PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 35636585-7 2022 Moreover, we verified the expression of 5 representative genes (ALDH1B1, ACAA2, ACSL3, ADH5, and EHHADH) related to fatty acid degradation pathway by RT-qPCR. Fatty Acids 116-126 acyl-CoA synthetase long chain family member 3 Homo sapiens 80-85 26667767-7 2015 Special mention deserves acyl-CoA synthetase long-chain family member 3 (ACSL3) and endothelial lipase (LIPG), which were downregulated by this stilbene and have been previously associated with fatty acid synthesis and obesity in other tissues. Fatty Acids 194-204 acyl-CoA synthetase long chain family member 3 Homo sapiens 25-71 33077484-10 2021 Our results suggest that the surge of ACSL4 levels by targeting AR signaling increases fatty acyl-CoAs biosynthesis and protein myristoylation, indicating the opposite yet complementary or Yin-Yang regulation of ACSL3 and 4 levels in sustaining fatty acid metabolism when targeting androgen-AR signaling. Fatty Acids 245-255 acyl-CoA synthetase long chain family member 3 Homo sapiens 212-223 33077484-12 2021 Implications: Androgen receptor coordinately regulates the expression of ACSL3 and ACSL4, such that AR pathway-independent prostate tumors become dependent on ACSL4-mediated fatty acid metabolism. Fatty Acids 174-184 acyl-CoA synthetase long chain family member 3 Homo sapiens 73-78 27477280-4 2016 We report that mutant KRAS regulates intracellular fatty acid metabolism through Acyl-coenzyme A (CoA) synthetase long-chain family member 3 (ACSL3), which converts fatty acids into fatty Acyl-CoA esters, the substrates for lipid synthesis and beta-oxidation. Fatty Acids 51-61 acyl-CoA synthetase long chain family member 3 Homo sapiens 142-147 27477280-4 2016 We report that mutant KRAS regulates intracellular fatty acid metabolism through Acyl-coenzyme A (CoA) synthetase long-chain family member 3 (ACSL3), which converts fatty acids into fatty Acyl-CoA esters, the substrates for lipid synthesis and beta-oxidation. Fatty Acids 165-176 acyl-CoA synthetase long chain family member 3 Homo sapiens 142-147 27477280-6 2016 Furthermore, mutant KRAS promotes the cellular uptake, retention, accumulation, and beta-oxidation of fatty acids in lung cancer cells in an ACSL3-dependent manner. Fatty Acids 102-113 acyl-CoA synthetase long chain family member 3 Homo sapiens 141-146 29526665-9 2018 Subcellular fractionation showed that at least 68% of ACSL3 remain at the ER even during extensive fatty acid supplementation. Fatty Acids 99-109 acyl-CoA synthetase long chain family member 3 Homo sapiens 54-59 26582048-5 2016 The mRNA levels of enzymes involved in fatty acid metabolism and beta-oxidation (ACSL1, ACSL3, CPT1, CPT2 and KAT) in Day-7 blastocysts were significantly upregulated by the addition of LR-BSA. Fatty Acids 39-49 acyl-CoA synthetase long chain family member 3 Homo sapiens 88-93 26667767-7 2015 Special mention deserves acyl-CoA synthetase long-chain family member 3 (ACSL3) and endothelial lipase (LIPG), which were downregulated by this stilbene and have been previously associated with fatty acid synthesis and obesity in other tissues. Fatty Acids 194-204 acyl-CoA synthetase long chain family member 3 Homo sapiens 73-78 22357706-3 2012 Fluorescence microscopy showed that ACSL3 is localized to the endoplasmic reticulum (ER) and LDs, with the distribution dependent on the cell type and the supply of fatty acids. Fatty Acids 165-176 acyl-CoA synthetase long chain family member 3 Homo sapiens 36-41 26118123-7 2015 Results showed that melanomas upregulated PPARGC1A transcription factor and its target genes regulating synthesis of fatty acids (SCD) and complex lipids (FABP3 and ACSL3). Fatty Acids 117-128 acyl-CoA synthetase long chain family member 3 Homo sapiens 165-170 23762027-8 2013 We show that activation of fatty acid import is linked to the up-regulation of cellular long chain acyl-CoA synthetase activity and identify the long chain acyl-CoA syntheatse3 (Acsl3) as a novel host factor required for polio replication. Fatty Acids 27-37 acyl-CoA synthetase long chain family member 3 Homo sapiens 178-183 22357706-7 2012 ACSL3 was effectively translocated from the ER to nascent LDs when neutral lipid synthesis was stimulated by the external addition of fatty acids. Fatty Acids 134-145 acyl-CoA synthetase long chain family member 3 Homo sapiens 0-5 22357706-8 2012 Cellular fatty acid uptake was increased by overexpression and reduced by RNA interference of ACSL3. Fatty Acids 9-19 acyl-CoA synthetase long chain family member 3 Homo sapiens 94-99 22357706-10 2012 ACSL3 not only esterifies fatty acids with CoA but is also involved in the cellular uptake of fatty acids, presumably indirectly by metabolic trapping. Fatty Acids 26-37 acyl-CoA synthetase long chain family member 3 Homo sapiens 0-5 22357706-10 2012 ACSL3 not only esterifies fatty acids with CoA but is also involved in the cellular uptake of fatty acids, presumably indirectly by metabolic trapping. Fatty Acids 94-105 acyl-CoA synthetase long chain family member 3 Homo sapiens 0-5 20308079-1 2010 ACSL3 is a member of the long chain acyl-CoA synthetase (ACSL) family that plays key roles in fatty acid metabolism in various tissues in an isozyme-specific manner. Fatty Acids 94-104 acyl-CoA synthetase long chain family member 3 Homo sapiens 0-5 20219900-7 2010 Our results suggest that LXR plays a regulatory role in fatty acid metabolism by direct regulation of ACSL3 in human placental trophoblast cells. Fatty Acids 56-66 acyl-CoA synthetase long chain family member 3 Homo sapiens 102-107 18003621-4 2008 In cultured human hepatoma Huh7 cells, ACSL3 is specifically required for incorporation of fatty acids into phosphatidylcholine. Fatty Acids 91-102 acyl-CoA synthetase long chain family member 3 Homo sapiens 39-44 15556626-1 2004 FAS and FACL3 are enzymes of fatty acid metabolism. Fatty Acids 29-39 acyl-CoA synthetase long chain family member 3 Homo sapiens 8-13 17761945-6 2007 We further show that overexpression of ACSL3 or ACSL5 alone in the absence of OM led to fatty acid partitioning into beta-oxidation. Fatty Acids 88-98 acyl-CoA synthetase long chain family member 3 Homo sapiens 39-44 17761945-7 2007 Importantly, we demonstrate that transfection of siRNAs targeted to ACSL3 and ACSL5 abrogated the enhancing effect of OM on fatty acid oxidation in HepG2 cells. Fatty Acids 124-134 acyl-CoA synthetase long chain family member 3 Homo sapiens 68-73 17761945-8 2007 CONCLUSIONS: These new findings identify ACSL3 and ACSL5 as OM-regulated genes that function in fatty acid metabolism and suggest a novel cellular mechanism by which OM directly lowers the plasma TG in hyperlipidemic animals through stimulating the transcription of ACSL specific isoforms in the liver. Fatty Acids 96-106 acyl-CoA synthetase long chain family member 3 Homo sapiens 41-46