PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2443494-0 1987 Autoacylation of myelin proteolipid protein with acyl coenzyme A. Rat brain myelin proteolipid protein (PLP) is known to contain long chain, covalently bound fatty acids. Fatty Acids 158-169 proteolipid protein 1 Rattus norvegicus 17-43 2443494-0 1987 Autoacylation of myelin proteolipid protein with acyl coenzyme A. Rat brain myelin proteolipid protein (PLP) is known to contain long chain, covalently bound fatty acids. Fatty Acids 158-169 proteolipid protein 1 Rattus norvegicus 76-102 2443494-0 1987 Autoacylation of myelin proteolipid protein with acyl coenzyme A. Rat brain myelin proteolipid protein (PLP) is known to contain long chain, covalently bound fatty acids. Fatty Acids 158-169 proteolipid protein 1 Rattus norvegicus 104-107 2446598-8 1987 The cell-free system exhibits specificity with respect to the chain length of the fatty acids, since myristic acid is incorporated into PLP at a lower rate when compared with palmitic and oleic acids. Fatty Acids 82-93 proteolipid protein 1 Rattus norvegicus 136-139 2446598-9 1987 The acylation of PLP is an enzymic reaction, since (1) maximum incorporation of [3H]palmitic acid into PLP occurred at physiological temperatures and decreased with an increase in the temperature; (2) acylation of PLP with [3H]palmitic acid and [14C]palmitoyl-CoA was severely inhibited by SDS (0.05%); and (3) the incorporation of fatty acid and palmitoyl-CoA into PLP was substantially decreased by the process of freezing-thawing and freeze-drying of myelin. Fatty Acids 332-342 proteolipid protein 1 Rattus norvegicus 17-20 2446598-9 1987 The acylation of PLP is an enzymic reaction, since (1) maximum incorporation of [3H]palmitic acid into PLP occurred at physiological temperatures and decreased with an increase in the temperature; (2) acylation of PLP with [3H]palmitic acid and [14C]palmitoyl-CoA was severely inhibited by SDS (0.05%); and (3) the incorporation of fatty acid and palmitoyl-CoA into PLP was substantially decreased by the process of freezing-thawing and freeze-drying of myelin. Fatty Acids 332-342 proteolipid protein 1 Rattus norvegicus 103-106 2446598-9 1987 The acylation of PLP is an enzymic reaction, since (1) maximum incorporation of [3H]palmitic acid into PLP occurred at physiological temperatures and decreased with an increase in the temperature; (2) acylation of PLP with [3H]palmitic acid and [14C]palmitoyl-CoA was severely inhibited by SDS (0.05%); and (3) the incorporation of fatty acid and palmitoyl-CoA into PLP was substantially decreased by the process of freezing-thawing and freeze-drying of myelin. Fatty Acids 332-342 proteolipid protein 1 Rattus norvegicus 103-106 2446598-9 1987 The acylation of PLP is an enzymic reaction, since (1) maximum incorporation of [3H]palmitic acid into PLP occurred at physiological temperatures and decreased with an increase in the temperature; (2) acylation of PLP with [3H]palmitic acid and [14C]palmitoyl-CoA was severely inhibited by SDS (0.05%); and (3) the incorporation of fatty acid and palmitoyl-CoA into PLP was substantially decreased by the process of freezing-thawing and freeze-drying of myelin. Fatty Acids 332-342 proteolipid protein 1 Rattus norvegicus 103-106 2446598-11 1987 Acylation of PLP in a cell-free system with fatty acids and palmitoyl-CoA suggests that a presynthesized pool of non-acylated PLP and DM-20 is available for acylation. Fatty Acids 44-55 proteolipid protein 1 Rattus norvegicus 13-16 2426408-0 1986 Acylation of rat brain myelin proteolipid protein with different fatty acids. Fatty Acids 65-76 proteolipid protein 1 Rattus norvegicus 23-49 3818589-9 1987 The product of the reaction was identified as myelin proteolipid protein and the fatty acid was shown to be attached to the protein via an ester linkage. Fatty Acids 81-91 proteolipid protein 1 Rattus norvegicus 46-72 2426408-7 1986 This is consistent with the fatty acid composition of the isolated PLP. Fatty Acids 28-38 proteolipid protein 1 Rattus norvegicus 67-70 20488092-4 1984 Experiments using time staggered injections of (14)C- and (3)H-labeled palmitic acid also showed that entry of the fatty acid into PLP of the various subfractions was simultaneous. Fatty Acids 115-125 proteolipid protein 1 Rattus norvegicus 131-134 2416880-0 1986 Fatty acid acylation of rat brain myelin proteolipid protein in vitro: identification of the lipid donor. Fatty Acids 0-10 proteolipid protein 1 Rattus norvegicus 34-60 7107590-1 1982 The incorporation of fatty acid into myelin proteolipid protein (PLP) was studied by incubating brain slices from 17-day-old rats with [9,10-3H]palmitic acid. Fatty Acids 21-31 proteolipid protein 1 Rattus norvegicus 37-63 7107590-1 1982 The incorporation of fatty acid into myelin proteolipid protein (PLP) was studied by incubating brain slices from 17-day-old rats with [9,10-3H]palmitic acid. Fatty Acids 21-31 proteolipid protein 1 Rattus norvegicus 65-68 7068653-3 1982 Most of the radioactivity associated with PLP was removed when the gels were treated with hydroxylamine and then fluorographed, indicating that fatty acids were bound to PLP by ester linkage. Fatty Acids 144-155 proteolipid protein 1 Rattus norvegicus 42-45 7068653-3 1982 Most of the radioactivity associated with PLP was removed when the gels were treated with hydroxylamine and then fluorographed, indicating that fatty acids were bound to PLP by ester linkage. Fatty Acids 144-155 proteolipid protein 1 Rattus norvegicus 170-173 7068653-6 1982 Gas-liquid chromatography of the fatty acids associated with PLP distinctly revealed the presence of methyl palmitate and a detectable peak of methyl stearate. Fatty Acids 33-44 proteolipid protein 1 Rattus norvegicus 61-64 1560018-1 1992 A protein fatty acylesterase activity that catalyzes the removal of fatty acid from exogenous proteolipid protein (PLP) has been demonstrated in isolated rat brain myelin. Fatty Acids 68-78 proteolipid protein 1 Rattus norvegicus 94-113 10823577-2 2000 In this study, the amount and pattern of fatty acids covalently bound to rat PLP were determined during brain development and in myelin subfractions. Fatty Acids 41-52 proteolipid protein 1 Rattus norvegicus 77-80 10823577-4 2000 At all ages examined, PLP had the same amount of covalently-bound fatty acids (3-4% w/w) and palmitate, oleate and stearate were always the major acyl chains. Fatty Acids 66-77 proteolipid protein 1 Rattus norvegicus 22-25 10823577-5 2000 In contrast to myelin lipids, the fatty acid composition of PLP showed only minor changes between 15-days and 90-days of age. Fatty Acids 34-44 proteolipid protein 1 Rattus norvegicus 60-63 10823577-6 2000 The amount and pattern of fatty acids bound to PLP prepared from three myelin subfractions were also indistinguishable. Fatty Acids 26-37 proteolipid protein 1 Rattus norvegicus 47-50 10823577-7 2000 The conservation of a characteristic PLP-fatty acid make-up during brain development and in various myelin compartments suggests that this post-translational modification is essential for the normal functioning of the protein. Fatty Acids 41-51 proteolipid protein 1 Rattus norvegicus 37-40 9417076-1 1998 Proteolipid protein (PLP), the major protein of central nervous system myelin, contains covalently bound fatty acids, predominantly palmitic acid. Fatty Acids 105-116 proteolipid protein 1 Rattus norvegicus 0-19 9417076-1 1998 Proteolipid protein (PLP), the major protein of central nervous system myelin, contains covalently bound fatty acids, predominantly palmitic acid. Fatty Acids 105-116 proteolipid protein 1 Rattus norvegicus 21-24 9417076-7 1998 The uptake of 18O into the carbonyl groups of fatty acids derived from PLP, phospholipids, and the free fatty acid pool was measured by gas-liquid chromatography/mass spectrometry of the respective methyl esters. Fatty Acids 46-57 proteolipid protein 1 Rattus norvegicus 71-74 11700955-5 2001 The amount of fatty acids bound to PLP and the rate of deacylation were unaffected by NO. Fatty Acids 14-25 proteolipid protein 1 Rattus norvegicus 35-38 10349873-7 1999 Determination of the number of PLP molecules modified by each of these reactions during development suggests that the ATP-dependent process is important during the formation and/or compaction of the myelin sheath, whereas the ATP-independent mechanism is likely to play a role in myelin maintenance, perhaps by participating in the periodic repair of thioester linkages between the fatty acids and the protein. Fatty Acids 382-393 proteolipid protein 1 Rattus norvegicus 31-34 1560018-6 1992 The myelin-associated protein fatty acylesterase was present throughout brain development and in all myelin subfractions, in agreement with the dynamic metabolism of PLP-bound fatty acids. Fatty Acids 176-187 proteolipid protein 1 Rattus norvegicus 166-169 1560018-1 1992 A protein fatty acylesterase activity that catalyzes the removal of fatty acid from exogenous proteolipid protein (PLP) has been demonstrated in isolated rat brain myelin. Fatty Acids 68-78 proteolipid protein 1 Rattus norvegicus 115-118 1894605-0 1991 Rapid metabolism of fatty acids covalently bound to myelin proteolipid protein. Fatty Acids 20-31 proteolipid protein 1 Rattus norvegicus 59-78 1894605-1 1991 Proteolipid protein (PLP), the major protein of central nervous system myelin, contains approximately 2 mol of covalently bound fatty acids. Fatty Acids 128-139 proteolipid protein 1 Rattus norvegicus 0-19 1894605-1 1991 Proteolipid protein (PLP), the major protein of central nervous system myelin, contains approximately 2 mol of covalently bound fatty acids. Fatty Acids 128-139 proteolipid protein 1 Rattus norvegicus 21-24 1894605-3 1991 The apparent half-life of total fatty acids bound to PLP was approximately 7 days. Fatty Acids 32-43 proteolipid protein 1 Rattus norvegicus 53-56 1894605-10 1991 Finally, pulse-chase experiments in a cell-free system showed that PLP-bound fatty acids turn over with a half-life shorter than 10 min. Fatty Acids 77-88 proteolipid protein 1 Rattus norvegicus 67-70