메뉴 건너뛰기




Volumn 8, Issue 12, 2013, Pages

Structure-function features of a mycoplasma glycolipid synthase derived from structural data integration, molecular simulations, and mutational analysis

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; GLYCOSYLTRANSFERASE; GLYCOSYLTRANSFERASE GT A; ISOLEUCINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 84891786243     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0081990     Document Type: Article
Times cited : (9)

References (47)
  • 1
    • 77950865786 scopus 로고    scopus 로고
    • Highlights of mycoplasma research. An historical perspective
    • doi:10.1016/j.biologicals.2009.11.008. PubMed: 20149687
    • Razin S, Hayflick L (2010) Highlights of mycoplasma research. An historical perspective. Biologicals 38: 183-190. doi:10.1016/j.biologicals.2009. 11.008. PubMed: 20149687.
    • (2010) Biologicals , vol.38 , pp. 183-190
    • Razin, S.1    Hayflick, L.2
  • 2
    • 0031770391 scopus 로고    scopus 로고
    • Molecular biology and pathogenicity of mycoplasmas
    • PubMed: 9841667
    • Razin S, Yogev D, Naot Y (1998) Molecular biology and pathogenicity of mycoplasmas. Microbiol Mol Biol Rev 62: 1094-1156. PubMed: 9841667.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1094-1156
    • Razin, S.1    Yogev, D.2    Naot, Y.3
  • 3
    • 0031441913 scopus 로고    scopus 로고
    • The comparative metabolism of the Mollicutes (Mycoplasmas): The utility for taxonomic classification and the relationship of putative gene annotation and phylogeny to enzymic function in the smallest free-living cells
    • doi:10.3109/10408419709115140. PubMed: 9439886
    • Pollack JD, Williams MV, Mcelhaney RN (1997) The comparative metabolism of the Mollicutes (Mycoplasmas): the utility for taxonomic classification and the relationship of putative gene annotation and phylogeny to enzymic function in the smallest free-living cells. Crit Rev Microbiol 23: 269-354. doi:10.3109/10408419709115140. PubMed: 9439886.
    • (1997) Crit Rev Microbiol , vol.23 , pp. 269-354
    • Pollack, J.D.1    Williams, M.V.2    Mcelhaney, R.N.3
  • 4
    • 0023052449 scopus 로고
    • Phase equilibria of membrane lipids from Acholeplasma laidlawii: Importance of a single lipid forming nonlamellar phases
    • doi:10.1021/bi00371a037. PubMed: 3801429
    • Lindblom G, Brentel I, Sjölund M, Wikander G, Wieslander A (1986) Phase equilibria of membrane lipids from Acholeplasma laidlawii: importance of a single lipid forming nonlamellar phases. Biochemistry 25: 7502-7510. doi:10.1021/bi00371a037. PubMed: 3801429.
    • (1986) Biochemistry , vol.25 , pp. 7502-7510
    • Lindblom, G.1    Brentel, I.2    Sjölund, M.3    Wikander, G.4    Wieslander, A.5
  • 5
    • 0028800111 scopus 로고
    • Efficient modulation of glucolipid enzyme activities in membranes of Acholeplasma laidlawii by the type of lipids in the bilayer matrix
    • doi:10.1021/bi00041a015. PubMed: 7577924
    • Dahlqvist A, Nordström S, Karlsson OP, Mannock DA, McElhaney RN et al. (1995) Efficient modulation of glucolipid enzyme activities in membranes of Acholeplasma laidlawii by the type of lipids in the bilayer matrix. Biochemistry 34: 13381-13389. doi:10.1021/bi00041a015. PubMed: 7577924.
    • (1995) Biochemistry , vol.34 , pp. 13381-13389
    • Dahlqvist, A.1    Nordström, S.2    Karlsson, O.P.3    Mannock, D.A.4    McElhaney, R.N.5
  • 6
    • 0033608954 scopus 로고    scopus 로고
    • Key role of the diglucosyldiacylglycerol synthase for the nonbilayer-bilayer lipid balance of Acholeplasma laidlawii membranes
    • doi:10.1021/bi982532m. PubMed: 10220338
    • Vikström S, Li L, Karlsson OP, Wieslander A (1999) Key role of the diglucosyldiacylglycerol synthase for the nonbilayer-bilayer lipid balance of Acholeplasma laidlawii membranes. Biochemistry 38: 5511-5520. doi:10.1021/bi982532m. PubMed: 10220338.
    • (1999) Biochemistry , vol.38 , pp. 5511-5520
    • Vikström, S.1    Li, L.2    Karlsson, O.P.3    Wieslander, A.4
  • 7
    • 84861745137 scopus 로고    scopus 로고
    • Bacterial glycoglycerolipid synthases: Processive and non-processive glycosyltransferases in mycoplasma
    • doi:10.3109/10242422.2012.674733
    • Andrés E, Biarnés X, Faijes M, Planas A (2012) Bacterial glycoglycerolipid synthases: processive and non-processive glycosyltransferases in mycoplasma. Biocatal Biotransform 30: 274-287. doi:10.3109/10242422.2012. 674733.
    • (2012) Biocatal Biotransform , vol.30 , pp. 274-287
    • Andrés, E.1    Biarnés, X.2    Faijes, M.3    Planas, A.4
  • 8
    • 0030843984 scopus 로고    scopus 로고
    • A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities
    • PubMed: 9334165
    • Campbell JA, Davies GJ, Bulone V, Henrissat B (1997) A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem J 326: 929-939. PubMed: 9334165.
    • (1997) Biochem J , vol.326 , pp. 929-939
    • Campbell, J.A.1    Davies, G.J.2    Bulone, V.3    Henrissat, B.4
  • 9
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): An expert resource for Glycogenomics
    • doi:10.1093/nar/gkn663. PubMed: 18838391
    • Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V et al. (2009) The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res 37: D233-D238. doi:10.1093/nar/gkn663. PubMed: 18838391.
    • (2009) Nucleic Acids Res , vol.37
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5
  • 10
    • 49449087287 scopus 로고    scopus 로고
    • Glycosyltransferases: Structures, functions, and mechanisms
    • doi:10.1146/annurev.biochem.76.061005.092322. PubMed: 18518825
    • Lairson LL, Henrissat B, Davies GJ, Withers SG (2008) Glycosyltransferases: structures, functions, and mechanisms. Annu Rev Biochem 77: 521-555. doi:10.1146/annurev.biochem.76.061005.092322. PubMed: 18518825.
    • (2008) Annu Rev Biochem , vol.77 , pp. 521-555
    • Lairson, L.L.1    Henrissat, B.2    Davies, G.J.3    Withers, S.G.4
  • 11
    • 84867747900 scopus 로고    scopus 로고
    • Recent structures, evolution and mechanisms of glycosyltransferases
    • doi:10.1016/j.sbi.2012.06.007. PubMed: 22819665
    • Breton C, Fournel-Gigleux S, Palcic MM (2012) Recent structures, evolution and mechanisms of glycosyltransferases. Curr Opin Struct Biol 22: 540-549. doi:10.1016/j.sbi.2012.06.007. PubMed: 22819665.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 540-549
    • Breton, C.1    Fournel-Gigleux, S.2    Palcic, M.M.3
  • 12
    • 34548363832 scopus 로고    scopus 로고
    • A processive lipid glycosyltransferase in the small human pathogen Mycoplasma pneumoniae: Involvement in host immune response
    • doi:10.1111/j.1365-2958.2007.05865.x. PubMed: 17697098
    • Klement MLR, Ojemyr L, Tagscherer KE, Widmalm G, Wieslander A (2007) A processive lipid glycosyltransferase in the small human pathogen Mycoplasma pneumoniae: involvement in host immune response. Mol Microbiol 65: 1444-1457. doi:10.1111/j.1365-2958.2007.05865.x. PubMed: 17697098.
    • (2007) Mol Microbiol , vol.65 , pp. 1444-1457
    • Klement, M.L.R.1    Ojemyr, L.2    Tagscherer, K.E.3    Widmalm, G.4    Wieslander, A.5
  • 13
    • 80053919253 scopus 로고    scopus 로고
    • Expression and characterization of a Mycoplasma genitalium glycosyltransferase in membrane glycolipid biosynthesis: Potential target against mycoplasma infections
    • doi:10.1074/jbc.M110.214148. PubMed: 21835921
    • Andrés E, Martínez N, Planas A (2011) Expression and characterization of a Mycoplasma genitalium glycosyltransferase in membrane glycolipid biosynthesis: potential target against mycoplasma infections. J Biol Chem 286: 35367-35379. doi:10.1074/jbc.M110.214148. PubMed: 21835921.
    • (2011) J Biol Chem , vol.286 , pp. 35367-35379
    • Andrés, E.1    Martínez, N.2    Planas, A.3
  • 14
    • 33645880477 scopus 로고    scopus 로고
    • The atypical pneumonias: Clinical diagnosis and importance
    • 12-24
    • Cunha BA (2006) The atypical pneumonias: clinical diagnosis and importance. Clin Microbiol Infect 12 Suppl 3:12-24.: 12-24
    • (2006) Clin Microbiol Infect , vol.12 , Issue.SUPPL. 3 , pp. 12-24
    • Cunha, B.A.1
  • 15
    • 84862491013 scopus 로고    scopus 로고
    • The role of atypical pathogens in community-acquired pneumonia
    • doi:10.1055/s-0032-1315636. PubMed: 22718210
    • Marrie TJ, Costain N, La SB, Patrick W, Forgie S, Xu Z et al. (2012) The role of atypical pathogens in community-acquired pneumonia. Semin Respir Crit Care Med 33: 244-256. doi:10.1055/s-0032-1315636. PubMed: 22718210.
    • (2012) Semin Respir Crit Care Med , vol.33 , pp. 244-256
    • Marrie, T.J.1    Costain, N.2    La, S.B.3    Patrick, W.4    Forgie, S.5    Xu, Z.6
  • 16
    • 0027305503 scopus 로고
    • Association of Mycoplasma genitalium with acute non-gonococcal urethritis
    • doi:10.1016/0140-6736(93)91411-E. PubMed: 8102721
    • Horner PJ, Gilroy CB, Thomas BJ, Naidoo RO, Taylor-Robinson D (1993) Association of Mycoplasma genitalium with acute non-gonococcal urethritis. Lancet 342: 582-585. doi:10.1016/0140-6736(93)91411-E. PubMed: 8102721.
    • (1993) Lancet , vol.342 , pp. 582-585
    • Horner, P.J.1    Gilroy, C.B.2    Thomas, B.J.3    Naidoo, R.O.4    Taylor-Robinson, D.5
  • 17
    • 13544271664 scopus 로고    scopus 로고
    • Signs and symptoms of urethritis and cervicitis among women with or without Mycoplasma genitalium or Chlamydia trachomatis infection
    • doi:10.1136/sti.2004.010439. PubMed: 15681728
    • Falk L, Fredlund H, Jensen JS (2005) Signs and symptoms of urethritis and cervicitis among women with or without Mycoplasma genitalium or Chlamydia trachomatis infection. Sex Transm Infect 81: 73-78. doi:10.1136/sti.2004.010439. PubMed: 15681728.
    • (2005) Sex Transm Infect , vol.81 , pp. 73-78
    • Falk, L.1    Fredlund, H.2    Jensen, J.S.3
  • 18
    • 0037424229 scopus 로고    scopus 로고
    • Structural features of glycosyltransferases synthesizing major bilayer and nonbilayer-prone membrane lipids in Acholeplasma laidlawii and Streptococcus pneumoniae
    • doi:10.1074/jbc.M211492200. PubMed: 12464611
    • Edman M, Berg S, Storm P, Wikström M, Vikström S et al. (2003) Structural features of glycosyltransferases synthesizing major bilayer and nonbilayer-prone membrane lipids in Acholeplasma laidlawii and Streptococcus pneumoniae. J Biol Chem 278: 8420-8428. doi:10.1074/jbc.M211492200. PubMed: 12464611.
    • (2003) J Biol Chem , vol.278 , pp. 8420-8428
    • Edman, M.1    Berg, S.2    Storm, P.3    Wikström, M.4    Vikström, S.5
  • 19
    • 27144556229 scopus 로고    scopus 로고
    • Molecular modeling and site-directed mutagenesis of plant chloroplast monogalactosyldiacylglycerol synthase reveal critical residues for activity
    • doi:10.1074/jbc.M505622200. PubMed: 16009708
    • Botté C, Jeanneau C, Snajdrova L, Bastien O, Imberty A et al. (2005) Molecular modeling and site-directed mutagenesis of plant chloroplast monogalactosyldiacylglycerol synthase reveal critical residues for activity. J Biol Chem 280: 34691-34701. doi:10.1074/jbc.M505622200. PubMed: 16009708.
    • (2005) J Biol Chem , vol.280 , pp. 34691-34701
    • Botté, C.1    Jeanneau, C.2    Snajdrova, L.3    Bastien, O.4    Imberty, A.5
  • 20
    • 56649112704 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis glucosyl-3-phosphoglycerate synthase: Structure of a key enzyme in methylglucose lipopolysaccharide biosynthesis
    • doi:10.1371/journal.pone.0003748. PubMed: 19015727
    • Pereira PJB, Empadinhas N, Albuquerque L, Sá-Moura B, da Costa MS et al. (2008) Mycobacterium tuberculosis glucosyl-3-phosphoglycerate synthase: structure of a key enzyme in methylglucose lipopolysaccharide biosynthesis. PLOS ONE 3: e3748. doi:10.1371/journal.pone.0003748. PubMed: 19015727.
    • (2008) PLOS ONE , vol.3
    • Pereira, P.J.B.1    Empadinhas, N.2    Albuquerque, L.3    Sá-Moura, B.4    Da Costa, M.S.5
  • 21
    • 79955426783 scopus 로고    scopus 로고
    • Substrate and metal ion promiscuity in mannosylglycerate synthase
    • doi:10.1074/jbc.M110.199844. PubMed: 21288903
    • Nielsen MM, Suits MDL, Yang M, Barry CS, Martinez-Fleites C et al. (2011) Substrate and metal ion promiscuity in mannosylglycerate synthase. J Biol Chem 286: 15155-15164. doi:10.1074/jbc.M110.199844. PubMed: 21288903.
    • (2011) J Biol Chem , vol.286 , pp. 15155-15164
    • Nielsen, M.M.1    Suits, M.D.L.2    Yang, M.3    Barry, C.S.4    Martinez-Fleites, C.5
  • 22
    • 0035190313 scopus 로고    scopus 로고
    • Identification of Residues Involved in Catalytic Activity of the Inverting Glycosyl Transferase WbbE from Salmonella enterica Serovar Borreze
    • PubMed: 11114903
    • Keenleyside WJ, Clarke AJ, Whitfield C (2001) Identification of Residues Involved in Catalytic Activity of the Inverting Glycosyl Transferase WbbE from Salmonella enterica Serovar Borreze. J Bacteriol 183: 77-85. PubMed: 11114903.
    • (2001) J Bacteriol , vol.183 , pp. 77-85
    • Keenleyside, W.J.1    Clarke, A.J.2    Whitfield, C.3
  • 23
    • 55549117483 scopus 로고    scopus 로고
    • Crystal structure of a UDP-glucose-specific glycosyltransferase from a Mycobacterium species
    • doi:10.1074/jbc.M801853200. PubMed: 18667419
    • Fulton Z, McAlister A, Wilce MCJ, Brammananth R, Zaker-Tabrizi L et al. (2008) Crystal structure of a UDP-glucose-specific glycosyltransferase from a Mycobacterium species. J Biol Chem 283: 27881-27890. doi:10.1074/jbc.M801853200. PubMed: 18667419.
    • (2008) J Biol Chem , vol.283 , pp. 27881-27890
    • Fulton, Z.1    McAlister, A.2    Wilce, M.C.J.3    Brammananth, R.4    Zaker-Tabrizi, L.5
  • 24
    • 0035824876 scopus 로고    scopus 로고
    • Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: A comparison with related NDP-sugar glycosyltransferases
    • doi:10.1006/jmbi.2001.5159. PubMed: 11733986
    • Tarbouriech N, Charnock SJ, Davies GJ (2001) Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar glycosyltransferases. J Mol Biol 314: 655-661. doi:10.1006/jmbi.2001.5159. PubMed: 11733986.
    • (2001) J Mol Biol , vol.314 , pp. 655-661
    • Tarbouriech, N.1    Charnock, S.J.2    Davies, G.J.3
  • 25
    • 0034613392 scopus 로고    scopus 로고
    • Identification of essential amino acid residues in the Sinorhizobium meliloti glucosyltransferase ExoM
    • doi:10.1074/jbc.M004524200. PubMed: 10908566
    • Garinot-Schneider C, Lellouch AC, Geremia RA (2000) Identification of essential amino acid residues in the Sinorhizobium meliloti glucosyltransferase ExoM. J Biol Chem 275: 31407-31413. doi:10.1074/jbc.M004524200. PubMed: 10908566.
    • (2000) J Biol Chem , vol.275 , pp. 31407-31413
    • Garinot-Schneider, C.1    Lellouch, A.C.2    Geremia, R.A.3
  • 26
    • 7444220526 scopus 로고    scopus 로고
    • The beginnings of mucin biosynthesis: The crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1
    • doi:10.1073/pnas.0405657101. PubMed: 15486088
    • Fritz TA, Hurley JH, Trinh LB, Shiloach J, Tabak LA (2004) The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1. Proc Natl Acad Sci U S A 101: 15307-15312. doi:10.1073/pnas.0405657101. PubMed: 15486088.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 15307-15312
    • Fritz, T.A.1    Hurley, J.H.2    Trinh, L.B.3    Shiloach, J.4    Tabak, L.A.5
  • 27
    • 0345254937 scopus 로고    scopus 로고
    • Roles of individual enzyme-substrate interactions by alpha-1,3- galactosyltransferase in catalysis and specificity
    • doi:10.1021/bi035430r. PubMed: 14621997
    • Zhang Y, Swaminathan GJ, Deshpande A, Boix E, Natesh R et al. (2003) Roles of individual enzyme-substrate interactions by alpha-1,3- galactosyltransferase in catalysis and specificity. Biochemistry 42: 13512-13521. doi:10.1021/bi035430r. PubMed: 14621997.
    • (2003) Biochemistry , vol.42 , pp. 13512-13521
    • Zhang, Y.1    Swaminathan, G.J.2    Deshpande, A.3    Boix, E.4    Natesh, R.5
  • 28
    • 0036725060 scopus 로고    scopus 로고
    • The structural basis for specificity in human ABO(H) blood group biosynthesis
    • doi:10.1038/nsb832. PubMed: 12198488
    • Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL et al. (2002) The structural basis for specificity in human ABO(H) blood group biosynthesis. Nat Struct Biol 9: 685-690. doi:10.1038/nsb832. PubMed: 12198488.
    • (2002) Nat Struct Biol , vol.9 , pp. 685-690
    • Patenaude, S.I.1    Seto, N.O.2    Borisova, S.N.3    Szpacenko, A.4    Marcus, S.L.5
  • 29
    • 84863798084 scopus 로고    scopus 로고
    • Mechanistic insights into the retaining glucosyl-3-phosphoglycerate synthase from mycobacteria
    • doi:10.1074/jbc.M112.368191. PubMed: 22637481
    • Urresti S, Albesa-Jové D, Schaeffer F, Pham HT, Kaur D et al. (2012) Mechanistic insights into the retaining glucosyl-3-phosphoglycerate synthase from mycobacteria. J Biol Chem 287: 24649-24661. doi:10.1074/jbc.M112. 368191. PubMed: 22637481.
    • (2012) J Biol Chem , vol.287 , pp. 24649-24661
    • Urresti, S.1    Albesa-Jové, D.2    Schaeffer, F.3    Pham, H.T.4    Kaur, D.5
  • 30
    • 19544388989 scopus 로고    scopus 로고
    • Multiple flexible structure alignment using partial order graphs
    • doi:10.1093/bioinformatics/bti353. PubMed: 15746292
    • Ye Y, Godzik A (2005) Multiple flexible structure alignment using partial order graphs. Bioinformatics 21: 2362-2369. doi:10.1093/bioinformatics/bti353. PubMed: 15746292.
    • (2005) Bioinformatics , vol.21 , pp. 2362-2369
    • Ye, Y.1    Godzik, A.2
  • 31
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • doi:10.1002/bip.360221211. PubMed: 6667333
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637. doi:10.1002/bip.360221211. PubMed: 6667333.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 32
    • 23144444979 scopus 로고    scopus 로고
    • Protein structure prediction servers at University College London
    • doi:10.1093/nar/gni035. PubMed: 15980489
    • Bryson K, McGuffin LJ, Marsden RL, Ward JJ, Sodhi JS et al. (2005) Protein structure prediction servers at University College London. Nucleic Acids Res 33: W36-W38. doi:10.1093/nar/gni035. PubMed: 15980489.
    • (2005) Nucleic Acids Res , vol.33
    • Bryson, K.1    McGuffin, L.J.2    Marsden, R.L.3    Ward, J.J.4    Sodhi, J.S.5
  • 33
    • 34248532415 scopus 로고    scopus 로고
    • PROMALS: Towards accurate multiple sequence alignments of distantly related proteins
    • doi:10.1093/bioinformatics/btm017. PubMed: 17267437
    • Pei J, Grishin NV (2007) PROMALS: towards accurate multiple sequence alignments of distantly related proteins. Bioinformatics 23: 802-808. doi:10.1093/bioinformatics/btm017. PubMed: 17267437.
    • (2007) Bioinformatics , vol.23 , pp. 802-808
    • Pei, J.1    Grishin, N.V.2
  • 34
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • doi:10.1016/0263-7855(96)00018-5. PubMed: 8744570
    • Humphrey W, Dalke A, Schulten K (1996) VMD: Visual molecular dynamics. J Mol Graph 14: 33-38. doi:10.1016/0263-7855(96)00018-5. PubMed: 8744570.
    • (1996) J Mol Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 35
    • 79959931985 scopus 로고    scopus 로고
    • HMMER web server: Interactive sequence similarity searching
    • doi:10.1093/nar/gkr367. PubMed: 21593126
    • Finn RD, Clements J, Eddy SR (2011) HMMER web server: interactive sequence similarity searching. Nucleic Acids Res 39: W29-W37. doi:10.1093/nar/gkr367. PubMed: 21593126.
    • (2011) Nucleic Acids Res , vol.39
    • Finn, R.D.1    Clements, J.2    Eddy, S.R.3
  • 36
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • PubMed: 3447015
    • Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4: 406-425. PubMed: 3447015.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 37
    • 0033990046 scopus 로고    scopus 로고
    • Phylogenetic analysis using PHYLIP
    • PubMed: 10547839
    • Retief JD (2000) Phylogenetic analysis using PHYLIP. Methods Mol Biol 132: 243-258. PubMed: 10547839.
    • (2000) Methods Mol Biol , vol.132 , pp. 243-258
    • Retief, J.D.1
  • 38
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • doi:10.1006/jmbi.1993.1626. PubMed: 8254673
    • Sali A, Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815. doi:10.1006/jmbi.1993.1626. PubMed: 8254673.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 39
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • doi:10.1110/ps.9.9.1753. PubMed: 11045621
    • Fiser A, Do RK, Sali A (2000) Modeling of loops in protein structures. Protein Sci 9: 1753-1773. doi:10.1110/ps.9.9.1753. PubMed: 11045621.
    • (2000) Protein Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 40
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • doi:10.1110/ps.062416606. PubMed: 17075131
    • Shen MY, Sali A (2006) Statistical potential for assessment and prediction of protein structures. Protein Sci 15: 2507-2524. doi:10.1110/ps.062416606. PubMed: 17075131.
    • (2006) Protein Sci , vol.15 , pp. 2507-2524
    • Shen, M.Y.1    Sali, A.2
  • 41
    • 0000243829 scopus 로고
    • PROCHECK a program to check the stereochemical quality of protein structures
    • Volumes 1993 20: 19; doi:10.1107/S0021889892009944
    • Laskowski RA Volumes 1993 20: 19 (1993); PROCHECK a program to check the stereochemical quality of protein structures. J Appl Crystallography 26: 283-291 doi:10.1107/S0021889892009944.
    • (1993) J Appl Crystallography , vol.26 , pp. 283-291
    • Laskowski, R.A.1
  • 42
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen HJC (1991) GROMACS: a message-passing parallel molecular dynamics implementation. Comp Phys Comm 91: 43-56
    • (1991) Comp Phys Comm , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1
  • 43
    • 23144457576 scopus 로고    scopus 로고
    • H++: A server for estimating pKas and adding missing hydrogens to macromolecules
    • doi:10.1093/nar/gki464. PubMed: 15980491
    • Gordon JC, Myers JB, Folta T, Shoja V, Heath LS et al. (2005) H++: a server for estimating pKas and adding missing hydrogens to macromolecules. Nucleic Acids Res 33: W368-W371. doi:10.1093/nar/gki464. PubMed: 15980491.
    • (2005) Nucleic Acids Res , vol.33
    • Gordon, J.C.1    Myers, J.B.2    Folta, T.3    Shoja, V.4    Heath, L.S.5
  • 44
    • 0042357447 scopus 로고    scopus 로고
    • Potential Energy Hypersurfaces of Nucleotide Sugars: Ab Initio Calculations, Force-Field Parametrization, and Exploration of the Flexibility
    • doi:10.1021/ja983854g
    • Petrová P, Koca J, Imberty A (1999) Potential Energy Hypersurfaces of Nucleotide Sugars: Ab Initio Calculations, Force-Field Parametrization, and Exploration of the Flexibility. J Am Chem Soc 121: 5535-5547. doi:10.1021/ja983854g.
    • (1999) J Am Chem Soc , vol.121 , pp. 5535-5547
    • Petrová, P.1    Koca, J.2    Imberty, A.3
  • 45
    • 0033556236 scopus 로고    scopus 로고
    • Peptide folding: When simulation meets experiment
    • doi:10.1002/(SICI)1521-3773(19990115)38:1/2
    • Daura X, Gademann K, Jaun B, Seebach D, van Gunsteren WF et al. (1999) Peptide folding: When simulation meets experiment . Angew Chem - Int Ed 38: 236-240. doi:10.1002/(SICI)1521-3773(19990115)38:1/2.
    • (1999) Angew Chem - Int Ed , vol.38 , pp. 236-240
    • Daura, X.1    Gademann, K.2    Jaun, B.3    Seebach, D.4    Van Gunsteren, W.F.5
  • 46
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • doi:10.1002/(SICI)1096-987X(19981115)19:14
    • Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE et al. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem 19: 1639-1662. doi:10.1002/(SICI)1096- 987X(19981115)19:14.
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5
  • 47
    • 58949085244 scopus 로고    scopus 로고
    • An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol
    • doi:10.1186/1472-6750-8-91. PubMed: 19055817
    • Liu H, Naismith JH (2008) An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol. BMC Biotechnol 8: 91. doi:10.1186/1472-6750-8-91. PubMed: 19055817.
    • (2008) BMC Biotechnol , vol.8 , pp. 91
    • Liu, H.1    Naismith, J.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.