메뉴 건너뛰기




Volumn 12, Issue 1, 2011, Pages

Fatty acyl-CoA reductases of birds

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOESTER; WAX; ALDEHYDE DEHYDROGENASE; AVIAN PROTEIN; HEXADECANAL DEHYDROGENASE (ACYLATING);

EID: 83155185481     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-12-64     Document Type: Article
Times cited : (41)

References (57)
  • 1
    • 0033759056 scopus 로고    scopus 로고
    • Purification of a jojoba embryo fatty acyl-coenzyme A reductase and expression of its cDNA in high erucic acid rapeseed
    • 10.1104/pp.122.3.635 10712526
    • Purification of a jojoba embryo fatty acyl-coenzyme A reductase and expression of its cDNA in high erucic acid rapeseed. Metz JG, Pollard MR, Anderson L, Hayes TR, Lassner MW, Plant Physiol 2000 122 3 635 644 10.1104/pp.122.3.635 10712526
    • (2000) Plant Physiol , vol.122 , Issue.3 , pp. 635-644
    • Metz, J.G.1    Pollard, M.R.2    Anderson, L.3    Hayes, T.R.4    Lassner, M.W.5
  • 2
    • 0031002077 scopus 로고    scopus 로고
    • Isolation of mutants of Acinetobacter calcoaceticus deficient in wax ester synthesis and complementation of one mutation with a gene encoding a fatty acyl coenzyme A reductase
    • Isolation of mutants of Acinetobacter calcoaceticus deficient in wax ester synthesis and complementation of one mutation with a gene encoding a fatty acyl coenzyme A reductase. Reiser S, Somerville C, J Bacteriol 1997 179 9 2969 2975 9139916 (Pubitemid 27194447)
    • (1997) Journal of Bacteriology , vol.179 , Issue.9 , pp. 2969-2975
    • Reiser, S.1    Somerville, C.2
  • 3
    • 0019958289 scopus 로고
    • Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex
    • Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex. Riendeau D, Rodriguez A, Meighen E, J Biol Chem 1982 257 12 6908 6915 7085612 (Pubitemid 12022284)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.12 , pp. 6908-6915
    • Riendeau, D.1    Rodriguez, A.2    Meighen, E.3
  • 4
    • 0021111862 scopus 로고
    • Purification of the acyl coenzyme A reductase component from a complex responsible for the reduction of fatty acids in biolumniscent bacteria. Properties and acyltransferase activity
    • 6833298
    • Purification of the acyl coenzyme A reductase component from a complex responsible for the reduction of fatty acids in biolumniscent bacteria. Properties and acyltransferase activity. Rodriguez A, Riendeau D, Meighen E, J Biol Chem 1983 258 8 5233 5237 6833298
    • (1983) J Biol Chem , vol.258 , Issue.8 , pp. 5233-5237
    • Rodriguez, A.1    Riendeau, D.2    Meighen, E.3
  • 5
    • 0029125582 scopus 로고
    • Solubilization and purification of aldehyde-generating fatty acyl-CoA reductase from green alga Botryococcus braunii
    • 10.1016/0014-5793(95)00781-4 7649295
    • Solubilization and purification of aldehyde-generating fatty acyl-CoA reductase from green alga Botryococcus braunii. Wang X, Kolattukudy PE, FEBS Lett 1995 370 1-2 15 18 10.1016/0014-5793(95)00781-4 7649295
    • (1995) FEBS Lett , vol.370 , Issue.1-2 , pp. 15-18
    • Wang, X.1    Kolattukudy, P.E.2
  • 6
    • 0031127392 scopus 로고    scopus 로고
    • Resolution and purification of an aldehyde-generating and an alcohol- generating fatty acyl-CoA reductase from pea leaves (Pisum sativum L.)
    • DOI 10.1006/abbi.1997.9932
    • Resolution and purification of an aldehyde-generating and an alcohol-generating fatty acyl-CoA reductase from pea leaves (Pisum sativum L.). Vioque J, Kolattukudy PE, Arch Biochem Biophys 1997 340 1 64 72 10.1006/abbi.1997.9932 9126278 (Pubitemid 27200275)
    • (1997) Archives of Biochemistry and Biophysics , vol.340 , Issue.1 , pp. 64-72
    • Vioque, J.1    Kolattukudy, P.E.2
  • 7
    • 65549089961 scopus 로고    scopus 로고
    • Purification, characterization, and potential bacterial wax production role of an NADPH-dependent fatty aldehyde reductase from Marinobacter aquaeolei VT8
    • 10.1128/AEM.02578-08 19270127
    • Purification, characterization, and potential bacterial wax production role of an NADPH-dependent fatty aldehyde reductase from Marinobacter aquaeolei VT8. Wahlen BD, Oswald WS, Seefeldt LC, Barney BM, Appl Environ Microbiol 2009 75 9 2758 2764 10.1128/AEM.02578-08 19270127
    • (2009) Appl Environ Microbiol , vol.75 , Issue.9 , pp. 2758-2764
    • Wahlen, B.D.1    Oswald, W.S.2    Seefeldt, L.C.3    Barney, B.M.4
  • 8
    • 77955690169 scopus 로고    scopus 로고
    • Three Arabidopsis fatty acyl-coenzyme A reductases, FAR1, FAR4, and FAR5, generate primary fatty alcohols associated with suberin deposition
    • 10.1104/pp.110.158238 20571114
    • Three Arabidopsis fatty acyl-coenzyme A reductases, FAR1, FAR4, and FAR5, generate primary fatty alcohols associated with suberin deposition. Domergue F, Vishwanath SJ, Joubes J, Ono J, Lee JA, Bourdon M, Alhattab R, Lowe C, Pascal S, Lessire R, et al. Plant Physiol 2010 153 4 1539 1554 10.1104/pp.110.158238 20571114
    • (2010) Plant Physiol , vol.153 , Issue.4 , pp. 1539-1554
    • Domergue, F.1    Vishwanath, S.J.2    Joubes, J.3    Ono, J.4    Lee, J.A.5    Bourdon, M.6    Alhattab, R.7    Lowe, C.8    Pascal, S.9    Lessire, R.10
  • 9
    • 65049083862 scopus 로고    scopus 로고
    • Functional expression of five Arabidopsis fatty acyl-CoA reductase genes in Escherichia coli
    • 10.1016/j.jplph.2008.10.003 19062129
    • Functional expression of five Arabidopsis fatty acyl-CoA reductase genes in Escherichia coli. Doan TT, Carlsson AS, Hamberg M, Bulow L, Stymne S, Olsson P, J Plant Physiol 2009 166 8 787 796 10.1016/j.jplph.2008.10.003 19062129
    • (2009) J Plant Physiol , vol.166 , Issue.8 , pp. 787-796
    • Doan, T.T.1    Carlsson, A.S.2    Hamberg, M.3    Bulow, L.4    Stymne, S.5    Olsson, P.6
  • 10
    • 33751110474 scopus 로고    scopus 로고
    • CER4 encodes an alcohol-forming fatty acyl-coenzyme A reductase involved in cuticular wax production in Arabidopsis
    • DOI 10.1104/pp.106.086785
    • CER4 encodes an alcohol-forming fatty acyl-coenzyme A reductase involved in cuticular wax production in Arabidopsis. Rowland O, Zheng H, Hepworth SR, Lam P, Jetter R, Kunst L, Plant Physiol 2006 142 3 866 877 10.1104/pp.106.086785 16980563 (Pubitemid 44764615)
    • (2006) Plant Physiology , vol.142 , Issue.3 , pp. 866-877
    • Rowland, O.1    Zheng, H.2    Hepworth, S.R.3    Lam, P.4    Jetter, R.5    Kunst, L.6
  • 11
    • 0036017865 scopus 로고    scopus 로고
    • Male gametophyte development in bread wheat (Triticum aestivum L.): Molecular, cellular, and biochemical analyses of a sporophytic contribution to pollen wall ontogeny
    • DOI 10.1046/j.1365-313X.2002.01313.x
    • Male gametophyte development in bread wheat (Triticum aestivum L.): molecular, cellular, and biochemical analyses of a sporophytic contribution to pollen wall ontogeny. Wang A, Xia Q, Xie W, Dumonceaux T, Zou J, Datla R, Selvaraj G, Plant J 2002 30 6 613 623 10.1046/j.1365-313X.2002.01313.x 12061894 (Pubitemid 34696055)
    • (2002) Plant Journal , vol.30 , Issue.6 , pp. 613-623
    • Wang, A.1    Xia, Q.2    Xie, W.3    Dumonceaux, T.4    Zou, J.5    Datla, R.6    Selvaraj, G.7
  • 12
    • 4444258170 scopus 로고    scopus 로고
    • Mammalian wax biosynthesis: I. Identification of two fatty acyl-coenzyme A reductases with different substrate specificities and tissue distributions
    • DOI 10.1074/jbc.M406225200
    • Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions. Cheng JB, Russell DW, J Biol Chem 2004 279 36 37789 37797 10.1074/jbc.M406225200 15220348 (Pubitemid 39195493)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37789-37797
    • Cheng, J.B.1    Russell, D.W.2
  • 14
    • 77956181781 scopus 로고    scopus 로고
    • A fatty acyl-CoA reductase highly expressed in the head of honey bee (Apis mellifera) involves biosynthesis of a wide range of aliphatic fatty alcohols
    • 10.1016/j.ibmb.2010.06.004 20542116
    • A fatty acyl-CoA reductase highly expressed in the head of honey bee (Apis mellifera) involves biosynthesis of a wide range of aliphatic fatty alcohols. Teerawanichpan P, Robertson AJ, Qiu X, Insect Biochem Mol Biol 2010 40 9 641 649 10.1016/j.ibmb.2010.06.004 20542116
    • (2010) Insect Biochem Mol Biol , vol.40 , Issue.9 , pp. 641-649
    • Teerawanichpan, P.1    Robertson, A.J.2    Qiu, X.3
  • 17
    • 60549085039 scopus 로고    scopus 로고
    • Pheromone-gland-specific fatty-acyl reductase in the adzuki bean borer, Ostrinia scapulalis (Lepidoptera: Crambidae)
    • 10.1016/j.ibmb.2008.10.008 19041942
    • Pheromone-gland-specific fatty-acyl reductase in the adzuki bean borer, Ostrinia scapulalis (Lepidoptera: Crambidae). Antony B, Fujii T, Moto K, Matsumoto S, Fukuzawa M, Nakano R, Tatsuki S, Ishikawa Y, Insect Biochem Mol Biol 2009 39 2 90 95 10.1016/j.ibmb.2008.10.008 19041942
    • (2009) Insect Biochem Mol Biol , vol.39 , Issue.2 , pp. 90-95
    • Antony, B.1    Fujii, T.2    Moto, K.3    Matsumoto, S.4    Fukuzawa, M.5    Nakano, R.6    Tatsuki, S.7    Ishikawa, Y.8
  • 18
    • 0028910763 scopus 로고
    • Solubilization, purification and characterization of fatty acyl-CoA reductase from duck uropygial gland
    • 10.1006/bbrc.1995.1325 7887931
    • Solubilization, purification and characterization of fatty acyl-CoA reductase from duck uropygial gland. Wang X, Kolattukudy PE, Biochem Biophys Res Commun 1995 208 1 210 215 10.1006/bbrc.1995.1325 7887931
    • (1995) Biochem Biophys Res Commun , vol.208 , Issue.1 , pp. 210-215
    • Wang, X.1    Kolattukudy, P.E.2
  • 19
    • 77949875486 scopus 로고    scopus 로고
    • Fatty acyl-CoA reductase and wax synthase from Euglena gracilis in the biosynthesis of medium-chain wax esters
    • 10.1007/s11745-010-3395-2 20195781
    • Fatty acyl-CoA reductase and wax synthase from Euglena gracilis in the biosynthesis of medium-chain wax esters. Teerawanichpan P, Qiu X, Lipids 2010 45 3 263 273 10.1007/s11745-010-3395-2 20195781
    • (2010) Lipids , vol.45 , Issue.3 , pp. 263-273
    • Teerawanichpan, P.1    Qiu, X.2
  • 20
    • 0014930876 scopus 로고
    • Reduction of fatty acids to alcohols by cell-free preparations of Euglena gracilis
    • 10.1021/bi00807a007 4313936
    • Reduction of fatty acids to alcohols by cell-free preparations of Euglena gracilis. Kolattukudy PE, Biochemistry 1970 9 5 1095 1102 10.1021/bi00807a007 4313936
    • (1970) Biochemistry , vol.9 , Issue.5 , pp. 1095-1102
    • Kolattukudy, P.E.1
  • 21
    • 77249119232 scopus 로고    scopus 로고
    • Molecular mechanisms underlying sex pheromone production in moths
    • 10.1271/bbb.90756 20139627
    • Molecular mechanisms underlying sex pheromone production in moths. Matsumoto S, Biosci Biotechnol Biochem 2010 74 2 223 231 10.1271/bbb.90756 20139627
    • (2010) Biosci Biotechnol Biochem , vol.74 , Issue.2 , pp. 223-231
    • Matsumoto, S.1
  • 22
    • 4444272576 scopus 로고    scopus 로고
    • Mammalian wax biosynthesis: II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family
    • DOI 10.1074/jbc.M406226200
    • Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family. Cheng JB, Russell DW, J Biol Chem 2004 279 36 37798 37807 10.1074/jbc.M406226200 15220349 (Pubitemid 39195494)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37798-37807
    • Cheng, J.B.1    Russell, D.W.2
  • 23
    • 77950551803 scopus 로고    scopus 로고
    • Posttranslational regulation of fatty acyl-CoA reductase 1, Far1, controls ether glycerophospholipid synthesis
    • 10.1074/jbc.M109.083311 20071337
    • Posttranslational regulation of fatty acyl-CoA reductase 1, Far1, controls ether glycerophospholipid synthesis. Honsho M, Asaoku S, Fujiki Y, J Biol Chem 2010 285 12 8537 8542 10.1074/jbc.M109.083311 20071337
    • (2010) J Biol Chem , vol.285 , Issue.12 , pp. 8537-8542
    • Honsho, M.1    Asaoku, S.2    Fujiki, Y.3
  • 24
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • DOI 10.1146/annurev.biochem.74.082803.133329
    • Biochemistry of mammalian peroxisomes revisited. Wanders RJ, Waterham HR, Annu Rev Biochem 2006 75 295 332 10.1146/annurev.biochem.74.082803.133329 16756494 (Pubitemid 44118035)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 295-332
    • Wanders, R.J.A.1    Waterham, H.R.2
  • 25
    • 34247134608 scopus 로고    scopus 로고
    • Putative chemical signals about sex, individuality, and genetic background in the preputial gland and urine of the house mouse (mus musculus)
    • DOI 10.1093/chemse/bjl058
    • Putative chemical signals about sex, individuality, and genetic background in the preputial gland and urine of the house mouse (Mus musculus). Zhang JX, Rao XP, Sun L, Zhao CH, Qin XW, Chem Senses 2007 32 3 293 303 17251176 (Pubitemid 46585587)
    • (2007) Chemical Senses , vol.32 , Issue.3 , pp. 293-303
    • Zhang, J.-X.1    Rao, X.-P.2    Sun, L.3    Zhao, C.-H.4    Qin, X.-W.5
  • 26
    • 53149106233 scopus 로고    scopus 로고
    • Dual role of preputial gland secretion and its major components in sex recognition of mice
    • 10.1016/j.physbeh.2008.07.002 18657559
    • Dual role of preputial gland secretion and its major components in sex recognition of mice. Zhang JX, Liu YJ, Zhang JH, Sun L, Physiol Behav 2008 95 3 388 394 10.1016/j.physbeh.2008.07.002 18657559
    • (2008) Physiol Behav , vol.95 , Issue.3 , pp. 388-394
    • Zhang, J.X.1    Liu, Y.J.2    Zhang, J.H.3    Sun, L.4
  • 27
    • 69249225559 scopus 로고    scopus 로고
    • Physiological and biochemical aspects of the avian uropygial gland
    • 19675950
    • Physiological and biochemical aspects of the avian uropygial gland. Salibian A, Montalti D, Braz J Biol 2009 69 2 437 446 19675950
    • (2009) Braz J Biol , vol.69 , Issue.2 , pp. 437-446
    • Salibian, A.1    Montalti, D.2
  • 28
    • 84970627094 scopus 로고
    • Studies in Waxes XXI. The branched-chain acids of the preen gland wax of goose
    • 10.1071/CH9620510
    • Studies in Waxes XXI. The branched-chain acids of the preen gland wax of goose. Murray KE, Australian Journal of Chemistry 1962 15 3 510 520 10.1071/CH9620510
    • (1962) Australian Journal of Chemistry , vol.15 , Issue.3 , pp. 510-520
    • Murray, K.E.1
  • 29
    • 0016691456 scopus 로고
    • Lipid biosynthesis in the sebaceous glands: Synthesis of multibranched fatty acids from methylmalonyl-coenzyme A in cell-free preparations from the uropygial gland of goose
    • 10.1021/bi00679a033 235967
    • Lipid biosynthesis in the sebaceous glands: synthesis of multibranched fatty acids from methylmalonyl-coenzyme A in cell-free preparations from the uropygial gland of goose. Buckner JS, Kolattukudy PE, Biochemistry 1975 14 8 1774 1782 10.1021/bi00679a033 235967
    • (1975) Biochemistry , vol.14 , Issue.8 , pp. 1774-1782
    • Buckner, J.S.1    Kolattukudy, P.E.2
  • 30
    • 0016066910 scopus 로고
    • Chemical composition of uropygial gland secretions of owls
    • 4827914
    • Chemical composition of uropygial gland secretions of owls. Jacob J, Poltz J, J Lipid Res 1974 15 3 243 248 4827914
    • (1974) J Lipid Res , vol.15 , Issue.3 , pp. 243-248
    • Jacob, J.1    Poltz, J.2
  • 31
    • 0017111283 scopus 로고
    • Synthesis of 2,3-diols in chicken uropygial glands
    • 10.1016/0305-0491(76)90126-7 939090
    • Synthesis of 2,3-diols in chicken uropygial glands. Tang BY, Hansen IA, Comp Biochem Physiol B 1976 54 4 483 488 10.1016/0305-0491(76)90126-7 939090
    • (1976) Comp Biochem Physiol B , vol.54 , Issue.4 , pp. 483-488
    • Tang, B.Y.1    Hansen, I.A.2
  • 32
    • 0017256680 scopus 로고
    • Wax ester synthesis in the uropygial glands of the chicken and turkey
    • 10.1016/0305-0491(76)90197-8 1261233
    • Wax ester synthesis in the uropygial glands of the chicken and turkey. Tang BY, Hansen IA, Comp Biochem Physiol B 1976 53 4 451 453 10.1016/0305-0491(76)90197-8 1261233
    • (1976) Comp Biochem Physiol B , vol.53 , Issue.4 , pp. 451-453
    • Tang, B.Y.1    Hansen, I.A.2
  • 33
    • 0015494326 scopus 로고
    • Lipogenesis in chicken uropygial glands
    • 10.1111/j.1432-1033.1972.tb02543.x 4405242
    • Lipogenesis in chicken uropygial glands. Tang BY, Hansen IA, Eur J Biochem 1972 31 2 372 377 10.1111/j.1432-1033.1972.tb02543.x 4405242
    • (1972) Eur J Biochem , vol.31 , Issue.2 , pp. 372-377
    • Tang, B.Y.1    Hansen, I.A.2
  • 34
    • 77953882085 scopus 로고    scopus 로고
    • Uropygial gland-secreted alkanols contribute to olfactory sex signals in budgerigars
    • 10.1093/chemse/bjq025 20212012
    • Uropygial gland-secreted alkanols contribute to olfactory sex signals in budgerigars. Zhang JX, Wei W, Zhang JH, Yang WH, Chem Senses 2010 35 5 375 382 10.1093/chemse/bjq025 20212012
    • (2010) Chem Senses , vol.35 , Issue.5 , pp. 375-382
    • Zhang, J.X.1    Wei, W.2    Zhang, J.H.3    Yang, W.H.4
  • 35
    • 58249098401 scopus 로고    scopus 로고
    • The role of uropygial gland on sexual behavior in domestic chicken Gallus gallus domesticus
    • 10.1016/j.beproc.2008.10.006 19013507
    • The role of uropygial gland on sexual behavior in domestic chicken Gallus gallus domesticus. Hirao A, Aoyama M, Sugita S, Behav Processes 2009 80 2 115 120 10.1016/j.beproc.2008.10.006 19013507
    • (2009) Behav Processes , vol.80 , Issue.2 , pp. 115-120
    • Hirao, A.1    Aoyama, M.2    Sugita, S.3
  • 39
    • 0017805082 scopus 로고
    • Synthesis of multimethyl-branched fatty acids by avian and mammalian fatty acid synthetase and its regulation by malonyl-CoA decarboxylase in the uropygial gland
    • Synthesis of multimethyl-branched fatty acids by avian and mammalian fatty acid synthetase and its regulation by malonyl-CoA decarboxylase in the uropygial gland. Buckner JS, Kolattukudy PE, Rogers L, Arch Biochem Biophys 1978 186 1 152 163 10.1016/0003-9861(78)90474-5 629531 (Pubitemid 8290495)
    • (1978) Archives of Biochemistry and Biophysics , vol.186 , Issue.1 , pp. 152-163
    • Buckner, J.S.1    Kolattukudy, P.E.2    Rogers, L.3
  • 40
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ, Nucleic Acids Res 1997 25 17 3389 3402 10.1093/nar/25.17.3389 9254694 (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 41
    • 27144489108 scopus 로고    scopus 로고
    • Protein database searches using compositionally adjusted substitution matrices
    • DOI 10.1111/j.1742-4658.2005.04945.x
    • Protein database searches using compositionally adjusted substitution matrices. Altschul SF, Wootton JC, Gertz EM, Agarwala R, Morgulis A, Schaffer AA, Yu YK, Febs J 2005 272 20 5101 5109 10.1111/j.1742-4658.2005.04945.x 16218944 (Pubitemid 41503143)
    • (2005) FEBS Journal , vol.272 , Issue.20 , pp. 5101-5109
    • Altschul, S.F.1    Wootton, J.C.2    Gertz, E.M.3    Agarwala, R.4    Morgulis, A.5    Schaffer, A.A.6    Yu, Y.-K.7
  • 42
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. Krogh A, Larsson B, von Heijne G, Sonnhammer EL, J Mol Biol 2001 305 3 567 580 10.1006/jmbi.2000.4315 11152613 (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 43
    • 0031614678 scopus 로고    scopus 로고
    • A hidden Markov model for predicting transmembrane helices in protein sequences
    • 9783223
    • A hidden Markov model for predicting transmembrane helices in protein sequences. Sonnhammer EL, von Heijne G, Krogh A, Proc Int Conf Intell Syst Mol Biol 1998 6 175 182 9783223
    • (1998) Proc Int Conf Intell Syst Mol Biol , vol.6 , pp. 175-182
    • Sonnhammer, E.L.1    Von Heijne, G.2    Krogh, A.3
  • 44
    • 0034899781 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane spanning regions
    • Evaluation of methods for the prediction of membrane spanning regions. Moller S, Croning MD, Apweiler R, Bioinformatics 2001 17 7 646 653 10.1093/bioinformatics/17.7.646 11448883 (Pubitemid 32707587)
    • (2001) Bioinformatics , vol.17 , Issue.7 , pp. 646-653
    • Moller, S.1    Croning, M.D.R.2    Apweiler, R.3
  • 45
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: Protein domain annotations on the fly
    • Web Server
    • CD-Search: protein domain annotations on the fly. Marchler-Bauer A, Bryant SH, Nucleic Acids Res 2004 32 Web Server 327 331
    • (2004) Nucleic Acids Res , vol.32 , pp. 23327-331
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 50
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • 10.2307/2408678
    • Confidence limits on phylogenies: An approach using the bootstrap. Felsenstein J, Evolution 1985 39 783 791 10.2307/2408678
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 51
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • 3447015
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees. Saitou N, Nei M, Mol Biol Evol 1987 4 4 406 425 3447015
    • (1987) Mol Biol Evol , vol.4 , Issue.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 52
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular Evolutionary Genetics Analysis using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony Methods
    • MEGA5: Molecular Evolutionary Genetics Analysis using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony Methods. Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S, Mol Biol Evol 2011
    • (2011) Mol Biol Evol
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 54
    • 77958176797 scopus 로고    scopus 로고
    • Identification and characterization of an acyl-CoA:diacylglycerol acyltransferase 2 (DGAT2) gene from the microalga O. tauri
    • 10.1016/j.plaphy.2010.03.008 20400321
    • Identification and characterization of an acyl-CoA:diacylglycerol acyltransferase 2 (DGAT2) gene from the microalga O. tauri. Wagner M, Hoppe K, Czabany T, Heilmann M, Daum G, Feussner I, Fulda M, Plant Physiol Biochem 2010 48 6 407 416 10.1016/j.plaphy.2010.03.008 20400321
    • (2010) Plant Physiol Biochem , vol.48 , Issue.6 , pp. 407-416
    • Wagner, M.1    Hoppe, K.2    Czabany, T.3    Heilmann, M.4    Daum, G.5    Feussner, I.6    Fulda, M.7
  • 55
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • 10.1139/o59-099 13671378
    • A rapid method of total lipid extraction and purification. Bligh EG, Dyer WJ, Canadian Journal of Biochemistry and Physiology 1959 37 8 911 917 10.1139/o59-099 13671378
    • (1959) Canadian Journal of Biochemistry and Physiology , vol.37 , Issue.8 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 56
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3 942051
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Bradford MM, Anal Biochem 1976 72 248 254 10.1016/0003-2697(76)90527-3 942051
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 57
    • 0014293951 scopus 로고
    • 2-methyl substituted and 2-enoic fatty acids by Favorsky rearrangement of haloketones
    • 10.1016/0009-3084(68)90025-X 5696953
    • 2-methyl substituted and 2-enoic fatty acids by Favorsky rearrangement of haloketones. Gerson T, Schlenk H, Chem Phys Lipids 1968 2 2 213 219 10.1016/0009-3084(68)90025-X 5696953
    • (1968) Chem Phys Lipids , vol.2 , Issue.2 , pp. 213-219
    • Gerson, T.1    Schlenk, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.