메뉴 건너뛰기




Volumn 40, Issue 6, 2005, Pages 559-568

Stability of fatty acyl-coenzyme A thioester ligands of hepatocyte nuclear factor-4α and peroxisome proliferator-activated receptor-α

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CELLS; CRYSTALLIZATION; CRYSTALS; DEGRADATION; ESTERS; HYDROLYSIS; STABILITY; X RAYS;

EID: 22844452801     PISSN: 00244201     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11745-005-1416-y     Document Type: Article
Times cited : (24)

References (52)
  • 1
    • 0032473950 scopus 로고    scopus 로고
    • Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4α
    • Hertz, R., Magenheim, J., Berman, I., and Bar-Tana, J. (1998) Fatty Acyl-CoA Thioesters Are Ligands of Hepatic Nuclear Factor-4α, Nature 392, 512-516.
    • (1998) Nature , vol.392 , pp. 512-516
    • Hertz, R.1    Magenheim, J.2    Berman, I.3    Bar-Tana, J.4
  • 2
    • 0037025344 scopus 로고    scopus 로고
    • Ligand specificity and conformational dependence of the hepatic nuclear factor-4α (HNF-4α)
    • Petrescu, A.D., Hertz, R., Bar-Tana, J., Schroeder, F., and Kier, A.B. (2002) Ligand Specificity and Conformational Dependence of the Hepatic Nuclear Factor-4α (HNF-4α), J. Biol. Chem. 277, 23988-23999.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23988-23999
    • Petrescu, A.D.1    Hertz, R.2    Bar-Tana, J.3    Schroeder, F.4    Kier, A.B.5
  • 4
    • 20444475700 scopus 로고    scopus 로고
    • Role of regulatory F-domain in hepatocyte nuclear factor-4α ligand specificity
    • Petrescu, A., Huang, H., Hertz, R., Bar-Tana, J., Schroeder, F., and Kier, A.B. (2005) Role of Regulatory F-Domain in Hepatocyte Nuclear Factor-4α Ligand Specificity, J. Biol. Chem. 280, 16714-16727.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16714-16727
    • Petrescu, A.1    Huang, H.2    Hertz, R.3    Bar-Tana, J.4    Schroeder, F.5    Kier, A.B.6
  • 6
    • 0035862979 scopus 로고    scopus 로고
    • Fatty acyl CoA thioesters inhibit recruitment of steroid receptor co-activator 1 to α and γ isoforms of peroxisome proliferator activated receptors by competing with agonists
    • Murakami, K., Ide, T., Nakazawa, T., Okazaki, T., Mochizuki, T., and Kadowaki, T. (2001) Fatty Acyl CoA Thioesters Inhibit Recruitment of Steroid Receptor Co-activator 1 to α and γ Isoforms of Peroxisome Proliferator Activated Receptors by Competing with Agonists, Biochem. J. 353, 231-238.
    • (2001) Biochem. J. , vol.353 , pp. 231-238
    • Murakami, K.1    Ide, T.2    Nakazawa, T.3    Okazaki, T.4    Mochizuki, T.5    Kadowaki, T.6
  • 7
    • 21444456038 scopus 로고    scopus 로고
    • Peroxisome proliferator activated receptor alpha (PPARα) interacts with high affinity and is conformationally responsive to endogenous ligands
    • Hosteller, H.A., Petrescu, A.D., Kier, A.B., and Schroeder, F. (2005) Peroxisome Proliferator Activated Receptor Alpha (PPARα) Interacts with High Affinity and Is Conformationally Responsive to Endogenous Ligands, J. Biol. Chem. 280, 18667-18682.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18667-18682
    • Hosteller, H.A.1    Petrescu, A.D.2    Kier, A.B.3    Schroeder, F.4
  • 11
    • 0032079544 scopus 로고    scopus 로고
    • Acyl coenzyme A binding protein: Conformational sensitivity to long chain fatty acyl-CoA
    • Frolov, A.A., and Schroeder, F. (1998) Acyl Coenzyme A Binding Protein: Conformational Sensitivity to Long Chain Fatty Acyl-CoA, J. Biol. Chem. 273, 11049-11055.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11049-11055
    • Frolov, A.A.1    Schroeder, F.2
  • 12
    • 0029751076 scopus 로고    scopus 로고
    • Sterol carrier protein-2, a new fatty acyl coenzyme A-binding protein
    • Frolov, A., Cho, T.H., Billheimer, J.T., and Schroeder, F. (1996) Sterol Carrier Protein-2, a New Fatty Acyl Coenzyme A-Binding Protein, J. Biol. Chem. 271, 31878-31884.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31878-31884
    • Frolov, A.1    Cho, T.H.2    Billheimer, J.T.3    Schroeder, F.4
  • 13
    • 0031008197 scopus 로고    scopus 로고
    • Isoforms of rat liver fatty acid binding protein differ in structure and affinity for fatty acids and fatty acyl CoAs
    • Frolov, A., Cho, T.H., Murphy, E.J., and Schroeder, F. (1997) Isoforms of Rat Liver Fatty Acid Binding Protein Differ in Structure and Affinity for Fatty Acids and Fatty Acyl CoAs, Biochemistry 36, 6545-6555.
    • (1997) Biochemistry , vol.36 , pp. 6545-6555
    • Frolov, A.1    Cho, T.H.2    Murphy, E.J.3    Schroeder, F.4
  • 14
    • 0033278397 scopus 로고    scopus 로고
    • Fatty acids, eicosanoids, and hypolipidemic agents regulate gene expression through direct binding to peroxisome proliferator activated receptors
    • (Nigam, S., and Pace-Asciak, C.R., eds.), Plenum Press, New York
    • Wahli, W., Devchand, P.R., Ijpenberg, A., and Desvergne, B. (1999) Fatty Acids, Eicosanoids, and Hypolipidemic Agents Regulate Gene Expression Through Direct Binding to Peroxisome Proliferator Activated Receptors, in Lipoxygenases and Their Metabolites (Nigam, S., and Pace-Asciak, C.R., eds.), pp. 199-209, Plenum Press, New York.
    • (1999) Lipoxygenases and Their Metabolites , pp. 199-209
    • Wahli, W.1    Devchand, P.R.2    Ijpenberg, A.3    Desvergne, B.4
  • 15
    • 0033613869 scopus 로고    scopus 로고
    • Phytanic acid activates the peroxisome proliferator-activated receptor α (PPARα) in sterol carrier protein-2/sterol carrier protein x-deficient mice
    • Ellinghaus, P., Wolfrum, C., Assmann, G., Spener, F., and Seedorf, U. (1999) Phytanic Acid Activates the Peroxisome Proliferator-Activated Receptor α (PPARα) in Sterol Carrier Protein-2/Sterol Carrier Protein x-Deficient Mice, J. Biol. Chem. 274, 2766-2772.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2766-2772
    • Ellinghaus, P.1    Wolfrum, C.2    Assmann, G.3    Spener, F.4    Seedorf, U.5
  • 16
    • 0032850195 scopus 로고    scopus 로고
    • Modulation of transcriptional activation and coactivator interaction by a splicing variation in the F domain of nuclear receptor HNF4α
    • Sladek, F.M., Ruse, M.D., Nepomuceno, L., Huang, S.-M., and Stallcup, M.R. (1999) Modulation of Transcriptional Activation and Coactivator Interaction by a Splicing Variation in the F Domain of Nuclear Receptor HNF4α, Mol. Cell. Biol. 19, 6509-6522.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6509-6522
    • Sladek, F.M.1    Ruse, M.D.2    Nepomuceno, L.3    Huang, S.-M.4    Stallcup, M.R.5
  • 17
    • 0035431321 scopus 로고    scopus 로고
    • Structure of the PPARα and γ ligand binding domain in complex with AZ 242a: Ligand selectivity and agonist activation in the PPAR family
    • Cronet, P., Peterson, J.F.W., Folmer, R., Blomberg, N., Sjoblom, K., Karlsson, U., Lindstedt, E.-L., and Bamberg, K. (2001) Structure of the PPARα and γ Ligand Binding Domain in Complex with AZ 242a: Ligand Selectivity and Agonist Activation in the PPAR Family, Structure 9, 699-706.
    • (2001) Structure , vol.9 , pp. 699-706
    • Cronet, P.1    Peterson, J.F.W.2    Folmer, R.3    Blomberg, N.4    Sjoblom, K.5    Karlsson, U.6    Lindstedt, E.-L.7    Bamberg, K.8
  • 19
    • 0037063997 scopus 로고    scopus 로고
    • Crystal structure of the HNF4α ligand binding domain in complex with endogenous fatty acid ligand
    • Dhe-Paganon, S., Duda, K., Iwamoto, M., Chi, Y.-I., and Shoelson, S.E. (2002) Crystal Structure of the HNF4α Ligand Binding Domain in Complex with Endogenous Fatty Acid Ligand, J. Biol. Chem. 277, 37973-37976.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37973-37976
    • Dhe-Paganon, S.1    Duda, K.2    Iwamoto, M.3    Chi, Y.-I.4    Shoelson, S.E.5
  • 20
    • 0036296945 scopus 로고    scopus 로고
    • Opposing effects of fatty acids and acyl-CoA esters on conformation and cofactor recruitment of peroxisome proliferator activated receptors
    • Jorgensen, C., Krogsdam, A.-M., Kratchamarova, I., Willson, T.M., Knudsen, J., Mandrup, S., and Kristiansen, K. (2002) Opposing Effects of Fatty Acids and acyl-CoA Esters on Conformation and Cofactor Recruitment of Peroxisome Proliferator Activated Receptors, Ann. N.Y. Acad. Sci. 967, 431-439.
    • (2002) Ann. N.Y. Acad. Sci. , vol.967 , pp. 431-439
    • Jorgensen, C.1    Krogsdam, A.-M.2    Kratchamarova, I.3    Willson, T.M.4    Knudsen, J.5    Mandrup, S.6    Kristiansen, K.7
  • 21
    • 0035342271 scopus 로고    scopus 로고
    • Suppression of hepatocyte nuclear factor 4α by acyl-CoA thioesters of hypolipidemic peroxisome proliferators
    • Hertz, R., Sheena, V., Kalderon, B., Berman, I., and Bar-Tana, J. (2001) Suppression of Hepatocyte Nuclear Factor 4α by Acyl-CoA Thioesters of Hypolipidemic Peroxisome Proliferators, Biochem. Pharmacol. 61, 1057-1062.
    • (2001) Biochem. Pharmacol. , vol.61 , pp. 1057-1062
    • Hertz, R.1    Sheena, V.2    Kalderon, B.3    Berman, I.4    Bar-Tana, J.5
  • 23
    • 0029970860 scopus 로고    scopus 로고
    • The extreme C terminus of the progesterone receptor contains a transcriptional repressor domain that functions through a putative corepressor
    • Xu, J., Nawaz, Z., Tsai, S.Y., Tsai, M.-J., and O'Malley, B.W. (1996) The Extreme C Terminus of the Progesterone Receptor Contains a Transcriptional Repressor Domain That Functions Through a Putative Corepressor, Proc. Natl. Acad. Sci. USA 93, 12195-12199.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12195-12199
    • Xu, J.1    Nawaz, Z.2    Tsai, S.Y.3    Tsai, M.-J.4    O'Malley, B.W.5
  • 24
    • 0034678088 scopus 로고    scopus 로고
    • Peroxisome proliferator activated receptors: Insights into multiple cellular functions
    • Escher, P., and Wahli, W. (2000) Peroxisome Proliferator Activated Receptors: Insights into Multiple Cellular Functions, Mutat. Res. 448, 121-138.
    • (2000) Mutat. Res. , vol.448 , pp. 121-138
    • Escher, P.1    Wahli, W.2
  • 26
    • 0347695020 scopus 로고    scopus 로고
    • Physical and functional interaction of acyl CoA binding protein (ACBP) with hepatocyte nuclear factor-4α (HNF4α)
    • Petrescu, A.D., Payne, H.R., Boedeker, A.L., Chao, H., Hertz, R., Bar-Tana, J., Schroeder, F., and Kier, A.B. (2003) Physical and Functional Interaction of Acyl CoA Binding Protein (ACBP) with Hepatocyte Nuclear Factor-4α (HNF4α), J. Biol. Chem. 278, 51813-51824.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51813-51824
    • Petrescu, A.D.1    Payne, H.R.2    Boedeker, A.L.3    Chao, H.4    Hertz, R.5    Bar-Tana, J.6    Schroeder, F.7    Kier, A.B.8
  • 27
    • 0033991851 scopus 로고    scopus 로고
    • Microsomal fatty acyl CoA transacylation and hydrolysis: Fatty acyl CoA species dependent modulation by liver fatty acyl CoA binding proteins
    • Jolly, C.A., Wilton, D.A., and Schroeder, F. (2000) Microsomal Fatty Acyl CoA Transacylation and Hydrolysis: Fatty Acyl CoA Species Dependent Modulation by Liver Fatty Acyl CoA Binding Proteins, Biochim. Biophys. Acta 1483, 185-197.
    • (2000) Biochim. Biophys. Acta , vol.1483 , pp. 185-197
    • Jolly, C.A.1    Wilton, D.A.2    Schroeder, F.3
  • 29
    • 0037143494 scopus 로고    scopus 로고
    • Membrane charge and curvature determine interaction with acyl CoA binding protein (ACBP) and fatty acyl CoA targeting
    • Chao, H., Martin, G., Russell, W.K., Waghela, S.D., Russell, D.H., Schroeder, F., and Kier, A.B. (2002) Membrane Charge and Curvature Determine Interaction with Acyl CoA Binding Protein (ACBP) and Fatty Acyl CoA Targeting, Biochemistry 41, 10540-10553.
    • (2002) Biochemistry , vol.41 , pp. 10540-10553
    • Chao, H.1    Martin, G.2    Russell, W.K.3    Waghela, S.D.4    Russell, D.H.5    Schroeder, F.6    Kier, A.B.7
  • 31
    • 0033524415 scopus 로고    scopus 로고
    • Ligand selectivity of the peroxisome proliferator-activated receptor α
    • Lin, Q., Ruuska, S.E., Shaw, N.S., Dong, D., and Noy, N. (1999) Ligand Selectivity of the Peroxisome Proliferator-Activated Receptor α, Biochemistry 38, 185-190.
    • (1999) Biochemistry , vol.38 , pp. 185-190
    • Lin, Q.1    Ruuska, S.E.2    Shaw, N.S.3    Dong, D.4    Noy, N.5
  • 32
    • 0027930011 scopus 로고
    • Isolation and quantitation of long-chain acyl-coenzyme A esters in brain tissue by solid-phase extraction
    • Deutsch, J., Grange, E., Rapoport, S.I., and Purdon, A.D. (1994) Isolation and Quantitation of Long-Chain Acyl-Coenzyme A Esters in Brain Tissue by Solid-Phase Extraction, Anal. Biochem. 220, 321-323.
    • (1994) Anal. Biochem. , vol.220 , pp. 321-323
    • Deutsch, J.1    Grange, E.2    Rapoport, S.I.3    Purdon, A.D.4
  • 33
    • 0035128174 scopus 로고    scopus 로고
    • A novel technique for the sensitive quantification of fatty acyl CoA esters from plant tissues
    • Larson, T.R., and Graham, I.A. (2001) A Novel Technique for the Sensitive Quantification of Fatty Acyl CoA Esters from Plant Tissues, Plant J. 25, 115-125.
    • (2001) Plant J. , vol.25 , pp. 115-125
    • Larson, T.R.1    Graham, I.A.2
  • 34
    • 1542267766 scopus 로고    scopus 로고
    • Liver fatty acid binding protein colocalizes with peroxisome proliferator receptor α and enhances ligand distribution to nuclei of living cells
    • Huang, H., Starodub, O., McIntosh, A., Atshaves, B.P., Woldegiorgis, G., Kier, A.B., and Schroeder, F. (2004) Liver Fatty Acid Binding Protein Colocalizes with Peroxisome Proliferator Receptor α and Enhances Ligand Distribution to Nuclei of Living Cells, Biochemistry 43, 2484-2500.
    • (2004) Biochemistry , vol.43 , pp. 2484-2500
    • Huang, H.1    Starodub, O.2    McIntosh, A.3    Atshaves, B.P.4    Woldegiorgis, G.5    Kier, A.B.6    Schroeder, F.7
  • 36
    • 0016817502 scopus 로고
    • Thermal regulation of the membrane lipid composition of Escherichia coli. Evidence for the direct control of fatty acid synthesis
    • Cronan, J.E., Jr. (1975) Thermal Regulation of the Membrane Lipid Composition of Escherichia coli. Evidence for the Direct Control of Fatty Acid Synthesis, J. Biol. Chem. 250, 7074-7077.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7074-7077
    • Cronan Jr., J.E.1
  • 38
    • 0030897513 scopus 로고    scopus 로고
    • Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signaling
    • Faergeman, N.J., and Knudsen, J. (1997) Role of Long-Chain Fatty Acyl-CoA Esters in the Regulation of Metabolism and in Cell Signaling, Biochem. J. 323, 1-12.
    • (1997) Biochem. J. , vol.323 , pp. 1-12
    • Faergeman, N.J.1    Knudsen, J.2
  • 40
    • 0037013275 scopus 로고    scopus 로고
    • Polyunsaturated fatty acyl CoA suppress the glucose-6-phosphate promoter activity by modulating the DNA binding of hepatocyte nuclear factor 4α
    • Rajas, F., Gautier, A., Bady, I., Montano, S., and Mithieux, G. (2002) Polyunsaturated Fatty Acyl CoA Suppress the Glucose-6-phosphate Promoter Activity by Modulating the DNA Binding of Hepatocyte Nuclear Factor 4α, J. Biol. Chem. 277, 15736-15744.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15736-15744
    • Rajas, F.1    Gautier, A.2    Bady, I.3    Montano, S.4    Mithieux, G.5
  • 41
    • 0026713687 scopus 로고
    • Characterization of FadR, a global transcriptional regulator of fatty acid metabolism in Escherichia coli. Interaction with the fadB promoter is prevented by long chain fatty acyl coenzyme A
    • DiRusso, C.C., Heimert, T.L., and Metzger, A.K. (1992) Characterization of FadR, a Global Transcriptional Regulator of Fatty Acid Metabolism in Escherichia coli. Interaction with the fadB Promoter Is Prevented by Long Chain Fatty Acyl Coenzyme A, J. Biol. Chem. 267, 8685-8691
    • (1992) J. Biol. Chem. , vol.267 , pp. 8685-8691
    • DiRusso, C.C.1    Heimert, T.L.2    Metzger, A.K.3
  • 42
    • 0026523921 scopus 로고
    • published erratum appears
    • [published erratum appears in J. Biol. Chem. 267, 22693 (1992)].
    • (1992) J. Biol. Chem. , vol.267 , pp. 22693
  • 44
    • 0019071560 scopus 로고
    • Physiochemical properties of the long chain acyl CoA hydrolase from rat liver microsomes
    • Berge, R.K. (1980) Physiochemical Properties of the Long Chain Acyl CoA Hydrolase from Rat Liver Microsomes, Eur. J. Biochem. 111, 61-12.
    • (1980) Eur. J. Biochem. , vol.111 , pp. 61-112
    • Berge, R.K.1
  • 45
    • 0021297283 scopus 로고
    • Specificity of purified monoacylglycerol lipase, palmitoyl-CoA hydrolase, palmitoyl-carnitine hydrolase, and nonspecific carboxylesterase from rat liver microsomes
    • Mentlein, R., Suttorp, M., and Heymann, E. (1984) Specificity of Purified Monoacylglycerol Lipase, Palmitoyl-CoA Hydrolase, Palmitoyl-Carnitine Hydrolase, and Nonspecific Carboxylesterase from Rat Liver Microsomes, Arch. Biochem. Biophys. 228, 230-246.
    • (1984) Arch. Biochem. Biophys. , vol.228 , pp. 230-246
    • Mentlein, R.1    Suttorp, M.2    Heymann, E.3
  • 46
    • 0032581367 scopus 로고    scopus 로고
    • cDNA cloning and genomic organization of peroxisome proliferator- inducible long chain acyl CoA hydrolase from rat liver cytosol
    • Yamada, J., Suga, K., Furihata, T., Kitahara, M., Watanabe, T., Hosokawa, M., Satoh, T., and Suga, T. (1998) cDNA Cloning and Genomic Organization of Peroxisome Proliferator-Inducible Long Chain Acyl CoA Hydrolase from Rat Liver Cytosol, Biochem. Biophys. Res. Commun. 248, 608-612.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 608-612
    • Yamada, J.1    Suga, K.2    Furihata, T.3    Kitahara, M.4    Watanabe, T.5    Hosokawa, M.6    Satoh, T.7    Suga, T.8
  • 47
    • 0028967783 scopus 로고
    • Purification, properties, and specificity of rat brain cytosolic fatty acyl CoA hydrolase
    • Broustas, C.G., and Hajra, A.K. (1995) Purification, Properties, and Specificity of Rat Brain Cytosolic Fatty Acyl CoA Hydrolase, J. Neurochem. 64, 2345-2353.
    • (1995) J. Neurochem. , vol.64 , pp. 2345-2353
    • Broustas, C.G.1    Hajra, A.K.2
  • 48
    • 0032008122 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a mitochondrial peroxisome proliferator induced acyl CoA thioesterase from rat liver
    • Svensson, L.T., Enberg, S.T., Aoyama, T., Usuda, N., Alexson, S.E.H., and Hashimoto, T. (1998) Molecular Cloning and Characterization of a Mitochondrial Peroxisome Proliferator Induced Acyl CoA Thioesterase from Rat Liver, Biochem. J. 329, 608.
    • (1998) Biochem. J. , vol.329 , pp. 608
    • Svensson, L.T.1    Enberg, S.T.2    Aoyama, T.3    Usuda, N.4    Alexson, S.E.H.5    Hashimoto, T.6
  • 49
    • 2542472615 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two mouse peroxisomal proliferator activated receptor α (PPARα)-regulated peroxisomal acyl CoA thioesterases
    • Westin, M.A.K., Alexson, S.E.H., and Hunt, M.C. (2004) Molecular Cloning and Characterization of Two Mouse Peroxisomal Proliferator Activated Receptor α (PPARα)-Regulated Peroxisomal Acyl CoA Thioesterases, J. Biol. Chem. 279, 21841-21848.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21841-21848
    • Westin, M.A.K.1    Alexson, S.E.H.2    Hunt, M.C.3
  • 50
    • 2542496085 scopus 로고    scopus 로고
    • Structural basis for HNF4α activation by ligand and coactivator binding
    • Duda, K., Chi, Y.-I., and Shoelson, S.E. (2004) Structural Basis for HNF4α Activation by Ligand and Coactivator Binding, J. Biol. Chem. 279, 23311-23316.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23311-23316
    • Duda, K.1    Chi, Y.-I.2    Shoelson, S.E.3
  • 51
    • 0023767035 scopus 로고
    • The molecular evolution of genes and proteins: A tale of two serines
    • Brenner, S. (1988) The Molecular Evolution of Genes and Proteins: A Tale of Two Serines, Nature 343, 528-530.
    • (1988) Nature , vol.343 , pp. 528-530
    • Brenner, S.1
  • 52
    • 0037207126 scopus 로고    scopus 로고
    • The catalytic cycle of biosynthetic thiolase: A conformational journey of an acetyl group through four binding modes and two oxyanion holes
    • Kursula, P., Ojala, J., Lambier, A.M., and Wieringa, R.K. (2002) The Catalytic Cycle of Biosynthetic Thiolase: A Conformational Journey of an Acetyl Group Through Four Binding Modes and Two Oxyanion Holes, Biochemistry 41, 15543-15556.
    • (2002) Biochemistry , vol.41 , pp. 15543-15556
    • Kursula, P.1    Ojala, J.2    Lambier, A.M.3    Wieringa, R.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.