메뉴 건너뛰기




Volumn 12, Issue 7, 2014, Pages 1-11

Structure of a Membrane-Embedded Prenyltransferase Homologous to UBIAD1

Author keywords

[No Author keywords available]

Indexed keywords

DIMETHYLALLYLTRANSFERASE; ISOPRENYL DIPHOSPHATE; MAGNESIUM ION; PHOSPHORUS ACID DERIVATIVE; PROTEIN MENA; UBIA PRENYLTRANSFERASE DOMAIN CONTAINING 1; UNCLASSIFIED DRUG;

EID: 84905368152     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001911     Document Type: Article
Times cited : (91)

References (50)
  • 1
    • 84887850766 scopus 로고    scopus 로고
    • Menadione (vitamin k3) is a catabolic product of oral phylloquinone (vitamin k1) in the intestine and a circulating precursor of tissue menaquinone-4 (vitamin k2) in rats
    • Hirota Y, Tsugawa N, Nakagawa K, Suhara Y, Tanaka K, et al. (2013) Menadione (vitamin k3) is a catabolic product of oral phylloquinone (vitamin k1) in the intestine and a circulating precursor of tissue menaquinone-4 (vitamin k2) in rats. J Biol Chem 288: 33071-33080.
    • (2013) J Biol Chem , vol.288 , pp. 33071-33080
    • Hirota, Y.1    Tsugawa, N.2    Nakagawa, K.3    Suhara, Y.4    Tanaka, K.5
  • 2
    • 78149280201 scopus 로고    scopus 로고
    • Identification of UBIAD1 as a novel human menaquinone-4 biosynthetic enzyme
    • Nakagawa K, Hirota Y, Sawada N, Yuge N, Watanabe M, et al. (2010) Identification of UBIAD1 as a novel human menaquinone-4 biosynthetic enzyme. Nature 468: 117-121.
    • (2010) Nature , vol.468 , pp. 117-121
    • Nakagawa, K.1    Hirota, Y.2    Sawada, N.3    Yuge, N.4    Watanabe, M.5
  • 3
    • 84861983560 scopus 로고    scopus 로고
    • Vitamin K2 is a mitochondrial electron carrier that rescues pink1 deficiency
    • Vos M, Esposito G, Edirisinghe JN, Vilain S, Haddad DM, et al. (2012) Vitamin K2 is a mitochondrial electron carrier that rescues pink1 deficiency. Science 336: 1306-1310.
    • (2012) Science , vol.336 , pp. 1306-1310
    • Vos, M.1    Esposito, G.2    Edirisinghe, J.N.3    Vilain, S.4    Haddad, D.M.5
  • 4
    • 84873324400 scopus 로고    scopus 로고
    • Ubiad1 is an antioxidant enzyme that regulates eNOS activity by CoQ10 synthesis
    • Mugoni V, Postel R, Catanzaro V, De Luca E, Turco E, et al. (2013) Ubiad1 is an antioxidant enzyme that regulates eNOS activity by CoQ10 synthesis. Cell 152: 504-518.
    • (2013) Cell , vol.152 , pp. 504-518
    • Mugoni, V.1    Postel, R.2    Catanzaro, V.3    De Luca, E.4    Turco, E.5
  • 5
    • 34848877291 scopus 로고    scopus 로고
    • Mutations in the UBIAD1 gene, encoding a potential prenyltransferase, are causal for Schnyder crystalline corneal dystrophy
    • Orr A, Dube MP, Marcadier J, Jiang H, Federico A, et al. (2007) Mutations in the UBIAD1 gene, encoding a potential prenyltransferase, are causal for Schnyder crystalline corneal dystrophy. PLoS ONE 2: e685.
    • (2007) PLoS ONE , vol.2
    • Orr, A.1    Dube, M.P.2    Marcadier, J.3    Jiang, H.4    Federico, A.5
  • 6
    • 0026731820 scopus 로고
    • COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate:polyprenyltransferase
    • Ashby MN, Kutsunai SY, Ackerman S, Tzagoloff A, Edwards PA, (1992) COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate:polyprenyltransferase. J Biol Chem 267: 4128-4136.
    • (1992) J Biol Chem , vol.267 , pp. 4128-4136
    • Ashby, M.N.1    Kutsunai, S.Y.2    Ackerman, S.3    Tzagoloff, A.4    Edwards, P.A.5
  • 7
    • 0031596770 scopus 로고    scopus 로고
    • Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli
    • Suvarna K, Stevenson D, Meganathan R, Hudspeth ME, (1998) Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli. J Bacteriol 180: 2782-2787.
    • (1998) J Bacteriol , vol.180 , pp. 2782-2787
    • Suvarna, K.1    Stevenson, D.2    Meganathan, R.3    Hudspeth, M.E.4
  • 8
    • 0015321309 scopus 로고
    • Biochemical and genetic studies on ubiquinone biosynthesis in Escherichia coli K-12:4-hydroxybenzoate octaprenyltransferase
    • Young IG, Leppik RA, Hamilton JA, Gibson F, (1972) Biochemical and genetic studies on ubiquinone biosynthesis in Escherichia coli K-12:4-hydroxybenzoate octaprenyltransferase. J Bacteriol 110: 18-25.
    • (1972) J Bacteriol , vol.110 , pp. 18-25
    • Young, I.G.1    Leppik, R.A.2    Hamilton, J.A.3    Gibson, F.4
  • 9
    • 0030942249 scopus 로고    scopus 로고
    • Characterization of chlorophyll a and bacteriochlorophyll a synthases by heterologous expression in Escherichia coli
    • Oster U, Bauer CE, Rudiger W, (1997) Characterization of chlorophyll a and bacteriochlorophyll a synthases by heterologous expression in Escherichia coli. J Biol Chem 272: 9671-9676.
    • (1997) J Biol Chem , vol.272 , pp. 9671-9676
    • Oster, U.1    Bauer, C.E.2    Rudiger, W.3
  • 10
    • 0027442655 scopus 로고
    • In vitro heme O synthesis by the cyoE gene product from Escherichia coli
    • Saiki K, Mogi T, Ogura K, Anraku Y, (1993) In vitro heme O synthesis by the cyoE gene product from Escherichia coli. J Biol Chem 268: 26041-26044.
    • (1993) J Biol Chem , vol.268 , pp. 26041-26044
    • Saiki, K.1    Mogi, T.2    Ogura, K.3    Anraku, Y.4
  • 11
    • 9644264034 scopus 로고    scopus 로고
    • (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and characterization of a membrane-intrinsic prenyltransferase involved in the biosynthesis of archaeal ether-linked membrane lipids
    • Hemmi H, Shibuya K, Takahashi Y, Nakayama T, Nishino T, (2004) (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and characterization of a membrane-intrinsic prenyltransferase involved in the biosynthesis of archaeal ether-linked membrane lipids. J Biol Chem 279: 50197-50203.
    • (2004) J Biol Chem , vol.279 , pp. 50197-50203
    • Hemmi, H.1    Shibuya, K.2    Takahashi, Y.3    Nakayama, T.4    Nishino, T.5
  • 12
    • 70350722384 scopus 로고    scopus 로고
    • Prenylation of aromatic compounds, a key diversification of plant secondary metabolites
    • Yazaki K, Sasaki K, Tsurumaru Y, (2009) Prenylation of aromatic compounds, a key diversification of plant secondary metabolites. Phytochemistry 70: 1739-1745.
    • (2009) Phytochemistry , vol.70 , pp. 1739-1745
    • Yazaki, K.1    Sasaki, K.2    Tsurumaru, Y.3
  • 13
    • 84866035527 scopus 로고    scopus 로고
    • Mutagenesis and biochemical studies on AuaA confirmed the importance of the two conserved aspartate-rich motifs and suggested difference in the amino acids for substrate binding in membrane-bound prenyltransferases
    • Stec E, Li SM, (2012) Mutagenesis and biochemical studies on AuaA confirmed the importance of the two conserved aspartate-rich motifs and suggested difference in the amino acids for substrate binding in membrane-bound prenyltransferases. Arch Microbiol 194: 589-595.
    • (2012) Arch Microbiol , vol.194 , pp. 589-595
    • Stec, E.1    Li, S.M.2
  • 14
    • 0035201588 scopus 로고    scopus 로고
    • Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis
    • Collakova E, DellaPenna D, (2001) Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol 127: 1113-1124.
    • (2001) Plant Physiol , vol.127 , pp. 1113-1124
    • Collakova, E.1    DellaPenna, D.2
  • 15
    • 0035876240 scopus 로고    scopus 로고
    • A novel phytyltransferase from Synechocystis sp. PCC 6803 involved in tocopherol biosynthesis
    • Schledz M, Seidler A, Beyer P, Neuhaus G, (2001) A novel phytyltransferase from Synechocystis sp. PCC 6803 involved in tocopherol biosynthesis. FEBS Lett 499: 15-20.
    • (2001) FEBS Lett , vol.499 , pp. 15-20
    • Schledz, M.1    Seidler, A.2    Beyer, P.3    Neuhaus, G.4
  • 16
    • 21644453614 scopus 로고    scopus 로고
    • Identification and active expression of the Mycobacterium tuberculosis gene encoding 5-phospho-{alpha}-d-ribose-1-diphosphate: decaprenyl-phosphate 5-phosphoribosyltransferase, the first enzyme committed to decaprenylphosphoryl-d-arabinose synthesis
    • Huang H, Scherman MS, D'Haeze W, Vereecke D, Holsters M, et al. (2005) Identification and active expression of the Mycobacterium tuberculosis gene encoding 5-phospho-{alpha}-d-ribose-1-diphosphate: decaprenyl-phosphate 5-phosphoribosyltransferase, the first enzyme committed to decaprenylphosphoryl-d-arabinose synthesis. J Biol Chem 280: 24539-24543.
    • (2005) J Biol Chem , vol.280 , pp. 24539-24543
    • Huang, H.1    Scherman, M.S.2    D'Haeze, W.3    Vereecke, D.4    Holsters, M.5
  • 17
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • von Heijne G, Gavel Y, (1988) Topogenic signals in integral membrane proteins. Eur J Biochem 174: 671-678.
    • (1988) Eur J Biochem , vol.174 , pp. 671-678
    • von Heijne, G.1    Gavel, Y.2
  • 18
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley DO, Rapp M, Granseth E, Melen K, Drew D, et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308: 1321-1323.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4    Drew, D.5
  • 19
    • 84894286780 scopus 로고    scopus 로고
    • Structural insights into ubiquinone biosynthesis in membranes
    • Cheng W, Li W, (2014) Structural insights into ubiquinone biosynthesis in membranes. Science 343: 878-881.
    • (2014) Science , vol.343 , pp. 878-881
    • Cheng, W.1    Li, W.2
  • 20
    • 67650468659 scopus 로고    scopus 로고
    • Reaction kinetics, catalytic mechanisms, conformational changes, and inhibitor design for prenyltransferases
    • Liang PH, (2009) Reaction kinetics, catalytic mechanisms, conformational changes, and inhibitor design for prenyltransferases. Biochemistry 48: 6562-6570.
    • (2009) Biochemistry , vol.48 , pp. 6562-6570
    • Liang, P.H.1
  • 21
    • 1542275565 scopus 로고    scopus 로고
    • Structural basis for bisphosphonate-mediated inhibition of isoprenoid biosynthesis
    • Hosfield DJ, Zhang Y, Dougan DR, Broun A, Tari LW, et al. (2004) Structural basis for bisphosphonate-mediated inhibition of isoprenoid biosynthesis. J Biol Chem 279: 8526-8529.
    • (2004) J Biol Chem , vol.279 , pp. 8526-8529
    • Hosfield, D.J.1    Zhang, Y.2    Dougan, D.R.3    Broun, A.4    Tari, L.W.5
  • 22
    • 48949120151 scopus 로고    scopus 로고
    • Cloning and characterization of naringenin 8-prenyltransferase, a flavonoid-specific prenyltransferase of Sophora flavescens
    • Sasaki K, Mito K, Ohara K, Yamamoto H, Yazaki K, (2008) Cloning and characterization of naringenin 8-prenyltransferase, a flavonoid-specific prenyltransferase of Sophora flavescens. Plant Physiol 146: 1075-1084.
    • (2008) Plant Physiol , vol.146 , pp. 1075-1084
    • Sasaki, K.1    Mito, K.2    Ohara, K.3    Yamamoto, H.4    Yazaki, K.5
  • 23
    • 44049105743 scopus 로고    scopus 로고
    • A structural model of the membrane-bound aromatic prenyltransferase UbiA from E. coli
    • Brauer L, Brandt W, Schulze D, Zakharova S, Wessjohann L, (2008) A structural model of the membrane-bound aromatic prenyltransferase UbiA from E. coli. Chembiochem 9: 982-992.
    • (2008) Chembiochem , vol.9 , pp. 982-992
    • Brauer, L.1    Brandt, W.2    Schulze, D.3    Zakharova, S.4    Wessjohann, L.5
  • 24
    • 67650898865 scopus 로고    scopus 로고
    • Functional characterization of LePGT1, a membrane-bound prenyltransferase involved in the geranylation of p-hydroxybenzoic acid
    • Ohara K, Muroya A, Fukushima N, Yazaki K, (2009) Functional characterization of LePGT1, a membrane-bound prenyltransferase involved in the geranylation of p-hydroxybenzoic acid. Biochem J 421: 231-241.
    • (2009) Biochem J , vol.421 , pp. 231-241
    • Ohara, K.1    Muroya, A.2    Fukushima, N.3    Yazaki, K.4
  • 25
    • 0017177848 scopus 로고
    • Biosynthesis of bacterial menaquinones: the membrane-associated 1,4-dihydroxy-2-naphthoate octaprenyltransferase of Escherichia coli
    • Shineberg B, Young IG, (1976) Biosynthesis of bacterial menaquinones: the membrane-associated 1,4-dihydroxy-2-naphthoate octaprenyltransferase of Escherichia coli. Biochemistry 15: 2754-2758.
    • (1976) Biochemistry , vol.15 , pp. 2754-2758
    • Shineberg, B.1    Young, I.G.2
  • 26
    • 79953035880 scopus 로고    scopus 로고
    • Schnyder corneal dystrophy in a Saudi Arabian family with heterozygous UBIAD1 mutation (p.L121F)
    • Al-Ghadeer H, Mohamed JY, Khan AO, (2011) Schnyder corneal dystrophy in a Saudi Arabian family with heterozygous UBIAD1 mutation (p.L121F). Middle East Afr J Ophthalmol 18: 61-64.
    • (2011) Middle East Afr J Ophthalmol , vol.18 , pp. 61-64
    • Al-Ghadeer, H.1    Mohamed, J.Y.2    Khan, A.O.3
  • 27
    • 68149158504 scopus 로고    scopus 로고
    • A novel UBIAD1 mutation identified in a Chinese family with Schnyder crystalline corneal dystrophy
    • Jing Y, Liu C, Xu J, Wang L, (2009) A novel UBIAD1 mutation identified in a Chinese family with Schnyder crystalline corneal dystrophy. Mol Vis 15: 1463-1469.
    • (2009) Mol Vis , vol.15 , pp. 1463-1469
    • Jing, Y.1    Liu, C.2    Xu, J.3    Wang, L.4
  • 28
    • 67349158306 scopus 로고    scopus 로고
    • In vivo laser confocal microscopy findings and mutational analysis for Schnyder's crystalline corneal dystrophy
    • Kobayashi A, Fujiki K, Murakami A, Sugiyama K, (2009) In vivo laser confocal microscopy findings and mutational analysis for Schnyder's crystalline corneal dystrophy. Ophthalmology 116: 1029-e1021, 1029-1037, e1021.
    • (2009) Ophthalmology , vol.116
    • Kobayashi, A.1    Fujiki, K.2    Murakami, A.3    Sugiyama, K.4
  • 29
    • 67649646191 scopus 로고    scopus 로고
    • Surgical management and genetic analysis of a Chinese family with the S171P mutation in the UBIAD1 gene, the gene for Schnyder corneal dystrophy
    • Mehta JS, Vithana EN, Venkataraman D, Venkatraman A, Yong VH, et al. (2009) Surgical management and genetic analysis of a Chinese family with the S171P mutation in the UBIAD1 gene, the gene for Schnyder corneal dystrophy. Br J Ophthalmol 93: 926-931.
    • (2009) Br J Ophthalmol , vol.93 , pp. 926-931
    • Mehta, J.S.1    Vithana, E.N.2    Venkataraman, D.3    Venkatraman, A.4    Yong, V.H.5
  • 30
    • 84873093558 scopus 로고    scopus 로고
    • The UBIAD1 prenyltransferase links menaquinone-4 [corrected] synthesis to cholesterol metabolic enzymes
    • Nickerson ML, Bosley AD, Weiss JS, Kostiha BN, Hirota Y, et al. (2013) The UBIAD1 prenyltransferase links menaquinone-4 [corrected] synthesis to cholesterol metabolic enzymes. Hum Mutat 34: 317-329.
    • (2013) Hum Mutat , vol.34 , pp. 317-329
    • Nickerson, M.L.1    Bosley, A.D.2    Weiss, J.S.3    Kostiha, B.N.4    Hirota, Y.5
  • 31
    • 77956295727 scopus 로고    scopus 로고
    • UBIAD1 mutation alters a mitochondrial prenyltransferase to cause Schnyder corneal dystrophy
    • Nickerson ML, Kostiha BN, Brandt W, Fredericks W, Xu KP, et al. (2010) UBIAD1 mutation alters a mitochondrial prenyltransferase to cause Schnyder corneal dystrophy. PLoS ONE 5: e10760.
    • (2010) PLoS ONE , vol.5
    • Nickerson, M.L.1    Kostiha, B.N.2    Brandt, W.3    Fredericks, W.4    Xu, K.P.5
  • 32
    • 38949212779 scopus 로고    scopus 로고
    • Genetic analysis of 14 families with Schnyder crystalline corneal dystrophy reveals clues to UBIAD1 protein function
    • Weiss JS, Kruth HS, Kuivaniemi H, Tromp G, Karkera J, et al. (2008) Genetic analysis of 14 families with Schnyder crystalline corneal dystrophy reveals clues to UBIAD1 protein function. Am J Med Genet A 146: 271-283.
    • (2008) Am J Med Genet A , vol.146 , pp. 271-283
    • Weiss, J.S.1    Kruth, H.S.2    Kuivaniemi, H.3    Tromp, G.4    Karkera, J.5
  • 33
    • 38449112757 scopus 로고    scopus 로고
    • Mutations in the UBIAD1 gene on chromosome short arm 1, region 36, cause Schnyder crystalline corneal dystrophy
    • Weiss JS, Kruth HS, Kuivaniemi H, Tromp G, White PS, et al. (2007) Mutations in the UBIAD1 gene on chromosome short arm 1, region 36, cause Schnyder crystalline corneal dystrophy. Invest Ophthalmol Vis Sci 48: 5007-5012.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 5007-5012
    • Weiss, J.S.1    Kruth, H.S.2    Kuivaniemi, H.3    Tromp, G.4    White, P.S.5
  • 34
    • 77954423187 scopus 로고    scopus 로고
    • Newly reported p.Asp240Asn mutation in UBIAD1 suggests central discoid corneal dystrophy is a variant of Schnyder corneal dystrophy
    • Weiss JS, Wiaux C, Yellore V, Raber I, Eagle R, et al. (2010) Newly reported p.Asp240Asn mutation in UBIAD1 suggests central discoid corneal dystrophy is a variant of Schnyder corneal dystrophy. Cornea 29: 777-780.
    • (2010) Cornea , vol.29 , pp. 777-780
    • Weiss, J.S.1    Wiaux, C.2    Yellore, V.3    Raber, I.4    Eagle, R.5
  • 35
    • 34848859527 scopus 로고    scopus 로고
    • Identification of mutations in UBIAD1 following exclusion of coding mutations in the chromosome 1p36 locus for Schnyder crystalline corneal dystrophy
    • Yellore VS, Khan MA, Bourla N, Rayner SA, Chen MC, et al. (2007) Identification of mutations in UBIAD1 following exclusion of coding mutations in the chromosome 1p36 locus for Schnyder crystalline corneal dystrophy. Mol Vis 13: 1777-1782.
    • (2007) Mol Vis , vol.13 , pp. 1777-1782
    • Yellore, V.S.1    Khan, M.A.2    Bourla, N.3    Rayner, S.A.4    Chen, M.C.5
  • 36
    • 0025364138 scopus 로고
    • Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase
    • Ashby MN, Edwards PA, (1990) Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase. J Biol Chem 265: 13157-13164.
    • (1990) J Biol Chem , vol.265 , pp. 13157-13164
    • Ashby, M.N.1    Edwards, P.A.2
  • 37
    • 0018276851 scopus 로고
    • Farnesyl pyrophosphate synthetase. Mechanistic studies of the 1′-4 coupling reaction with 2-fluorogeranyl pyrophosphate
    • Poulter CD, Argyle JC, Mash EA, (1978) Farnesyl pyrophosphate synthetase. Mechanistic studies of the 1′-4 coupling reaction with 2-fluorogeranyl pyrophosphate. J Biol Chem 253: 7227-7233.
    • (1978) J Biol Chem , vol.253 , pp. 7227-7233
    • Poulter, C.D.1    Argyle, J.C.2    Mash, E.A.3
  • 38
    • 33746836518 scopus 로고    scopus 로고
    • The crystal structure of human geranylgeranyl pyrophosphate synthase reveals a novel hexameric arrangement and inhibitory product binding
    • Kavanagh KL, Dunford JE, Bunkoczi G, Russell RG, Oppermann U, (2006) The crystal structure of human geranylgeranyl pyrophosphate synthase reveals a novel hexameric arrangement and inhibitory product binding. J Biol Chem 281: 22004-22012.
    • (2006) J Biol Chem , vol.281 , pp. 22004-22012
    • Kavanagh, K.L.1    Dunford, J.E.2    Bunkoczi, G.3    Russell, R.G.4    Oppermann, U.5
  • 40
    • 84859186669 scopus 로고    scopus 로고
    • Catalytic mechanism of aromatic prenylation by NphB
    • Yang Y, Miao Y, Wang B, Cui G, Merz KM Jr, (2012) Catalytic mechanism of aromatic prenylation by NphB. Biochemistry 51: 2606-2618.
    • (2012) Biochemistry , vol.51 , pp. 2606-2618
    • Yang, Y.1    Miao, Y.2    Wang, B.3    Cui, G.4    Merz Jr., K.M.5
  • 41
    • 70149099367 scopus 로고    scopus 로고
    • The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria
    • Metzger U, Schall C, Zocher G, Unsold I, Stec E, et al. (2009) The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria. Proc Natl Acad Sci U S A 106: 14309-14314.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14309-14314
    • Metzger, U.1    Schall, C.2    Zocher, G.3    Unsold, I.4    Stec, E.5
  • 42
    • 78549293840 scopus 로고    scopus 로고
    • Structure and mechanism of the magnesium-independent aromatic prenyltransferase CloQ from the clorobiocin biosynthetic pathway
    • Metzger U, Keller S, Stevenson CE, Heide L, Lawson DM, (2010) Structure and mechanism of the magnesium-independent aromatic prenyltransferase CloQ from the clorobiocin biosynthetic pathway. J Mol Biol 404: 611-626.
    • (2010) J Mol Biol , vol.404 , pp. 611-626
    • Metzger, U.1    Keller, S.2    Stevenson, C.E.3    Heide, L.4    Lawson, D.M.5
  • 43
    • 77956613642 scopus 로고    scopus 로고
    • The New York Consortium on Membrane Protein Structure (NYCOMPS): a high-throughput platform for structural genomics of integral membrane proteins
    • Love J, Mancia F, Shapiro L, Punta M, Rost B, et al. (2010) The New York Consortium on Membrane Protein Structure (NYCOMPS): a high-throughput platform for structural genomics of integral membrane proteins. J Struct Funct Genomics 11: 191-199.
    • (2010) J Struct Funct Genomics , vol.11 , pp. 191-199
    • Love, J.1    Mancia, F.2    Shapiro, L.3    Punta, M.4    Rost, B.5
  • 44
    • 67649392795 scopus 로고    scopus 로고
    • Crystallizing membrane proteins using lipidic mesophases
    • Caffrey M, Cherezov V, (2009) Crystallizing membrane proteins using lipidic mesophases. Nat Protoc 4: 706-731.
    • (2009) Nat Protoc , vol.4 , pp. 706-731
    • Caffrey, M.1    Cherezov, V.2
  • 45
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray crystallographic data in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray crystallographic data in oscillation mode. Methods Enzymol 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 49
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N, (2010) ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res 38: W529-W533.
    • (2010) Nucleic Acids Res , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 50
    • 0025944865 scopus 로고
    • Dimethyl sulfoxide reductase is not required for trimethylamine N-oxide reduction in Escherichia coli
    • Daruwala R, Meganathan R, (1991) Dimethyl sulfoxide reductase is not required for trimethylamine N-oxide reduction in Escherichia coli. FEMS Microbiol Lett 67: 255-259.
    • (1991) FEMS Microbiol Lett , vol.67 , pp. 255-259
    • Daruwala, R.1    Meganathan, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.