PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25820384-6 2015 After internalization and lysosomal release, Cbl binds to the cytosolic chaperon MMACHC that is responsible for (i) flavin-dependent decyanation of [CN-Co(3+) Cbl to [Co(2+)]Cbl; (ii) glutathione-dependent dealkylation of MeCbl and AdoCbl to [Co(2+/1+)]Cbl; and (iii) glutathione-dependent decyanation of CNCbl or reduction of HOCbl under anaerobic conditions. mecobalamin 222-227 Cbl proto-oncogene Homo sapiens 45-48 26464686-1 2015 Methylmalonic aciduria and homocystinuria, cblC type, is the most common disorder of intracellular vitamin B12 (cobalamin, cbl) metabolism, which results in impaired biosynthesis of methylcobalamin and adenosylcobalamin. mecobalamin 182-197 Cbl proto-oncogene Homo sapiens 43-46 25820384-7 2015 MMACHC shows a broad specificity for Cbl forms and supplies the Cbl(2+) intermediate for synthesis of MeCbl and AdoCbl. mecobalamin 102-107 Cbl proto-oncogene Homo sapiens 37-40 25820384-7 2015 MMACHC shows a broad specificity for Cbl forms and supplies the Cbl(2+) intermediate for synthesis of MeCbl and AdoCbl. mecobalamin 102-107 Cbl proto-oncogene Homo sapiens 64-67 25117994-3 2015 Vitamin B12 (cyancobalamin, Cbl) has two active co-enzyme forms, methylcobalamin (MeCbl) and adenosylcobalamin (AdCbl). mecobalamin 82-87 Cbl proto-oncogene Homo sapiens 28-31 24722857-1 2014 In humans vitamin B12 (cobalamin, Cbl) must be converted into two coenzyme forms, methylcobalamin (MeCbl) and adenosylcobalamin (AdoCbl), in order to maintain intracellular homeostasis of homocysteine and methylmalonic acid, respectively. mecobalamin 82-97 Cbl proto-oncogene Homo sapiens 34-37 24722857-1 2014 In humans vitamin B12 (cobalamin, Cbl) must be converted into two coenzyme forms, methylcobalamin (MeCbl) and adenosylcobalamin (AdoCbl), in order to maintain intracellular homeostasis of homocysteine and methylmalonic acid, respectively. mecobalamin 99-104 Cbl proto-oncogene Homo sapiens 34-37 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. mecobalamin 125-140 Cbl proto-oncogene Homo sapiens 45-48 16464094-1 2006 The electrochemical (EC) reduction mechanism of methylcobalamin (Me-Cbl) in a mixed DMF/MeOH solvent in 0.2 M tetrabutylammonium fluoroborate electrolyte was studied as a function of temperature and solvent ratio vs a nonaqueous Ag/AgCl/Cl(-) reference electrode. mecobalamin 48-63 Cbl proto-oncogene Homo sapiens 68-71 11237251-3 2001 The models of this process show that in both methylcobalamin (CH3Cbl) and AdoCbl, compression of the axial Co-N bond does engender upward folding of the corrin ring, and that the extent of such upward folding is smaller in an analog in which the normal 5,6-dimethylbenzimidazole axial ligand is replaced by the sterically smaller ligand, imidazole (CH3(lm)Cbl and Ado(lm)Cbl). mecobalamin 45-60 Cbl proto-oncogene Homo sapiens 65-68 11375680-1 2001 Glutathionylcobalamin (gamma-glutamylcysteinylglycinylcobalamin; gamma-GluCysGly-Cbl) is a natural product which functions as an intermediate in the biosynthesis of the active B(12) coenzymes adenosylcobalamin and methylcobalamin. mecobalamin 214-229 Cbl proto-oncogene Homo sapiens 81-84 12021520-2 2002 methylcobalamin (Me-Cbl), the coenzymatically active form of vitamin B12 that acts as a cofactor for methionine synthase in the conversion of total homocysteine (tHcy) to methionine, with or without oral folic acid (FA) supplementation, on fasting tHcy levels in hemodialysis (HD) patients. mecobalamin 0-15 Cbl proto-oncogene Homo sapiens 20-23 1744096-2 1991 Methylcobalamin (Me-Cbl) is tightly bound to methionine synthase and is required for enzymatic activity. mecobalamin 0-15 Cbl proto-oncogene Homo sapiens 20-23 1516297-1 1992 Several of the inborn errors of vitamin B12 (cobalamin, Cbl) metabolism (cblC, cblD, cblE, cblF, cblG) are associated with homocystinuria and hypomethioninemia due to a functional deficiency of the cytoplasmic enzyme methionine synthase which requires methylcobalamin (MeCbl) as a cofactor. mecobalamin 252-267 Cbl proto-oncogene Homo sapiens 56-59 1516297-1 1992 Several of the inborn errors of vitamin B12 (cobalamin, Cbl) metabolism (cblC, cblD, cblE, cblF, cblG) are associated with homocystinuria and hypomethioninemia due to a functional deficiency of the cytoplasmic enzyme methionine synthase which requires methylcobalamin (MeCbl) as a cofactor. mecobalamin 269-274 Cbl proto-oncogene Homo sapiens 56-59 3589492-4 1987 Methyl-cobalamin (Me-Cbl) was found only in the sap fraction and could not be detected in the total homogenate. mecobalamin 0-16 Cbl proto-oncogene Homo sapiens 21-24 28538514-3 2017 Cbl is then processed in the cytoplasm and mitochondria by complementation factors leading to its active metabolites; methylcobalamin and 5-deoxyadenosyl-cobalamin. mecobalamin 118-133 Cbl proto-oncogene Homo sapiens 0-3 26799654-4 2016 Total Cbl was significantly lower in older control subjects (> 60 yrs of age), primarily reflecting a >10-fold age-dependent decline in the level of MeCbl. mecobalamin 155-160 Cbl proto-oncogene Homo sapiens 6-9 7282599-6 1981 Methylcobalamin was the most abundant Cbl of milk. mecobalamin 0-15 Cbl proto-oncogene Homo sapiens 38-41 418497-2 1978 Plasma total cobalamin was lower in myeloma patients than in either of the control groups and methylcobalamin (Me-Cbl) was disproportionately reduced. mecobalamin 94-109 Cbl proto-oncogene Homo sapiens 114-117 963297-1 1976 The uptake of 57Co-cyanocobalamin (CN-Cbl) and its conversion to 5-deoxyadenosylcobalamin (Ado-Cbl), methylcobalamin (Me-Cbl), and hydroxocobalamin (OH-Cbl) has been studied in phytohemagglutinin (PHA)-transformed lymphocytes from normal subjects and patients with patients with pernicious anemia. mecobalamin 101-116 Cbl proto-oncogene Homo sapiens 38-41