메뉴 건너뛰기




Volumn 10, Issue 8, 2014, Pages

P. aeruginosa SGNH Hydrolase-Like Proteins AlgJ and AlgX Have Similar Topology but Separate and Distinct Roles in Alginate Acetylation

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ALGINIC ACID; HYDROLASE; MANNURONIC ACID; PEPTIDES AND PROTEINS; SGNH HYDROLASE; SGNH HYDROLASE LIKE PROTEIN ALGJ; SGNH HYDROLASE LIKE PROTEIN ALGX; UNCLASSIFIED DRUG; ALGJ PROTEIN, PSEUDOMONAS AERUGINOSA; BACTERIAL PROTEIN; GLUCURONIC ACID; HEXURONIC ACID;

EID: 84935913390     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004334     Document Type: Article
Times cited : (56)

References (82)
  • 1
    • 28244499587 scopus 로고    scopus 로고
    • The exopolysaccharide alginate protects Pseudomonas aeruginosa biofilm bacteria from IFN-gamma-mediated macrophage killing
    • Leid JG, Willson CJ, Shirtliff ME, Hassett DJ, Parsek MR, et al. (2005) The exopolysaccharide alginate protects Pseudomonas aeruginosa biofilm bacteria from IFN-gamma-mediated macrophage killing. J Immunol 175: 7512–7518.
    • (2005) J Immunol , vol.175 , pp. 7512-7518
    • Leid, J.G.1    Willson, C.J.2    Shirtliff, M.E.3    Hassett, D.J.4    Parsek, M.R.5
  • 2
    • 0037313237 scopus 로고    scopus 로고
    • Understanding biofilm resistance to antibacterial agents
    • Davies D, (2003) Understanding biofilm resistance to antibacterial agents. Nat Rev Drug Discov 2: 114–122.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 114-122
    • Davies, D.1
  • 3
    • 0027054496 scopus 로고
    • Alginate–its role in neutrophil responses and signal transduction towards mucoid Pseudomonas aeruginosa bacteria
    • Konig B, Friedl P, Pedersen SS, Konig W, (1992) Alginate–its role in neutrophil responses and signal transduction towards mucoid Pseudomonas aeruginosa bacteria. Int Arch Allergy Immunol 99: 98–106.
    • (1992) Int Arch Allergy Immunol , vol.99 , pp. 98-106
    • Konig, B.1    Friedl, P.2    Pedersen, S.S.3    Konig, W.4
  • 4
    • 0036023487 scopus 로고    scopus 로고
    • Role of dose concentration in biocide efficacy against Pseudomonas aeruginosa biofilms
    • Grobe KJ, Zahller J, Stewart PS, (2002) Role of dose concentration in biocide efficacy against Pseudomonas aeruginosa biofilms. J Ind Microbiol Biotechnol 29: 10–15.
    • (2002) J Ind Microbiol Biotechnol , vol.29 , pp. 10-15
    • Grobe, K.J.1    Zahller, J.2    Stewart, P.S.3
  • 6
    • 79551521160 scopus 로고    scopus 로고
    • The pel polysaccharide can serve a structural and protective role in the biofilm matrix of Pseudomonas aeruginosa
    • Colvin KM, Gordon VD, Murakami K, Borlee BR, Wozniak DJ, et al. (2011) The pel polysaccharide can serve a structural and protective role in the biofilm matrix of Pseudomonas aeruginosa. PLoS Pathog 7: e1001264.
    • (2011) PLoS Pathog , vol.7 , pp. e1001264
    • Colvin, K.M.1    Gordon, V.D.2    Murakami, K.3    Borlee, B.R.4    Wozniak, D.J.5
  • 7
    • 79953165038 scopus 로고    scopus 로고
    • Aminoglycoside resistance of Pseudomonas aeruginosa biofilms modulated by extracellular polysaccharide
    • Khan W, Bernier SP, Kuchma SL, Hammond JH, Hasan F, et al. (2010) Aminoglycoside resistance of Pseudomonas aeruginosa biofilms modulated by extracellular polysaccharide. Int Microbiol 13: 207–212.
    • (2010) Int Microbiol , vol.13 , pp. 207-212
    • Khan, W.1    Bernier, S.P.2    Kuchma, S.L.3    Hammond, J.H.4    Hasan, F.5
  • 8
    • 84860188732 scopus 로고    scopus 로고
    • Biosynthesis of the Pseudomonas aeruginosa Extracellular Polysaccharides, Alginate, Pel, and Psl
    • Franklin MJ, Nivens DE, Weadge JT, Howell PL, (2011) Biosynthesis of the Pseudomonas aeruginosa Extracellular Polysaccharides, Alginate, Pel, and Psl. Front Microbiol 2: 167.
    • (2011) Front Microbiol , vol.2 , pp. 167
    • Franklin, M.J.1    Nivens, D.E.2    Weadge, J.T.3    Howell, P.L.4
  • 9
    • 84864379470 scopus 로고    scopus 로고
    • The Pel and Psl polysaccharides provide Pseudomonas aeruginosa structural redundancy within the biofilm matrix
    • Colvin KM, Irie Y, Tart CS, Urbano R, Whitney JC, et al. (2012) The Pel and Psl polysaccharides provide Pseudomonas aeruginosa structural redundancy within the biofilm matrix. Environ Microbiol 14: 1913–1928.
    • (2012) Environ Microbiol , vol.14 , pp. 1913-1928
    • Colvin, K.M.1    Irie, Y.2    Tart, C.S.3    Urbano, R.4    Whitney, J.C.5
  • 10
    • 0025908061 scopus 로고
    • Alginate synthesis by Pseudomonas aeruginosa: a key pathogenic factor in chronic pulmonary infections of cystic fibrosis patients
    • May TB, Shinabarger D, Maharaj R, Kato J, Chu L, et al. (1991) Alginate synthesis by Pseudomonas aeruginosa: a key pathogenic factor in chronic pulmonary infections of cystic fibrosis patients. Clin Microbiol Rev 4: 191–206.
    • (1991) Clin Microbiol Rev , vol.4 , pp. 191-206
    • May, T.B.1    Shinabarger, D.2    Maharaj, R.3    Kato, J.4    Chu, L.5
  • 11
    • 0020070286 scopus 로고
    • Utilization of human respiratory secretions by mucoid Pseudomonas aeruginosa of cystic fibrosis origin
    • Ohman DE, Chakrabarty AM, (1982) Utilization of human respiratory secretions by mucoid Pseudomonas aeruginosa of cystic fibrosis origin. Infect Immun 37: 662–669.
    • (1982) Infect Immun , vol.37 , pp. 662-669
    • Ohman, D.E.1    Chakrabarty, A.M.2
  • 12
    • 0027291330 scopus 로고
    • Identification of algF in the alginate biosynthetic gene cluster of Pseudomonas aeruginosa which is required for alginate acetylation
    • Franklin MJ, Ohman DE, (1993) Identification of algF in the alginate biosynthetic gene cluster of Pseudomonas aeruginosa which is required for alginate acetylation. J Bacteriol 175: 5057–5065.
    • (1993) J Bacteriol , vol.175 , pp. 5057-5065
    • Franklin, M.J.1    Ohman, D.E.2
  • 13
    • 0036097264 scopus 로고    scopus 로고
    • Mutant analysis and cellular localization of the AlgI, AlgJ, and AlgF proteins required for O acetylation of alginate in Pseudomonas aeruginosa
    • Franklin MJ, Ohman DE, (2002) Mutant analysis and cellular localization of the AlgI, AlgJ, and AlgF proteins required for O acetylation of alginate in Pseudomonas aeruginosa. J Bacteriol 184: 3000–3007.
    • (2002) J Bacteriol , vol.184 , pp. 3000-3007
    • Franklin, M.J.1    Ohman, D.E.2
  • 14
    • 0031801558 scopus 로고    scopus 로고
    • Bacterial alginate biosynthesis–recent progress and future prospects
    • Gacesa P, (1998) Bacterial alginate biosynthesis–recent progress and future prospects. Microbiology 144 (Pt 5) 1133–1143.
    • (1998) Microbiology , vol.144 , pp. 1133-1143
    • Gacesa, P.1
  • 15
    • 0001765872 scopus 로고
    • A Polysaccharide Resembling Alginic Acid from a Pseudomonas Micro-Organism
    • Linker A, Jones RS, (1964) A Polysaccharide Resembling Alginic Acid from a Pseudomonas Micro-Organism. Nature 204: 187–188.
    • (1964) Nature , vol.204 , pp. 187-188
    • Linker, A.1    Jones, R.S.2
  • 16
    • 11144237620 scopus 로고    scopus 로고
    • A crucial role for exopolysaccharide modification in bacterial biofilm formation, immune evasion, and virulence
    • Vuong C, Kocianova S, Voyich JM, Yao Y, Fischer ER, et al. (2004) A crucial role for exopolysaccharide modification in bacterial biofilm formation, immune evasion, and virulence. J Biol Chem 279: 54881–54886.
    • (2004) J Biol Chem , vol.279 , pp. 54881-54886
    • Vuong, C.1    Kocianova, S.2    Voyich, J.M.3    Yao, Y.4    Fischer, E.R.5
  • 17
    • 34447249875 scopus 로고    scopus 로고
    • Molecular basis for preferential protective efficacy of antibodies directed to the poorly acetylated form of staphylococcal poly-N-acetyl-beta-(1–6)-glucosamine
    • Cerca N, Jefferson KK, Maira-Litran T, Pier DB, Kelly-Quintos C, et al. (2007) Molecular basis for preferential protective efficacy of antibodies directed to the poorly acetylated form of staphylococcal poly-N-acetyl-beta-(1–6)-glucosamine. Infect Immun 75: 3406–3413.
    • (2007) Infect Immun , vol.75 , pp. 3406-3413
    • Cerca, N.1    Jefferson, K.K.2    Maira-Litran, T.3    Pier, D.B.4    Kelly-Quintos, C.5
  • 18
    • 47049129510 scopus 로고    scopus 로고
    • Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-beta-1,6-N-acetyl-D-glucosamine
    • Itoh Y, Rice JD, Goller C, Pannuri A, Taylor J, et al. (2008) Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-beta-1,6-N-acetyl-D-glucosamine. J Bacteriol 190: 3670–3680.
    • (2008) J Bacteriol , vol.190 , pp. 3670-3680
    • Itoh, Y.1    Rice, J.D.2    Goller, C.3    Pannuri, A.4    Taylor, J.5
  • 19
    • 1942443593 scopus 로고    scopus 로고
    • The pgaABCD locus of Escherichia coli promotes the synthesis of a polysaccharide adhesin required for biofilm formation
    • Wang X, Preston JF, 3rdRomeo T, (2004) The pgaABCD locus of Escherichia coli promotes the synthesis of a polysaccharide adhesin required for biofilm formation. J Bacteriol 186: 2724–2734.
    • (2004) J Bacteriol , vol.186 , pp. 2724-2734
    • Wang, X.1    Preston, J.F.2    Romeo, T.3
  • 20
    • 84877994854 scopus 로고    scopus 로고
    • PelA deacetylase activity is required for Pel polysaccharide synthesis in Pseudomonas aeruginosa
    • Colvin KM, Alnabelseya N, Baker P, Whitney JC, Howell PL, et al. (2013) PelA deacetylase activity is required for Pel polysaccharide synthesis in Pseudomonas aeruginosa. J Bacteriol 195: 2329–2339.
    • (2013) J Bacteriol , vol.195 , pp. 2329-2339
    • Colvin, K.M.1    Alnabelseya, N.2    Baker, P.3    Whitney, J.C.4    Howell, P.L.5
  • 21
    • 84876699602 scopus 로고    scopus 로고
    • The adhesive and cohesive properties of a bacterial polysaccharide adhesin are modulated by a deacetylase
    • Wan Z, Brown PJ, Elliott EN, Brun YV, (2013) The adhesive and cohesive properties of a bacterial polysaccharide adhesin are modulated by a deacetylase. Mol Microbiol 88: 486–500.
    • (2013) Mol Microbiol , vol.88 , pp. 486-500
    • Wan, Z.1    Brown, P.J.2    Elliott, E.N.3    Brun, Y.V.4
  • 22
    • 84892830772 scopus 로고    scopus 로고
    • O-acetylation of plant cell wall polysaccharides
    • Gille S, Pauly M, (2012) O-acetylation of plant cell wall polysaccharides. Front Plant Sci 3: 12.
    • (2012) Front Plant Sci , vol.3 , pp. 12
    • Gille, S.1    Pauly, M.2
  • 23
    • 84899560055 scopus 로고    scopus 로고
    • Chemical biology of peptidoglycan acetylation and deacetylation
    • Moynihan PJ, Sychantha D, Clarke AJ, (2014) Chemical biology of peptidoglycan acetylation and deacetylation. Bioorg Chem 54C: 44–50.
    • (2014) Bioorg Chem , vol.54C , pp. 44-50
    • Moynihan, P.J.1    Sychantha, D.2    Clarke, A.J.3
  • 24
    • 39149102149 scopus 로고    scopus 로고
    • Structural variation in the glycan strands of bacterial peptidoglycan
    • Vollmer W, (2008) Structural variation in the glycan strands of bacterial peptidoglycan. FEMS Microbiol Rev 32: 287–306.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 287-306
    • Vollmer, W.1
  • 25
    • 34247542105 scopus 로고    scopus 로고
    • Neisseria gonorrheae O-acetylpeptidoglycan esterase, a serine esterase with a Ser-His-Asp catalytic triad
    • Weadge JT, Clarke AJ, (2007) Neisseria gonorrheae O-acetylpeptidoglycan esterase, a serine esterase with a Ser-His-Asp catalytic triad. Biochemistry 46: 4932–4941.
    • (2007) Biochemistry , vol.46 , pp. 4932-4941
    • Weadge, J.T.1    Clarke, A.J.2
  • 26
    • 80255137078 scopus 로고    scopus 로고
    • O-Acetylated peptidoglycan: controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems
    • Moynihan PJ, Clarke AJ, (2011) O-Acetylated peptidoglycan: controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems. Int J Biochem Cell Biol 43: 1655–1659.
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 1655-1659
    • Moynihan, P.J.1    Clarke, A.J.2
  • 27
    • 77951243041 scopus 로고    scopus 로고
    • O-acetylation of peptidoglycan in gram-negative bacteria: identification and characterization of peptidoglycan O-acetyltransferase in Neisseria gonorrhoeae
    • Moynihan PJ, Clarke AJ, (2010) O-acetylation of peptidoglycan in gram-negative bacteria: identification and characterization of peptidoglycan O-acetyltransferase in Neisseria gonorrhoeae. J Biol Chem 285: 13264–13273.
    • (2010) J Biol Chem , vol.285 , pp. 13264-13273
    • Moynihan, P.J.1    Clarke, A.J.2
  • 28
    • 79959863188 scopus 로고    scopus 로고
    • Characterization of O-acetylation of N-acetylglucosamine: a novel structural variation of bacterial peptidoglycan
    • Bernard E, Rolain T, Courtin P, Guillot A, Langella P, et al. (2011) Characterization of O-acetylation of N-acetylglucosamine: a novel structural variation of bacterial peptidoglycan. J Biol Chem 286: 23950–23958.
    • (2011) J Biol Chem , vol.286 , pp. 23950-23958
    • Bernard, E.1    Rolain, T.2    Courtin, P.3    Guillot, A.4    Langella, P.5
  • 29
    • 13444282403 scopus 로고    scopus 로고
    • Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus
    • Bera A, Herbert S, Jakob A, Vollmer W, Gotz F, (2005) Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Mol Microbiol 55: 778–787.
    • (2005) Mol Microbiol , vol.55 , pp. 778-787
    • Bera, A.1    Herbert, S.2    Jakob, A.3    Vollmer, W.4    Gotz, F.5
  • 30
    • 0035114574 scopus 로고    scopus 로고
    • Role of alginate O acetylation in resistance of mucoid Pseudomonas aeruginosa to opsonic phagocytosis
    • Pier GB, Coleman F, Grout M, Franklin M, Ohman DE, (2001) Role of alginate O acetylation in resistance of mucoid Pseudomonas aeruginosa to opsonic phagocytosis. Infect Immun 69: 1895–1901.
    • (2001) Infect Immun , vol.69 , pp. 1895-1901
    • Pier, G.B.1    Coleman, F.2    Grout, M.3    Franklin, M.4    Ohman, D.E.5
  • 31
    • 0030002441 scopus 로고    scopus 로고
    • Identification of algI and algJ in the Pseudomonas aeruginosa alginate biosynthetic gene cluster which are required for alginate O acetylation
    • Franklin MJ, Ohman DE, (1996) Identification of algI and algJ in the Pseudomonas aeruginosa alginate biosynthetic gene cluster which are required for alginate O acetylation. J Bacteriol 178: 2186–2195.
    • (1996) J Bacteriol , vol.178 , pp. 2186-2195
    • Franklin, M.J.1    Ohman, D.E.2
  • 32
    • 84881252716 scopus 로고    scopus 로고
    • Structural and functional characterization of Pseudomonas aeruginosa AlgX: role of AlgX in alginate acetylation
    • Riley LM, Weadge JT, Baker P, Robinson H, Codee JD, et al. (2013) Structural and functional characterization of Pseudomonas aeruginosa AlgX: role of AlgX in alginate acetylation. J Biol Chem 288: 22299–22314.
    • (2013) J Biol Chem , vol.288 , pp. 22299-22314
    • Riley, L.M.1    Weadge, J.T.2    Baker, P.3    Robinson, H.4    Codee, J.D.5
  • 33
    • 3042732173 scopus 로고    scopus 로고
    • Evidence that the algI/algJ gene cassette, required for O acetylation of Pseudomonas aeruginosa alginate, evolved by lateral gene transfer
    • Franklin MJ, Douthit SA, McClure MA, (2004) Evidence that the algI/algJ gene cassette, required for O acetylation of Pseudomonas aeruginosa alginate, evolved by lateral gene transfer. J Bacteriol 186: 4759–4773.
    • (2004) J Bacteriol , vol.186 , pp. 4759-4773
    • Franklin, M.J.1    Douthit, S.A.2    McClure, M.A.3
  • 34
    • 84881252716 scopus 로고    scopus 로고
    • Structural and functional characterization of Pseudomonas aeruginosa AlgX: role of AlgX in alginate acetylation
    • Riley LM, Weadge JT, Baker P, Robinson H, Codee JD, et al. (2013) Structural and functional characterization of Pseudomonas aeruginosa AlgX: role of AlgX in alginate acetylation. J Biol Chem 288: 22299–22314.
    • (2013) J Biol Chem , vol.288 , pp. 22299-22314
    • Riley, L.M.1    Weadge, J.T.2    Baker, P.3    Robinson, H.4    Codee, J.D.5
  • 35
    • 0035152936 scopus 로고    scopus 로고
    • Role of alginate and its O acetylation in formation of Pseudomonas aeruginosa microcolonies and biofilms
    • Nivens DE, Ohman DE, Williams J, Franklin MJ, (2001) Role of alginate and its O acetylation in formation of Pseudomonas aeruginosa microcolonies and biofilms. J Bacteriol 183: 1047–1057.
    • (2001) J Bacteriol , vol.183 , pp. 1047-1057
    • Nivens, D.E.1    Ohman, D.E.2    Williams, J.3    Franklin, M.J.4
  • 36
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL, (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305: 567–580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 39
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom L, (2002) Serine protease mechanism and specificity. Chem Rev 102: 4501–4524.
    • (2002) Chem Rev , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 40
    • 84873845734 scopus 로고    scopus 로고
    • Mechanism of action of Neisseria gonorrhoeae O-acetylpeptidoglycan esterase, an SGNH serine esterase
    • Pfeffer JM, Weadge JT, Clarke AJ, (2013) Mechanism of action of Neisseria gonorrhoeae O-acetylpeptidoglycan esterase, an SGNH serine esterase. J Biol Chem 288: 2605–2613.
    • (2013) J Biol Chem , vol.288 , pp. 2605-2613
    • Pfeffer, J.M.1    Weadge, J.T.2    Clarke, A.J.3
  • 41
    • 0032232233 scopus 로고    scopus 로고
    • Unfolding of proteins monitored by electrospray ionization mass spectrometry: a comparison of positive and negative ion modes
    • Konermann L, Douglas DJ, (1998) Unfolding of proteins monitored by electrospray ionization mass spectrometry: a comparison of positive and negative ion modes. J Am Soc Mass Spectrom 9: 1248–1254.
    • (1998) J Am Soc Mass Spectrom , vol.9 , pp. 1248-1254
    • Konermann, L.1    Douglas, D.J.2
  • 42
    • 0037258408 scopus 로고    scopus 로고
    • Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry
    • Grandori R, (2003) Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry. J Mass Spectrom 38: 11–15.
    • (2003) J Mass Spectrom , vol.38 , pp. 11-15
    • Grandori, R.1
  • 43
    • 84856137749 scopus 로고    scopus 로고
    • Reflections on charge state distributions, protein structure, and the mystical mechanism of electrospray ionization
    • Hamdy OM, Julian RR, (2012) Reflections on charge state distributions, protein structure, and the mystical mechanism of electrospray ionization. J Am Soc Mass Spectrom 23: 1–6.
    • (2012) J Am Soc Mass Spectrom , vol.23 , pp. 1-6
    • Hamdy, O.M.1    Julian, R.R.2
  • 44
    • 84865858205 scopus 로고    scopus 로고
    • Do charge state signatures guarantee protein conformations?
    • Hall Z, Robinson CV, (2012) Do charge state signatures guarantee protein conformations? J Am Soc Mass Spectrom 23: 1161–1168.
    • (2012) J Am Soc Mass Spectrom , vol.23 , pp. 1161-1168
    • Hall, Z.1    Robinson, C.V.2
  • 45
    • 50849098485 scopus 로고    scopus 로고
    • Do ionic charges in ESI MS provide useful information on macromolecular structure?
    • Kaltashov IA, Abzalimov RR, (2008) Do ionic charges in ESI MS provide useful information on macromolecular structure? J Am Soc Mass Spectrom 19: 1239–1246.
    • (2008) J Am Soc Mass Spectrom , vol.19 , pp. 1239-1246
    • Kaltashov, I.A.1    Abzalimov, R.R.2
  • 46
    • 24344484686 scopus 로고    scopus 로고
    • Prediction of interface residues in protein-protein complexes by a consensus neural network method: test against NMR data
    • Chen H, Zhou HX, (2005) Prediction of interface residues in protein-protein complexes by a consensus neural network method: test against NMR data. Proteins 61: 21–35.
    • (2005) Proteins , vol.61 , pp. 21-35
    • Chen, H.1    Zhou, H.X.2
  • 47
    • 0035882570 scopus 로고    scopus 로고
    • Prediction of protein interaction sites from sequence profile and residue neighbor list
    • Zhou HX, Shan Y, (2001) Prediction of protein interaction sites from sequence profile and residue neighbor list. Proteins 44: 336–343.
    • (2001) Proteins , vol.44 , pp. 336-343
    • Zhou, H.X.1    Shan, Y.2
  • 48
    • 0028920506 scopus 로고
    • The high non-enzymatic conjugation rates of some glutathione S-transferase (GST) substrates at high glutathione concentrations
    • Satoh K, (1995) The high non-enzymatic conjugation rates of some glutathione S-transferase (GST) substrates at high glutathione concentrations. Carcinogenesis 16: 869–874.
    • (1995) Carcinogenesis , vol.16 , pp. 869-874
    • Satoh, K.1
  • 49
    • 84864757329 scopus 로고    scopus 로고
    • Pseudo-enzymatic hydrolysis of 4-nitrophenyl acetate by human serum albumin: pH-dependence of rates of individual steps
    • Ascenzi P, Gioia M, Fanali G, Coletta M, Fasano M, (2012) Pseudo-enzymatic hydrolysis of 4-nitrophenyl acetate by human serum albumin: pH-dependence of rates of individual steps. Biochem Biophys Res Commun 424: 451–455.
    • (2012) Biochem Biophys Res Commun , vol.424 , pp. 451-455
    • Ascenzi, P.1    Gioia, M.2    Fanali, G.3    Coletta, M.4    Fasano, M.5
  • 50
    • 53049095404 scopus 로고    scopus 로고
    • Pseudo-esterase activity of human albumin: slow turnover on tyrosine 411 and stable acetylation of 82 residues including 59 lysines
    • Lockridge O, Xue W, Gaydess A, Grigoryan H, Ding SJ, et al. (2008) Pseudo-esterase activity of human albumin: slow turnover on tyrosine 411 and stable acetylation of 82 residues including 59 lysines. J Biol Chem 283: 22582–22590.
    • (2008) J Biol Chem , vol.283 , pp. 22582-22590
    • Lockridge, O.1    Xue, W.2    Gaydess, A.3    Grigoryan, H.4    Ding, S.J.5
  • 51
    • 84879229569 scopus 로고    scopus 로고
    • Assay for peptidoglycan O-acetyltransferase: a potential new antibacterial target
    • Moynihan PJ, Clarke AJ, (2013) Assay for peptidoglycan O-acetyltransferase: a potential new antibacterial target. Anal Biochem 439: 73–79.
    • (2013) Anal Biochem , vol.439 , pp. 73-79
    • Moynihan, P.J.1    Clarke, A.J.2
  • 52
    • 0023050603 scopus 로고
    • Monomer sequence and acetylation pattern in some bacterial alginates
    • Skjak-Braek G, Grasdalen H, Larsen B, (1986) Monomer sequence and acetylation pattern in some bacterial alginates. Carbohydr Res 154: 239–250.
    • (1986) Carbohydr Res , vol.154 , pp. 239-250
    • Skjak-Braek, G.1    Grasdalen, H.2    Larsen, B.3
  • 53
    • 84856297644 scopus 로고    scopus 로고
    • Identification of a periplasmic AlgK-AlgX-MucD multiprotein complex in Pseudomonas aeruginosa involved in biosynthesis and regulation of alginate
    • Hay ID, Schmidt O, Filitcheva J, Rehm BH, (2012) Identification of a periplasmic AlgK-AlgX-MucD multiprotein complex in Pseudomonas aeruginosa involved in biosynthesis and regulation of alginate. Appl Microbiol Biotechnol 93: 215–227.
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 215-227
    • Hay, I.D.1    Schmidt, O.2    Filitcheva, J.3    Rehm, B.H.4
  • 54
    • 75849138999 scopus 로고    scopus 로고
    • AlgK is a TPR-containing protein and the periplasmic component of a novel exopolysaccharide secretin
    • Keiski CL, Harwich M, Jain S, Neculai AM, Yip P, et al. (2010) AlgK is a TPR-containing protein and the periplasmic component of a novel exopolysaccharide secretin. Structure 18: 265–273.
    • (2010) Structure , vol.18 , pp. 265-273
    • Keiski, C.L.1    Harwich, M.2    Jain, S.3    Neculai, A.M.4    Yip, P.5
  • 55
    • 80051966444 scopus 로고    scopus 로고
    • Structural basis for alginate secretion across the bacterial outer membrane
    • Whitney JC, Hay ID, Li C, Eckford PD, Robinson H, et al. (2011) Structural basis for alginate secretion across the bacterial outer membrane. Proc Natl Acad Sci U S A 108: 13083–13088.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 13083-13088
    • Whitney, J.C.1    Hay, I.D.2    Li, C.3    Eckford, P.D.4    Robinson, H.5
  • 56
    • 25444481824 scopus 로고    scopus 로고
    • Role of an alginate lyase for alginate transport in mucoid Pseudomonas aeruginosa
    • Jain S, Ohman DE, (2005) Role of an alginate lyase for alginate transport in mucoid Pseudomonas aeruginosa. Infect Immun 73: 6429–6436.
    • (2005) Infect Immun , vol.73 , pp. 6429-6436
    • Jain, S.1    Ohman, D.E.2
  • 57
    • 0344211855 scopus 로고    scopus 로고
    • The dual roles of AlgG in C-5-epimerization and secretion of alginate polymers in Pseudomonas aeruginosa
    • Jain S, Franklin MJ, Ertesvag H, Valla S, Ohman DE, (2003) The dual roles of AlgG in C-5-epimerization and secretion of alginate polymers in Pseudomonas aeruginosa. Mol Microbiol 47: 1123–1133.
    • (2003) Mol Microbiol , vol.47 , pp. 1123-1133
    • Jain, S.1    Franklin, M.J.2    Ertesvag, H.3    Valla, S.4    Ohman, D.E.5
  • 58
    • 0141484352 scopus 로고    scopus 로고
    • Biofilm formation at the air-liquid interface by the Pseudomonas fluorescens SBW25 wrinkly spreader requires an acetylated form of cellulose
    • Spiers AJ, Bohannon J, Gehrig SM, Rainey PB, (2003) Biofilm formation at the air-liquid interface by the Pseudomonas fluorescens SBW25 wrinkly spreader requires an acetylated form of cellulose. Mol Microbiol 50: 15–27.
    • (2003) Mol Microbiol , vol.50 , pp. 15-27
    • Spiers, A.J.1    Bohannon, J.2    Gehrig, S.M.3    Rainey, P.B.4
  • 59
    • 78651267246 scopus 로고    scopus 로고
    • Pseudomonas Genome Database: improved comparative analysis and population genomics capability for Pseudomonas genomes
    • Winsor GL, Lam DK, Fleming L, Lo R, Whiteside MD, et al. (2011) Pseudomonas Genome Database: improved comparative analysis and population genomics capability for Pseudomonas genomes. Nucleic Acids Res 39: D596–600.
    • (2011) Nucleic Acids Res , vol.39 , pp. D596-600
    • Winsor, G.L.1    Lam, D.K.2    Fleming, L.3    Lo, R.4    Whiteside, M.D.5
  • 60
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley LA, Sternberg MJ, (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 4: 363–371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 61
    • 0034793650 scopus 로고    scopus 로고
    • Structure of E. coli 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases
    • Lee JE, Cornell KA, Riscoe MK, Howell PL, (2001) Structure of E. coli 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases. Structure 9: 941–953.
    • (2001) Structure , vol.9 , pp. 941-953
    • Lee, J.E.1    Cornell, K.A.2    Riscoe, M.K.3    Howell, P.L.4
  • 62
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. New Jersey: Elsevier. pp. 307–326.
    • (1997) New Jersey: Elsevier , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 65
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126–2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 68
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J, Merritt EA, (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D Biol Crystallogr 62: 439–450.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 69
    • 3242887525 scopus 로고    scopus 로고
    • STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins
    • Heinig M, Frishman D, (2004) STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins. Nucleic Acids Res 32: W500–502.
    • (2004) Nucleic Acids Res , vol.32 , pp. W500-502
    • Heinig, M.1    Frishman, D.2
  • 70
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky TJ, Czodrowski P, Li H, Nielsen JE, Jensen JH, et al. (2007) PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Res 35: W522–525.
    • (2007) Nucleic Acids Res , vol.35 , pp. W522-525
    • Dolinsky, T.J.1    Czodrowski, P.2    Li, H.3    Nielsen, J.E.4    Jensen, J.H.5
  • 71
    • 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: W529–533.
    • (2010) Nucleic Acids Res , vol.38 , pp. W529-533
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 72
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774–797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 74
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC, (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792–1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 75
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: a multiple sequence alignment method with reduced time and space complexity
    • Edgar RC, (2004) MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5: 113.
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 76
    • 0028231880 scopus 로고
    • Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7-A resolution
    • Zdanov A, Li Y, Bundle DR, Deng SJ, MacKenzie CR, et al. (1994) Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7-A resolution. Proc Natl Acad Sci U S A 91: 6423–6427.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 6423-6427
    • Zdanov, A.1    Li, Y.2    Bundle, D.R.3    Deng, S.J.4    MacKenzie, C.R.5
  • 79
    • 84884997937 scopus 로고    scopus 로고
    • Quantifying protein-ligand interactions by direct electrospray ionization-MS analysis: evidence of nonuniform response factors induced by high molecular weight molecules and complexes
    • Lin H, Kitova EN, Klassen JS, (2013) Quantifying protein-ligand interactions by direct electrospray ionization-MS analysis: evidence of nonuniform response factors induced by high molecular weight molecules and complexes. Anal Chem 85: 8919–8922.
    • (2013) Anal Chem , vol.85 , pp. 8919-8922
    • Lin, H.1    Kitova, E.N.2    Klassen, J.S.3
  • 80
    • 84861581271 scopus 로고    scopus 로고
    • Quantifying carbohydrate-protein interactions by electrospray ionization mass spectrometry analysis
    • El-Hawiet A, Kitova EN, Klassen JS, (2012) Quantifying carbohydrate-protein interactions by electrospray ionization mass spectrometry analysis. Biochemistry 51: 4244–4253.
    • (2012) Biochemistry , vol.51 , pp. 4244-4253
    • El-Hawiet, A.1    Kitova, E.N.2    Klassen, J.S.3
  • 81
    • 33646589615 scopus 로고    scopus 로고
    • Method for distinguishing specific from nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry
    • Sun J, Kitova EN, Wang W, Klassen JS, (2006) Method for distinguishing specific from nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry. Anal Chem 78: 3010–3018.
    • (2006) Anal Chem , vol.78 , pp. 3010-3018
    • Sun, J.1    Kitova, E.N.2    Wang, W.3    Klassen, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.