메뉴 건너뛰기




Volumn 192, Issue 1-2, 1999, Pages 95-103

Role of acylCoA binding protein in acylCoA transport, metabolism and cell signaling

Author keywords

ACBP; AcylCoA; AcylCoA binding protein; Regulation and cell signaling; Transport

Indexed keywords

ACYL COENZYME A; FATTY ACID BINDING PROTEIN; PALMITOYL COENZYME A HYDROLASE; RECEPTOR; STEROL CARRIER PROTEIN 2;

EID: 0032960138     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-1-4615-4929-1_11     Document Type: Conference Paper
Times cited : (114)

References (88)
  • 1
    • 0030897513 scopus 로고    scopus 로고
    • The role of long-chain fatty acids in regulation of metabolism and in cell signalling
    • Færgemann NJ, Knudsen J: The role of long-chain fatty acids in regulation of metabolism and in cell signalling. Biochem J 323: 1-12, 1997
    • (1997) Biochem J , vol.323 , pp. 1-12
    • Færgemann, N.J.1    Knudsen, J.2
  • 3
    • 0029751076 scopus 로고    scopus 로고
    • Sterol carrier protein-2 a new fatty acid coenzyme A-binding protein
    • Frolow A, Cho T, Billheimer JT, Schroeder F: Sterol carrier protein-2 a new fatty acid coenzyme A-binding protein. J Biol Chem 271: 31878-31884, 1996
    • (1996) J Biol Chem , vol.271 , pp. 31878-31884
    • Frolow, A.1    Cho, T.2    Billheimer, J.T.3    Schroeder, F.4
  • 4
    • 0030239495 scopus 로고    scopus 로고
    • Cellular fatty acid-binding proteins: Their function and physiological significance
    • Glatz JFC, van der Vusse GJ: Cellular fatty acid-binding proteins: Their function and physiological significance. Prog Lipid Res 35:243-282, 1996
    • (1996) Prog Lipid Res , vol.35 , pp. 243-282
    • Glatz, J.F.C.1    Van Der Vusse, G.J.2
  • 5
    • 0015922248 scopus 로고
    • Reversal by CoA of palmityl-CoA inhibition of long chain acyl-CoA synthetase activity
    • Pande SV: Reversal by CoA of palmityl-CoA inhibition of long chain acyl-CoA synthetase activity. Biochim Biophys Acta 306: 15-20, 1973
    • (1973) Biochim Biophys Acta , vol.306 , pp. 15-20
    • Pande, S.V.1
  • 6
    • 0018718907 scopus 로고
    • Intracellular localization of long-chain acyl-coenzyme A hydrolase and acyl-L-carnitine hydrolase in brown adipose tissue from guinea pigs
    • Berge RK, Slinde E, Farstad M: Intracellular localization of long-chain acyl-coenzyme A hydrolase and acyl-L-carnitine hydrolase in brown adipose tissue from guinea pigs. Biochem J 182: 347-351, 1979
    • (1979) Biochem J , vol.182 , pp. 347-351
    • Berge, R.K.1    Slinde, E.2    Farstad, M.3
  • 7
    • 0023148729 scopus 로고
    • A novel acyl-CoA-binding protein from bovine liver. Effect on fatty acid synthesis
    • Mogensen IB, Schulenberg H, Hansen HO, Spener F, Knudsen J: A novel acyl-CoA-binding protein from bovine liver. Effect on fatty acid synthesis. Biochem J 214: 189-192, 1987
    • (1987) Biochem J , vol.214 , pp. 189-192
    • Mogensen, I.B.1    Schulenberg, H.2    Hansen, H.O.3    Spener, F.4    Knudsen, J.5
  • 8
  • 9
    • 0023657108 scopus 로고
    • Acyl-CoA-binding protein from cow. Binding characteristics and cellular and tissue distribution
    • Mikkelsen J, Knudsen J: Acyl-CoA-binding protein from cow. Binding characteristics and cellular and tissue distribution. Biochem J 248: 709-714, 1987
    • (1987) Biochem J , vol.248 , pp. 709-714
    • Mikkelsen, J.1    Knudsen, J.2
  • 10
    • 0028929410 scopus 로고
    • Detection of acyl-CoA-binding protein in human red blood cells and investigation of its role in membrane phospholipid renewal
    • Fyrst H, Knudsen J, Schott MA, Lubin BH, Kuypers FA: Detection of acyl-CoA-binding protein in human red blood cells and investigation of its role in membrane phospholipid renewal. Biochem J 306: 793-799, 1995
    • (1995) Biochem J , vol.306 , pp. 793-799
    • Fyrst, H.1    Knudsen, J.2    Schott, M.A.3    Lubin, B.H.4    Kuypers, F.A.5
  • 11
    • 0022363286 scopus 로고
    • Diazepam-binding inhibitor: A neuropeptide located in selected neuronal populations of rat brain
    • Alho HE, Costa P, Ferrero M, Fujimoto D, Cosenza Murphy, Guidotti A: Diazepam-binding inhibitor: A neuropeptide located in selected neuronal populations of rat brain. Science 229: 179-182, 1985
    • (1985) Science , vol.229 , pp. 179-182
    • Alho, H.E.1    Costa, P.2    Ferrero, M.3    Fujimoto, D.4    Murphy, C.5    Guidotti, A.6
  • 12
    • 0025300030 scopus 로고
    • Distribution and characterization of diazepam binding inhibitor (DBI) in peripheral tissues of rat
    • Bovolin P, Schlichting J, Miyata M, Ferrarese C, Guidotti A, Alho H: Distribution and characterization of diazepam binding inhibitor (DBI) in peripheral tissues of rat. Regul Pept 29: 267-281, 1990
    • (1990) Regul Pept , vol.29 , pp. 267-281
    • Bovolin, P.1    Schlichting, J.2    Miyata, M.3    Ferrarese, C.4    Guidotti, A.5    Alho, H.6
  • 13
    • 0030606865 scopus 로고    scopus 로고
    • A novel endozepine-like peptide (ELP) is exclusively expressed in male germ cells
    • Pusch W, Balvers M, Hunt N, Ivell R: A novel endozepine-like peptide (ELP) is exclusively expressed in male germ cells. Mol Cell Endocrinol 122: 69-80, 1996
    • (1996) Mol Cell Endocrinol , vol.122 , pp. 69-80
    • Pusch, W.1    Balvers, M.2    Hunt, N.3    Ivell, R.4
  • 14
    • 0028108974 scopus 로고
    • Tissue-specific expression of diazepam-binding inhibitor in Drosophila melanogaster: Cloning, structure, and localization of the gene
    • Kolmer M, Roos C, Tirronen M, Myohanen S, Alho H: Tissue-specific expression of diazepam-binding inhibitor in Drosophila melanogaster: Cloning, structure, and localization of the gene. Mol Cell Biol 14: 6983-6995, 1994
    • (1994) Mol Cell Biol , vol.14 , pp. 6983-6995
    • Kolmer, M.1    Roos, C.2    Tirronen, M.3    Myohanen, S.4    Alho, H.5
  • 16
    • 0029794153 scopus 로고    scopus 로고
    • Probing the nature of noncovalent interations by mass spectrometry. A study of protein-CoA ligand binding and assembly
    • Robinson CV, Chung EW, Kragelund BB, Knudsen J, Aplin RT, Poulsen FM, Dobson CM: Probing the nature of noncovalent interations by mass spectrometry. A study of protein-CoA ligand binding and assembly. J Am Chem Soc 118: 8646-8653, 1996
    • (1996) J Am Chem Soc , vol.118 , pp. 8646-8653
    • Robinson, C.V.1    Chung, E.W.2    Kragelund, B.B.3    Knudsen, J.4    Aplin, R.T.5    Poulsen, F.M.6    Dobson, C.M.7
  • 17
    • 0027289149 scopus 로고
    • Three-dimensional structure of the complex between acyl-coenzyme A binding protein and palmitoyl-coenzyme A
    • Kragelund BB, Andersen KV, Madsen JC, Knudsen J, Poulsen FM: Three-dimensional structure of the complex between acyl-coenzyme A binding protein and palmitoyl-coenzyme A. J Mol Biol 230: 1260-1277, 1993
    • (1993) J Mol Biol , vol.230 , pp. 1260-1277
    • Kragelund, B.B.1    Andersen, K.V.2    Madsen, J.C.3    Knudsen, J.4    Poulsen, F.M.5
  • 18
    • 0029807051 scopus 로고    scopus 로고
    • Thermodynamics of ligand binding to acyl-coenzyme A binding protein studied by titration calorimetry
    • Færgeman NJ, Sigurskjold BW, Kragelund BB, Andersen KV, Knudsen J: Thermodynamics of ligand binding to acyl-coenzyme A binding protein studied by titration calorimetry. Biochemistry 35: 14118-14126, 1996
    • (1996) Biochemistry , vol.35 , pp. 14118-14126
    • Færgeman, N.J.1    Sigurskjold, B.W.2    Kragelund, B.B.3    Andersen, K.V.4    Knudsen, J.5
  • 19
    • 0025061083 scopus 로고
    • Comparison of the binding affinities of acyl-CoA-binding protein and fatty-acid-binding protein for long-chain acyl-CoA esters
    • Rasmussen JT, Borchers T, Knudsen J: Comparison of the binding affinities of acyl-CoA-binding protein and fatty-acid-binding protein for long-chain acyl-CoA esters. Biochem J 265: 849-855, 1990
    • (1990) Biochem J , vol.265 , pp. 849-855
    • Rasmussen, J.T.1    Borchers, T.2    Knudsen, J.3
  • 20
    • 0027534461 scopus 로고
    • Characterization of ligand binding to acyl-CoA-binding protein
    • Rosendal J, Ertbjerg P, Knudsen J: Characterization of ligand binding to acyl-CoA-binding protein. Biochem J 290: 321-326, 1993
    • (1993) Biochem J , vol.290 , pp. 321-326
    • Rosendal, J.1    Ertbjerg, P.2    Knudsen, J.3
  • 21
    • 0027295334 scopus 로고
    • Interation of acyl-CoA binding protein (ACBP) on processes for which acyl-CoA is a substrate, product or inhibitor
    • Rasmussen JT, Rosendal J, Knudsen J: Interation of acyl-CoA binding protein (ACBP) on processes for which acyl-CoA is a substrate, product or inhibitor. Biochem J 292: 907-913, 1993
    • (1993) Biochem J , vol.292 , pp. 907-913
    • Rasmussen, J.T.1    Rosendal, J.2    Knudsen, J.3
  • 23
    • 0027531656 scopus 로고
    • Effect of heterologous expression of acyl-CoA-binding protein on acyl-CoA level and composition in yeast
    • Mandrup S, Jepsen R, Skott H, Rosendal J, Hojrup P, Kristiansen K, Knudsen J: Effect of heterologous expression of acyl-CoA-binding protein on acyl-CoA level and composition in yeast. Biochem J 290: 369-374, 1993
    • (1993) Biochem J , vol.290 , pp. 369-374
    • Mandrup, S.1    Jepsen, R.2    Skott, H.3    Rosendal, J.4    Hojrup, P.5    Kristiansen, K.6    Knudsen, J.7
  • 24
    • 0029787239 scopus 로고    scopus 로고
    • Disruption of the gene encoding the acyl-CoA-binding protein (ACBl) perturbs acyl-CoA metabolism in Saccharomyces cerevisiae
    • Schjerling CK, Hummel R, Hansen JK, Borsting C, Mikkelsen JM, Kristiansen K, Knudsen J: Disruption of the gene encoding the acyl-CoA-binding protein (ACBl) perturbs acyl-CoA metabolism in Saccharomyces cerevisiae. J Biol Chem 271: 22514-22521, 1996
    • (1996) J Biol Chem , vol.271 , pp. 22514-22521
    • Schjerling, C.K.1    Hummel, R.2    Hansen, J.K.3    Borsting, C.4    Mikkelsen, J.M.5    Kristiansen, K.6    Knudsen, J.7
  • 25
    • 0343059870 scopus 로고
    • The inhibition of acetyl CoA carboxylase by long chaing acylCoA derivatives
    • Bortz WM, Lynen F: The inhibition of acetyl CoA carboxylase by long chaing acylCoA derivatives. Biochemische Zeitschrift 337: 505-509, 1963
    • (1963) Biochemische Zeitschrift , vol.337 , pp. 505-509
    • Bortz, W.M.1    Lynen, F.2
  • 26
    • 0026689241 scopus 로고
    • The effect of methyl-lidocain on the biosynthesis of phospholipds de novo in the isolated hamster heart
    • Tardi PG, Man RY, Choy PC: The effect of methyl-lidocain on the biosynthesis of phospholipds de novo in the isolated hamster heart. Biochem J 285: 161-166, 1992
    • (1992) Biochem J , vol.285 , pp. 161-166
    • Tardi, P.G.1    Man, R.Y.2    Choy, P.C.3
  • 27
    • 0026476541 scopus 로고
    • A fast and versatile method for extraction and quantitation of long-chain acyl-CoA esters from tissue: Content of individual long-chain acyl-CoA esters in various tissues from fed rat
    • Rosendal J, Knudsen J: A fast and versatile method for extraction and quantitation of long-chain acyl-CoA esters from tissue: Content of individual long-chain acyl-CoA esters in various tissues from fed rat. Anal Biochem 207: 63-67, 1992
    • (1992) Anal Biochem , vol.207 , pp. 63-67
    • Rosendal, J.1    Knudsen, J.2
  • 28
    • 0024987159 scopus 로고
    • Acyl CoAregulation of metabolism and signal transduction
    • Corkey BE, Deeney JT: Acyl CoAregulation of metabolism and signal transduction. Prog Clin Biol Res 321: 217-232, 1990
    • (1990) Prog Clin Biol Res , vol.321 , pp. 217-232
    • Corkey, B.E.1    Deeney, J.T.2
  • 29
    • 0028094479 scopus 로고
    • Induction of hepatic acyl-CoA-binding protein and liver fatty acid-binding protein by perfluorodecanoic acid in rats. Lack of correlation with hepatic long-chain acyl-CoA levels
    • Sterchele PF, van den Heuvel JP, Davis W, Shrago E, Knudsen J, Peterson RE: Induction of hepatic acyl-CoA-binding protein and liver fatty acid-binding protein by perfluorodecanoic acid in rats. Lack of correlation with hepatic long-chain acyl-CoA levels. Biochem Pharmacol 48: 955-966, 1994
    • (1994) Biochem Pharmacol , vol.48 , pp. 955-966
    • Sterchele, P.F.1    Van Den Heuvel, J.P.2    Davis, W.3    Shrago, E.4    Knudsen, J.5    Peterson, R.E.6
  • 30
    • 0025822788 scopus 로고
    • Protein kinase C isotypes and signaling in neutrophils. Differential substrate specificities of a translocatable calcium- and phospholipid-dependent beta-protein kinase C and a phospholipid-dependent protein kinase which is inhibited by long chain fatty acyl coenzyme A
    • Majumdar S, Rossi MW, Fujiki T, Phillips WA, Disa S, Queen CF, Johnston RB Jr, Rosen OM, Corkey BE, Korchak HM: Protein kinase C isotypes and signaling in neutrophils. Differential substrate specificities of a translocatable calcium- and phospholipid-dependent beta-protein kinase C and a phospholipid-dependent protein kinase which is inhibited by long chain fatty acyl coenzyme A. J. Biol Chem 266: 9285-9294, 1991
    • (1991) J. Biol Chem , vol.266 , pp. 9285-9294
    • Majumdar, S.1    Rossi, M.W.2    Fujiki, T.3    Phillips, W.A.4    Disa, S.5    Queen, C.F.6    Johnston R.B., Jr.7    Rosen, O.M.8    Corkey, B.E.9    Korchak, H.M.10
  • 31
    • 0026733643 scopus 로고
    • Malonyl-CoA and long chain acyl-CoA esters as metabolic coupling factors in nutrient-induced insulin secretion
    • Prentki M, Vischer S, Glennon MC, Regazzi R, Deeney JT, Corkey BE: Malonyl-CoA and long chain acyl-CoA esters as metabolic coupling factors in nutrient-induced insulin secretion. J Biol Chem 267: 5802-5810, 1992
    • (1992) J Biol Chem , vol.267 , pp. 5802-5810
    • Prentki, M.1    Vischer, S.2    Glennon, M.C.3    Regazzi, R.4    Deeney, J.T.5    Corkey, B.E.6
  • 33
    • 0013773444 scopus 로고
    • Variations in tissue contents of coenzyme A thio esters and possible metabolic implications
    • Tubbs PK, Garland PB: Variations in tissue contents of coenzyme A thio esters and possible metabolic implications. Biochem J 93: 550-557, 1964
    • (1964) Biochem J , vol.93 , pp. 550-557
    • Tubbs, P.K.1    Garland, P.B.2
  • 34
    • 0020581524 scopus 로고    scopus 로고
    • Hepatic enzymes, CoASH and long-chain acyl-CoA in subcellular fractions as affected by drugs inducing peroxisomes and smooth endoplasmic reticulum
    • Berge RK, Aarsland A, Bakke OM, Farstad M: hepatic enzymes, CoASH and long-chain acyl-CoA in subcellular fractions as affected by drugs inducing peroxisomes and smooth endoplasmic reticulum. Int J Biochem 15: 191-204
    • Int J Biochem , vol.15 , pp. 191-204
    • Berge, R.K.1    Aarsland, A.2    Bakke, O.M.3    Farstad, M.4
  • 35
    • 0023858473 scopus 로고
    • Micellization of fatty acid acyl-CoA mixtures and its relevance to the fatty acyl selectivity of acyl-transferases
    • Constantinides PP, Steim JM: Micellization of fatty acid acyl-CoA mixtures and its relevance to the fatty acyl selectivity of acyl-transferases. Arch Biochem Biophys 261: 430-436, 1988
    • (1988) Arch Biochem Biophys , vol.261 , pp. 430-436
    • Constantinides, P.P.1    Steim, J.M.2
  • 36
    • 0020479806 scopus 로고
    • Specific inhibition of glucokinase by long chain acyl coenzymes a below the critical micelle concentration
    • Tippet PS, Neet KE: Specific inhibition of glucokinase by long chain acyl coenzymes A below the critical micelle concentration. J Biol Chem 257: 12839-12845, 1982
    • (1982) J Biol Chem , vol.257 , pp. 12839-12845
    • Tippet, P.S.1    Neet, K.E.2
  • 37
    • 0017824474 scopus 로고
    • Coenzyme a and carnitine distribution in normal and ischemic hearts
    • Idell Wenger JA, Grotohann LW, Neely JR: Coenzyme A and carnitine distribution in normal and ischemic hearts. J Biol Chem 253: 4310-4318, 1978
    • (1978) J Biol Chem , vol.253 , pp. 4310-4318
    • Idell Wenger, J.A.1    Grotohann, L.W.2    Neely, J.R.3
  • 38
    • 0026511594 scopus 로고
    • Fasting induced alterations in mitochondrial palmitoyl-CoA metabolism may inhibit adipocyte pyruvate dehydrogenase activity
    • Moore KH, Dandurand DM, Kiechle FL: Fasting induced alterations in mitochondrial palmitoyl-CoA metabolism may inhibit adipocyte pyruvate dehydrogenase activity. Int J Biochem 24: 809-814, 1992
    • (1992) Int J Biochem , vol.24 , pp. 809-814
    • Moore, K.H.1    Dandurand, D.M.2    Kiechle, F.L.3
  • 39
    • 0016438089 scopus 로고
    • Regulation of long chain fatty acid activation in heart muscle
    • Oram JF, Wenger JI, Neely JR: Regulation of long chain fatty acid activation in heart muscle. J Biol Chem 250: 73-78, 1975
    • (1975) J Biol Chem , vol.250 , pp. 73-78
    • Oram, J.F.1    Wenger, J.I.2    Neely, J.R.3
  • 44
    • 0025836775 scopus 로고
    • Human DBI (endozepine): Relationship to a homologous membrane associated protein (MA-DBI)
    • Todaro GJ, Rose TM, Shoyab M: Human DBI (endozepine): Relationship to a homologous membrane associated protein (MA-DBI). Neuropharmacology 30: 1373-1380, 1991
    • (1991) Neuropharmacology , vol.30 , pp. 1373-1380
    • Todaro, G.J.1    Rose, T.M.2    Shoyab, M.3
  • 45
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteins
    • Peitzsch RM, McLaughlin S: Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteins. Biochemistry 32: 10436-10443, 1993
    • (1993) Biochemistry , vol.32 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 46
    • 0028848883 scopus 로고
    • Differential penetration of fatty acyl-coenzyme A and fatty acylcarnitines into phospholipid monolayers
    • Requero MA, Gonzalez M, Goni FM, Alonso A, Fidelio G: Differential penetration of fatty acyl-coenzyme A and fatty acylcarnitines into phospholipid monolayers. FEBS Lett 357: 75-78, 1995
    • (1995) FEBS Lett , vol.357 , pp. 75-78
    • Requero, M.A.1    Gonzalez, M.2    Goni, F.M.3    Alonso, A.4    Fidelio, G.5
  • 47
    • 0018398166 scopus 로고
    • Purification and characterization of long-chain acyl-CoA hydrolase from rat liver mitochondria
    • Berge RK, Farstad M: Purification and characterization of long-chain acyl-CoA hydrolase from rat liver mitochondria. Eur J Biochim 96: 393-401, 1979
    • (1979) Eur J Biochim , vol.96 , pp. 393-401
    • Berge, R.K.1    Farstad, M.2
  • 48
    • 0021257310 scopus 로고
    • Enzymatic changes in rat liver associated with low and high doses of a peroxisome proliferator
    • Berge RK, Hosoy LH, Aarsland A, Bakke OM, Farstad M: Enzymatic changes in rat liver associated with low and high doses of a peroxisome proliferator. Toxicol Appl Pharmacol 73: 35-41, 1984
    • (1984) Toxicol Appl Pharmacol , vol.73 , pp. 35-41
    • Berge, R.K.1    Hosoy, L.H.2    Aarsland, A.3    Bakke, O.M.4    Farstad, M.5
  • 49
    • 0026590873 scopus 로고
    • Origins and fates of fatty acyl-CoA esters
    • Waku K: Origins and fates of fatty acyl-CoA esters. Biochim Biophys Acta 1124: 101-111, 1992
    • (1992) Biochim Biophys Acta , vol.1124 , pp. 101-111
    • Waku, K.1
  • 50
    • 0016734489 scopus 로고
    • Acyl-CoA hydrolase(s) in rabbit mammary gland which control the chain length of fatty acids synthesised
    • Knudsen J, Clark S, Dils R: Acyl-CoA hydrolase(s) in rabbit mammary gland which control the chain length of fatty acids synthesised. Biochem Biophys Res Commun 65: 921-926, 1975
    • (1975) Biochem Biophys Res Commun , vol.65 , pp. 921-926
    • Knudsen, J.1    Clark, S.2    Dils, R.3
  • 51
    • 0017119593 scopus 로고
    • Purficiation and some properties of a medium-chain acyl-thioester hydrolase from lactating-rabbit mammary gland which terminates chain elongation in fatty acid synthesis
    • Knudsen J, Clark S, Dils R: Purficiation and some properties of a medium-chain acyl-thioester hydrolase from lactating-rabbit mammary gland which terminates chain elongation in fatty acid synthesis. Biochem J 160: 683-691, 1976
    • (1976) Biochem J , vol.160 , pp. 683-691
    • Knudsen, J.1    Clark, S.2    Dils, R.3
  • 52
    • 0028967783 scopus 로고
    • Purification, properties and specificity of rat brain cytosolic fatty acyl coenzyme A hydrolase
    • Broustas CG, Hajra AK: Purification, properties and specificity of rat brain cytosolic fatty acyl coenzyme A hydrolase. J Neurochem 64: 2345-2353, 1995
    • (1995) J Neurochem , vol.64 , pp. 2345-2353
    • Broustas, C.G.1    Hajra, A.K.2
  • 53
    • 0030022978 scopus 로고    scopus 로고
    • Long-chain acyl-CoA hydrolase from rat brain cytosol: Purification, characterization and immunohistochemical localization
    • Yamada J, Furihata T, Tamura H, Watanabe T, Suga T: Long-chain acyl-CoA hydrolase from rat brain cytosol: Purification, characterization and immunohistochemical localization. Arch Biochem Biophys 326: 106-114, 1996
    • (1996) Arch Biochem Biophys , vol.326 , pp. 106-114
    • Yamada, J.1    Furihata, T.2    Tamura, H.3    Watanabe, T.4    Suga, T.5
  • 54
    • 0017879460 scopus 로고
    • Inhibition of rat-liver acetyl-coenzyme-A caboxylase by palmitoyl-coenzyme A. Formation of equimola enzyme-inhibitor complex
    • Ogiwara H, Tanabe T, Nikawa J, Numa S: Inhibition of rat-liver acetyl-coenzyme-A caboxylase by palmitoyl-coenzyme A. Formation of equimola enzyme-inhibitor complex. Eur J biochem 89: 33-41, 1978
    • (1978) Eur J Biochem , vol.89 , pp. 33-41
    • Ogiwara, H.1    Tanabe, T.2    Nikawa, J.3    Numa, S.4
  • 55
    • 0028296147 scopus 로고
    • Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis
    • Rasmussen JT, Færgemann NJ, Kristiansen K, Knudsen J: Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis. Biochem J 299: 165-170, 1994
    • (1994) Biochem J , vol.299 , pp. 165-170
    • Rasmussen, J.T.1    Færgemann, N.J.2    Kristiansen, K.3    Knudsen, J.4
  • 56
    • 0023642627 scopus 로고
    • A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis
    • Carling D, Zammit VA, Hardie DG: A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis. FEBS Lett 223: 217-222, 1987
    • (1987) FEBS Lett , vol.223 , pp. 217-222
    • Carling, D.1    Zammit, V.A.2    Hardie, D.G.3
  • 57
    • 0018400882 scopus 로고
    • Fatty acyl group transport into mitochondria: Carnatine palmitoyl transferase EC 2.3.1.23 and the carnitine-acylcarnatine translocase
    • Halperin ML, Pande SV: Fatty acyl group transport into mitochondria: Carnatine palmitoyl transferase EC 2.3.1.23 and the carnitine-acylcarnatine translocase. Methods Enzymol 56: 368-378, 1979
    • (1979) Methods Enzymol , vol.56 , pp. 368-378
    • Halperin, M.L.1    Pande, S.V.2
  • 58
    • 0019876974 scopus 로고
    • Modulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase by lipid inhibitors, substrates and cytosolic factors
    • Lehrer G, Panini SR, Rogers DH, Rudney H: Modulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase by lipid inhibitors, substrates and cytosolic factors. J Biol Chem 256: 5612-5619, 1981
    • (1981) J Biol Chem , vol.256 , pp. 5612-5619
    • Lehrer, G.1    Panini, S.R.2    Rogers, D.H.3    Rudney, H.4
  • 59
    • 0023657289 scopus 로고
    • Some differences in the properties of carnitine palmitoyltransferase activities of the mitochondrial outer and inner membranes
    • Murthy MS, Pande SV: Some differences in the properties of carnitine palmitoyltransferase activities of the mitochondrial outer and inner membranes. Biochem J 248: 727-733, 1987
    • (1987) Biochem J , vol.248 , pp. 727-733
    • Murthy, M.S.1    Pande, S.V.2
  • 60
    • 0023657746 scopus 로고
    • Interaction of acyl coenzyme A substrates and analgues with pig kidney medium-chain acyl-CoA dehydrogenase
    • Powell PJ, Lau SM, Killian D, Thorpe C: Interaction of acyl coenzyme A substrates and analgues with pig kidney medium-chain acyl-CoA dehydrogenase. Biochemistry 26: 3704-3710, 1987
    • (1987) Biochemistry , vol.26 , pp. 3704-3710
    • Powell, P.J.1    Lau, S.M.2    Killian, D.3    Thorpe, C.4
  • 61
    • 0026774987 scopus 로고
    • Inhibition of hormone-sensitive lipase by intermediary lipid metabolites
    • Jepson VA, Yeaman SJ: Inhibition of hormone-sensitive lipase by intermediary lipid metabolites. FEBS Lett 310: 197-200, 1992
    • (1992) FEBS Lett , vol.310 , pp. 197-200
    • Jepson, V.A.1    Yeaman, S.J.2
  • 62
    • 0020491484 scopus 로고
    • Studies on the interaction of palmutoyl coenzyme A with the adenine nucleotide translocase
    • Woldegoirgis G, Yousufzai SY, Shrago E: Studies on the interaction of palmutoyl coenzyme A with the adenine nucleotide translocase. J Biol Chem 257: 14783-14787, 1982
    • (1982) J Biol Chem , vol.257 , pp. 14783-14787
    • Woldegoirgis, G.1    Yousufzai, S.Y.2    Shrago, E.3
  • 63
    • 0020479821 scopus 로고
    • An allosteric model for the inhibition of glucokinase by long chain acyl coenzyme A
    • Tippett PS, Neet KE: An allosteric model for the inhibition of glucokinase by long chain acyl coenzyme A. J Biol Chem 257: 12846-12852, 1982
    • (1982) J Biol Chem , vol.257 , pp. 12846-12852
    • Tippett, P.S.1    Neet, K.E.2
  • 65
    • 0029981240 scopus 로고    scopus 로고
    • Counter modulation of adipocyte motochondrial processes by insulun and S-oxalyl-glutathione
    • Moore KH, Tsatso P, Staudacher DM, Kiechle FL: Counter modulation of adipocyte motochondrial processes by insulun and S-oxalyl-glutathione. Int J Biochem Cell Biol 28: 183-191, 1996
    • (1996) Int J Biochem Cell Biol , vol.28 , pp. 183-191
    • Moore, K.H.1    Tsatso, P.2    Staudacher, D.M.3    Kiechle, F.L.4
  • 66
    • 0028031858 scopus 로고
    • Fatty acyl-CoA esters induce calcium release from terminal cisternae of skeletal muscle
    • Fulceri R, Nori A, Gamberucci A, Volpe P, Giunti R, Benedetti A: Fatty acyl-CoA esters induce calcium release from terminal cisternae of skeletal muscle. Cell Calcium 15: 109-116, 1994
    • (1994) Cell Calcium , vol.15 , pp. 109-116
    • Fulceri, R.1    Nori, A.2    Gamberucci, A.3    Volpe, P.4    Giunti, R.5    Benedetti, A.6
  • 67
    • 0029964450 scopus 로고    scopus 로고
    • 2+ release elicited by cyclic ADP-ribose
    • 2+ release elicited by cyclic ADP-ribose. Am J Physiol 270: C530-C537, 1996
    • (1996) Am J Physiol , vol.270
    • Chini, E.N.1    Dousa, T.P.2
  • 68
    • 0027996810 scopus 로고
    • Modification of GTP-activated calcium translocation by fatty acyl-Coa esters. Evidence for a GTP-induced prefusion event
    • Rys Sikora Kem Ghosh TK, Gill DL: Modification of GTP-activated calcium translocation by fatty acyl-CoA esters. Evidence for a GTP-induced prefusion event. J Biol Chem 269: 31607-31613, 1994
    • (1994) J Biol Chem , vol.269 , pp. 31607-31613
    • Rys Sikora Kem Ghosh, T.K.1    Gill, D.L.2
  • 69
    • 0027435948 scopus 로고
    • CoA and fatty acid acyl-CoA derivatives mobilize calcium from a liver reticular pool
    • Fulceri R, Gamberucci A, Bellomo G, Giunti R, Benedetti A: CoA and fatty acid acyl-CoA derivatives mobilize calcium from a liver reticular pool. Biochem J 295: 663-669, 1993
    • (1993) Biochem J , vol.295 , pp. 663-669
    • Fulceri, R.1    Gamberucci, A.2    Bellomo, G.3    Giunti, R.4    Benedetti, A.5
  • 71
    • 0023108440 scopus 로고
    • Contro of cardiac sodium pump by long-chain acyl coenzymes A
    • Kaker SS, Huang WH, Askari A: Contro of cardiac sodium pump by long-chain acyl coenzymes A. J Biol Chem 262: 42-45, 1987
    • (1987) J Biol Chem , vol.262 , pp. 42-45
    • Kaker, S.S.1    Huang, W.H.2    Askari, A.3
  • 72
    • 0023777952 scopus 로고
    • Palmyitoyl-CoA inhibits the mitochondrial inner membrane anion-conducting chanel
    • Hall Smith SC, Murray AG, Selwyn MJ: Palmyitoyl-CoA inhibits the mitochondrial inner membrane anion-conducting chanel. FEBD Lett 236: 155-158, 1988
    • (1988) FEBD Lett , vol.236 , pp. 155-158
    • Hall Smith, S.C.1    Murray, A.G.2    Selwyn, M.J.3
  • 74
    • 0023951837 scopus 로고
    • Diacylglycerol activation of protein kinase C is modulated by long-chain acyl-CoA
    • Bronfman M, Morales MN, Orellana A: Diacylglycerol activation of protein kinase C is modulated by long-chain acyl-CoA. Biochem Biophys Res Commun 152: 987-992, 1988
    • (1988) Biochem Biophys Res Commun , vol.152 , pp. 987-992
    • Bronfman, M.1    Morales, M.N.2    Orellana, A.3
  • 75
    • 0027404756 scopus 로고
    • Fatty acyl-CoA binding activity of the nuclear thyroid hormone receptor
    • Li Q, Yamamoto N, Morisawa S, Inoue A: Fatty acyl-CoA binding activity of the nuclear thyroid hormone receptor. J Cell Biochem 51: 458-464, 1993
    • (1993) J Cell Biochem , vol.51 , pp. 458-464
    • Li, Q.1    Yamamoto, N.2    Morisawa, S.3    Inoue, A.4
  • 76
    • 0026713687 scopus 로고
    • Characterization of FadR, a global transciptional regulator of fatty acid metabolism in Escherichia coli. Interaction with the FadB promoter is prevented by long chain fatty acy coenzyme A
    • published erratum appears in J Biol Chem 1992 Nov 5; 267(31): 22693
    • DiRusso CC, Heimert TL, Metzger AK: Characterization of FadR, a global transciptional regulator of fatty acid metabolism in Escherichia coli. Interaction with the FadB promoter is prevented by long chain fatty acy coenzyme A [published erratum appears in J Biol Chem 1992 Nov 5; 267(31): 22693] J Biol Chem 267: 8685-8691, 1992
    • (1992) J Biol Chem , vol.267 , pp. 8685-8691
    • DiRusso, C.C.1    Heimert, T.L.2    Metzger, A.K.3
  • 77
    • 0025249975 scopus 로고
    • Fatty acylation promotes fusion of transport vesicles with Golgi cisternae
    • Pfanner N, Glick BS, Arden SR, Rothman JE: Fatty acylation promotes fusion of transport vesicles with Golgi cisternae. J Cell Biol 110: 995-961, 1990
    • (1990) J Cell Biol , vol.110 , pp. 995-1961
    • Pfanner, N.1    Glick, B.S.2    Arden, S.R.3    Rothman, J.E.4
  • 78
  • 79
    • 0027400254 scopus 로고
    • 2+ release and vesicle fusion in rat liver microsomal vesicles
    • 2+ release and vesicle fusion in rat liver microsomal vesicles. Biochem J 289: 561-567, 1993
    • (1993) Biochem J , vol.289 , pp. 561-567
    • Comerford, J.G.1    Dawson, A.P.2
  • 80
    • 0025176928 scopus 로고
    • Inhibition of proline endopeptidase activity by acyl-coenzyme A esters
    • Yamakawa N, Shimeno H, Soeda S, Nagamutsu A: Inhibition of proline endopeptidase activity by acyl-coenzyme A esters. Biochim Biophys Acta 1037: 302-306, 1990
    • (1990) Biochim Biophys Acta , vol.1037 , pp. 302-306
    • Yamakawa, N.1    Shimeno, H.2    Soeda, S.3    Nagamutsu, A.4
  • 81
    • 0030036294 scopus 로고    scopus 로고
    • Characterization and isolation of enzymes that hydrolyze short-chain acyl-CoA in rat-liver mitochondria
    • Svensson LT, Kilpelainen SH, Hiltunen JK, Alexson SE: Characterization and isolation of enzymes that hydrolyze short-chain acyl-CoA in rat-liver mitochondria. Eur J Biochem 239: 526-531, 1996
    • (1996) Eur J Biochem , vol.239 , pp. 526-531
    • Svensson, L.T.1    Kilpelainen, S.H.2    Hiltunen, J.K.3    Alexson, S.E.4
  • 82
    • 0028265730 scopus 로고
    • Cellular transport and metabolism of vitamin A: Roles of the cellular retinoid-binding proteins
    • Ong DE: Cellular transport and metabolism of vitamin A: Roles of the cellular retinoid-binding proteins. Nutr Rev 52: S24-S31, 1994
    • (1994) Nutr Rev , vol.52
    • Ong, D.E.1
  • 83
    • 0029977972 scopus 로고    scopus 로고
    • Cellular retinol-binding protein-supported retinoic acid synthesis. Relative rolse of microsomes and cytosol
    • Boerman MH, Napoli JL: Cellular retinol-binding protein-supported retinoic acid synthesis. Relative rolse of microsomes and cytosol. J Biol Chem 271: 5610-5616, 1996
    • (1996) J Biol Chem , vol.271 , pp. 5610-5616
    • Boerman, M.H.1    Napoli, J.L.2
  • 84
    • 0016372210 scopus 로고
    • Regulation of lipogenosis in animal tissues
    • Numa S, Yamashita S: Regulation of lipogenosis in animal tissues. Curr Top Cell Regul 8: 197-246, 1974
    • (1974) Curr Top Cell Regul , vol.8 , pp. 197-246
    • Numa, S.1    Yamashita, S.2
  • 85
    • 2242479945 scopus 로고
    • Evidence that acyl coenzyme A synthetase activity is required forrepression of yeast acetyl coenzyme A carboxylase by exogenous fatty acids
    • Kamiryo T, Parthasarathy S, Numa S: Evidence that acyl coenzyme A synthetase activity is required forrepression of yeast acetyl coenzyme A carboxylase by exogenous fatty acids. Proc Natl Acad Sci USA 73: 386-390, 1976
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 386-390
    • Kamiryo, T.1    Parthasarathy, S.2    Numa, S.3
  • 86
    • 0030040585 scopus 로고    scopus 로고
    • Regulatory elements that control transcription activation and unsaturated fatty acid-mediated repression of the Saccharomyces cerevisia OLE1 gene
    • Choi JY, Stukey J, Hwang, SY, Martin CE: Regulatory elements that control transcription activation and unsaturated fatty acid-mediated repression of the Saccharomyces cerevisia OLE1 gene. J Biol Chem 271: 3581-3589, 1996
    • (1996) J Biol Chem , vol.271 , pp. 3581-3589
    • Choi, J.Y.1    Stukey, J.2    Hwang, S.Y.3    Martin, C.E.4
  • 87
    • 0028860254 scopus 로고
    • Analysis of acyl coenzyme A binding to the transcription factor FadR and identification of amino acid residues in the carboxyl terminus required for ligand binding
    • Raman N, DiRusso CC: Analysis of acyl coenzyme A binding to the transcription factor FadR and identification of amino acid residues in the carboxyl terminus required for ligand binding. J Biol Chem 270: 1092-1097, 1995
    • (1995) J Biol Chem , vol.270 , pp. 1092-1097
    • Raman, N.1    DiRusso, C.C.2
  • 88
    • 0345466240 scopus 로고
    • Adipocyte differentiation is dependent onthe induction of the acyl-CoA binding protein
    • Baldursson T, Gram C, Knudsen J, Krisiansen K, Mandrup S: Adipocyte differentiation is dependent onthe induction of the acyl-CoA binding protein. NATO ASI Series, Vol H92: 365374, 1995
    • (1995) NATO ASI Series , vol.H92 , pp. 365374
    • Baldursson, T.1    Gram, C.2    Knudsen, J.3    Krisiansen, K.4    Mandrup, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.