메뉴 건너뛰기




Volumn 81, Issue 16, 2015, Pages 5363-5374

Dynamics of the Streptococcus gordonii transcriptome in response to medium, salivary α-amylase, and starch

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; AMYLASES; BACTERIA; ENVIRONMENTAL REGULATIONS; ENZYMES; FATTY ACIDS; FLAVORS; GENES; GLUCOSE; NUTRITION; PLANTS (BOTANY); POLYMERASE CHAIN REACTION; POLYSACCHARIDES; PROTEINS; RNA; SIGNAL TRANSDUCTION; STARCH; TRANSCRIPTION;

EID: 84937847828     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01221-15     Document Type: Article
Times cited : (10)

References (43)
  • 1
    • 0028519945 scopus 로고
    • Emergence in human dental plaque and host distribution of amylase-binding streptococci
    • Scannapieco FA, Solomon L, Wadenya RO. 1994. Emergence in human dental plaque and host distribution of amylase-binding streptococci. J Dent Res 73:1627-1635.
    • (1994) J Dent Res , vol.73 , pp. 1627-1635
    • Scannapieco, F.A.1    Solomon, L.2    Wadenya, R.O.3
  • 2
    • 74549181808 scopus 로고    scopus 로고
    • Starch: structure, properties, chemistry, and enzymology
    • Fraser-Ried BO, Tatsuta K, Thiem J, Cote GL (ed), Springer-Verlag, Berlin, Germany
    • Robyt JF. 2008. Starch: structure, properties, chemistry, and enzymology, p 1437-1472. In Fraser-Ried BO, Tatsuta K, Thiem J, Cote GL (ed), Glycoscience. Springer-Verlag, Berlin, Germany.
    • (2008) Glycoscience , pp. 1437-1472
    • Robyt, J.F.1
  • 3
    • 0020653638 scopus 로고
    • The binding of human salivary alpha-amylase by oral strains of streptococcal bacteria
    • Douglas CW. 1983. The binding of human salivary alpha-amylase by oral strains of streptococcal bacteria. Arch Oral Biol 28:567-573. http://dx.doi .org/10.1016/0003-9969(83)90003-1.
    • (1983) Arch Oral Biol , vol.28 , pp. 567-573
    • Douglas, C.W.1
  • 4
    • 0025514044 scopus 로고
    • Characterization of the alpha-amylase receptor of Streptococcus gordonii NCTC 7868
    • Douglas CW. 1990. Characterization of the alpha-amylase receptor of Streptococcus gordonii NCTC 7868. J Dent Res 69:1746-1752. http://dx .doi.org/10.1177/00220345900690110701.
    • (1990) J Dent Res , vol.69 , pp. 1746-1752
    • Douglas, C.W.1
  • 5
    • 0025107844 scopus 로고
    • Ability to bind salivary alpha-amylase discriminates certain viridans group streptococcal species
    • Kilian M, Nyvad B. 1990. Ability to bind salivary alpha-amylase discriminates certain viridans group streptococcal species. J Clin Microbiol 28:2576-2577.
    • (1990) J Clin Microbiol , vol.28 , pp. 2576-2577
    • Kilian, M.1    Nyvad, B.2
  • 6
    • 0024386609 scopus 로고
    • Characterization of salivary alpha-amylase binding to Streptococcus sanguis
    • Scannapieco FA, Bergey EJ, Reddy MS, Levine MJ. 1989. Characterization of salivary alpha-amylase binding to Streptococcus sanguis. Infect Immun 57:2853-2863.
    • (1989) Infect Immun , vol.57 , pp. 2853-2863
    • Scannapieco, F.A.1    Bergey, E.J.2    Reddy, M.S.3    Levine, M.J.4
  • 7
    • 0026600528 scopus 로고
    • Enzymic activity of salivary amylase when bound to the surface of oral streptococci
    • Douglas CW, Heath J, Gwynn JP. 1992. Enzymic activity of salivary amylase when bound to the surface of oral streptococci. FEMS Microbiol Lett 71:193-197.
    • (1992) FEMS Microbiol Lett , vol.71 , pp. 193-197
    • Douglas, C.W.1    Heath, J.2    Gwynn, J.P.3
  • 8
    • 0034778554 scopus 로고    scopus 로고
    • Role of Streptococcus gordonii amylase-binding protein A in adhesion to hydroxyapatite, starch metabolism, and biofilm formation
    • Rogers JD, Palmer RJ, Jr, Kolenbrander PE, Scannapieco FA. 2001. Role of Streptococcus gordonii amylase-binding protein A in adhesion to hydroxyapatite, starch metabolism, and biofilm formation. Infect Immun 69:7046-7056. http://dx.doi.org/10.1128/IAI.69.11.7046-7056.2001.
    • (2001) Infect Immun , vol.69 , pp. 7046-7056
    • Rogers, J.D.1    Palmer, R.J.2    Kolenbrander, P.E.3    Scannapieco, F.A.4
  • 9
    • 0025551141 scopus 로고
    • Structural relationship between the enzymatic and streptococcal binding sites of human salivary alpha-amylase
    • Scannapieco FA, Bhandary K, Ramasubbu N, Levine MJ. 1990. Structural relationship between the enzymatic and streptococcal binding sites of human salivary alpha-amylase. Biochem Biophys Res Commun 173:1109-1115. http://dx.doi.org/10.1016/S0006-291X(05)80900-3.
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 1109-1115
    • Scannapieco, F.A.1    Bhandary, K.2    Ramasubbu, N.3    Levine, M.J.4
  • 10
    • 0026445987 scopus 로고
    • Characterization of an amylase-binding component of Streptococcus gordonii G9B
    • Scannapieco FA, Haraszthy GG, Cho MI, Levine MJ. 1992. Characterization of an amylase-binding component of Streptococcus gordonii G9B. Infect Immun 60:4726-4733.
    • (1992) Infect Immun , vol.60 , pp. 4726-4733
    • Scannapieco, F.A.1    Haraszthy, G.G.2    Cho, M.I.3    Levine, M.J.4
  • 11
    • 0037008123 scopus 로고    scopus 로고
    • Identification and analysis of the amylase-binding protein B (AbpB) and gene (abpB) from Streptococcus gordonii
    • Li L, Tanzer JM, Scannapieco FA. 2002. Identification and analysis of the amylase-binding protein B (AbpB) and gene (abpB) from Streptococcus gordonii. FEMS Microbiol Lett 212:151-157. http://dx.doi.org/10.1111/j .1574-6968.2002.tb11259.x.
    • (2002) FEMS Microbiol Lett , vol.212 , pp. 151-157
    • Li, L.1    Tanzer, J.M.2    Scannapieco, F.A.3
  • 12
    • 0035118522 scopus 로고    scopus 로고
    • Oral colonization and cariogenicity of Streptococcus gordonii in specific pathogen-free TAN:SPFOM(OM)BR rats consuming starch or sucrose diets
    • Tanzer JM, Baranowski LK, Rogers JD, Haase EM, Scannapieco FA. 2001. Oral colonization and cariogenicity of Streptococcus gordonii in specific pathogen-free TAN:SPFOM(OM)BR rats consuming starch or sucrose diets. Arch Oral Biol 46:323-333. http://dx.doi.org/10.1016/S0003-9969(00)00126-6.
    • (2001) Arch Oral Biol , vol.46 , pp. 323-333
    • Tanzer, J.M.1    Baranowski, L.K.2    Rogers, J.D.3    Haase, E.M.4    Scannapieco, F.A.5
  • 13
    • 84857812295 scopus 로고    scopus 로고
    • Response of fatty acid synthesis genes to the binding of human salivary amylase by Streptococcus gordonii
    • Nikitkova AE, Haase EM, Vickerman MM, Gill SR, Scannapieco FA. 2012. Response of fatty acid synthesis genes to the binding of human salivary amylase by Streptococcus gordonii. Appl Environ Microbiol 78:1865-1875. http://dx.doi.org/10.1128/AEM.07071-11.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 1865-1875
    • Nikitkova, A.E.1    Haase, E.M.2    Vickerman, M.M.3    Gill, S.R.4    Scannapieco, F.A.5
  • 14
    • 84863590645 scopus 로고    scopus 로고
    • Effect of starch and amylase on the expression of amylase-binding protein A in Streptococcus gordonii
    • Nikitkova AE, Haase EM, Scannapieco FA. 2012. Effect of starch and amylase on the expression of amylase-binding protein A in Streptococcus gordonii. Mol Oral Microbiol 27:284-294. http://dx.doi.org/10.1111/j .2041-1014.2012.00644.x.
    • (2012) Mol Oral Microbiol , vol.27 , pp. 284-294
    • Nikitkova, A.E.1    Haase, E.M.2    Scannapieco, F.A.3
  • 15
    • 50649089207 scopus 로고    scopus 로고
    • RNASeq:an assessment of technical reproducibility and comparison with gene expression arrays
    • Marioni JC, Mason CE, Mane SM, Stephens M, Gilad Y. 2008. RNASeq:an assessment of technical reproducibility and comparison with gene expression arrays. Genome Res 18:1509-1517. http://dx.doi.org/10.1101/gr.079558.108.
    • (2008) Genome Res , vol.18 , pp. 1509-1517
    • Marioni, J.C.1    Mason, C.E.2    Mane, S.M.3    Stephens, M.4    Gilad, Y.5
  • 16
    • 70949102952 scopus 로고    scopus 로고
    • Next generation sequencing of microbial transcriptomes:challenges and opportunities
    • van Vliet AH. 2010. Next generation sequencing of microbial transcriptomes:challenges and opportunities. FEMS Microbiol Lett 302:1-7. http://dx.doi.org/10.1111/j.1574-6968.2009.01767.x.
    • (2010) FEMS Microbiol Lett , vol.302 , pp. 1-7
    • van Vliet, A.H.1
  • 17
    • 84872141736 scopus 로고    scopus 로고
    • Transcriptional response of mucoid Pseudomonas aeruginosa to human respiratory mucus
    • Cattoir V, Narasimhan G, Skurnik D, Aschard H, Roux D, Ramphal R, Jyot J, Lory S. 2013. Transcriptional response of mucoid Pseudomonas aeruginosa to human respiratory mucus. mBio 3:e00410-12. http://dx.doi .org/10.1128/mBio.00410-12.
    • (2013) mBio , vol.3 , pp. e00410-e00412
    • Cattoir, V.1    Narasimhan, G.2    Skurnik, D.3    Aschard, H.4    Roux, D.5    Ramphal, R.6    Jyot, J.7    Lory, S.8
  • 18
    • 80051915419 scopus 로고    scopus 로고
    • RNA-Seq-based monitoring of infection-linked changes in Vibrio cholerae gene expression
    • Mandlik A, Livny J, Robins WP, Ritchie JM, Mekalanos JJ, Waldor MK. 2011. RNA-Seq-based monitoring of infection-linked changes in Vibrio cholerae gene expression. Cell Host Microbe 10:165-174. http://dx.doi.org /10.1016/j.chom.2011.07.007.
    • (2011) Cell Host Microbe , vol.10 , pp. 165-174
    • Mandlik, A.1    Livny, J.2    Robins, W.P.3    Ritchie, J.M.4    Mekalanos, J.J.5    Waldor, M.K.6
  • 19
    • 84890244434 scopus 로고    scopus 로고
    • Global transcriptome analysis of Staphylococcus aureus biofilms in response to innate immune cells
    • Scherr TD, Roux CM, Hanke ML, Angle A, Dunman PM, Kielian T. 2013. Global transcriptome analysis of Staphylococcus aureus biofilms in response to innate immune cells. Infect Immun 81:4363-4376. http://dx .doi.org/10.1128/IAI.00819-13.
    • (2013) Infect Immun , vol.81 , pp. 4363-4376
    • Scherr, T.D.1    Roux, C.M.2    Hanke, M.L.3    Angle, A.4    Dunman, P.M.5    Kielian, T.6
  • 20
    • 0024395661 scopus 로고
    • Spontaneous switching of the sucrose-promoted colony phenotype in Streptococcus sanguis
    • Tardif G, Sulavik MC, Jones GW, Clewell DB. 1989. Spontaneous switching of the sucrose-promoted colony phenotype in Streptococcus sanguis. Infect Immun 57:3945-3948.
    • (1989) Infect Immun , vol.57 , pp. 3945-3948
    • Tardif, G.1    Sulavik, M.C.2    Jones, G.W.3    Clewell, D.B.4
  • 22
    • 0033965303 scopus 로고    scopus 로고
    • Streptococcus gordonii biofilm formation: identification of genes that code for biofilm phenotypes
    • Loo CY, Corliss DA, Ganeshkumar N. 2000. Streptococcus gordonii biofilm formation: identification of genes that code for biofilm phenotypes. J Bacteriol 182:1374-1382. http://dx.doi.org/10.1128/JB.182.5.1374-1382.2000.
    • (2000) J Bacteriol , vol.182 , pp. 1374-1382
    • Loo, C.Y.1    Corliss, D.A.2    Ganeshkumar, N.3
  • 23
    • 0020013552 scopus 로고
    • Molecular cloning in the streptococci
    • Hollander A, DeMoss R, Kaplan S, Konisky J, Savage D, Wolfe R (ed), Plenum Publishing Corp, New York, NY
    • Macrina FL, Tobian JA, Jones KR, Evans RP. 1982. Molecular cloning in the streptococci, p 195-210. In Hollander A, DeMoss R, Kaplan S, Konisky J, Savage D, Wolfe R (ed), Genetic engineering of microorganisms for chemicals. Plenum Publishing Corp, New York, NY.
    • (1982) Genetic engineering of microorganisms for chemicals , pp. 195-210
    • Macrina, F.L.1    Tobian, J.A.2    Jones, K.R.3    Evans, R.P.4
  • 24
    • 0014803356 scopus 로고
    • Growth and development of competence in the group H streptococci
    • Lawson JW, Gooder H. 1970. Growth and development of competence in the group H streptococci. J Bacteriol 102:820-825.
    • (1970) J Bacteriol , vol.102 , pp. 820-825
    • Lawson, J.W.1    Gooder, H.2
  • 25
    • 0026708281 scopus 로고
    • Identification of a gene, rgg, which regulates expression of glucosyltransferase and influences the Spp phenotype of Streptococcus gordonii Challis
    • Sulavik MC, Tardif G, Clewell DB. 1992. Identification of a gene, rgg, which regulates expression of glucosyltransferase and influences the Spp phenotype of Streptococcus gordonii Challis. J Bacteriol 174:3577-3586.
    • (1992) J Bacteriol , vol.174 , pp. 3577-3586
    • Sulavik, M.C.1    Tardif, G.2    Clewell, D.B.3
  • 26
    • 0023269941 scopus 로고
    • Transfer functions of the Streptococcus faecalis plasmid pAD1: organization of plasmid DNA encoding response to sex pheromone
    • Ehrenfeld EE, Clewell DB. 1987. Transfer functions of the Streptococcus faecalis plasmid pAD1: organization of plasmid DNA encoding response to sex pheromone. J Bacteriol 169:3473-3481.
    • (1987) J Bacteriol , vol.169 , pp. 3473-3481
    • Ehrenfeld, E.E.1    Clewell, D.B.2
  • 27
    • 0024370174 scopus 로고
    • Oral mucosal pellicle: adsorption and transpeptidation of salivary components to buccal epithelial cells
    • Bradway SD, Bergey EJ, Jones PC, Levine MJ. 1989. Oral mucosal pellicle: adsorption and transpeptidation of salivary components to buccal epithelial cells. Biochem J 261:887-896.
    • (1989) Biochem J , vol.261 , pp. 887-896
    • Bradway, S.D.1    Bergey, E.J.2    Jones, P.C.3    Levine, M.J.4
  • 28
    • 0015306097 scopus 로고
    • Some properties of salivary amylase: a survey of the literature and some observations
    • Jacobsen N, Melvaer KL, Hensten-Pettersen A. 1972. Some properties of salivary amylase: a survey of the literature and some observations. J Dent Res 51:381-388. http://dx.doi.org/10.1177/00220345720510022501.
    • (1972) J Dent Res , vol.51 , pp. 381-388
    • Jacobsen, N.1    Melvaer, K.L.2    Hensten-Pettersen, A.3
  • 29
    • 53649104629 scopus 로고    scopus 로고
    • Amylase-binding protein B of Streptococcus gordonii is an extracellular dipeptidyl-peptidase
    • Chaudhuri B, Paju S, Haase EM, Vickerman MM, Tanzer JM, Scannapieco FA. 2008. Amylase-binding protein B of Streptococcus gordonii is an extracellular dipeptidyl-peptidase. Infect Immun 76:4530-4537. http://dx.doi.org/10.1128/IAI.00186-08.
    • (2008) Infect Immun , vol.76 , pp. 4530-4537
    • Chaudhuri, B.1    Paju, S.2    Haase, E.M.3    Vickerman, M.M.4    Tanzer, J.M.5    Scannapieco, F.A.6
  • 30
    • 0034924241 scopus 로고    scopus 로고
    • Determination of minimum inhibitory concentrations
    • Andrews JM. 2001. Determination of minimum inhibitory concentrations. J Antimicrob Chemother 48(Suppl 1):S5-S16.
    • (2001) J Antimicrob Chemother , vol.48 , pp. S5-S16
    • Andrews, J.M.1
  • 31
    • 0141532266 scopus 로고    scopus 로고
    • A 6×6 drop plate method for simultaneous colony counting and MPN enumeration of Campylobacter jejuni, Listeria monocytogenes, and Escherichia coli
    • Chen CY, Nace GW, Irwin PL. 2003. A 6×6 drop plate method for simultaneous colony counting and MPN enumeration of Campylobacter jejuni, Listeria monocytogenes, and Escherichia coli. J Microbiol Methods 55:475-479. http://dx.doi.org/10.1016/S0167-7012(03)00194-5.
    • (2003) J Microbiol Methods , vol.55 , pp. 475-479
    • Chen, C.Y.1    Nace, G.W.2    Irwin, P.L.3
  • 32
    • 84937947894 scopus 로고    scopus 로고
    • Mass spectrometic analysis of whole secretome and amylase-precipitated secretome proteins from Streptococcus gordonii
    • Maddi A, Haase EM, Scannapieco FA. 2014. Mass spectrometic analysis of whole secretome and amylase-precipitated secretome proteins from Streptococcus gordonii. J Proteomics Bioinform 7:287-295.
    • (2014) J Proteomics Bioinform , vol.7 , pp. 287-295
    • Maddi, A.1    Haase, E.M.2    Scannapieco, F.A.3
  • 33
    • 0035026476 scopus 로고    scopus 로고
    • RegG, a CcpA homolog, participates in regulation of amylase-binding protein A gene (abpA) expression in Streptococcus gordonii
    • Rogers JD, Scannapieco FA. 2001. RegG, a CcpA homolog, participates in regulation of amylase-binding protein A gene (abpA) expression in Streptococcus gordonii. J Bacteriol 183:3521-3525. http://dx.doi.org/10.1128/JB .183.11.3521-3525.2001.
    • (2001) J Bacteriol , vol.183 , pp. 3521-3525
    • Rogers, J.D.1    Scannapieco, F.A.2
  • 34
    • 84937867006 scopus 로고    scopus 로고
    • Sortase B assemble amylase-binding protein A to streptococcal cell surface
    • 89th Gen Session Int Assoc Dent Res IADR, San Diego, CA
    • Liang X, Chen Y, Wu H. 2011. Sortase B assemble amylase-binding protein A to streptococcal cell surface, p 72. 89th Gen Session Int Assoc Dent Res IADR, San Diego, CA.
    • (2011) , pp. 72
    • Liang, X.1    Chen, Y.2    Wu, H.3
  • 35
    • 0026605348 scopus 로고
    • Characterization of the tet(M) determinant of Tn916: evidence for regulation by transcription attenuation
    • Su YA, He P, Clewell DB. 1992. Characterization of the tet(M) determinant of Tn916: evidence for regulation by transcription attenuation. Antimicrob Agents Chemother 36:769-778. http://dx.doi.org/10.1128/AAC .36.4.769.
    • (1992) Antimicrob Agents Chemother , vol.36 , pp. 769-778
    • Su, Y.A.1    He, P.2    Clewell, D.B.3
  • 36
    • 0035283403 scopus 로고    scopus 로고
    • An embarrassment of sortases: a richness of substrates?
    • Pallen MJ, Lam AC, Antonio M, Dunbar K. 2001. An embarrassment of sortases: a richness of substrates?. Trends Microbiol 9:97-102. http://dx .doi.org/10.1016/S0966-842X(01)01956-4.
    • (2001) Trends Microbiol , vol.9 , pp. 97-102
    • Pallen, M.J.1    Lam, A.C.2    Antonio, M.3    Dunbar, K.4
  • 37
    • 8844240627 scopus 로고    scopus 로고
    • Protein sorting to the cell wall envelope of Gram-positive bacteria
    • Ton-That H, Marraffini LA, Schneewind O. 2004. Protein sorting to the cell wall envelope of Gram-positive bacteria. Biochim Biophys Acta 1694:269-278. http://dx.doi.org/10.1016/j.bbamcr.2004.04.014.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 269-278
    • Ton-That, H.1    Marraffini, L.A.2    Schneewind, O.3
  • 38
    • 84931285731 scopus 로고    scopus 로고
    • The malQ gene is essential for starch metabolism in Streptococcus mutans
    • Sato Y, Okamoto-Shibayama K, Azuma T. 2013. The malQ gene is essential for starch metabolism in Streptococcus mutans. J Oral Microbiol http://dx.doi.org/10.3402/jom.v5i0.21285.
    • (2013) J Oral Microbiol
    • Sato, Y.1    Okamoto-Shibayama, K.2    Azuma, T.3
  • 39
    • 0035702148 scopus 로고    scopus 로고
    • Bacterial phosphotransferase system (PTS) in carbohydrate uptake and control of carbon metabolism
    • Kotrba P, Inui M, Yukawa H. 2001. Bacterial phosphotransferase system (PTS) in carbohydrate uptake and control of carbon metabolism. J Biosci Bioeng 92:502-517. http://dx.doi.org/10.1016/S1389-1723(01)80308-X.
    • (2001) J Biosci Bioeng , vol.92 , pp. 502-517
    • Kotrba, P.1    Inui, M.2    Yukawa, H.3
  • 40
    • 3042558397 scopus 로고    scopus 로고
    • Involvement of Streptococcus gordonii beta-glucoside metabolism systems in adhesion, biofilm formation, and in vivo gene expression
    • Kilic AO, Tao L, Zhang Y, Lei Y, Khammanivong A, Herzberg MC. 2004. Involvement of Streptococcus gordonii beta-glucoside metabolism systems in adhesion, biofilm formation, and in vivo gene expression. J Bacteriol 186:4246-4253. http://dx.doi.org/10.1128/JB.186.13.4246-4253.2004.
    • (2004) J Bacteriol , vol.186 , pp. 4246-4253
    • Kilic, A.O.1    Tao, L.2    Zhang, Y.3    Lei, Y.4    Khammanivong, A.5    Herzberg, M.C.6
  • 41
    • 34447619346 scopus 로고    scopus 로고
    • Interaction of salivary alpha-amylase and amylase-binding-protein A (AbpA) of Streptococcus gordonii with glucosyltransferase of S. gordonii and Streptococcus mutans
    • Chaudhuri B, Rojek J, Vickerman MM, Tanzer JM, Scannapieco FA. 2007. Interaction of salivary alpha-amylase and amylase-binding-protein A (AbpA) of Streptococcus gordonii with glucosyltransferase of S. gordonii and Streptococcus mutans.BMCMicrobiol 7:60. http://dx.doi.org/10.1186/1471-2180-7-60.
    • (2007) BMCMicrobiol , vol.7 , pp. 60
    • Chaudhuri, B.1    Rojek, J.2    Vickerman, M.M.3    Tanzer, J.M.4    Scannapieco, F.A.5
  • 42
    • 67651205583 scopus 로고    scopus 로고
    • Bacterial PEP-dependent carbohydrate: phosphotransferase systems couple sensing and global control mechanisms
    • Lengeler JW, Jahreis K. 2009. Bacterial PEP-dependent carbohydrate: phosphotransferase systems couple sensing and global control mechanisms. Contrib Microbiol 16:65-87. http://dx.doi.org/10.1159/000219373.
    • (2009) Contrib Microbiol , vol.16 , pp. 65-87
    • Lengeler, J.W.1    Jahreis, K.2
  • 43
    • 0033791468 scopus 로고    scopus 로고
    • Two-component signal transduction
    • Stock AM, Robinson VL, Goudreau PN. 2000. Two-component signal transduction. Annu Rev Biochem 69:183-215. http://dx.doi.org/10.1146/annurev.biochem.69.1.183.
    • (2000) Annu Rev Biochem , vol.69 , pp. 183-215
    • Stock, A.M.1    Robinson, V.L.2    Goudreau, P.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.