PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26950611-4 2016 X-ray photoelectron spectroscopy and PCE degradation by cement components (SiO2, Al2O3, and CaO) revealed that both the reduced Co species in Cbl(III) and the presence of Ca in cement played an important role for the enhanced reductive dechlorination of PCE. Cobalt 128-130 Cbl proto-oncogene Homo sapiens 142-145 25994134-2 2015 Formyl-Cbl, acetyl-Cbl, and propionyl-Cbl were decomposed by a NH2OH treatment, forming formo-, aceto-, and propionohydroxamic acids, respectively, which offers a proof for the presence of "activated" acyl groups and for their structures of Co-acyl-Cbls. Cobalt 241-243 Cbl proto-oncogene Homo sapiens 7-10 25994134-2 2015 Formyl-Cbl, acetyl-Cbl, and propionyl-Cbl were decomposed by a NH2OH treatment, forming formo-, aceto-, and propionohydroxamic acids, respectively, which offers a proof for the presence of "activated" acyl groups and for their structures of Co-acyl-Cbls. Cobalt 241-243 Cbl proto-oncogene Homo sapiens 19-22 25994134-2 2015 Formyl-Cbl, acetyl-Cbl, and propionyl-Cbl were decomposed by a NH2OH treatment, forming formo-, aceto-, and propionohydroxamic acids, respectively, which offers a proof for the presence of "activated" acyl groups and for their structures of Co-acyl-Cbls. Cobalt 241-243 Cbl proto-oncogene Homo sapiens 19-22 24206708-2 2014 In this study, cobalt containing compounds, namely Co(II), cyanocobalamin (CN-Cbl) and hydroxylcobalamin (OH-Cbl), were well separated by reversed phase HPLC with a C8-HPLC column as the stationary phase and 8 mmol L(-1) ammonium acetate in 22%v/v methanol solution (pH 4) as the mobile phase using isocratic elution. Cobalt 15-21 Cbl proto-oncogene Homo sapiens 78-81 24206708-2 2014 In this study, cobalt containing compounds, namely Co(II), cyanocobalamin (CN-Cbl) and hydroxylcobalamin (OH-Cbl), were well separated by reversed phase HPLC with a C8-HPLC column as the stationary phase and 8 mmol L(-1) ammonium acetate in 22%v/v methanol solution (pH 4) as the mobile phase using isocratic elution. Cobalt 15-21 Cbl proto-oncogene Homo sapiens 109-112 22568547-9 2012 Charge decomposition analysis (CDA) and extended charge decomposition analysis (ECDA), especially with BP86 shows the similar charge transfer nature of the Co-S bond in GS-Cbl and the Co-C bond in CH(3)Cbl. Cobalt 156-160 Cbl proto-oncogene Homo sapiens 172-175 22568547-9 2012 Charge decomposition analysis (CDA) and extended charge decomposition analysis (ECDA), especially with BP86 shows the similar charge transfer nature of the Co-S bond in GS-Cbl and the Co-C bond in CH(3)Cbl. Cobalt 156-160 Cbl proto-oncogene Homo sapiens 202-205 22568547-9 2012 Charge decomposition analysis (CDA) and extended charge decomposition analysis (ECDA), especially with BP86 shows the similar charge transfer nature of the Co-S bond in GS-Cbl and the Co-C bond in CH(3)Cbl. Cobalt 156-158 Cbl proto-oncogene Homo sapiens 172-175 16441149-6 2006 Considerably faster reactions with Cbl(II) proceed through initial Cbl(II)-RSNO intermediates, which undergo subsequent electron-transfer processes leading to oxidation of the cobalt center and reduction of the nitrosothiol. Cobalt 176-182 Cbl proto-oncogene Homo sapiens 35-38 16834388-1 2006 The 4-coordinate, low-spin cob(I)alamin (Co1+Cbl) species, which can be obtained by heterolytic cleavage of the Co-C bond in methylcobalamin or the two-electron reduction of vitamin B12, is one of the most powerful nucleophiles known to date. Cobalt 41-43 Cbl proto-oncogene Homo sapiens 45-48 16441149-6 2006 Considerably faster reactions with Cbl(II) proceed through initial Cbl(II)-RSNO intermediates, which undergo subsequent electron-transfer processes leading to oxidation of the cobalt center and reduction of the nitrosothiol. Cobalt 176-182 Cbl proto-oncogene Homo sapiens 67-70 16305240-10 2005 Collectively, these observations provide direct evidence that enzymatic Co-C bond activation involves stabilization of the post-homolysis product, Co2+ Cbl, rather than destabilization of the Co3+ Cbl "ground" state. Cobalt 0-2 Cbl proto-oncogene Homo sapiens 152-155 11237251-4 2001 Furthermore, in AdoCbl, this upward folding of the corrin is accompanied by increases in the carbon-cobalt bond length and in the Co-C-C bond angle (which are also less pronounced in Ado(Im)Cbl), and which indicate that the Co-C bond is indeed destabilized by this mechanism. Cobalt 100-106 Cbl proto-oncogene Homo sapiens 19-22 11237251-9 2001 Stretching the Co-C bond to simulate the approach to the transition state was found to result in an upward folding of the corrin ring, a slight decrease in the axial Co-N bond length, a slight displacement of the metal atom from the plane of the equatorial nitrogens towards the "lower" axial ligand, and a decrease in strain energy amounting to about 8 kcal mol(-1) for both AdoCbl and Ado(Im)Cbl. Cobalt 15-17 Cbl proto-oncogene Homo sapiens 379-382