PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9972874-0 1999 Fatty acid composition of myelin proteolipid protein during vertebrate evolution. Fatty Acids 0-10 proteolipid protein 1 Homo sapiens 26-52 22778864-4 2011 Proteolipid protein (PLP), an important transmembrane protein component of myelin, has six cysteine residues acylated, via thioester linkages, with fatty acids, usually palmitic, that contribute to the stability of myelin. Fatty Acids 148-159 proteolipid protein 1 Homo sapiens 0-19 22778864-4 2011 Proteolipid protein (PLP), an important transmembrane protein component of myelin, has six cysteine residues acylated, via thioester linkages, with fatty acids, usually palmitic, that contribute to the stability of myelin. Fatty Acids 148-159 proteolipid protein 1 Homo sapiens 21-24 14643750-1 2004 In this study, the role of exogenous fatty acids in the regulation of proteolipid protein (PLP) gene expression was investigated using the following model culture system: C6 glioma cells expressing the green-fluorescent protein (eGFP) driven by different segments of PLP promoter. Fatty Acids 37-48 proteolipid protein 1 Homo sapiens 91-94 14643750-4 2004 PLP promoter activation was dependent on fatty acid concentration, with maximum activation at 200 microM. Fatty Acids 41-51 proteolipid protein 1 Homo sapiens 0-3 1281423-5 1992 The extreme hydrophobicity of PLP can therefore be explained by two structural features: a composition of approximately 50% apolar amino acid residues and a high degree of fatty acid acylation. Fatty Acids 172-182 proteolipid protein 1 Homo sapiens 30-33 1281423-0 1992 Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP. Fatty Acids 82-92 proteolipid protein 1 Homo sapiens 0-19 2464071-5 1988 When PLP was acylated with acyl-CoA as the fatty acid donor, the reaction occurred non-enzymatically as supported by the following observations: 1) acylation activity increased with increasing pH above pH 7.5, 2) acylation activity was heat stable, 3) acylation activity was not removed from PLP during purification in organic solvents or in Triton X-100-containing buffers, and 4) acylation of tryptic fragments occurred in the absence of an exogenously added enzyme source. Fatty Acids 43-53 proteolipid protein 1 Homo sapiens 5-8 1281423-0 1992 Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP. Fatty Acids 82-92 proteolipid protein 1 Homo sapiens 21-24 1704424-0 1991 Fatty acid composition of human myelin proteolipid protein in peroxisomal disorders. Fatty Acids 0-10 proteolipid protein 1 Homo sapiens 32-58 1704424-2 1991 In this study, the amount and composition of fatty acids covalently bound to human myelin PLP were determined during development and in peroxisomal disorders. Fatty Acids 45-56 proteolipid protein 1 Homo sapiens 90-93 1704424-6 1991 The total amount of fatty acid bound to PLP was not altered in any of the pathological cases examined. Fatty Acids 20-30 proteolipid protein 1 Homo sapiens 40-43 1704424-11 1991 The results indicate that, although a characteristic PLP fatty acid pattern is normally maintained, changes in the acyl chain pool can ultimately be reflected in the fatty acid composition of the protein. Fatty Acids 57-67 proteolipid protein 1 Homo sapiens 53-56 1700070-1 1990 Myelin proteolipid protein (PLP) is known to contain long-chain, covalently bound fatty acids. Fatty Acids 82-93 proteolipid protein 1 Homo sapiens 0-26 1700070-1 1990 Myelin proteolipid protein (PLP) is known to contain long-chain, covalently bound fatty acids. Fatty Acids 82-93 proteolipid protein 1 Homo sapiens 28-31 1700070-2 1990 Previous studies, including our own, have suggested the occurrence of an oxyester type of linkage between fatty acids and PLP. Fatty Acids 106-117 proteolipid protein 1 Homo sapiens 122-125 1700070-10 1990 These results demonstrate that a large proportion of fatty acids covalently bound to PLP are liked to -SH groups. Fatty Acids 53-64 proteolipid protein 1 Homo sapiens 85-88 34739144-3 2022 Here, using structural and bioinformatics information, we propose that there are proteins that also contain "MmpL3-like" (MMPL) transmembrane (TM) domains in many protozoa, including Trypanosoma cruzi, as well as in the bacterium Staphylococcus aureus, where the fatty acid transporter FarE has the same set of "active-site" residues as those found in the mycobacterial MmpL3s, and in T. cruzi. Fatty Acids 263-273 proteolipid protein 1 Homo sapiens 122-126 34739144-6 2022 Overall, the results are of interest since they show that MMPL-family proteins are present in essentially all life-forms: archaea, bacteria, protozoa, fungi, plants and animals and, where known, they are involved in "lipid" (glycolipid, phospholipid, sphingolipid, fatty acid, cholesterol, ergosterol) transport, powered by transmembrane molecular pumps having similar structures. Fatty Acids 265-275 proteolipid protein 1 Homo sapiens 58-62 2416880-4 1986 Omission of ATP, CoA, Mg2+, or all three reduced fatty acid incorporation into PLP to 44, 27, 8, and 4%, respectively, of the values in the complete system. Fatty Acids 49-59 proteolipid protein 1 Homo sapiens 79-82 2432924-1 1986 The effect of covalently bound fatty acid on the conformation of the myelin proteolipid protein has been studied by ultraviolet and intrinsic fluorescence spectroscopy. Fatty Acids 31-41 proteolipid protein 1 Homo sapiens 69-95 2416880-1 1986 The immediate acyl chain donor for fatty acid esterification of proteolipid protein (PLP) was identified in an in vitro system. Fatty Acids 35-45 proteolipid protein 1 Homo sapiens 64-83 2416880-1 1986 The immediate acyl chain donor for fatty acid esterification of proteolipid protein (PLP) was identified in an in vitro system. Fatty Acids 35-45 proteolipid protein 1 Homo sapiens 85-88