메뉴 건너뛰기




Volumn 4, Issue 6, 2013, Pages

Overproduction of flotillin influences cell differentiation and shape in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

FLOTILLIN; MEMBRANE PROTEIN; PROTEIN FLOA; PROTEIN FLOT; PROTEIN FTSH; PROTEINASE; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; FLOTILLINS; RECOMBINANT PROTEIN;

EID: 84891613679     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00719-13     Document Type: Article
Times cited : (36)

References (71)
  • 2
    • 77956069180 scopus 로고    scopus 로고
    • Protein subcellular localization in bacteria
    • doi:10.1101/ cshperspect.a000307
    • Rudner DZ, Losick R. 2010. Protein subcellular localization in bacteria. Cold Spring Harb. Perspect. Biol. 2:a000307. doi:10.1101/ cshperspect.a000307.
    • (2010) Cold Spring Harb. Perspect. Biol , vol.2
    • Rudner, D.Z.1    Losick, R.2
  • 3
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: New tools and insights
    • Simons K, Gerl MJ. 2010. Revitalizing membrane rafts: new tools and insights. Nat. Rev. Mol. Cell Biol. 11:688-699.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 4
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. 1997. Functional rafts in cell membranes. Nature 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 5
    • 84860448210 scopus 로고    scopus 로고
    • Membrane organization and lipid rafts
    • doi:10.1101/cshperspect.a004697
    • Simons K, Sampaio JL. 2011. Membrane organization and lipid rafts. Cold Spring Harb. Perspect. Biol 3:a004697. doi:10.1101/cshperspect.a004697.
    • (2011) Cold Spring Harb. Perspect. Biol , vol.3
    • Simons, K.1    Sampaio, J.L.2
  • 6
    • 77956292192 scopus 로고    scopus 로고
    • Functional microdomains in bacterial membranes
    • López D, Kolter R. 2010. Functional microdomains in bacterial membranes. Genes Dev. 24:1893-1902.
    • (2010) Genes Dev , vol.24 , pp. 1893-1902
    • López, D.1    Kolter, R.2
  • 7
    • 84866321770 scopus 로고    scopus 로고
    • Synthetic motility and cell shape defects for deletions of flotillin/reggie paralogs in Bacillus subtilis and interplay with NfeD proteins
    • Dempwolff F, Moller HM, Graumann PL. 2012. Synthetic motility and cell shape defects for deletions of flotillin/reggie paralogs in Bacillus subtilis and interplay with NfeD proteins. J. Bacteriol. 194:4652-4661.
    • (2012) J. Bacteriol , vol.194 , pp. 4652-4661
    • Dempwolff, F.1    Moller, H.M.2    Graumann, P.L.3
  • 8
    • 67650708496 scopus 로고    scopus 로고
    • Characterization and subcellular localization of a bacterial flotillin homologue
    • Donovan C, Bramkamp M. 2009. Characterization and subcellular localization of a bacterial flotillin homologue. Microbiology 155:1786-1799.
    • (2009) Microbiology , vol.155 , pp. 1786-1799
    • Donovan, C.1    Bramkamp, M.2
  • 10
    • 72549086774 scopus 로고    scopus 로고
    • The reggie/flotillin connection to growth
    • Stuermer CA. 2010. The reggie/flotillin connection to growth. Trends Cell Biol. 20:6-13.
    • (2010) Trends Cell Biol , vol.20 , pp. 6-13
    • Stuermer, C.A.1
  • 11
    • 23844462163 scopus 로고    scopus 로고
    • Flotillins and the PHB domain protein family: Rafts, worms and anaesthetics
    • Morrow IC, Parton RG. 2005. Flotillins and the PHB domain protein family: rafts, worms and anaesthetics. Traffic 6:725-740.
    • (2005) Traffic , vol.6 , pp. 725-740
    • Morrow, I.C.1    Parton, R.G.2
  • 12
    • 79851479445 scopus 로고    scopus 로고
    • Reggie/flotillin and the targeted delivery of cargo
    • Stuermer CA. 2011. Reggie/flotillin and the targeted delivery of cargo. J. Neurochem. 116:708-713.
    • (2011) J. Neurochem , vol.116 , pp. 708-713
    • Stuermer, C.A.1
  • 14
    • 0034714463 scopus 로고    scopus 로고
    • Localization of flotillins in human brain and their accumulation with the progression of Alzheimer's disease pathology
    • Kokubo H, Lemere CA, Yamaguchi H. 2000. Localization of flotillins in human brain and their accumulation with the progression of Alzheimer's disease pathology. Neurosci. Lett. 290:93-96.
    • (2000) Neurosci. Lett , vol.290 , pp. 93-96
    • Kokubo, H.1    Lemere, C.A.2    Yamaguchi, H.3
  • 17
    • 0031054457 scopus 로고    scopus 로고
    • Reggie-1 and reggie-2, two cell surface proteins expressed by retinal ganglion cells during axon regeneration
    • Schulte T, Paschke KA, Laessing U, Lottspeich F, Stuermer CA. 1997. Reggie-1 and reggie-2, two cell surface proteins expressed by retinal ganglion cells during axon regeneration. Development 124:577-587.
    • (1997) Development , vol.124 , pp. 577-587
    • Schulte, T.1    Paschke, K.A.2    Laessing, U.3    Lottspeich, F.4    Stuermer, C.A.5
  • 18
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro S. 2003. Lipid rafts: elusive or illusive? Cell 115:377-388.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 19
    • 33645803827 scopus 로고    scopus 로고
    • Identification of Bacillus subtilis sigma-dependent genes that provide intrinsic resistance to antimicrobial compounds produced by bacilli
    • Butcher BG, Helmann JD. 2006. Identification of Bacillus subtilis sigma-dependent genes that provide intrinsic resistance to antimicrobial compounds produced by bacilli. Mol. Microbiol. 60:765-782.
    • (2006) Mol. Microbiol , vol.60 , pp. 765-782
    • Butcher, B.G.1    Helmann, J.D.2
  • 20
    • 84879030282 scopus 로고    scopus 로고
    • Flotillins functionally organize the bacterial membrane
    • Bach JN, Bramkamp M. 2013. Flotillins functionally organize the bacterial membrane. Mol. Microbiol. 88:1205-1217.
    • (2013) Mol. Microbiol , vol.88 , pp. 1205-1217
    • Bach, J.N.1    Bramkamp, M.2
  • 21
    • 84866321770 scopus 로고    scopus 로고
    • Synthetic motility and cell shape defects associated with deletions of flotillin/reggie paralogs in Bacillus subtilis and interplay of these proteins with NfeD proteins
    • Dempwolff F, Möller HM, Graumann PL. 2012. Synthetic motility and cell shape defects associated with deletions of flotillin/reggie paralogs in Bacillus subtilis and interplay of these proteins with NfeD proteins. J. Bacteriol. 194:4652-4661.
    • (2012) J. Bacteriol , vol.194 , pp. 4652-4661
    • Dempwolff, F.1    Möller, H.M.2    Graumann, P.L.3
  • 23
    • 0035725498 scopus 로고    scopus 로고
    • The sporulation transcription factor Spo0A is required for biofilm development in Bacillus subtilis
    • Hamon MA, Lazazzera BA. 2001. The sporulation transcription factor Spo0A is required for biofilm development in Bacillus subtilis. Mol. Microbiol. 42:1199-1209.
    • (2001) Mol. Microbiol , vol.42 , pp. 1199-1209
    • Hamon, M.A.1    Lazazzera, B.A.2
  • 24
    • 57549105056 scopus 로고    scopus 로고
    • Generation of multiple cell types in Bacillus subtilis
    • Lopez D, Vlamakis H, Kolter R. 2009. Generation of multiple cell types in Bacillus subtilis. FEMS Microbiol. Rev. 33:152-163.
    • (2009) FEMS Microbiol. Rev , vol.33 , pp. 152-163
    • Lopez, D.1    Vlamakis, H.2    Kolter, R.3
  • 25
    • 65649111204 scopus 로고    scopus 로고
    • The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH metalloprotease
    • Le AT, Schumann W. 2009. The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH metalloprotease. Microbiology 155:1122-1132.
    • (2009) Microbiology , vol.155 , pp. 1122-1132
    • Le, A.T.1    Schumann, W.2
  • 26
    • 37449004861 scopus 로고    scopus 로고
    • The division inhibitor EzrA contains a seven-residue patch required for maintaining the dynamic nature of the medial FtsZ ring
    • Haeusser DP, Garza AC, Buscher AZ, Levin PA. 2007. The division inhibitor EzrA contains a seven-residue patch required for maintaining the dynamic nature of the medial FtsZ ring. J. Bacteriol. 189:9001-9010.
    • (2007) J. Bacteriol , vol.189 , pp. 9001-9010
    • Haeusser, D.P.1    Garza, A.C.2    Buscher, A.Z.3    Levin, P.A.4
  • 27
    • 2442546546 scopus 로고    scopus 로고
    • EzrA prevents aberrant cell division by modulating assembly of the cytoskeletal protein FtsZ
    • Haeusser DP, Schwartz RL, Smith AM, Oates ME, Levin PA. 2004. EzrA prevents aberrant cell division by modulating assembly of the cytoskeletal protein FtsZ. Mol. Microbiol. 52:801-814.
    • (2004) Mol. Microbiol , vol.52 , pp. 801-814
    • Haeusser, D.P.1    Schwartz, R.L.2    Smith, A.M.3    Oates, M.E.4    Levin, P.A.5
  • 28
    • 34648819672 scopus 로고    scopus 로고
    • A membrane protein, EzrA, regulates assembly dynamics of FtsZ by interacting with the C-terminal tail of FtsZ
    • Singh JK, Makde RD, Kumar V, Panda D. 2007. A membrane protein, EzrA, regulates assembly dynamics of FtsZ by interacting with the C-terminal tail of FtsZ. Biochemistry 46:11013-11022.
    • (2007) Biochemistry , vol.46 , pp. 11013-11022
    • Singh, J.K.1    Makde, R.D.2    Kumar, V.3    Panda, D.4
  • 30
    • 75749151681 scopus 로고    scopus 로고
    • Extracellular signals that define distinct and coexisting cell fates in Bacillus subtilis
    • López D, Kolter R. 2010. Extracellular signals that define distinct and coexisting cell fates in Bacillus subtilis. FEMS Microbiol. Rev. 34:134-149.
    • (2010) FEMS Microbiol. Rev , vol.34 , pp. 134-149
    • López, D.1    Kolter, R.2
  • 35
    • 0040973380 scopus 로고    scopus 로고
    • Control of synthesis and secretion of the Bacillus subtilis protein YqxM
    • Stöver AG, Driks A. 1999. Control of synthesis and secretion of the Bacillus subtilis protein YqxM. J. Bacteriol. 181:7065-7069.
    • (1999) J. Bacteriol , vol.181 , pp. 7065-7069
    • Stöver, A.G.1    Driks, A.2
  • 36
    • 0040973379 scopus 로고    scopus 로고
    • Regulation of synthesis of the Bacillus subtilis transition-phase, spore-associated antibacterial protein TasA
    • Stöver AG, Driks A. 1999. Regulation of synthesis of the Bacillus subtilis transition-phase, spore-associated antibacterial protein TasA. J. Bacteriol. 181:5476-5481.
    • (1999) J. Bacteriol , vol.181 , pp. 5476-5481
    • Stöver, A.G.1    Driks, A.2
  • 37
    • 33645085864 scopus 로고    scopus 로고
    • A major protein component of the Bacillus subtilis biofilm matrix
    • Branda SS, Chu F, Kearns DB, Losick R, Kolter R. 2006. A major protein component of the Bacillus subtilis biofilm matrix. Mol. Microbiol. 59: 1229-1238.
    • (2006) Mol. Microbiol , vol.59 , pp. 1229-1238
    • Branda, S.S.1    Chu, F.2    Kearns, D.B.3    Losick, R.4    Kolter, R.5
  • 38
    • 76649143766 scopus 로고    scopus 로고
    • Amyloid fibers provide structural integrity to Bacillus subtilis biofilms
    • Romero D, Aguilar C, Losick R, Kolter R. 2010. Amyloid fibers provide structural integrity to Bacillus subtilis biofilms. Proc. Natl. Acad. Sci. U. S. A. 107:2230-2234.
    • (2010) Proc. Natl. Acad. Sci. U. S. A , vol.107 , pp. 2230-2234
    • Romero, D.1    Aguilar, C.2    Losick, R.3    Kolter, R.4
  • 39
    • 79957460465 scopus 로고    scopus 로고
    • An accessory protein required for anchoring and assembly of amyloid fibres in B. Subtilis biofilms
    • Romero D, Vlamakis H, Losick R, Kolter R. 2011. An accessory protein required for anchoring and assembly of amyloid fibres in B. subtilis biofilms. Mol. Microbiol. 80:1155-1168.
    • (2011) Mol. Microbiol , vol.80 , pp. 1155-1168
    • Romero, D.1    Vlamakis, H.2    Losick, R.3    Kolter, R.4
  • 41
    • 33645056701 scopus 로고    scopus 로고
    • Targets of the master regulator of biofilm formation in Bacillus subtilis
    • Chu F, Kearns DB, Branda SS, Kolter R, Losick R. 2006. Targets of the master regulator of biofilm formation in Bacillus subtilis. Mol. Microbiol. 59:1216-1228.
    • (2006) Mol. Microbiol , vol.59 , pp. 1216-1228
    • Chu, F.1    Kearns, D.B.2    Branda, S.S.3    Kolter, R.4    Losick, R.5
  • 42
    • 58549115547 scopus 로고    scopus 로고
    • Structurally diverse natural products that cause potassium leakage trigger multicellularity in Bacillus subtilis
    • López D, Fischbach MA, Chu F, Losick R, Kolter R. 2009. Structurally diverse natural products that cause potassium leakage trigger multicellularity in Bacillus subtilis. Proc. Natl. Acad. Sci. U. S. A. 106:280-285.
    • (2009) Proc. Natl. Acad. Sci. U. S. A , vol.106 , pp. 280-285
    • López, D.1    Fischbach, M.A.2    Chu, F.3    Losick, R.4    Kolter, R.5
  • 43
    • 0032501971 scopus 로고    scopus 로고
    • Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases
    • Quadri LE, Weinreb PH, Lei M, Nakano MM, Zuber P, Walsh CT. 1998. Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases. Biochemistry 37:1585-1595.
    • (1998) Biochemistry , vol.37 , pp. 1585-1595
    • Quadri, L.E.1    Weinreb, P.H.2    Lei, M.3    Nakano, M.M.4    Zuber, P.5    Walsh, C.T.6
  • 44
    • 0033485259 scopus 로고    scopus 로고
    • Crystal structure of the surfactin synthetase-activating enzyme sfp: A prototype of the 4=-phosphopantetheinyl transferase superfamily
    • Reuter K, Mofid MR, Marahiel MA, Ficner R. 1999. Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4=-phosphopantetheinyl transferase superfamily. EMBO J. 18:6823-6831.
    • (1999) EMBO J , vol.18 , pp. 6823-6831
    • Reuter, K.1    Mofid, M.R.2    Marahiel, M.A.3    Ficner, R.4
  • 45
    • 0032965905 scopus 로고    scopus 로고
    • FtsH-a single-chain charonin
    • Schumann W. 1999. FtsH-a single-chain charonin? FEMS Microbiol. Rev. 23:1-11.
    • (1999) FEMS Microbiol. Rev , vol.23 , pp. 1-11
    • Schumann, W.1
  • 46
    • 25844525796 scopus 로고    scopus 로고
    • Cellular functions, mechanism of action, and regulation of FtsH protease
    • Ito K, Akiyama Y. 2005. Cellular functions, mechanism of action, and regulation of FtsH protease. Annu. Rev. Microbiol. 59:211-231.
    • (2005) Annu. Rev. Microbiol , vol.59 , pp. 211-231
    • Ito, K.1    Akiyama, Y.2
  • 48
    • 76049099304 scopus 로고    scopus 로고
    • The crystal structure of apo-FtsH reveals domain movements necessary for substrate un-folding and translocation
    • Bieniossek C, Niederhauser B, Baumann UM. 2009. The crystal structure of apo-FtsH reveals domain movements necessary for substrate un-folding and translocation. Proc. Natl. Acad. Sci. U. S. A. 106: 21579-21584.
    • (2009) Proc. Natl. Acad. Sci. U. S. A , vol.106 , pp. 21579-21584
    • Bieniossek, C.1    Niederhauser, B.2    Baumann, U.M.3
  • 50
    • 71749117953 scopus 로고    scopus 로고
    • AAA proteases in mitochondria: Diverse functions of membrane-bound proteolytic machines
    • Tatsuta T, Langer T. 2009. AAA proteases in mitochondria: diverse functions of membrane-bound proteolytic machines. Res. Microbiol. 160: 711-717.
    • (2009) Res. Microbiol , vol.160 , pp. 711-717
    • Tatsuta, T.1    Langer, T.2
  • 51
    • 0034047383 scopus 로고    scopus 로고
    • The FtsH protein accumulates at the septum of Bacillus subtilis during cell division and sporulation
    • Wehrl W, Niederweis M, Schumann W. 2000. The FtsH protein accumulates at the septum of Bacillus subtilis during cell division and sporulation. J. Bacteriol. 182:3870-3873.
    • (2000) J. Bacteriol , vol.182 , pp. 3870-3873
    • Wehrl, W.1    Niederweis, M.2    Schumann, W.3
  • 52
    • 0031706555 scopus 로고    scopus 로고
    • MinCD proteins control the septation process during sporulation of Bacillus subtilis
    • Barák I, Prepiak P, Schmeisser F. 1998. MinCD proteins control the septation process during sporulation of Bacillus subtilis. J. Bacteriol. 180: 5327-5333.
    • (1998) J. Bacteriol , vol.180 , pp. 5327-5333
    • Barák, I.1    Prepiak, P.2    Schmeisser, F.3
  • 53
    • 21344453558 scopus 로고    scopus 로고
    • FtsZ mutations affecting cell division frequency, placement and morphology in Bacillus subtilis
    • Feucht A, Errington J. 2005. ftsZ mutations affecting cell division frequency, placement and morphology in Bacillus subtilis. Microbiology 151: 2053-2064.
    • (2005) Microbiology , vol.151 , pp. 2053-2064
    • Feucht, A.1    Errington, J.2
  • 55
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi EF, Lutkenhaus J. 1991. FtsZ ring structure associated with division in Escherichia coli. Nature 354:161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.F.1    Lutkenhaus, J.2
  • 57
    • 0027513320 scopus 로고
    • Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring
    • Bi E, Lutkenhaus J. 1993. Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring. J. Bacteriol. 175:1118-1125.
    • (1993) J. Bacteriol , vol.175 , pp. 1118-1125
    • Bi, E.1    Lutkenhaus, J.2
  • 59
    • 64849091878 scopus 로고    scopus 로고
    • Isolation and use of rafts
    • Chapter 11:Unit 11.10. doi:10.1016/j.cell.2007.05.043
    • Brown DA. 2002. Isolation and use of rafts. Curr. Protoc. Immunol. Chapter 11:Unit 11.10. doi:10.1016/j.cell.2007.05.043.
    • (2002) Curr. Protoc. Immunol
    • Brown, D.A.1
  • 60
    • 38449114971 scopus 로고    scopus 로고
    • Detergent resistance as a tool in membrane research
    • Lingwood D, Simons K. 2007. Detergent resistance as a tool in membrane research. Nat. Protoc. 2:2159-2165.
    • (2007) Nat. Protoc , vol.2 , pp. 2159-2165
    • Lingwood, D.1    Simons, K.2
  • 61
    • 0033578438 scopus 로고    scopus 로고
    • Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis
    • Levin PA, Kurtser IG, Grossman AD. 1999. Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis. Proc. Natl. Acad. Sci. U. S. A. 96:9642-9647.
    • (1999) Proc. Natl. Acad. Sci. U. S. A , vol.96 , pp. 9642-9647
    • Levin, P.A.1    Kurtser, I.G.2    Grossman, A.D.3
  • 63
    • 0037310554 scopus 로고    scopus 로고
    • The absence of FtsH metalloprotease activity causes overexpression of the sigmaW-controlled pbpE gene, resulting in filamentous growth of Bacillus subtilis
    • Zellmeier S, Zuber U, Schumann W, Wiegert T. 2003. The absence of FtsH metalloprotease activity causes overexpression of the sigmaW-controlled pbpE gene, resulting in filamentous growth of Bacillus subtilis. J. Bacteriol. 185:973-982.
    • (2003) J. Bacteriol , vol.185 , pp. 973-982
    • Zellmeier, S.1    Zuber, U.2    Schumann, W.3    Wiegert, T.4
  • 65
    • 0026079801 scopus 로고
    • Genetic competence in Bacillus subtilis
    • Dubnau D. 1991. Genetic competence in Bacillus subtilis. Microbiol. Rev. 55:395-424.
    • (1991) Microbiol. Rev , vol.55 , pp. 395-424
    • Dubnau, D.1
  • 66
    • 0016352815 scopus 로고
    • Transduction in Bacillus subtilis by bacteriophage SPP1
    • Yasbin RE, Young FE. 1974. Transduction in Bacillus subtilis by bacteriophage SPP1. J. Virol. 14:1343-1348.
    • (1974) J. Virol , vol.14 , pp. 1343-1348
    • Yasbin, R.E.1    Young, F.E.2
  • 68
    • 0344392193 scopus 로고    scopus 로고
    • Spx-dependent global transcriptional control is induced by thiol-specific oxidative stress in Bacillus subtilis
    • Nakano S, Küster-Schöck E, Grossman AD, Zuber P. 2003. Spx-dependent global transcriptional control is induced by thiol-specific oxidative stress in Bacillus subtilis. Proc. Natl. Acad. Sci. U. S. A. 100: 13603-13608.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 13603-13608
    • Nakano, S.1    Küster-Schöck, E.2    Grossman, A.D.3    Zuber, P.4
  • 69
    • 0030605248 scopus 로고    scopus 로고
    • A xylose-inducible Bacillus subtilis integration vector and its application
    • Kim L, Mogk A, Schumann W. 1996. A xylose-inducible Bacillus subtilis integration vector and its application. Gene 181:71-76.
    • (1996) Gene , vol.181 , pp. 71-76
    • Kim, L.1    Mogk, A.2    Schumann, W.3
  • 70
    • 0033521857 scopus 로고    scopus 로고
    • GFP vectors for controlled expression and dual labelling of protein fusions in Bacillus subtilis
    • Lewis PJ, Marston AL. 1999. GFP vectors for controlled expression and dual labelling of protein fusions in Bacillus subtilis. Gene 227:101-110.
    • (1999) Gene , vol.227 , pp. 101-110
    • Lewis, P.J.1    Marston, A.L.2
  • 71
    • 84862760267 scopus 로고    scopus 로고
    • BslA(YuaB) forms a hydrophobic layer on the surface of Bacillus subtilis biofilms
    • Kobayashi K, Iwano M. 2012. BslA(YuaB) forms a hydrophobic layer on the surface of Bacillus subtilis biofilms. Mol. Microbiol. 85:51-66.
    • (2012) Mol. Microbiol , vol.85 , pp. 51-66
    • Kobayashi, K.1    Iwano, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.