메뉴 건너뛰기




Volumn 1, Issue 1, 2013, Pages 566-577

Functional characterization of genetic enzyme variations in human lipoxygenases

Author keywords

Eicosanoids; Gene polymorphism; Leukotrienes; Lipoxygenases; SNP

Indexed keywords

12 LIPOXYGENASE 12R TYPE; 15 LIPOXYGENASE TYPE 2; ARACHIDONATE 12 LIPOXYGENASE; ARACHIDONATE 15 LIPOXYGENASE; ARACHIDONATE 5 LIPOXYGENASE; EPIDERMIS TYPE LIPOXYGENASE 3; LIPOXYGENASE; UNCLASSIFIED DRUG; STOP CODON;

EID: 84893798556     PISSN: 22132317     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.redox.2013.11.001     Document Type: Article
Times cited : (27)

References (70)
  • 1
    • 80054052917 scopus 로고    scopus 로고
    • Lipoxygenase and leukotriene pathways: biochemistry, biology, and roles in disease
    • J.Z. Haeggström, C.D. Funk, Lipoxygenase and leukotriene pathways: biochemistry, biology, and roles in disease, Chem. Rev. 111 (2011) 5866-5898.
    • (2011) Chem. Rev , vol.111 , pp. 5866-5898
    • Haeggström, J.Z.1    Funk, C.D.2
  • 2
    • 0037393827 scopus 로고    scopus 로고
    • Free radicals and lipid signaling in endothelial cells
    • V.B. O'Donnell, Free radicals and lipid signaling in endothelial cells, Antioxid. Redox Signal. 5 (2) (2003) 195-203.
    • (2003) Antioxid. Redox Signal , vol.5 , Issue.2 , pp. 195-203
    • O'Donnell, V.B.1
  • 6
    • 38549129314 scopus 로고    scopus 로고
    • Conformational flexibility in mammalian 15S-lipoxygenase: reinterpretation of the crystallographic data
    • J. Choi, J.K. Chon, S. Kim, W. Shin, Conformational flexibility in mammalian 15S-lipoxygenase: reinterpretation of the crystallographic data, Proteins 70 (2008) 1023-1032.
    • (2008) Proteins , vol.70 , pp. 1023-1032
    • Choi, J.1    Chon, J.K.2    Kim, S.3    Shin, W.4
  • 8
    • 84865800398 scopus 로고    scopus 로고
    • Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis
    • S. Xu, T.C. Mueser, L.J. Marnett, M.O. Funk, Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis, Structure 20 (2012) 1490-1497.
    • (2012) Structure , vol.20 , pp. 1490-1497
    • Xu, S.1    Mueser, T.C.2    Marnett, L.J.3    Funk, M.O.4
  • 9
    • 76749132769 scopus 로고    scopus 로고
    • Leukotrienes in atherosclerosis: new target insights and future therapy perspectives
    • (2009) 737282
    • G. Riccioni, A. Zanasi, N. Vitulano, B. Mancini, N. D'Orazio, Leukotrienes in atherosclerosis: new target insights and future therapy perspectives, Mediators Inflamm. (2009) 737282. (2009).
    • (2009) Mediators Inflamm
    • Riccioni, G.1    Zanasi, A.2    Vitulano, N.3    Mancini, B.4    D'Orazio, N.5
  • 10
    • 33847638020 scopus 로고    scopus 로고
    • Eicosanoids in inflammation: biosynthesis, pharmacology, and therapeutic frontiers
    • S.P. Khanapure, D.S. Garvey, D.R. Janero, L.G. Letts, Eicosanoids in inflammation: biosynthesis, pharmacology, and therapeutic frontiers, Curr. Top. Med. Chem. 7 (2007) 311-340.
    • (2007) Curr. Top. Med. Chem. , vol.7 , pp. 311-340
    • Khanapure, S.P.1    Garvey, D.S.2    Janero, D.R.3    Letts, L.G.4
  • 11
    • 83855165094 scopus 로고    scopus 로고
    • Eicosanoid signalling pathways in the development and progression of colorectal cancer: novel approaches for prevention/intervention
    • M.C. Cathcart, J. Lysaght, G.P. Pidgeon, Eicosanoid signalling pathways in the development and progression of colorectal cancer: novel approaches for prevention/intervention, Cancer Metastasis Rev. 30 (2011) 363-385.
    • (2011) Cancer Metastasis Rev , vol.30 , pp. 363-385
    • Cathcart, M.C.1    Lysaght, J.2    Pidgeon, G.P.3
  • 12
    • 77955454197 scopus 로고    scopus 로고
    • Potential role of the lipoxygenase derived lipid mediators in atherosclerosis: leukotrienes, lipoxins and resolvins
    • M. Hersberger, Potential role of the lipoxygenase derived lipid mediators in atherosclerosis: leukotrienes, lipoxins and resolvins, Clin. Chem. Lab. Med. 48 (2010) 1063-1073.
    • (2010) Clin. Chem. Lab. Med. , vol.48 , pp. 1063-1073
    • Hersberger, M.1
  • 15
    • 84872705317 scopus 로고    scopus 로고
    • Association between genetic variants of the leukotriene biosynthesis pathway and the risk of stroke: a case-control study in the Chinese Han population
    • H. Sun, J. Zhang, J. Wang, T. Sun, H. Xiao, J.S. Zhang, Association between genetic variants of the leukotriene biosynthesis pathway and the risk of stroke: a case-control study in the Chinese Han population, Chin Med J (Engl) 126 (2013) 254-259.
    • (2013) Chin Med J (Engl) , vol.126 , pp. 254-259
    • Sun, H.1    Zhang, J.2    Wang, J.3    Sun, T.4    Xiao, H.5    Zhang, J.S.6
  • 19
    • 79551652304 scopus 로고    scopus 로고
    • Association of a functional polymorphism (Gln261Arg) in 12-lipoxygenase with breast cancer
    • V.V. Prasad, P. Kolli, D. Moganti, Association of a functional polymorphism (Gln261Arg) in 12-lipoxygenase with breast cancer, Exp. Ther. Med. 2 (2011) 317-323.
    • (2011) Exp. Ther. Med. , vol.2 , pp. 317-323
    • Prasad, V.V.1    Kolli, P.2    Moganti, D.3
  • 20
    • 77954529978 scopus 로고    scopus 로고
    • Association between polymorphisms of arachidonate 12-lipoxygenase (ALOX12) and schizophrenia in a Korean population
    • T. Kim, H.J. Kim, J.K. Park, J.W. Kim, J.H. Chung, Association between polymorphisms of arachidonate 12-lipoxygenase (ALOX12) and schizophrenia in a Korean population, Behav. Brain. Funct. 6 (2010) 44.
    • (2010) Behav. Brain. Funct. , vol.6 , pp. 44
    • Kim, T.1    Kim, H.J.2    Park, J.K.3    Kim, J.W.4    Chung, J.H.5
  • 21
    • 70350772548 scopus 로고    scopus 로고
    • Human platelet 12-lipoxygenase: naturally occurring Q261/R261 variants and N544L mutant show altered activity but unaffected substrate binding and membrane association behavior
    • A.M. Aleem, L. Wells, J. Jankun, M. Walther, H. Kühn, J. Reinartz, E. Skrzypczak-Jankun, Human platelet 12-lipoxygenase: naturally occurring Q261/R261 variants and N544L mutant show altered activity but unaffected substrate binding and membrane association behavior, Int. J. Mol. Med. 24 (2009) 759-764.
    • (2009) Int. J. Mol. Med. , vol.24 , pp. 759-764
    • Aleem, A.M.1    Wells, L.2    Jankun, J.3    Walther, M.4    Kühn, H.5    Reinartz, J.6    Skrzypczak-Jankun, E.7
  • 23
    • 79959903255 scopus 로고    scopus 로고
    • Molecular basis for the reduced catalytic activity of the naturally occurring T560M mutant of human 12/15-lipoxygenase that has been implicated in coronary artery disease
    • K. Schurmann, M. Anton, I. Ivanov, C. Richter, H. Kuhn, M. Walther, Molecular basis for the reduced catalytic activity of the naturally occurring T560M mutant of human 12/15-lipoxygenase that has been implicated in coronary artery disease, J. Biol. Chem. 286 (2011) 23920-23927.
    • (2011) J. Biol. Chem. , vol.286 , pp. 23920-23927
    • Schurmann, K.1    Anton, M.2    Ivanov, I.3    Richter, C.4    Kuhn, H.5    Walther, M.6
  • 25
    • 25444467735 scopus 로고    scopus 로고
    • Mutation spectrum and functional analysis of epidermis-type lipoxygenases in patients with autosomal recessive congenital ichthyosis
    • K.M. Eckl, P. Krieg, W. Küster, H. Traupe, F. André, N. Wittstruck, G. Fürstenberger, H.C. Hennies, Mutation spectrum and functional analysis of epidermis-type lipoxygenases in patients with autosomal recessive congenital ichthyosis, Hum. Mutat. 26 (2005) 351-361.
    • (2005) Hum. Mutat. , vol.26 , pp. 351-361
    • Eckl, K.M.1    Krieg, P.2    Küster, W.3    Traupe, H.4    André, F.5    Wittstruck, N.6    Fürstenberger, G.7    Hennies, H.C.8
  • 27
    • 54249118807 scopus 로고    scopus 로고
    • 5-lipoxygenase and 5-lipoxygenase-activating protein gene polymorphisms, dietary linoleic acid, and risk for breast cancer
    • J. Wang, E.M. John, S.A. Ingles, 5-lipoxygenase and 5-lipoxygenase-activating protein gene polymorphisms, dietary linoleic acid, and risk for breast cancer, Cancer Epidemiol. Biomarkers Prev. 17 (10) (2008) 2748-2754.
    • (2008) Cancer Epidemiol Biomarkers Prev , vol.17 , Issue.10 , pp. 2748-2754
    • Wang, J.1    John, E.M.2    Ingles, S.A.3
  • 29
    • 84883794867 scopus 로고    scopus 로고
    • Principal component analysis reveals the 1000 Genomes Project does not sufficiently cover the human genetic diversity in Asia
    • D. Lu, S. Xu, Principal component analysis reveals the 1000 Genomes Project does not sufficiently cover the human genetic diversity in Asia, Front Genet. 4 (2013) 127.
    • (2013) Front Genet , vol.4 , pp. 127
    • Lu, D.1    Xu, S.2
  • 30
    • 67650248242 scopus 로고    scopus 로고
    • Structural basis for pH-dependent alterations of reaction specificity of vertebrate lipoxygenase isoforms
    • 1791
    • M. Walther, J. Roffeis, C. Jansen, M. Anton, I. Ivanov, H. Kuhn, Structural basis for pH-dependent alterations of reaction specificity of vertebrate lipoxygenase isoforms, Biochim. Biophys. Acta. 827-835 (1791) 2009.
    • (2009) Biochim. Biophys. Acta. , pp. 827-835
    • Walther, M.1    Roffeis, J.2    Jansen, C.3    Anton, M.4    Ivanov, I.5    Kuhn, H.6
  • 31
    • 84872964202 scopus 로고    scopus 로고
    • Conversion of pro-inflammatory murine Alox5 into an antiinflammatory 15S-lipoxygenating enzyme by multiple mutations of sequence determinants
    • K. Hofheinz, K.R. Kakularam, S. Adel, M. Anton, A. Polymarasetty, P. Reddanna, H. Kuhn, T. Horn, Conversion of pro-inflammatory murine Alox5 into an antiinflammatory 15S-lipoxygenating enzyme by multiple mutations of sequence determinants, Arch. Biochem. Biophys. 530 (2013) 40-47.
    • (2013) Arch. Biochem. Biophys. , vol.530 , pp. 40-47
    • Hofheinz, K.1    Kakularam, K.R.2    Adel, S.3    Anton, M.4    Polymarasetty, A.5    Reddanna, P.6    Kuhn, H.7    Horn, T.8
  • 32
    • 84885418898 scopus 로고    scopus 로고
    • Qualitative and Quantitative analysis of 3D predicted arachidonate 15-lipoxygenase-B (15-LOX-2) from Homo sapiens
    • N. Arora, V.K. Singh, K. Shah, S. Pandey-Rai, Qualitative and Quantitative analysis of 3D predicted arachidonate 15-lipoxygenase-B (15-LOX-2) from Homo sapiens, Bioinformation 8 (2012) 555-561.
    • (2012) Bioinformation , vol.8 , pp. 555-561
    • Arora, N.1    Singh, V.K.2    Shah, K.3    Pandey-Rai, S.4
  • 34
    • 35748965848 scopus 로고    scopus 로고
    • Comparative protein structure modeling by combining multiple templates and optimizing sequence-to-structure alignments
    • N. Fernandez-Fuentes, B.K. Rai, C.J. Madrid-Aliste, J.E. Fajardo, A. Fiser, Comparative protein structure modeling by combining multiple templates and optimizing sequence-to-structure alignments, Bioinformatics 23 (2007) 2558-2565.
    • (2007) Bioinformatics , vol.23 , pp. 2558-2565
    • Fernandez-Fuentes, N.1    Rai, B.K.2    Madrid-Aliste, C.J.3    Fajardo, J.E.4    Fiser, A.5
  • 35
    • 84871034858 scopus 로고    scopus 로고
    • 3Drefine: consistent protein structure refinement by optimizing hydrogen bonding network and atomic-level energy minimization
    • D. Bhattacharya, J. Cheng, 3Drefine: consistent protein structure refinement by optimizing hydrogen bonding network and atomic-level energy minimization, Proteins 81 (2013) 119-131.
    • (2013) Proteins , vol.81 , pp. 119-131
    • Bhattacharya, D.1    Cheng, J.2
  • 38
    • 67650358909 scopus 로고    scopus 로고
    • QMEAN server for protein model quality estimation
    • P. Benkert, M. Künzli, T. Schwede, QMEAN server for protein model quality estimation, Nucleic Acids Res. 37 (2009) W510-W514.
    • (2009) Nucleic Acids Res , vol.37 , pp. W510-W514
    • Benkert, P.1    Künzli, M.2    Schwede, T.3
  • 40
  • 41
    • 80054795390 scopus 로고    scopus 로고
    • Stereocontrol of arachidonic acid oxygenation by vertebrate lipoxygenases: newly cloned zebrafish lipoxygenase 1 does not follow the Ala-versus-Gly concept
    • C. Jansen, K. Hofheinz, R. Vogel, J. Roffeis, M. Anton, P. Reddanna, H. Kuhn, M. Walther, Stereocontrol of arachidonic acid oxygenation by vertebrate lipoxygenases: newly cloned zebrafish lipoxygenase 1 does not follow the Ala-versus-Gly concept, J. Biol. Chem. 286 (2011) 37804-37812.
    • (2011) J. Biol. Chem. , vol.286 , pp. 37804-37812
    • Jansen, C.1    Hofheinz, K.2    Vogel, R.3    Roffeis, J.4    Anton, M.5    Reddanna, P.6    Kuhn, H.7    Walther, M.8
  • 42
    • 8144220042 scopus 로고    scopus 로고
    • A single active site residue directs oxygenation stereospecificity in lipoxygenases: stereocontrol is linked to the position of oxygenation
    • G. Coffa, A.R. Brash, A single active site residue directs oxygenation stereospecificity in lipoxygenases: stereocontrol is linked to the position of oxygenation, Proc. Natl. Acad. Sci. USA 101 (2004) 15579-15584.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15579-15584
    • Coffa, G.1    Brash, A.R.2
  • 43
    • 0025084538 scopus 로고
    • Oxygenation of biological membranes by the pure reticulocyte lipoxygenase
    • H. Kuhn, J. Belkner, R. Wiesner, A.R. Brash, Oxygenation of biological membranes by the pure reticulocyte lipoxygenase, J. Biol. Chem. 265 (1990) 18351-18361.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18351-18361
    • Kuhn, H.1    Belkner, J.2    Wiesner, R.3    Brash, A.R.4
  • 44
    • 0942276361 scopus 로고    scopus 로고
    • Investigations into calcium-dependent membrane association of 15-lipoxygenase-1 Mechanistic roles of surfaceexposed hydrophobic amino acids and calcium
    • M. Walther, R. Wiesner, H. Kuhn, Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. Mechanistic roles of surfaceexposed hydrophobic amino acids and calcium, J. Biol. Chem. 279 (2004) 3717-3725.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3717-3725
    • Walther, M.1    Wiesner, R.2    Kuhn, H.3
  • 45
    • 0029795583 scopus 로고    scopus 로고
    • Defining the arachidonic acid binding site of human 15-lipoxygenase Molecular modeling and mutagenesis
    • Q.F. Gan, M.F. Browner, D.L. Sloane, E. Sigal, Defining the arachidonic acid binding site of human 15-lipoxygenase. Molecular modeling and mutagenesis, J. Biol. Chem. 271 (1996) 25412-25418.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25412-25418
    • Gan, Q.F.1    Browner, M.F.2    Sloane, D.L.3    Sigal, E.4
  • 46
    • 77952726068 scopus 로고    scopus 로고
    • Insights into the mechanism of binding of arachidonic acid to mammalian 15-lipoxygenases
    • L. Toledo, L. Masgrau, J.D. Maréchal, J.M. Lluch, A. González-Lafont, Insights into the mechanism of binding of arachidonic acid to mammalian 15-lipoxygenases, J. Phys. Chem. B 114 (2010) 7037-7046.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7037-7046
    • Toledo, L.1    Masgrau, L.2    Maréchal, J.D.3    Lluch, J.M.4    González-Lafont, A.5
  • 48
    • 77952312969 scopus 로고    scopus 로고
    • Regulation of the activity of 5-lipoxygenase, a key enzyme in leukotriene biosynthesis
    • O. Rådmark, B. Samuelsson, Regulation of the activity of 5-lipoxygenase, a key enzyme in leukotriene biosynthesis, Biochem. Biophys. Res. Commun. 396 (2010) 105-110.
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 105-110
    • Rådmark, O.1    Samuelsson, B.2
  • 49
    • 0035808468 scopus 로고    scopus 로고
    • Structural basis for lipoxygenase specificity Conversion of the human leukocyte 5-lipoxygenase to a 15-lipoxygenating enzyme species by site-directed mutagenesis
    • K. Schwarz, M. Walther, M. Anton, C. Gerth, I. Feussner, H. Kuhn, Structural basis for lipoxygenase specificity. Conversion of the human leukocyte 5-lipoxygenase to a 15-lipoxygenating enzyme species by site-directed mutagenesis, J. Biol. Chem. 276 (2001) 773-779.
    • (2001) J. Biol. Chem. , vol.276 , pp. 773-779
    • Schwarz, K.1    Walther, M.2    Anton, M.3    Gerth, C.4    Feussner, I.5    Kuhn, H.6
  • 50
    • 0000822547 scopus 로고
    • Prostaglandin endoperoxides Novel transformations of arachidonic acid in human platelets
    • M. Hamberg, B. Samuelsson, Prostaglandin endoperoxides. Novel transformations of arachidonic acid in human platelets, Proc. Natl. Acad. Sci. USA 71 (1974) 3400-3404.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3400-3404
    • Hamberg, M.1    Samuelsson, B.2
  • 51
    • 84876807670 scopus 로고    scopus 로고
    • Lipoxygenase pathways in Homo neanderthalensis: functional comparison with Homo sapiens isoforms
    • P. Chaitidis, S. Adel, M. Anton, D. Heydeck, H. Kuhn, T. Horn, Lipoxygenase pathways in Homo neanderthalensis: functional comparison with Homo sapiens isoforms, J. Lipid. Res. 54 (2013) 1397-1409.
    • (2013) J. Lipid. Res. , vol.54 , pp. 1397-1409
    • Chaitidis, P.1    Adel, S.2    Anton, M.3    Heydeck, D.4    Kuhn, H.5    Horn, T.6
  • 54
    • 0033966938 scopus 로고    scopus 로고
    • Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2
    • M. Jisaka, R.B. Kim, W.E. Boeglin, A.R. Brash, Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2, J. Biol. Chem. 275 (2000) 1287-1293.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1287-1293
    • Jisaka, M.1    Kim, R.B.2    Boeglin, W.E.3    Brash, A.R.4
  • 55
    • 20644448592 scopus 로고    scopus 로고
    • Human 12(R)-lipoxygenase and the mouse ortholog Molecular cloning, expression, and gene chromosomal assignment
    • D. Sun, M. McDonnell, X.S. Chen, M.M. Lakkis, H. Li, S.N. Isaacs, S.H. Elsea, P.I. Patel, C.D. Funk, Human 12(R)-lipoxygenase and the mouse ortholog. Molecular cloning, expression, and gene chromosomal assignment, J. Biol. Chem. 273 (50) (1998) 33540-33547.
    • (1998) J. Biol. Chem. , vol.273 , Issue.50 , pp. 33540-33547
    • Sun, D.1    McDonnell, M.2    Chen, X.S.3    Lakkis, M.M.4    Li, H.5    Isaacs, S.N.6    Elsea, S.H.7    Patel, P.I.8    Funk, C.D.9
  • 56
    • 0032499790 scopus 로고    scopus 로고
    • A 12R-lipoxygenase in human skin: mechanistic evidence, molecular cloning, and expression
    • W.E. Boeglin, R.B. Kim, A.R. Brash, A 12R-lipoxygenase in human skin: mechanistic evidence, molecular cloning, and expression, Proc. Natl. Acad. Sci. USA 95 (1998) 6744-6749.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6744-6749
    • Boeglin, W.E.1    Kim, R.B.2    Brash, A.R.3
  • 57
    • 0033057031 scopus 로고    scopus 로고
    • Murine 12(R)- lipoxygenase: functional expression, genomic structure and chromosomal localization
    • P. Krieg, M. Siebert, A. Kinzig, R. Bettenhausen, F. Marks, G. Fürstenberger, Murine 12(R)- lipoxygenase: functional expression, genomic structure and chromosomal localization, FEBS Lett. 446 (1999) 142-148.
    • (1999) FEBS Lett , vol.446 , pp. 142-148
    • Krieg, P.1    Siebert, M.2    Kinzig, A.3    Bettenhausen, R.4    Marks, F.5    Fürstenberger, G.6
  • 59
    • 0035336301 scopus 로고    scopus 로고
    • A gene cluster encoding human epidermistype lipoxygenases at chromosome 17p13.1: cloning, physical mapping, and expression
    • P. Krieg, F. Marks, G. Fürstenberger, A gene cluster encoding human epidermistype lipoxygenases at chromosome 17p13.1: cloning, physical mapping, and expression, Genomics 73 (2001) 323-330.
    • (2001) Genomics , vol.73 , pp. 323-330
    • Krieg, P.1    Marks, F.2    Fürstenberger, G.3
  • 61
    • 33750706936 scopus 로고    scopus 로고
    • Human and mouse eLOX3 have distinct substrate specificities: implications for their linkage with lipoxygenases in skin
    • Z. Yu, C. Schneider, W.E. Boeglin, A.R. Brash, Human and mouse eLOX3 have distinct substrate specificities: implications for their linkage with lipoxygenases in skin, Arch. Biochem. Biophys. 455 (2) (2006) 188-196.
    • (2006) Arch. Biochem. Biophys. , vol.455 , Issue.2 , pp. 188-196
    • Yu, Z.1    Schneider, C.2    Boeglin, W.E.3    Brash, A.R.4
  • 62
    • 78650074364 scopus 로고    scopus 로고
    • On the role of molecular oxygen in lipoxygenase activation: comparison and contrast of epidermal lipoxygenase-3 with soybean lipoxygenase-1
    • Y. Zheng, A.R. Brash, On the role of molecular oxygen in lipoxygenase activation: comparison and contrast of epidermal lipoxygenase-3 with soybean lipoxygenase-1, J. Biol. Chem. 285 (51) (2010) 39876-39887.
    • (2010) J. Biol. Chem. , vol.285 , Issue.51 , pp. 39876-39887
    • Zheng, Y.1    Brash, A.R.2
  • 63
    • 78650037229 scopus 로고    scopus 로고
    • Dioxygenase activity of epidermal lipoxygenase-3 unveiled: typical and atypical features of its catalytic activity with natural and synthetic polyunsaturated fatty acids
    • Y. Zheng, A.R. Brash, Dioxygenase activity of epidermal lipoxygenase-3 unveiled: typical and atypical features of its catalytic activity with natural and synthetic polyunsaturated fatty acids, J. Biol. Chem. 285 (51) (2010) 39866-39875.
    • (2010) J. Biol. Chem. , vol.285 , Issue.51 , pp. 39866-39875
    • Zheng, Y.1    Brash, A.R.2
  • 64
    • 79551619981 scopus 로고    scopus 로고
    • Evolutionary evidence of the effect of rare variants on disease etiology
    • I.P. Gorlov, O.Y. Gorlova, M.L. Frazier, M.R. Spitz, C.I. Amos, Evolutionary evidence of the effect of rare variants on disease etiology, Clin. Genet. 79 (2011) 199-206.
    • (2011) Clin. Genet. , vol.79 , pp. 199-206
    • Gorlov, I.P.1    Gorlova, O.Y.2    Frazier, M.L.3    Spitz, M.R.4    Amos, C.I.5
  • 65
    • 42649089790 scopus 로고    scopus 로고
    • Resolving inflammation: dual antiinflammatory and pro-resolution lipid mediators
    • C.N. Serhan, N. Chiang, T.E. Van Dyke, Resolving inflammation: dual antiinflammatory and pro-resolution lipid mediators, Nat. Rev. Immunol. 8 (2008) 349-361.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 349-361
    • Serhan, C.N.1    Chiang, N.2    Van Dyke, T.E.3
  • 67
    • 80054803830 scopus 로고    scopus 로고
    • Structural insight of dopamine β-hydroxylase, a drug target for complex traits, and functional significance of exonic single nucleotide polymorphisms
    • A. Kapoor, M. Shandilya, S. Kundu, Structural insight of dopamine β-hydroxylase, a drug target for complex traits, and functional significance of exonic single nucleotide polymorphisms, PLoS One 6 (2011) e26509.
    • (2011) PLoS One , vol.6
    • Kapoor, A.1    Shandilya, M.2    Kundu, S.3
  • 68
    • 84885190937 scopus 로고    scopus 로고
    • The effects of non-synonymous single nucleotide polymorphisms (nsSNPs) on protein-protein interactions
    • C.M. Yates, M.J. Sternberg, The effects of non-synonymous single nucleotide polymorphisms (nsSNPs) on protein-protein interactions, J. Mol. Biol. 425 (21) (2013) 3949-3963.
    • (2013) J. Mol. Biol , vol.425 , Issue.21 , pp. 3949-3963
    • Yates, C.M.1    Sternberg, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.