product can be assigned a precursor radical formed by hydrogen abstraction from C-5, C-4 or C-3 of the ribose-5-phosphate molecule. Hydrogen 59-67 complement C3 Homo sapiens 97-100 32588927-2 2020 These pseudo-anomeric effects are apparent when electronegative CF 2 groups are placed at the C-2, C-4 and C-6 positions of the cyclohexane ring to render the C-3/5 axial hydrogens electropositive. Hydrogen 171-180 complement C3 Homo sapiens 159-162 5639923-5 1968 The location of five of the six labelled hydrogen atoms at C-3, C-9, C-18 and C-19 (two) confirms that the mechanism of cyclization of squalene expected from the biogenetic isoprene rule is functioning in vivo. Hydrogen 41-49 complement C3 Homo sapiens 59-62 31291611-7 2019 Molecular docking indicated potential interactions of demethylbellidifolin (1) with HCE 2 through two hydrogen bonds of the C-3 and C-5 hydroxy groups with amino acid residues Glu227 and Ser228 in the catalytic cavity, respectively. Hydrogen 102-110 complement C3 Homo sapiens 124-127 31744771-5 2020 We further recognised that the C NMR chemical shifts of the nominal phenyl carbons (C(3)/C(7) and C(4)/C(6)) encode information for intramolecular hydrogen bonding network formed by GA conformers. Hydrogen 147-155 complement C3 Homo sapiens 84-88 28701464-12 2017 We conclude that the most likely catalytic mechanism begins with abstraction of a hydrogen atom from C-4 (or possibly C-3) initiating the desaturation pathway, followed by a sequential abstraction of a hydrogen atom or proton-coupled electron transfer. Hydrogen 82-90 complement C3 Homo sapiens 118-121 28701464-12 2017 We conclude that the most likely catalytic mechanism begins with abstraction of a hydrogen atom from C-4 (or possibly C-3) initiating the desaturation pathway, followed by a sequential abstraction of a hydrogen atom or proton-coupled electron transfer. Hydrogen 202-210 complement C3 Homo sapiens 118-121 19226157-1 2009 We report here that the monodentate complexation of Me2AlCl to an ester group significantly enhances the selectivity of hydrogen transfer on acyclic radicals flanked by both an ester functionality and a stereogenic center, leading to C-2,C-3-anti products with high diastereoselectivity. Hydrogen 120-128 complement C3 Homo sapiens 238-241 23869809-6 2013 A hydroxyl group at C-3 enhances trichothecene toxicity, while this activity decreases gradually when C-3 is substituted with either hydrogen or an acetoxy group. Hydrogen 133-141 complement C3 Homo sapiens 102-105 23313634-4 2013 Overall, these studies showed that the combined presence of a phenyl group at C-3 and a methyl group at C-5 in the 1H,3H-pyrrolo[1,2-c]thiazole ring system is essential to ensure high cytotoxicty against MCF7 breast cancer cell lines. Hydrogen 115-117 complement C3 Homo sapiens 78-81 22413941-7 2012 To characterize the atomistic failure modes of ettringite, we performed stress-strain simulations to find that Ca-O bonds are responsible for failure of the calcium sulfate and tricalcium aluminate (C3A) column in ettringite during uniaxial compression and tension and that hydrogen bond re-formation during compression induces an increase in plastic strain beyond the material"s stress-strain proportionality limit. Hydrogen 274-282 complement C3 Homo sapiens 199-202 19744646-8 2009 The conformational populations were found to be in good agreement with the limited available NMR data except for the C-2-C-3 torsion (spanned by the O-2-O-4 hydrogen bond), where the NMR data support a more bent structure. Hydrogen 157-165 complement C3 Homo sapiens 121-124 28346703-0 2017 Tunable GLUT-Hexose Binding and Transport via Modulation of Hexose C-3 Hydrogen-Bonding Capabilities. Hydrogen 71-79 complement C3 Homo sapiens 67-70 28346703-2 2017 The presence of a hydrogen bond donor at the C-3 position of 2,5-anhydro-d-mannitol derivatives is essential for effective binding to GLUT5 and transport into tumor cells. Hydrogen 18-26 complement C3 Homo sapiens 45-48 28346703-3 2017 Surprisingly, installation of a group that can function only as a hydrogen bond acceptor at C-3 resulted in selective recognition by GLUT1 rather than GLUT5. Hydrogen 66-74 complement C3 Homo sapiens 92-95 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. Hydrogen 18-26 complement C3 Homo sapiens 107-110 25995909-2 2015 In the crystal, an O-H O hydrogen bond between the hy-droxy groups at the C-3 and C-2 positions connects homochiral mol-ecules into a column along the b axis. Hydrogen 25-33 complement C3 Homo sapiens 74-77 24257095-4 2013 A 77-residue human inflammatory protein (complement C3a) important in innate immunity is rationally transformed to equipotent small molecules, using peptide surrogates that incorporate a turn-inducing heterocycle with correctly positioned hydrogen-bond-accepting atoms. Hydrogen 239-247 complement C3 Homo sapiens 52-55 18493652-2 2008 We synthesized palmitic acid with carbons C-3 through C-16 perdeuterated, C-1 and C-2 with 13C atoms and hydrogens at C-2. Hydrogen 105-114 complement C3 Homo sapiens 42-45 18456336-0 2008 Dynamic structural changes during complement C3 activation analyzed by hydrogen/deuterium exchange mass spectrometry. Hydrogen 71-79 complement C3 Homo sapiens 34-47 16097692-6 2005 When pH>4, the fluorescence emission peak at 499 nm gradually blue-shifted to 455 nm as pH was increasing, and an iso-fluorescence emission point was formed at 484 nm, indicating the dissociation of hydrogen ion of carboxylic acid at C-3. Hydrogen 202-210 complement C3 Homo sapiens 237-240 16106293-7 2005 Together the results reveal that for the "natural" C-2 stereochemistry of 2S-naringenin, C-3 hydroxylation predominates (>9 : 1) over desaturation, probably due to the inaccessibility of the C-2 hydrogen to the iron centre. Hydrogen 198-206 complement C3 Homo sapiens 89-92 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. Hydrogen 133-141 complement C3 Homo sapiens 94-97 12739977-1 2003 Inter- and intramolecular hydrogen bonding of an N-H group in pyrazole complexes was studied using ligands with two different groups at pyrazole C-3 and C-5. Hydrogen 26-34 complement C3 Homo sapiens 145-148 15136842-0 2004 Stereochemistry of hydrogen removal from the "unactivated" C-3 position of 4-hydroxybutyryl-CoA catalysed by 4-hydroxybutyryl-CoA dehydratase. Hydrogen 19-27 complement C3 Homo sapiens 59-62 12739977-4 2003 The significance of the ligands is that by placing a ligating side chain on a ring carbon (C-3), rather than on a ring nitrogen, the ring nitrogen not bound to the metal and its attached proton are available for hydrogen bonding. Hydrogen 212-220 complement C3 Homo sapiens 91-94 11477109-9 2001 Val-349 contacts C-2 and C-3 of EPA and C-4 of LA orienting the carboxyl halves of these substrates so that the omega-ends are aligned properly for hydrogen abstraction. Hydrogen 148-156 complement C3 Homo sapiens 25-28 12228253-2 2002 The high affinity of SHBG for 2-MeOE2 relies primarily on hydrogen bonding between the hydroxyl at C-3 of 2-MeOE2 and Asp(65) and an interaction between the methoxy group at C-2 and the amido group of Asn(82). Hydrogen 58-66 complement C3 Homo sapiens 99-102 12228253-6 2002 The higher affinity of SHBG for estradiol derivatives with a halogen atom at C-2 is due to either enhanced hydrogen bonding between the hydroxyl at C-3 and Asp(65) (2-fluoroestradiol) or accommodation of the functional group at C-2 (2-bromoestradiol), rather than an interaction with Asn(82). Hydrogen 107-115 complement C3 Homo sapiens 148-151 12054929-6 2002 Clearly, DOIS recognizes the G-6-P substrate through specific hydrogen-bonding interactions, i.e., through a hydrogen-donating group for C-2 and an accepting group for C-3 of the substrate. Hydrogen 62-70 complement C3 Homo sapiens 168-171 11674219-2 1999 In monomer experiments employing C-3"-acylthymidine derivatives 2 and 3, a 1:1 mixture of isomers of the H-abstraction products was obtained when the photolysis was carried out in the presence of a hydrogen donor. Hydrogen 198-206 complement C3 Homo sapiens 33-36 11168357-15 2001 Evaluation of the two mutations at His480 allows us to propose that this residue may participate in the aromatization reaction (the third step) by acting as a hydrogen bond donor for the C-3 keto group of the substrate. Hydrogen 159-167 complement C3 Homo sapiens 187-190 11076080-9 2000 Molecular modelling suggests the formation of four hydrogen bonds between the hydroxyl groups at positions C-2, C-3 and C-4 of alpha-D-methyl-mannoside and the bridging and ring nitrogen atoms of the triazine scaffold, with aromatic stacking of a second ligand against the carbohydrate face. Hydrogen 51-59 complement C3 Homo sapiens 112-115