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Volumn 5, Issue , 2004, Pages

The Hotdog fold: Wrapping up a superfamily of thioesterases and dehydratases

Author keywords

[No Author keywords available]

Indexed keywords

DOMAIN-CONTAINING PROTEINS; ENVIRONMENTAL POLLUTANTS; EUKARYOTIC PROTEINS; FATTY ACID BIOSYNTHESIS; FATTY ACID METABOLISM; FUNCTIONAL DOMAINS; STRUCTURAL DETERMINATION; TRANSCRIPTIONAL REGULATION;

EID: 13244267005     PISSN: 14712105     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2105-5-109     Document Type: Article
Times cited : (153)

References (74)
  • 1
    • 0030584655 scopus 로고    scopus 로고
    • Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: Two catalytic activities in one active site
    • Leesong M, Henderson BS, Gillig JR, Schwab JM, Smith JL: Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 1996, 4:253-264.
    • (1996) Structure , vol.4 , pp. 253-264
    • Leesong, M.1    Henderson, B.S.2    Gillig, J.R.3    Schwab, J.M.4    Smith, J.L.5
  • 2
    • 0032509337 scopus 로고    scopus 로고
    • The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3
    • Benning MM, Wesenberg G, Liu R, Taylor KL, Dunaway-Mariano D, Holden HM: The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3. J Biol Chem 1998, 273:33572-33579.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33572-33579
    • Benning, M.M.1    Wesenberg, G.2    Liu, R.3    Taylor, K.L.4    Dunaway-Mariano, D.5    Holden, H.M.6
  • 3
    • 0242290213 scopus 로고    scopus 로고
    • The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp. strain SU
    • Thoden JB, Zhuang Z, Dunaway-Mariano D, Holden HM: The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp. strain SU. J Biol Chem 2003, 278:43709-43716.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43709-43716
    • Thoden, J.B.1    Zhuang, Z.2    Dunaway-Mariano, D.3    Holden, H.M.4
  • 4
    • 0346024117 scopus 로고    scopus 로고
    • The BH1999 protein of Bacillus halodurans C-125 is gentisyl-coenzyme A thioesterase
    • Zhuang Z, Song F, Takami H, Dunaway-Mariano D: The BH1999 protein of Bacillus halodurans C-125 is gentisyl-coenzyme A thioesterase. J Bacteriol 2004, 186:393-399.
    • (2004) J. Bacteriol. , vol.186 , pp. 393-399
    • Zhuang, Z.1    Song, F.2    Takami, H.3    Dunaway-Mariano, D.4
  • 5
    • 0033936807 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme
    • Li J, Derewenda U, Dauter Z, Smith S, Derewenda ZS: Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme. Nat Struct Biol 2000, 7: 55-559.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 555-559
    • Li, J.1    Derewenda, U.2    Dauter, Z.3    Smith, S.4    Derewenda, Z.S.5
  • 8
    • 0037414810 scopus 로고    scopus 로고
    • Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis
    • Hisano T, Tsuge T, Fukui T, Iwata T, Miki K, Doi Y: Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis. J Biol Chem 2003, 278:617-624.
    • (2003) J. Biol. Chem. , vol.278 , pp. 617-624
    • Hisano, T.1    Tsuge, T.2    Fukui, T.3    Iwata, T.4    Miki, K.5    Doi, Y.6
  • 9
    • 0037178828 scopus 로고    scopus 로고
    • X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase
    • Thoden JB, Holden HM, Zhuang Z, Dunaway-Mariano D: X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase. J Biol Chem 2002, 277:27468-27476.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27468-27476
    • Thoden, J.B.1    Holden, H.M.2    Zhuang, Z.3    Dunaway-Mariano, D.4
  • 11
    • 0034891848 scopus 로고    scopus 로고
    • Integrative data mining: The new direction in bioinformatics
    • Bertone P, Gerstein M: Integrative data mining: the new direction in bioinformatics. IEEE Eng Med Biol Mag 2001, 20: 3-40.
    • (2001) IEEE Eng. Med. Biol. Mag. , vol.20 , pp. 33-40
    • Bertone, P.1    Gerstein, M.2
  • 15
    • 1642330037 scopus 로고    scopus 로고
    • HMMER: Profile HMMs for protein sequence analysis
    • HMMER: profile HMMs for protein sequence analysis [http://hmmer.wustl.edu]
  • 16
    • 0036138306 scopus 로고    scopus 로고
    • The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism
    • Hunt MC, Alexson SE: The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog Lipid Res 2002, 41:99-130.
    • (2002) Prog. Lipid Res. , vol.41 , pp. 99-130
    • Hunt, M.C.1    Alexson, S.E.2
  • 17
    • 0035890798 scopus 로고    scopus 로고
    • BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown adipose tissue: Cloning, organization of the human gene and assessment of a potential link to obesity
    • Adams SH, Chui C, Schilbach SL, Yu XX, Goddard AD, Grimaldi JC, Lee J, Dowd P, Colman S, Lewin DA: BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown adipose tissue: cloning, organization of the human gene and assessment of a potential link to obesity. Biochem J 2001, 360:135-142.
    • (2001) Biochem. J. , vol.360 , pp. 135-142
    • Adams, S.H.1    Chui, C.2    Schilbach, S.L.3    Yu, X.X.4    Goddard, A.D.5    Grimaldi, J.C.6    Lee, J.7    Dowd, P.8    Colman, S.9    Lewin, D.A.10
  • 18
    • 0032901292 scopus 로고    scopus 로고
    • START: A lipid-binding domain in StAR, HD-ZIP and signalling proteins
    • Ponting CP, Aravind L: START: a lipid-binding domain in StAR, HD-ZIP and signalling proteins. Trends Biochem Sci 1999, 24:130-132.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 130-132
    • Ponting, C.P.1    Aravind, L.2
  • 19
    • 0029926496 scopus 로고    scopus 로고
    • Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis
    • Heath RJ, Rock CO: Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis. J Biol Chem 1996, 271: 7795-27801.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27795-27801
    • Heath, R.J.1    Rock, C.O.2
  • 20
    • 0031801222 scopus 로고    scopus 로고
    • Analysis of genes involved in biosynthesis of coronafacic acid, the polyketide component of the phytotoxin coronatine
    • Rangaswamy V, Mitchell R, Ullrich M, Bender C: Analysis of genes involved in biosynthesis of coronafacic acid, the polyketide component of the phytotoxin coronatine. J Bacteriol 1998, 180:3330-3338.
    • (1998) J. Bacteriol. , vol.180 , pp. 3330-3338
    • Rangaswamy, V.1    Mitchell, R.2    Ullrich, M.3    Bender, C.4
  • 21
    • 0032416724 scopus 로고    scopus 로고
    • Biosynthesis of the Pseudomonas polyketide coronafacic acid requires monofunctional and multifunctional polyketide synthase proteins
    • Rangaswamy V, Jiralerspong S, Parry R, Bender CL: Biosynthesis of the Pseudomonas polyketide coronafacic acid requires monofunctional and multifunctional polyketide synthase proteins. Proc Natl Acad Sci U S A 1998, 95:15469-15474.
    • (1998) Proc. Natl. Acad. Sci. U S A , vol.95 , pp. 15469-15474
    • Rangaswamy, V.1    Jiralerspong, S.2    Parry, R.3    Bender, C.L.4
  • 22
    • 0042337274 scopus 로고    scopus 로고
    • Identification and characterization of a new enoyl coenzyme A hydratase involved in biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli
    • Park SJ, Lee SY: Identification and characterization of a new enoyl coenzyme A hydratase involved in biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli. J Bacteriol 2003, 185:5391-5397.
    • (2003) J. Bacteriol. , vol.185 , pp. 5391-5397
    • Park, S.J.1    Lee, S.Y.2
  • 23
    • 0025076712 scopus 로고
    • Biosynthesis and composition of bacterial poly(hydroxyalkanoates)
    • Anderson AJ, Haywood GW, Dawes EA: Biosynthesis and composition of bacterial poly(hydroxyalkanoates). Int J Biol Macromol 1990, 12:102-105.
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 102-105
    • Anderson, A.J.1    Haywood, G.W.2    Dawes, E.A.3
  • 26
    • 0026485284 scopus 로고
    • Rhizobium nodM and nodN genes are common nod genes: nodM encodes functions for efficiency of nod signal production and bacteroid maturation
    • Baev N, Schultze M, Barlier I, Ha DC, Virelizier H, Kondorosi E, Kondorosi A: Rhizobium nodM and nodN genes are common nod genes: nodM encodes functions for efficiency of nod signal production and bacteroid maturation. J Bacteriol 1992, 174:7555-7565.
    • (1992) J. Bacteriol. , vol.174 , pp. 7555-7565
    • Baev, N.1    Schultze, M.2    Barlier, I.3    Ha, D.C.4    Virelizier, H.5    Kondorosi, E.6    Kondorosi, A.7
  • 27
    • 0037051944 scopus 로고    scopus 로고
    • The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis
    • Zhuang Z, Song F, Martin BM, Dunaway-Mariano D: The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis. FEBS Lett 2002, 516:161-163.
    • (2002) FEBS Lett. , vol.516 , pp. 161-163
    • Zhuang, Z.1    Song, F.2    Martin, B.M.3    Dunaway-Mariano, D.4
  • 28
    • 0035155704 scopus 로고    scopus 로고
    • Organisation and evolution of the tol-pal gene cluster
    • Sturgis JN: Organisation and evolution of the tol-pal gene cluster. J Mol Microbiol Biotechnol 2001, 3:113-122.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 113-122
    • Sturgis, J.N.1
  • 29
    • 0028557012 scopus 로고
    • The animal fatty acid synthase: One gene, one polypeptide, seven enzymes
    • Smith S: The animal fatty acid synthase: one gene, one polypeptide, seven enzymes. Faseb J 1994, 8:1248-1259.
    • (1994) Faseb J. , vol.8 , pp. 1248-1259
    • Smith, S.1
  • 30
    • 0025017436 scopus 로고
    • Biosynthesis and function of phospholipids in Escherichia coli
    • Raetz CR, Dowhan W: Biosynthesis and function of phospholipids in Escherichia coli. J Biol Chem 1990, 265: 235-1238.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1235-1238
    • Raetz, C.R.1    Dowhan, W.2
  • 31
    • 0025606149 scopus 로고
    • Molecular genetics of polyketides and its comparison to fatty acid biosynthesis
    • Hopwood DA, Sherman DH: Molecular genetics of polyketides and its comparison to fatty acid biosynthesis. Annu Rev Genet 1990, 24:37-66.
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 37-66
    • Hopwood, D.A.1    Sherman, D.H.2
  • 33
    • 0035987331 scopus 로고    scopus 로고
    • Structure and regulation of the omega-3 polyunsaturated fatty acid synthase genes from the deep-sea bacterium Photobacterium profundum strain SS9
    • Allen EE, Bartlett DH: Structure and regulation of the omega-3 polyunsaturated fatty acid synthase genes from the deep-sea bacterium Photobacterium profundum strain SS9. Microbiology 2002, 148:1903-1913.
    • (2002) Microbiology , vol.148 , pp. 1903-1913
    • Allen, E.E.1    Bartlett, D.H.2
  • 34
    • 0029665059 scopus 로고    scopus 로고
    • Cloning, sequencing and characterization of a fatty acid synthase-encoding gene from Mycobacterium tuberculosis var. bovis BCG
    • Fernandes ND, Kolattukudy PE: Cloning, sequencing and characterization of a fatty acid synthase-encoding gene from Mycobacterium tuberculosis var. bovis BCG. Gene 1996, 170: 5-99.
    • (1996) Gene , vol.170 , pp. 95-99
    • Fernandes, N.D.1    Kolattukudy, P.E.2
  • 35
    • 0029257162 scopus 로고
    • Palmitoyl-acyl carrier protein (ACP) thioesterase and the evolutionary origin of plant acyl-ACP thioesterases
    • Jones A, Davies HM, Voelker TA: Palmitoyl-acyl carrier protein (ACP) thioesterase and the evolutionary origin of plant acyl-ACP thioesterases. Plant Cell 1995, 7:359-371.
    • (1995) Plant Cell , vol.7 , pp. 359-371
    • Jones, A.1    Davies, H.M.2    Voelker, T.A.3
  • 37
    • 0036647410 scopus 로고    scopus 로고
    • Characterization of substrate specificity of plant FatA and FatB acyl-ACP thioesterases
    • Salas JJ, Ohlrogge JB: Characterization of substrate specificity of plant FatA and FatB acyl-ACP thioesterases. Arch Biochem Biophys 2002, 403:25-34.
    • (2002) Arch. Biochem. Biophys. , vol.403 , pp. 25-34
    • Salas, J.J.1    Ohlrogge, J.B.2
  • 39
    • 0030920271 scopus 로고    scopus 로고
    • Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation
    • Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S: Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J Biol Chem 1997, 272:13779-13785.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13779-13785
    • Liu, L.X.1    Margottin, F.2    Le Gall, S.3    Schwartz, O.4    Selig, L.5    Benarous, R.6    Benichou, S.7
  • 40
    • 0033515489 scopus 로고    scopus 로고
    • Identification of peroxisomal acyl-CoA thioesterases in yeast and humans
    • Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ: Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. J Biol Chem 1999, 274:9216-9223.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9216-9223
    • Jones, J.M.1    Nau, K.2    Geraghty, M.T.3    Erdmann, R.4    Gould, S.J.5
  • 41
    • 0034725614 scopus 로고    scopus 로고
    • The human thioesterase II protein binds to a site on HIV-1 Nef critical for CD4 down-regulation
    • Cohen GB, Rangan VS, Chen BK, Smith S, Baltimore D: The human thioesterase II protein binds to a site on HIV-1 Nef critical for CD4 down-regulation. J Biol Chem 2000, 275:23097-23105.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23097-23105
    • Cohen, G.B.1    Rangan, V.S.2    Chen, B.K.3    Smith, S.4    Baltimore, D.5
  • 42
    • 0037883296 scopus 로고    scopus 로고
    • Characterization of the 4-hydroxybenzoyl-coenzyme A thioesterase from Arthrobacter sp. strain SU
    • Zhuang Z, Gartemann KH, Eichenlaub R, Dunaway-Mariano D: Characterization of the 4-hydroxybenzoyl-coenzyme A thioesterase from Arthrobacter sp. strain SU. Appl Environ Microbiol 2003, 69: 707-2711.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2707-2711
    • Zhuang, Z.1    Gartemann, K.H.2    Eichenlaub, R.3    Dunaway-Mariano, D.4
  • 43
    • 0035815113 scopus 로고    scopus 로고
    • Evolution of function in protein superfamilies, from a structural perspective
    • Todd AE, Orengo CA, Thornton JM: Evolution of function in protein superfamilies, from a structural perspective. J Mol Biol 2001, 307:1113-1143.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1113-1143
    • Todd, A.E.1    Orengo, C.A.2    Thornton, J.M.3
  • 44
    • 0029959768 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular peptide factor that affects two different developmental pathways in Bacillus subtilis
    • Solomon JM, Lazazzera BA, Grossman AD: Purification and characterization of an extracellular peptide factor that affects two different developmental pathways in Bacillus subtilis. Genes Dev 1996, 10:2014-2024.
    • (1996) Genes Dev. , vol.10 , pp. 2014-2024
    • Solomon, J.M.1    Lazazzera, B.A.2    Grossman, A.D.3
  • 45
    • 0024460457 scopus 로고
    • Sequence and transcription mapping of Bacillus subtilis competence genes comB and comA, one of which is related to a family of bacterial regulatory determinants
    • Weinrauch Y, Guillen N, Dubnau DA: Sequence and transcription mapping of Bacillus subtilis competence genes comB and comA, one of which is related to a family of bacterial regulatory determinants. J Bacteriol 1989, 171:5362-5375.
    • (1989) J. Bacteriol. , vol.171 , pp. 5362-5375
    • Weinrauch, Y.1    Guillen, N.2    Dubnau, D.A.3
  • 47
    • 0037992415 scopus 로고    scopus 로고
    • FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis
    • Schujman GE, Paoletti L, Grossman AD, de Mendoza D: FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis. Dev Cell 2003, 4:663-672.
    • (2003) Dev. Cell , vol.4 , pp. 663-672
    • Schujman, G.E.1    Paoletti, L.2    Grossman, A.D.3    de Mendoza, D.4
  • 48
    • 0019509249 scopus 로고
    • Degradation of 4-chlorophenylacetic acid by a Pseudomonas species
    • Klages U, Markus A, Lingens F: Degradation of 4-chlorophenylacetic acid by a Pseudomonas species. J Bacteriol 1981, 146:64-68.
    • (1981) J. Bacteriol. , vol.146 , pp. 64-68
    • Klages, U.1    Markus, A.2    Lingens, F.3
  • 49
    • 0026760856 scopus 로고
    • Microbial breakdown of halogenated aromatic pesticides and related compounds
    • Haggblom MM: Microbial breakdown of halogenated aromatic pesticides and related compounds. FEMS Microbiol Rev 1992, 9: 9-71.
    • (1992) FEMS Microbiol. Rev. , vol.9 , pp. 29-71
    • Haggblom, M.M.1
  • 50
    • 0028672051 scopus 로고
    • On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway
    • Dunaway-Mariano D, Babbitt PC: On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway. Biodegradation 1994, 5:259-276.
    • (1994) Biodegradation , vol.5 , pp. 259-276
    • Dunaway-Mariano, D.1    Babbitt, P.C.2
  • 51
    • 0034722736 scopus 로고    scopus 로고
    • Genetic structure and functional implication of the fcb gene cluster for hydrolytic dechlorination of 4-chlorobenzoate from Pseudomonas sp. DJ-12
    • Chae JC, Kim Y, Kim YC, Zylstra GJ, Kim CK: Genetic structure and functional implication of the fcb gene cluster for hydrolytic dechlorination of 4-chlorobenzoate from Pseudomonas sp. DJ-12. Gene 2000, 258:109-116.
    • (2000) Gene , vol.258 , pp. 109-116
    • Chae, J.C.1    Kim, Y.2    Kim, Y.C.3    Zylstra, G.J.4    Kim, C.K.5
  • 52
    • 0036844165 scopus 로고    scopus 로고
    • Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus evansii
    • Gescher J, Zaar A, Mohamed M, Schagger H, Fuchs G: Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus evansii. J Bacteriol 2002, 184:6301-6315.
    • (2002) J. Bacteriol. , vol.184 , pp. 6301-6315
    • Gescher, J.1    Zaar, A.2    Mohamed, M.3    Schagger, H.4    Fuchs, G.5
  • 53
    • 0037125927 scopus 로고    scopus 로고
    • Kinetic, Raman, NMR, and site-directed mutagenesis studies of the Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase active site
    • Zhuang Z, Song F, Zhang W, Taylor K, Archambault A, Dunaway-Mariano D, Dong J, Carey PR: Kinetic, Raman, NMR, and site-directed mutagenesis studies of the Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase active site. Biochemistry 2002, 41:11152-11160.
    • (2002) Biochemistry , vol.41 , pp. 11152-11160
    • Zhuang, Z.1    Song, F.2    Zhang, W.3    Taylor, K.4    Archambault, A.5    Dunaway-Mariano, D.6    Dong, J.7    Carey, P.R.8
  • 54
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archaebacteria and the homocystinuria disease protein
    • Bateman A: The structure of a domain common to archaebacteria and the homocystinuria disease protein. Trends Biochem Sci 1997, 22:12-13.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 12-13
    • Bateman, A.1
  • 58
    • 0033523989 scopus 로고    scopus 로고
    • Protein interaction maps for complete genomes based on gene fusion events
    • Enright AJ, Iliopoulos I, Kyrpides NC, Ouzounis CA: Protein interaction maps for complete genomes based on gene fusion events. Nature 1999, 402:86-90.
    • (1999) Nature , vol.402 , pp. 86-90
    • Enright, A.J.1    Iliopoulos, I.2    Kyrpides, N.C.3    Ouzounis, C.A.4
  • 60
    • 0038419681 scopus 로고    scopus 로고
    • Functional links between proteins
    • Sali A: Functional links between proteins. Nature 1999, 402:23-26.
    • (1999) Nature , vol.402 , pp. 23-26
    • Sali, A.1
  • 61
    • 0032860477 scopus 로고    scopus 로고
    • Do you dig my groove?
    • Doolittle RF: Do you dig my groove? Nat Genet 1999, 23:6-8.
    • (1999) Nat. Genet. , vol.23 , pp. 6-8
    • Doolittle, R.F.1
  • 62
    • 0033639087 scopus 로고    scopus 로고
    • MASIA: Recognition of common patterns and properties in multiple aligned protein sequences
    • Zhu H, Schein CH, Braun W: MASIA: recognition of common patterns and properties in multiple aligned protein sequences. Bioinformatics 2000, 16:950-951.
    • (2000) Bioinformatics , vol.16 , pp. 950-951
    • Zhu, H.1    Schein, C.H.2    Braun, W.3
  • 64
    • 0242580787 scopus 로고    scopus 로고
    • Identification, characterization, and inhibition of Plasmodium falciparum beta-hydroxyacylacyl carrier protein dehydratase (FabZ)
    • Sharma SK, Kapoor M, Ramya TN, Kumar S, Kumar G, Modak R, Sharma S, Surolia N, Surolia A: Identification, characterization, and inhibition of Plasmodium falciparum beta-hydroxyacylacyl carrier protein dehydratase (FabZ). J Biol Chem 2003, 278:45661-45671.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45661-45671
    • Sharma, S.K.1    Kapoor, M.2    Ramya, T.N.3    Kumar, S.4    Kumar, G.5    Modak, R.6    Sharma, S.7    Surolia, N.8    Surolia, A.9
  • 66
    • 84874660168 scopus 로고    scopus 로고
    • GeConT Home Page
    • GeConT Home Page [http://www.ibt.unam.mx/biocomputo/gecont.html]
  • 67
    • 84874656715 scopus 로고    scopus 로고
    • Pfam Home Page
    • Pfam Home Page [http://www.sanger.ac.uk/Software/Pfam/]
  • 68
    • 84874652150 scopus 로고    scopus 로고
    • MASIA 2.0 Home Page
    • MASIA 2.0 Home Page [http://129.109.59.108/masia/]
  • 69
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P: MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991, 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 70
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic Molecular Graphics
    • Merritt EA, Bacon DJ: Raster3D: Photorealistic Molecular Graphics. Methods Enzymol 1997, 277:505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 71
    • 0042589136 scopus 로고    scopus 로고
    • Total sequence decomposition distinguishes functional modules, "molegos" in apurinic/apyrimidinic endonucleases
    • Schein CH, Ozgun N, Izumi T, Braun W: Total sequence decomposition distinguishes functional modules, "molegos" in apurinic/apyrimidinic endonucleases. BMC Bioinformatics 2002, 3:37.
    • (2002) BMC Bioinformatics , vol.3 , pp. 37
    • Schein, C.H.1    Ozgun, N.2    Izumi, T.3    Braun, W.4
  • 72
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh K, Misawa K, Kuma K, Miyata T: MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res 2002, 30:3059-3066.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 73
    • 0034791613 scopus 로고    scopus 로고
    • CHROMA: Consensus-based colouring of multiple alignments for publication
    • Goodstadt L, Ponting CP: CHROMA: consensus-based colouring of multiple alignments for publication. Bioinformatics 2001, 17:845-846.
    • (2001) Bioinformatics , vol.17 , pp. 845-846
    • Goodstadt, L.1    Ponting, C.P.2
  • 74
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff JA, Barton GJ: Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 2000, 40:502-511.
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.