메뉴 건너뛰기




Volumn 6, Issue 11, 2011, Pages

Identification and localization of Myxococcus xanthus porins and lipoproteins

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BACTERIAL PROTEIN; BETA BARREL PROTEIN; CELL PROTEIN; CYSTEINE; LIPOPROTEIN; MEMBRANE PROTEIN; OAR PROTEIN; OUTER MEMBRANE PROTEIN; PORIN; PROTEIN FIBA; PROTEOME; UNCLASSIFIED DRUG; SCLEROPROTEIN; SIGNAL PEPTIDE;

EID: 81555212296     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0027475     Document Type: Article
Times cited : (24)

References (58)
  • 1
    • 0032717993 scopus 로고    scopus 로고
    • Intercellular signaling during fruiting body development of Myxococcus xanthus
    • Shimkets LJ, Gill RE, Kaiser D, (1999) Intercellular signaling during fruiting body development of Myxococcus xanthus. Annu Rev Microbiol 53: 525-549.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 525-549
    • Shimkets, L.J.1    Gill, R.E.2    Kaiser, D.3
  • 2
    • 0041428149 scopus 로고    scopus 로고
    • The versatile beta-barrel membrane protein
    • Wimley WC, (2003) The versatile beta-barrel membrane protein. Curr Opin Struct Biol 13: 404-411.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 3
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H, (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67: 593-656.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 4
    • 34347369410 scopus 로고    scopus 로고
    • TonB system, in vivo assays and characterization
    • Postle K, (2007) TonB system, in vivo assays and characterization. Methods Enzymol 422: 245-269.
    • (2007) Methods Enzymol , vol.422 , pp. 245-269
    • Postle, K.1
  • 5
    • 23044513554 scopus 로고    scopus 로고
    • The FadL family: unusual transporters for unusual substrates
    • van den Berg B, (2005) The FadL family: unusual transporters for unusual substrates. Curr Opin Struct Biol 15: 401-407.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 401-407
    • van den Berg, B.1
  • 6
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the gram-negative bacterial outer membrane
    • Bos MP, Robert V, Tommassen J, (2007) Biogenesis of the gram-negative bacterial outer membrane. Annu Rev Microbiol 61: 191-214.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 7
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux R, Bos MP, Geurtsen J, Mols M, Tommassen J, (2003) Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299: 262-265.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 9
    • 77957351822 scopus 로고    scopus 로고
    • Profiling the outer membrane proteome during growth and development of the social bacterium Myxococcus xanthus by selective biotinylation and analyses of outer membrane vesicles
    • Kahnt J, Aguiluz K, Koch J, Treuner-Lange A, Konovalova A, et al. (2010) Profiling the outer membrane proteome during growth and development of the social bacterium Myxococcus xanthus by selective biotinylation and analyses of outer membrane vesicles. J Proteome Res 9: 5197-5208.
    • (2010) J Proteome Res , vol.9 , pp. 5197-5208
    • Kahnt, J.1    Aguiluz, K.2    Koch, J.3    Treuner-Lange, A.4    Konovalova, A.5
  • 11
    • 58149295961 scopus 로고    scopus 로고
    • Lipoprotein biogenesis in Gram-positive bacteria: knowing when to hold 'em, knowing when to fold 'em
    • Hutchings MI, Palmer T, Harrington DJ, Sutcliffe IC, (2009) Lipoprotein biogenesis in Gram-positive bacteria: knowing when to hold 'em, knowing when to fold 'em. Trends Microbiol 17: 13-21.
    • (2009) Trends Microbiol , vol.17 , pp. 13-21
    • Hutchings, M.I.1    Palmer, T.2    Harrington, D.J.3    Sutcliffe, I.C.4
  • 12
    • 0032701349 scopus 로고    scopus 로고
    • Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection
    • Seydel A, Gounon P, Pugsley AP, (1999) Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection. Mol Microbiol 34: 810-821.
    • (1999) Mol Microbiol , vol.34 , pp. 810-821
    • Seydel, A.1    Gounon, P.2    Pugsley, A.P.3
  • 13
    • 0037188471 scopus 로고    scopus 로고
    • Elucidation of the function of lipoprotein-sorting signals that determine membrane localization
    • Masuda K, Matsuyama S, Tokuda H, (2002) Elucidation of the function of lipoprotein-sorting signals that determine membrane localization. Proc Natl Acad Sci U S A 99: 7390-7395.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 7390-7395
    • Masuda, K.1    Matsuyama, S.2    Tokuda, H.3
  • 14
    • 34250353151 scopus 로고    scopus 로고
    • Characterization of the Pseudomonas aeruginosa Lol system as a lipoprotein sorting mechanism
    • Tanaka SY, Narita S, Tokuda H, (2007) Characterization of the Pseudomonas aeruginosa Lol system as a lipoprotein sorting mechanism. J Biol Chem 282.
    • (2007) J Biol Chem , vol.282
    • Tanaka, S.Y.1    Narita, S.2    Tokuda, H.3
  • 15
    • 3242743729 scopus 로고    scopus 로고
    • Sorting of lipoproteins to the outer membrane in E. coli
    • Tokuda H, Matsuyama S, (2004) Sorting of lipoproteins to the outer membrane in E. coli. Biochim Biophys Acta 1693: 5-13.
    • (2004) Biochim Biophys Acta , vol.1693 , pp. 5-13
    • Tokuda, H.1    Matsuyama, S.2
  • 16
    • 35649022212 scopus 로고    scopus 로고
    • Proteins associated with the Myxococcus xanthus extracellular matrix
    • Curtis PD, Atwood J 3rd, Orlando R, Shimkets LJ, (2007) Proteins associated with the Myxococcus xanthus extracellular matrix. J Bacteriol 189: 7634-7642.
    • (2007) J Bacteriol , vol.189 , pp. 7634-7642
    • Curtis, P.D.1    Atwood III, J.2    Orlando, R.3    Shimkets, L.J.4
  • 18
    • 0025280947 scopus 로고
    • Complete sequence of the ompH gene encoding the 16-kDa cationic outer membrane protein of Salmonella typhimurium
    • Koski P, Hirvas L, Vaara M, (1990) Complete sequence of the ompH gene encoding the 16-kDa cationic outer membrane protein of Salmonella typhimurium. Gene 88: 117-120.
    • (1990) Gene , vol.88 , pp. 117-120
    • Koski, P.1    Hirvas, L.2    Vaara, M.3
  • 19
    • 0027233420 scopus 로고
    • The MIP family of integral membrane channel proteins: sequence comparisons, evolutionary relationships, reconstructed pathway of evolution, and proposed functional differentiation of the two repeated halves of the proteins
    • Reizer J, Reizer A, Saier MH Jr, (1993) The MIP family of integral membrane channel proteins: sequence comparisons, evolutionary relationships, reconstructed pathway of evolution, and proposed functional differentiation of the two repeated halves of the proteins. Crit Rev Biochem Mol Biol 28: 235-257.
    • (1993) Crit Rev Biochem Mol Biol , vol.28 , pp. 235-257
    • Reizer, J.1    Reizer, A.2    Saier Jr., M.H.3
  • 20
    • 0033515434 scopus 로고    scopus 로고
    • Alignment and structure prediction of divergent protein families: periplasmic and outer membrane proteins of bacterial efflux pumps
    • Johnson JM, Church GM, (1999) Alignment and structure prediction of divergent protein families: periplasmic and outer membrane proteins of bacterial efflux pumps. J Mol Biol 287: 695-715.
    • (1999) J Mol Biol , vol.287 , pp. 695-715
    • Johnson, J.M.1    Church, G.M.2
  • 21
    • 36749048640 scopus 로고    scopus 로고
    • Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain
    • Bos MP, Robert V, Tommassen J, (2007) Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain. EMBO Rep 8: 1149-1154.
    • (2007) EMBO Rep , vol.8 , pp. 1149-1154
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 23
    • 0042890478 scopus 로고    scopus 로고
    • Membrane localization of motility, signaling, and polyketide synthetase proteins in Myxococcus xanthus
    • Simunovic V, Gherardini FC, Shimkets LJ, (2003) Membrane localization of motility, signaling, and polyketide synthetase proteins in Myxococcus xanthus. J Bacteriol 185: 5066-5075.
    • (2003) J Bacteriol , vol.185 , pp. 5066-5075
    • Simunovic, V.1    Gherardini, F.C.2    Shimkets, L.J.3
  • 25
    • 0020534656 scopus 로고
    • Developmental cell interactions in Myxococcus xanthus and the spoC locus
    • Shimkets LJ, Gill RE, Kaiser D, (1983) Developmental cell interactions in Myxococcus xanthus and the spoC locus. Proc Natl Acad Sci U S A 80: 1406-1410.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 1406-1410
    • Shimkets, L.J.1    Gill, R.E.2    Kaiser, D.3
  • 26
    • 0017979559 scopus 로고
    • Synergism between morphogenetic mutants of Myxococcus xanthus
    • Hagen DC, Bretscher AP, Kaiser D, (1978) Synergism between morphogenetic mutants of Myxococcus xanthus. Dev Biol 64: 284-296.
    • (1978) Dev Biol , vol.64 , pp. 284-296
    • Hagen, D.C.1    Bretscher, A.P.2    Kaiser, D.3
  • 27
    • 0029013781 scopus 로고
    • The esg locus of Myxococcus xanthus encodes the E1 alpha and E1 beta subunits of a branched-chain keto acid dehydrogenase
    • Toal DR, Clifton SW, Roe BA, Downard J, (1995) The esg locus of Myxococcus xanthus encodes the E1 alpha and E1 beta subunits of a branched-chain keto acid dehydrogenase. Mol Microbiol 16: 177-189.
    • (1995) Mol Microbiol , vol.16 , pp. 177-189
    • Toal, D.R.1    Clifton, S.W.2    Roe, B.A.3    Downard, J.4
  • 28
    • 0020434711 scopus 로고
    • Induction of coordinated movement of Myxococcus xanthus cells
    • Shimkets LJ, Kaiser D, (1982) Induction of coordinated movement of Myxococcus xanthus cells. J Bacteriol 152: 451-461.
    • (1982) J Bacteriol , vol.152 , pp. 451-461
    • Shimkets, L.J.1    Kaiser, D.2
  • 31
    • 79960193537 scopus 로고    scopus 로고
    • Heterologous protein transfer within structured myxobacteria biofilms
    • Wei X, Pathak DT, Wall D, (2011) Heterologous protein transfer within structured myxobacteria biofilms. Mol Microbiol 81: 315-326.
    • (2011) Mol Microbiol , vol.81 , pp. 315-326
    • Wei, X.1    Pathak, D.T.2    Wall, D.3
  • 32
    • 0019939637 scopus 로고
    • Fruiting body morphogenesis in submerged cultures of Myxococcus xanthus
    • Kuner JM, Kaiser D, (1982) Fruiting body morphogenesis in submerged cultures of Myxococcus xanthus. J Bacteriol 151: 458-461.
    • (1982) J Bacteriol , vol.151 , pp. 458-461
    • Kuner, J.M.1    Kaiser, D.2
  • 33
    • 34447339675 scopus 로고    scopus 로고
    • Mechanics of force propagation in TonB-dependent outer membrane transport
    • Gumbart J, Wiener MC, Tajkhorshid E, (2007) Mechanics of force propagation in TonB-dependent outer membrane transport. Biophys J 93: 496-504.
    • (2007) Biophys J , vol.93 , pp. 496-504
    • Gumbart, J.1    Wiener, M.C.2    Tajkhorshid, E.3
  • 34
    • 0030943591 scopus 로고    scopus 로고
    • TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli
    • Letain TE, Postle K, (1997) TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli. Mol Microbiol 24: 271-283.
    • (1997) Mol Microbiol , vol.24 , pp. 271-283
    • Letain, T.E.1    Postle, K.2
  • 35
    • 0025163861 scopus 로고
    • Cell alignment required in differentiation of Myxococcus xanthus
    • Kim SK, Kaiser D, (1990a) Cell alignment required in differentiation of Myxococcus xanthus. Science 249: 926-928.
    • (1990) Science , vol.249 , pp. 926-928
    • Kim, S.K.1    Kaiser, D.2
  • 36
    • 0025362665 scopus 로고
    • Cell motility is required for the transmission of C-factor, an intercellular signal that coordinates fruiting body morphogenesis of Myxococcus xanthus
    • Kim SK, Kaiser D, (1990b) Cell motility is required for the transmission of C-factor, an intercellular signal that coordinates fruiting body morphogenesis of Myxococcus xanthus. Genes Dev 4: 896-904.
    • (1990) Genes Dev , vol.4 , pp. 896-904
    • Kim, S.K.1    Kaiser, D.2
  • 37
    • 0035047789 scopus 로고    scopus 로고
    • C-signal: a cell surface-associated morphogen that induces and co-ordinates multicellular fruiting body morphogenesis and sporulation in Myxococcus xanthus
    • Kruse T, Lobedanz S, Berthelsen NM, Sogaard-Andersen L, (2001) C-signal: a cell surface-associated morphogen that induces and co-ordinates multicellular fruiting body morphogenesis and sporulation in Myxococcus xanthus. Mol Microbiol 40: 156-168.
    • (2001) Mol Microbiol , vol.40 , pp. 156-168
    • Kruse, T.1    Lobedanz, S.2    Berthelsen, N.M.3    Sogaard-Andersen, L.4
  • 38
    • 33845455856 scopus 로고    scopus 로고
    • Lysophosphatidylethanolamine is a substrate for the short-chain alcohol dehydrogenase SocA from Myxococcus xanthus
    • Avadhani M, Geyer R, White DC, Shimkets LJ, (2006) Lysophosphatidylethanolamine is a substrate for the short-chain alcohol dehydrogenase SocA from Myxococcus xanthus. J Bacteriol 188: 8543-8550.
    • (2006) J Bacteriol , vol.188 , pp. 8543-8550
    • Avadhani, M.1    Geyer, R.2    White, D.C.3    Shimkets, L.J.4
  • 39
    • 0036188944 scopus 로고    scopus 로고
    • An extracellular matrix-associated zinc metalloprotease is required for dilauroyl phosphatidylethanolamine chemotactic excitation in Myxococcus xanthus
    • Kearns DB, Bonner PJ, Smith DR, Shimkets LJ, (2002) An extracellular matrix-associated zinc metalloprotease is required for dilauroyl phosphatidylethanolamine chemotactic excitation in Myxococcus xanthus. J Bacteriol 184: 1678-1684.
    • (2002) J Bacteriol , vol.184 , pp. 1678-1684
    • Kearns, D.B.1    Bonner, P.J.2    Smith, D.R.3    Shimkets, L.J.4
  • 40
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley AP, (1993) The complete general secretory pathway in gram-negative bacteria. Microbiol Rev 57: 50-108.
    • (1993) Microbiol Rev , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 41
    • 0027249655 scopus 로고
    • The role of the lipoprotein sorting signal (aspartate +2) in pullulanase secretion
    • Poquet I, Kornacker MG, Pugsley AP, (1993) The role of the lipoprotein sorting signal (aspartate +2) in pullulanase secretion. Mol Microbiol 9: 1061-1069.
    • (1993) Mol Microbiol , vol.9 , pp. 1061-1069
    • Poquet, I.1    Kornacker, M.G.2    Pugsley, A.P.3
  • 42
    • 3242879514 scopus 로고    scopus 로고
    • BOMP: a program to predict integral beta-barrel outer membrane proteins encoded within genomes of Gram-negative bacteria
    • Berven FS, Flikka K, Jensen HB, Eidhammer I, (2004) BOMP: a program to predict integral beta-barrel outer membrane proteins encoded within genomes of Gram-negative bacteria. Nucleic Acids Res 32: W394-399.
    • (2004) Nucleic Acids Res , vol.32
    • Berven, F.S.1    Flikka, K.2    Jensen, H.B.3    Eidhammer, I.4
  • 43
    • 23144440152 scopus 로고    scopus 로고
    • TMB-Hunt: a web server to screen sequence sets for transmembrane beta-barrel proteins
    • Garrow AG, Agnew A, Westhead DR, (2005) TMB-Hunt: a web server to screen sequence sets for transmembrane beta-barrel proteins. Nucleic Acids Res 33: W188-192.
    • (2005) Nucleic Acids Res , vol.33
    • Garrow, A.G.1    Agnew, A.2    Westhead, D.R.3
  • 44
    • 23144463913 scopus 로고    scopus 로고
    • TMBETA-NET: discrimination and prediction of membrane spanning beta-strands in outer membrane protein
    • Gromiha MM, Ahmad S, Suwa M, (2005) TMBETA-NET: discrimination and prediction of membrane spanning beta-strands in outer membrane protein. Nucleic Acids Res 33: W164-167.
    • (2005) Nucleic Acids Res , vol.33
    • Gromiha, M.M.1    Ahmad, S.2    Suwa, M.3
  • 45
    • 43249097732 scopus 로고    scopus 로고
    • TMBETADISC-RBF: Discrimination of beta-barrel membrane proteins using RBF networks and PSSM profiles
    • Ou YY, Gromiha MM, Chen SA, Suwa M, (2008) TMBETADISC-RBF: Discrimination of beta-barrel membrane proteins using RBF networks and PSSM profiles. Comput Biol Chem 32: 227-231.
    • (2008) Comput Biol Chem , vol.32 , pp. 227-231
    • Ou, Y.Y.1    Gromiha, M.M.2    Chen, S.A.3    Suwa, M.4
  • 47
    • 28444448722 scopus 로고    scopus 로고
    • Discrimination of outer membrane proteins using support vector machines
    • Park KJ, Gromiha MM, Horton P, Suwa M, (2005) Discrimination of outer membrane proteins using support vector machines. Bioinformatics 21: 4223-4229.
    • (2005) Bioinformatics , vol.21 , pp. 4223-4229
    • Park, K.J.1    Gromiha, M.M.2    Horton, P.3    Suwa, M.4
  • 48
    • 0042890478 scopus 로고    scopus 로고
    • Membrane localization of motility, signaling, and polyketide synthetase proteins in Myxococcus xanthus
    • Simunovic V, Gherardini FC, Shimkets LJ, (2003) Membrane localization of motility, signaling, and polyketide synthetase proteins in Myxococcus xanthus. J Bacteriol 185: 5066-5075.
    • (2003) J Bacteriol , vol.185 , pp. 5066-5075
    • Simunovic, V.1    Gherardini, F.C.2    Shimkets, L.J.3
  • 49
    • 0018074492 scopus 로고
    • Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and definition of the permeability barrier
    • Hancock RE, Nikaido H, (1978) Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and definition of the permeability barrier. J Bacteriol 136: 381-390.
    • (1978) J Bacteriol , vol.136 , pp. 381-390
    • Hancock, R.E.1    Nikaido, H.2
  • 50
    • 8344284323 scopus 로고    scopus 로고
    • A common open representation of mass spectrometry data and its application to proteomics research
    • Pedrioli PGA, Eng JK, Hubley R, Vogelzang M, Deutsch EW, et al. (2004) A common open representation of mass spectrometry data and its application to proteomics research. Nat Biotech 22: 1459-1466.
    • (2004) Nat Biotech , vol.22 , pp. 1459-1466
    • Pedrioli, P.G.A.1    Eng, J.K.2    Hubley, R.3    Vogelzang, M.4    Deutsch, E.W.5
  • 51
    • 33750971117 scopus 로고    scopus 로고
    • Multidimensional proteomic analysis of the soluble subproteome of the emerging nosocomial pathogen Ochrobactrum anthropi
    • Graham RL, Pollock CE, O'Loughlin SN, Ternan NG, Weatherly DB, et al. (2006) Multidimensional proteomic analysis of the soluble subproteome of the emerging nosocomial pathogen Ochrobactrum anthropi. J Proteome Res 5: 3145-3153.
    • (2006) J Proteome Res , vol.5 , pp. 3145-3153
    • Graham, R.L.1    Pollock, C.E.2    O'Loughlin, S.N.3    Ternan, N.G.4    Weatherly, D.B.5
  • 52
    • 41849106505 scopus 로고    scopus 로고
    • Discovery of the autonomously replicating plasmid pMF1 from Myxococcus fulvus and development of a gene cloning system in Myxococcus xanthus
    • Zhao JY, Zhong L, Shen MJ, Xia ZJ, Cheng QX, et al. (2008) Discovery of the autonomously replicating plasmid pMF1 from Myxococcus fulvus and development of a gene cloning system in Myxococcus xanthus. Appl Environ Microbiol 74: 1980-1987.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 1980-1987
    • Zhao, J.Y.1    Zhong, L.2    Shen, M.J.3    Xia, Z.J.4    Cheng, Q.X.5
  • 53
    • 0029285787 scopus 로고
    • PCR-mediated recombination and mutagenesis
    • Horton R, (1995) PCR-mediated recombination and mutagenesis. Molecular Biotechnology 3: 93-99.
    • (1995) Molecular Biotechnology , vol.3 , pp. 93-99
    • Horton, R.1
  • 54
    • 15644383107 scopus 로고    scopus 로고
    • Regulation of expression of the pilA gene in Myxococcus xanthus
    • Wu SS, Kaiser D, (1997) Regulation of expression of the pilA gene in Myxococcus xanthus. J Bacteriol 179: 7748-7758.
    • (1997) J Bacteriol , vol.179 , pp. 7748-7758
    • Wu, S.S.1    Kaiser, D.2
  • 55
    • 0026332722 scopus 로고
    • Extracellular fibrils and contact-mediated cell interactions in Myxococcus xanthus
    • Behmlander RM, Dworkin M, (1991) Extracellular fibrils and contact-mediated cell interactions in Myxococcus xanthus. J Bacteriol 173: 7810-7820.
    • (1991) J Bacteriol , vol.173 , pp. 7810-7820
    • Behmlander, R.M.1    Dworkin, M.2
  • 56
    • 0018536781 scopus 로고
    • Social gliding is correlated with the presence of pili in Myxococcus xanthus
    • Kaiser D, (1979) Social gliding is correlated with the presence of pili in Myxococcus xanthus. Proc Natl Acad Sci U S A 76: 5952-5956.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 5952-5956
    • Kaiser, D.1
  • 57
    • 0027138814 scopus 로고
    • Identification of esg, a genetic locus involved in cell-cell signaling during Myxococcus xanthus development
    • Downard J, Ramaswamy SV, Kil KS, (1993) Identification of esg, a genetic locus involved in cell-cell signaling during Myxococcus xanthus development. J Bacteriol 175: 7762-7770.
    • (1993) J Bacteriol , vol.175 , pp. 7762-7770
    • Downard, J.1    Ramaswamy, S.V.2    Kil, K.S.3
  • 58
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C, Vieira J, Messing J, (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33: 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.