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Volumn 8, Issue 3, 2012, Pages

Multiple peptidoglycan modification networks modulate helicobacter pylori's cell shape, motility, and colonization potential

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDOGLYCAN; BACTERIAL PROTEIN;

EID: 84861220120     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002603     Document Type: Article
Times cited : (115)

References (58)
  • 1
    • 0035374653 scopus 로고    scopus 로고
    • Living dangerously: how Helicobacter pylori survives in the human stomach
    • Montecucco C, Rappuoli R, (2001) Living dangerously: how Helicobacter pylori survives in the human stomach. Nat Rev Mol Cell Biol 2: 457-466.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 457-466
    • Montecucco, C.1    Rappuoli, R.2
  • 3
    • 0022634633 scopus 로고
    • Campylobacter pyloridis and gastritis: association with intercellular spaces and adaptation to an environment of mucus as important factors in colonization of the gastric epithelium
    • Hazell SL, Lee A, Brady L, Hennessy W, (1986) Campylobacter pyloridis and gastritis: association with intercellular spaces and adaptation to an environment of mucus as important factors in colonization of the gastric epithelium. J Infect Dis 153: 658-663.
    • (1986) J Infect Dis , vol.153 , pp. 658-663
    • Hazell, S.L.1    Lee, A.2    Brady, L.3    Hennessy, W.4
  • 4
    • 20144367704 scopus 로고    scopus 로고
    • Rapid loss of motility of Helicobacter pylori in the gastric lumen in vivo
    • Schreiber S, Bucker R, Groll C, Azevedo-Vethacke M, Garten D, et al. (2005) Rapid loss of motility of Helicobacter pylori in the gastric lumen in vivo. Infect Immun 73: 1584-1589.
    • (2005) Infect Immun , vol.73 , pp. 1584-1589
    • Schreiber, S.1    Bucker, R.2    Groll, C.3    Azevedo-Vethacke, M.4    Garten, D.5
  • 5
    • 0030002653 scopus 로고    scopus 로고
    • Colonization of gnotobiotic piglets by Helicobacter pylori deficient in two flagellin genes
    • Eaton KA, Suerbaum S, Josenhans C, Krakowka S, (1996) Colonization of gnotobiotic piglets by Helicobacter pylori deficient in two flagellin genes. Infect Immun 64: 2445-2448.
    • (1996) Infect Immun , vol.64 , pp. 2445-2448
    • Eaton, K.A.1    Suerbaum, S.2    Josenhans, C.3    Krakowka, S.4
  • 7
    • 12844264798 scopus 로고    scopus 로고
    • Chemotaxis plays multiple roles during Helicobacter pylori animal infection
    • Terry K, Williams SM, Connolly L, Ottemann KM, (2005) Chemotaxis plays multiple roles during Helicobacter pylori animal infection. Infect Immun 73: 803-811.
    • (2005) Infect Immun , vol.73 , pp. 803-811
    • Terry, K.1    Williams, S.M.2    Connolly, L.3    Ottemann, K.M.4
  • 8
    • 80052567553 scopus 로고    scopus 로고
    • ChePep Controls Helicobacter pylori Infection of the Gastric Glands and Chemotaxis in the Epsilonproteobacteria
    • Howitt MR, Lee JY, Lertsethtakarn P, Vogelmann R, Joubert LM, et al. (2011) ChePep Controls Helicobacter pylori Infection of the Gastric Glands and Chemotaxis in the Epsilonproteobacteria. MBio 2: e00098-11.
    • (2011) MBio , vol.2
    • Howitt, M.R.1    Lee, J.Y.2    Lertsethtakarn, P.3    Vogelmann, R.4    Joubert, L.M.5
  • 9
    • 0018424447 scopus 로고
    • Movement of microorganisms in viscous environments
    • Berg HC, Turner L, (1979) Movement of microorganisms in viscous environments. Nature 278: 349-351.
    • (1979) Nature , vol.278 , pp. 349-351
    • Berg, H.C.1    Turner, L.2
  • 10
    • 0016856950 scopus 로고
    • Letter: Enhanced translational motion of Leptospira in viscous environments
    • Kaiser GE, Doetsch RN, (1975) Letter: Enhanced translational motion of Leptospira in viscous environments. Nature 255: 656-657.
    • (1975) Nature , vol.255 , pp. 656-657
    • Kaiser, G.E.1    Doetsch, R.N.2
  • 11
    • 0035996993 scopus 로고    scopus 로고
    • A mathematical explanation of an increase in bacterial swimming speed with viscosity in linear-polymer solutions
    • Magariyama Y, Kudo S, (2002) A mathematical explanation of an increase in bacterial swimming speed with viscosity in linear-polymer solutions. Biophys J 83: 733-739.
    • (2002) Biophys J , vol.83 , pp. 733-739
    • Magariyama, Y.1    Kudo, S.2
  • 12
    • 0023776341 scopus 로고
    • Motility of Campylobacter jejuni in a viscous environment: comparison with conventional rod-shaped bacteria
    • Ferrero RL, Lee A, (1988) Motility of Campylobacter jejuni in a viscous environment: comparison with conventional rod-shaped bacteria. J Gen Microbiol 134: 53-59.
    • (1988) J Gen Microbiol , vol.134 , pp. 53-59
    • Ferrero, R.L.1    Lee, A.2
  • 13
    • 77953265009 scopus 로고    scopus 로고
    • Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization
    • Sycuro LK, Pincus Z, Gutierrez KD, Biboy J, Stern CA, et al. (2010) Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization. Cell 141: 822-833.
    • (2010) Cell , vol.141 , pp. 822-833
    • Sycuro, L.K.1    Pincus, Z.2    Gutierrez, K.D.3    Biboy, J.4    Stern, C.A.5
  • 15
    • 57749083521 scopus 로고    scopus 로고
    • Molecular organization of Gram-negative peptidoglycan
    • Gan L, Chen S, Jensen GJ, (2008) Molecular organization of Gram-negative peptidoglycan. Proc Natl Acad Sci U S A 105: 18953-18957.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 18953-18957
    • Gan, L.1    Chen, S.2    Jensen, G.J.3
  • 16
    • 50049104157 scopus 로고    scopus 로고
    • Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
    • Vollmer W, Bertsche U, (2008) Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli. Biochim Biophys Acta 1778: 1714-1734.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1714-1734
    • Vollmer, W.1    Bertsche, U.2
  • 17
    • 0032864204 scopus 로고    scopus 로고
    • Identification of a novel penicillin-binding protein from Helicobacter pylori
    • Krishnamurthy P, Parlow MH, Schneider J, Burroughs S, Wickland C, et al. (1999) Identification of a novel penicillin-binding protein from Helicobacter pylori. J Bacteriol 181: 5107-5110.
    • (1999) J Bacteriol , vol.181 , pp. 5107-5110
    • Krishnamurthy, P.1    Parlow, M.H.2    Schneider, J.3    Burroughs, S.4    Wickland, C.5
  • 18
    • 0032981371 scopus 로고    scopus 로고
    • The morphological transition of Helicobacter pylori cells from spiral to coccoid is preceded by a substantial modification of the cell wall
    • Costa K, Bacher G, Allmaier G, Dominguez-Bello MG, Engstrand L, et al. (1999) The morphological transition of Helicobacter pylori cells from spiral to coccoid is preceded by a substantial modification of the cell wall. J Bacteriol 181: 3710-3715.
    • (1999) J Bacteriol , vol.181 , pp. 3710-3715
    • Costa, K.1    Bacher, G.2    Allmaier, G.3    Dominguez-Bello, M.G.4    Engstrand, L.5
  • 19
    • 0038824980 scopus 로고    scopus 로고
    • An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid
    • Chamaillard M, Hashimoto M, Horie Y, Masumoto J, Qiu S, et al. (2003) An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid. Nat Immunol 4: 702-707.
    • (2003) Nat Immunol , vol.4 , pp. 702-707
    • Chamaillard, M.1    Hashimoto, M.2    Horie, Y.3    Masumoto, J.4    Qiu, S.5
  • 20
    • 33749527914 scopus 로고    scopus 로고
    • Role of AmiA in the morphological transition of Helicobacter pylori and in immune escape
    • Chaput C, Ecobichon C, Cayet N, Girardin SE, Werts C, et al. (2006) Role of AmiA in the morphological transition of Helicobacter pylori and in immune escape. PLoS Pathog 2: e97.
    • (2006) PLoS Pathog , vol.2
    • Chaput, C.1    Ecobichon, C.2    Cayet, N.3    Girardin, S.E.4    Werts, C.5
  • 21
    • 0038615855 scopus 로고    scopus 로고
    • Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan
    • Girardin SE, Boneca IG, Carneiro LA, Antignac A, Jehanno M, et al. (2003) Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan. Science 300: 1584-1587.
    • (2003) Science , vol.300 , pp. 1584-1587
    • Girardin, S.E.1    Boneca, I.G.2    Carneiro, L.A.3    Antignac, A.4    Jehanno, M.5
  • 22
    • 78349259363 scopus 로고    scopus 로고
    • A M23B family metallopeptidase of Helicobacter pylori required for cell shape, pole formation and virulence
    • Bonis M, Ecobichon C, Guadagnini S, Prevost MC, Boneca IG, (2010) A M23B family metallopeptidase of Helicobacter pylori required for cell shape, pole formation and virulence. Mol Microbiol 78: 809-819.
    • (2010) Mol Microbiol , vol.78 , pp. 809-819
    • Bonis, M.1    Ecobichon, C.2    Guadagnini, S.3    Prevost, M.C.4    Boneca, I.G.5
  • 23
    • 84861214451 scopus 로고    scopus 로고
    • Peptidoglycan-modifying enzyme Pgp1 is required for helical cell shape and pathogenicity traits in Campylobacter jejuni
    • doi: 10.1371/journal.ppat.1002602
    • Frirdich E, Biboy J, Adams C, Lee J, Ellermeier J, et al. (2012) Peptidoglycan-modifying enzyme Pgp1 is required for helical cell shape and pathogenicity traits in Campylobacter jejuni. PloS Pathog doi:10.1371/journal.ppat.1002602.
    • (2012) PloS Pathog
    • Frirdich, E.1    Biboy, J.2    Adams, C.3    Lee, J.4    Ellermeier, J.5
  • 24
    • 34247559789 scopus 로고    scopus 로고
    • Peptide transport in Helicobacter pylori: roles of dpp and opp systems and evidence for additional peptide transporters
    • Weinberg MV, Maier RJ, (2007) Peptide transport in Helicobacter pylori: roles of dpp and opp systems and evidence for additional peptide transporters. J Bacteriol 189: 3392-3402.
    • (2007) J Bacteriol , vol.189 , pp. 3392-3402
    • Weinberg, M.V.1    Maier, R.J.2
  • 25
    • 0033543723 scopus 로고    scopus 로고
    • The Zn-peptidase superfamily: functional convergence after evolutionary divergence
    • Makarova KS, Grishin NV, (1999) The Zn-peptidase superfamily: functional convergence after evolutionary divergence. J Mol Biol 292: 11-17.
    • (1999) J Mol Biol , vol.292 , pp. 11-17
    • Makarova, K.S.1    Grishin, N.V.2
  • 26
    • 0021837555 scopus 로고
    • Purification and partial characterization of the extracellular gamma-D-glutamyl-(L)meso-diaminopimelate endopeptidase I, from Bacillus sphaericus NCTC 9602
    • Garnier M, Vacheron MJ, Guinand M, Michel G, (1985) Purification and partial characterization of the extracellular gamma-D-glutamyl-(L)meso-diaminopimelate endopeptidase I, from Bacillus sphaericus NCTC 9602. Eur J Biochem 148: 539-543.
    • (1985) Eur J Biochem , vol.148 , pp. 539-543
    • Garnier, M.1    Vacheron, M.J.2    Guinand, M.3    Michel, G.4
  • 27
    • 0027271928 scopus 로고
    • Characterization of the sporulation-related gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular design of the protein
    • Hourdou ML, Guinand M, Vacheron MJ, Michel G, Denoroy L, et al. (1993) Characterization of the sporulation-related gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular design of the protein. Biochem J 292 (Pt 2): 563-570.
    • (1993) Biochem J , vol.292 , Issue.Pt 2 , pp. 563-570
    • Hourdou, M.L.1    Guinand, M.2    Vacheron, M.J.3    Michel, G.4    Denoroy, L.5
  • 28
    • 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
  • 29
    • 1842557330 scopus 로고    scopus 로고
    • Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity
    • Reverter D, Maskos K, Tan F, Skidgel RA, Bode W, (2004) Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity. J Mol Biol 338: 257-269.
    • (2004) J Mol Biol , vol.338 , pp. 257-269
    • Reverter, D.1    Maskos, K.2    Tan, F.3    Skidgel, R.A.4    Bode, W.5
  • 30
    • 0031001363 scopus 로고    scopus 로고
    • Introduction of unmarked mutations in the Helicobacter pylori vacA gene with a sucrose sensitivity marker
    • Copass M, Grandi G, Rappuoli R, (1997) Introduction of unmarked mutations in the Helicobacter pylori vacA gene with a sucrose sensitivity marker. Infect Immun 65: 1949-1952.
    • (1997) Infect Immun , vol.65 , pp. 1949-1952
    • Copass, M.1    Grandi, G.2    Rappuoli, R.3
  • 31
    • 0026749753 scopus 로고
    • SH3-an abundant protein domain in search of a function
    • Musacchio A, Gibson T, Lehto VP, Saraste M, (1992) SH3-an abundant protein domain in search of a function. FEBS Lett 307: 55-61.
    • (1992) FEBS Lett , vol.307 , pp. 55-61
    • Musacchio, A.1    Gibson, T.2    Lehto, V.P.3    Saraste, M.4
  • 32
    • 0033057517 scopus 로고    scopus 로고
    • Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer
    • Ponting CP, Aravind L, Schultz J, Bork P, Koonin EV, (1999) Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer. J Mol Biol 289: 729-745.
    • (1999) J Mol Biol , vol.289 , pp. 729-745
    • Ponting, C.P.1    Aravind, L.2    Schultz, J.3    Bork, P.4    Koonin, E.V.5
  • 34
    • 77950621399 scopus 로고    scopus 로고
    • Bacterial membrane vesicles deliver peptidoglycan to NOD1 in epithelial cells
    • Kaparakis M, Turnbull L, Carneiro L, Firth S, Coleman HA, et al. (2010) Bacterial membrane vesicles deliver peptidoglycan to NOD1 in epithelial cells. Cell Microbiol 12: 372-385.
    • (2010) Cell Microbiol , vol.12 , pp. 372-385
    • Kaparakis, M.1    Turnbull, L.2    Carneiro, L.3    Firth, S.4    Coleman, H.A.5
  • 35
    • 9244245293 scopus 로고    scopus 로고
    • Nod1 responds to peptidoglycan delivered by the Helicobacter pylori cag pathogenicity island
    • Viala J, Chaput C, Boneca IG, Cardona A, Girardin SE, et al. (2004) Nod1 responds to peptidoglycan delivered by the Helicobacter pylori cag pathogenicity island. Nat Immunol 5: 1166-1174.
    • (2004) Nat Immunol , vol.5 , pp. 1166-1174
    • Viala, J.1    Chaput, C.2    Boneca, I.G.3    Cardona, A.4    Girardin, S.E.5
  • 36
    • 28544434876 scopus 로고    scopus 로고
    • Murine Nod1 but not its human orthologue mediates innate immune detection of tracheal cytotoxin
    • Magalhaes JG, Philpott DJ, Nahori MA, Jehanno M, Fritz J, et al. (2005) Murine Nod1 but not its human orthologue mediates innate immune detection of tracheal cytotoxin. EMBO Rep 6: 1201-1207.
    • (2005) EMBO Rep , vol.6 , pp. 1201-1207
    • Magalhaes, J.G.1    Philpott, D.J.2    Nahori, M.A.3    Jehanno, M.4    Fritz, J.5
  • 37
    • 33846849047 scopus 로고    scopus 로고
    • Identification of Helicobacter pylori genes that contribute to stomach colonization
    • Baldwin DN, Shepherd B, Kraemer P, Hall MK, Sycuro LK, et al. (2007) Identification of Helicobacter pylori genes that contribute to stomach colonization. Infect Immun 75: 1005-1016.
    • (2007) Infect Immun , vol.75 , pp. 1005-1016
    • Baldwin, D.N.1    Shepherd, B.2    Kraemer, P.3    Hall, M.K.4    Sycuro, L.K.5
  • 38
    • 72249106415 scopus 로고    scopus 로고
    • Cag3 is a novel essential component of the Helicobacter pylori Cag type IV secretion system outer membrane subcomplex
    • Pinto-Santini DM, Salama NR, (2009) Cag3 is a novel essential component of the Helicobacter pylori Cag type IV secretion system outer membrane subcomplex. J Bacteriol 191: 7343-7352.
    • (2009) J Bacteriol , vol.191 , pp. 7343-7352
    • Pinto-Santini, D.M.1    Salama, N.R.2
  • 40
    • 0036262344 scopus 로고    scopus 로고
    • Reduced activation of inflammatory responses in host cells by mouse-adapted Helicobacter pylori isolates
    • Philpott DJ, Belaid D, Troubadour P, Thiberge JM, Tankovic J, et al. (2002) Reduced activation of inflammatory responses in host cells by mouse-adapted Helicobacter pylori isolates. Cell Microbiol 4: 285-296.
    • (2002) Cell Microbiol , vol.4 , pp. 285-296
    • Philpott, D.J.1    Belaid, D.2    Troubadour, P.3    Thiberge, J.M.4    Tankovic, J.5
  • 41
    • 67449126811 scopus 로고    scopus 로고
    • The CD4+ T cell-mediated IFN-gamma response to Helicobacter infection is essential for clearance and determines gastric cancer risk
    • Sayi A, Kohler E, Hitzler I, Arnold I, Schwendener R, et al. (2009) The CD4+ T cell-mediated IFN-gamma response to Helicobacter infection is essential for clearance and determines gastric cancer risk. J Immunol 182: 7085-7101.
    • (2009) J Immunol , vol.182 , pp. 7085-7101
    • Sayi, A.1    Kohler, E.2    Hitzler, I.3    Arnold, I.4    Schwendener, R.5
  • 42
    • 0026680505 scopus 로고
    • Motility as a factor in the colonisation of gnotobiotic piglets by Helicobacter pylori
    • Eaton KA, Morgan DR, Krakowka S, (1992) Motility as a factor in the colonisation of gnotobiotic piglets by Helicobacter pylori. J Med Microbiol 37: 123-127.
    • (1992) J Med Microbiol , vol.37 , pp. 123-127
    • Eaton, K.A.1    Morgan, D.R.2    Krakowka, S.3
  • 43
    • 73649117859 scopus 로고    scopus 로고
    • A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori
    • Waidner B, Specht M, Dempwolff F, Haeberer K, Schaetzle S, et al. (2009) A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori. PLoS Pathog 5: e1000669.
    • (2009) PLoS Pathog , vol.5
    • Waidner, B.1    Specht, M.2    Dempwolff, F.3    Haeberer, K.4    Schaetzle, S.5
  • 45
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Höltje JV, (1998) Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol Mol Biol Rev 62: 181-203.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 181-203
    • Höltje, J.V.1
  • 46
    • 65649100437 scopus 로고    scopus 로고
    • Bacterial cell curvature through mechanical control of cell growth
    • Cabeen MT, Charbon G, Vollmer W, Born P, Ausmees N, et al. (2009) Bacterial cell curvature through mechanical control of cell growth. Embo J 28: 1208-1219.
    • (2009) Embo J , vol.28 , pp. 1208-1219
    • Cabeen, M.T.1    Charbon, G.2    Vollmer, W.3    Born, P.4    Ausmees, N.5
  • 48
    • 78650497005 scopus 로고    scopus 로고
    • Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases
    • Paradis-Bleau C, Markovski M, Uehara T, Lupoli TJ, Walker S, et al. (2010) Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell 143: 1110-1120.
    • (2010) Cell , vol.143 , pp. 1110-1120
    • Paradis-Bleau, C.1    Markovski, M.2    Uehara, T.3    Lupoli, T.J.4    Walker, S.5
  • 49
    • 0032915889 scopus 로고    scopus 로고
    • A novel membrane protein influencing cell shape and multicellular swarming of Proteus mirabilis
    • Hay NA, Tipper DJ, Gygi D, Hughes C, (1999) A novel membrane protein influencing cell shape and multicellular swarming of Proteus mirabilis. J Bacteriol 181: 2008-2016.
    • (1999) J Bacteriol , vol.181 , pp. 2008-2016
    • Hay, N.A.1    Tipper, D.J.2    Gygi, D.3    Hughes, C.4
  • 50
    • 79955717294 scopus 로고    scopus 로고
    • BacM, an N-terminally processed bactofilin of Myxococcus xanthus, is crucial for proper cell shape
    • Koch MK, McHugh CA, Hoiczyk E, (2011) BacM, an N-terminally processed bactofilin of Myxococcus xanthus, is crucial for proper cell shape. Mol Microbiol 80: 1031-51.
    • (2011) Mol Microbiol , vol.80 , pp. 1031-1051
    • Koch, M.K.1    McHugh, C.A.2    Hoiczyk, E.3
  • 51
    • 75049083437 scopus 로고    scopus 로고
    • Bactofilins, a ubiquitous class of cytoskeletal proteins mediating polar localization of a cell wall synthase in Caulobacter crescentus
    • Kuhn J, Briegel A, Morschel E, Kahnt J, Leser K, et al. (2011) Bactofilins, a ubiquitous class of cytoskeletal proteins mediating polar localization of a cell wall synthase in Caulobacter crescentus. EMBO J 29: 327-339.
    • (2011) EMBO J , vol.29 , pp. 327-339
    • Kuhn, J.1    Briegel, A.2    Morschel, E.3    Kahnt, J.4    Leser, K.5
  • 52
    • 38549141229 scopus 로고    scopus 로고
    • Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre
    • Bennett-Lovsey RM, Herbert AD, Sternberg MJ, Kelley LA, (2008) Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre. Proteins 70: 611-625.
    • (2008) Proteins , vol.70 , pp. 611-625
    • Bennett-Lovsey, R.M.1    Herbert, A.D.2    Sternberg, M.J.3    Kelley, L.A.4
  • 53
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: progress and challenges
    • DeLano WL, (2002) Unraveling hot spots in binding interfaces: progress and challenges. Curr Opin Struct Biol 12: 14-20.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 14-20
    • DeLano, W.L.1
  • 54
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high-performance liquid chromatography
    • Glauner B, (1988) Separation and quantification of muropeptides with high-performance liquid chromatography. Anal Biochem 172: 451-464.
    • (1988) Anal Biochem , vol.172 , pp. 451-464
    • Glauner, B.1
  • 55
    • 0023677844 scopus 로고
    • The composition of the murein of Escherichia coli
    • Glauner B, Holtje JV, Schwarz U, (1988) The composition of the murein of Escherichia coli. J Biol Chem 263: 10088-10095.
    • (1988) J Biol Chem , vol.263 , pp. 10088-10095
    • Glauner, B.1    Holtje, J.V.2    Schwarz, U.3
  • 56
    • 72249108588 scopus 로고    scopus 로고
    • Functional Analysis of the Helicobacter pylori Flagellar Switch Proteins
    • Lowenthal AC, Hill M, Sycuro LK, Mehmood K, Salama NR, et al. (2009) Functional Analysis of the Helicobacter pylori Flagellar Switch Proteins. J Bacteriol 191: 7147-7156.
    • (2009) J Bacteriol , vol.191 , pp. 7147-7156
    • Lowenthal, A.C.1    Hill, M.2    Sycuro, L.K.3    Mehmood, K.4    Salama, N.R.5
  • 57
    • 47749093168 scopus 로고    scopus 로고
    • Helicobacter pylori AddAB helicase-nuclease and RecA promote recombination-related DNA repair and survival during stomach colonization
    • Amundsen SK, Fero J, Hansen LM, Cromie GA, Solnick JV, et al. (2008) Helicobacter pylori AddAB helicase-nuclease and RecA promote recombination-related DNA repair and survival during stomach colonization. Mol Microbiol 69: 994-1007.
    • (2008) Mol Microbiol , vol.69 , pp. 994-1007
    • Amundsen, S.K.1    Fero, J.2    Hansen, L.M.3    Cromie, G.A.4    Solnick, J.V.5
  • 58
    • 34248336147 scopus 로고    scopus 로고
    • Genetic analysis of Helicobacter pylori strain populations colonizing the stomach at different times postinfection
    • Salama NR, Gonzalez-Valencia G, Deatherage B, Aviles-Jimenez F, Atherton JC, et al. (2007) Genetic analysis of Helicobacter pylori strain populations colonizing the stomach at different times postinfection. J Bacteriol 189: 3834-3845.
    • (2007) J Bacteriol , vol.189 , pp. 3834-3845
    • Salama, N.R.1    Gonzalez-Valencia, G.2    Deatherage, B.3    Aviles-Jimenez, F.4    Atherton, J.C.5


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