메뉴 건너뛰기




Volumn 69, Issue , 2016, Pages 1-50

The Journey of Lipoproteins Through the Cell: One Birthplace, Multiple Destinations

Author keywords

BamA; Gram negative bacteria; Lipoprotein biogenesis; Lipoprotein sorting; Lol system; LolA; RcsF; Surface exposed lipoproteins

Indexed keywords

ACYLTRANSFERASE; BACTERIAL PROTEIN; CYSTEINE; FLIPPASE; LGT ENZYME; LIPOPROTEIN; LNT ENZYME; LSP ENZYME; PROTEIN BAM; PROTEIN BAMC; PROTEIN FHBP; PROTEIN LBPB; PROTEIN LOLA; PROTEIN LOLB; PROTEIN LPP; PROTEIN NALP; PROTEIN PAL; PROTEIN PRECURSOR; PROTEIN RCSF; SERINE PROTEINASE; SIGNAL PEPTIDASE; SIGNAL PEPTIDE; SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE; TRANSFERASE; TRANSFERRIN BINDING PROTEIN B; UNCLASSIFIED DRUG; OUTER MEMBRANE PROTEIN;

EID: 85015350349     PISSN: 00652911     EISSN: None     Source Type: Book Series    
DOI: 10.1016/bs.ampbs.2016.07.003     Document Type: Chapter
Times cited : (33)

References (198)
  • 2
    • 79960974503 scopus 로고    scopus 로고
    • Structural basis of outer membrane protein biogenesis in bacteria
    • Albrecht, R., Zeth, K., Structural basis of outer membrane protein biogenesis in bacteria. The Journal of Biological Chemistry 286:31 (2011), 27792–27803, 10.1074/jbc.M111.238931.
    • (2011) The Journal of Biological Chemistry , vol.286 , Issue.31 , pp. 27792-27803
    • Albrecht, R.1    Zeth, K.2
  • 5
    • 38349035685 scopus 로고    scopus 로고
    • A cross-reactive neisserial antigen encoded by the NMB0035 locus shows high sequence conservation but variable surface accessibility
    • Arenas, J., Abel, A., Sanchez, S., Marzoa, J., Berron, S., van der Ley, P.,.. Ferreiros, C.M., A cross-reactive neisserial antigen encoded by the NMB0035 locus shows high sequence conservation but variable surface accessibility. Journal of Medical Microbiology 57:Pt. 1 (2008), 80–87, 10.1099/jmm.0.47172-0.
    • (2008) Journal of Medical Microbiology , vol.57 , pp. 80-87
    • Arenas, J.1    Abel, A.2    Sanchez, S.3    Marzoa, J.4    Berron, S.5    van der Ley, P.6    Ferreiros, C.M.7
  • 6
    • 84890923974 scopus 로고    scopus 로고
    • Enteric YaiW is a surface-exposed outer membrane lipoprotein that affects sensitivity to an antimicrobial peptide
    • Arnold, M.F., Caro-Hernandez, P., Tan, K., Runti, G., Wehmeier, S., Scocchi, M.,.. Ferguson, G.P., Enteric YaiW is a surface-exposed outer membrane lipoprotein that affects sensitivity to an antimicrobial peptide. Journal of Bacteriology 196:2 (2014), 436–444, 10.1128/jb.01179-13.
    • (2014) Journal of Bacteriology , vol.196 , Issue.2 , pp. 436-444
    • Arnold, M.F.1    Caro-Hernandez, P.2    Tan, K.3    Runti, G.4    Wehmeier, S.5    Scocchi, M.6    Ferguson, G.P.7
  • 7
    • 79951905038 scopus 로고    scopus 로고
    • Structural evidence of alpha-aminoacylated lipoproteins of Staphylococcus aureus
    • Asanuma, M., Kurokawa, K., Ichikawa, R., Ryu, K.H., Chae, J.H., Dohmae, N.,.. Nakayama, H., Structural evidence of alpha-aminoacylated lipoproteins of Staphylococcus aureus. The FEBS Journal 278:5 (2011), 716–728, 10.1111/j.1742-4658.2010.07990.x.
    • (2011) The FEBS Journal , vol.278 , Issue.5 , pp. 716-728
    • Asanuma, M.1    Kurokawa, K.2    Ichikawa, R.3    Ryu, K.H.4    Chae, J.H.5    Dohmae, N.6    Nakayama, H.7
  • 8
    • 33947407705 scopus 로고    scopus 로고
    • CapA, an autotransporter protein of Campylobacter jejuni, mediates association with human epithelial cells and colonization of the chicken gut
    • Ashgar, S.S., Oldfield, N.J., Wooldridge, K.G., Jones, M.A., Irving, G.J., Turner, D.P., Ala'Aldeen, D.A., CapA, an autotransporter protein of Campylobacter jejuni, mediates association with human epithelial cells and colonization of the chicken gut. Journal of Bacteriology 189:5 (2007), 1856–1865, 10.1128/jb.01427-06.
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1856-1865
    • Ashgar, S.S.1    Oldfield, N.J.2    Wooldridge, K.G.3    Jones, M.A.4    Irving, G.J.5    Turner, D.P.6    Ala'Aldeen, D.A.7
  • 9
    • 33645972887 scopus 로고    scopus 로고
    • A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins
    • Babu, M.M., Priya, M.L., Selvan, A.T., Madera, M., Gough, J., Aravind, L., Sankaran, K., A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins. Journal of Bacteriology 188:8 (2006), 2761–2773, 10.1128/JB.188.8.2761-2773.2006.
    • (2006) Journal of Bacteriology , vol.188 , Issue.8 , pp. 2761-2773
    • Babu, M.M.1    Priya, M.L.2    Selvan, A.T.3    Madera, M.4    Gough, J.5    Aravind, L.6    Sankaran, K.7
  • 10
    • 84955147754 scopus 로고    scopus 로고
    • The structure of the beta-barrel assembly machinery complex
    • Bakelar, J., Buchanan, S.K., Noinaj, N., The structure of the beta-barrel assembly machinery complex. Science 351:6269 (2016), 180–186, 10.1126/science.aad3460.
    • (2016) Science , vol.351 , Issue.6269 , pp. 180-186
    • Bakelar, J.1    Buchanan, S.K.2    Noinaj, N.3
  • 11
    • 84897514974 scopus 로고    scopus 로고
    • Mycobacterial outer membrane is a lipid bilayer and the inner membrane is unusually rich in diacyl phosphatidylinositol dimannosides
    • Bansal-Mutalik, R., Nikaido, H., Mycobacterial outer membrane is a lipid bilayer and the inner membrane is unusually rich in diacyl phosphatidylinositol dimannosides. Proceedings of the National Academy of Sciences of the United States of America 111:13 (2014), 4958–4963, 10.1073/pnas.1403078111.
    • (2014) Proceedings of the National Academy of Sciences of the United States of America , vol.111 , Issue.13 , pp. 4958-4963
    • Bansal-Mutalik, R.1    Nikaido, H.2
  • 13
    • 79958120924 scopus 로고    scopus 로고
    • Chapter 6: Structure, function and biogenesis of the Borrelia cell envelope
    • D.S. Samuels J.D. Radolf Caister Academic Press Norfolk, UK
    • Bergström, S., Zückert, W.R., Chapter 6: Structure, function and biogenesis of the Borrelia cell envelope. Samuels, D.S., Radolf, J.D., (eds.) Borrelia: Molecular biology, host interaction and pathogenesis, 2010, Caister Academic Press, Norfolk, UK, 139–166.
    • (2010) Borrelia: Molecular biology, host interaction and pathogenesis , pp. 139-166
    • Bergström, S.1    Zückert, W.R.2
  • 14
    • 84935740159 scopus 로고    scopus 로고
    • Looks can be deceiving: Recent insights into the mechanism of protein secretion by the autotransporter pathway
    • Bernstein, H.D., Looks can be deceiving: Recent insights into the mechanism of protein secretion by the autotransporter pathway. Molecular Microbiology 97:2 (2015), 205–215, 10.1111/mmi.13031.
    • (2015) Molecular Microbiology , vol.97 , Issue.2 , pp. 205-215
    • Bernstein, H.D.1
  • 15
    • 0031747819 scopus 로고    scopus 로고
    • Preparation and characterization of Neisseria meningitidis mutants deficient in production of the human lactoferrin-binding proteins LbpA and LbpB
    • Bonnah, R.A., Schryvers, A.B., Preparation and characterization of Neisseria meningitidis mutants deficient in production of the human lactoferrin-binding proteins LbpA and LbpB. Journal of Bacteriology 180:12 (1998), 3080–3090.
    • (1998) Journal of Bacteriology , vol.180 , Issue.12 , pp. 3080-3090
    • Bonnah, R.A.1    Schryvers, A.B.2
  • 16
    • 0029587287 scopus 로고
    • Biochemical analysis of lactoferrin receptors in the Neisseriaceae: Identification of a second bacterial lactoferrin receptor protein
    • Bonnah, R.A., Yu, R., Schryvers, A.B., Biochemical analysis of lactoferrin receptors in the Neisseriaceae: Identification of a second bacterial lactoferrin receptor protein. Microbial Pathogenesis 19:5 (1995), 285–297.
    • (1995) Microbial Pathogenesis , vol.19 , Issue.5 , pp. 285-297
    • Bonnah, R.A.1    Yu, R.2    Schryvers, A.B.3
  • 17
    • 0029080722 scopus 로고
    • Surface exposure of outer membrane protein and lipopolysaccharide epitopes in Brucella species studied by enzyme-linked immunosorbent assay and flow cytometry
    • Bowden, R.A., Cloeckaert, A., Zygmunt, M.S., Bernard, S., Dubray, G., Surface exposure of outer membrane protein and lipopolysaccharide epitopes in Brucella species studied by enzyme-linked immunosorbent assay and flow cytometry. Infection and Immunity 63:10 (1995), 3945–3952.
    • (1995) Infection and Immunity , vol.63 , Issue.10 , pp. 3945-3952
    • Bowden, R.A.1    Cloeckaert, A.2    Zygmunt, M.S.3    Bernard, S.4    Dubray, G.5
  • 18
    • 0016748566 scopus 로고
    • Covalent lipoprotein from the outer membrane of Escherichia coli
    • Braun, V., Covalent lipoprotein from the outer membrane of Escherichia coli. Biochimica et Biophysica Acta 415:3 (1975), 335–377.
    • (1975) Biochimica et Biophysica Acta , vol.415 , Issue.3 , pp. 335-377
    • Braun, V.1
  • 19
    • 0014594651 scopus 로고
    • Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure
    • Braun, V., Rehn, K., Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure. European Journal of Biochemistry 10:3 (1969), 426–438.
    • (1969) European Journal of Biochemistry , vol.10 , Issue.3 , pp. 426-438
    • Braun, V.1    Rehn, K.2
  • 20
    • 84927539176 scopus 로고    scopus 로고
    • The structure of lactoferrin-binding protein B from Neisseria meningitidis suggests roles in iron acquisition and neutralization of host defences
    • Brooks, C.L., Arutyunova, E., Lemieux, M.J., The structure of lactoferrin-binding protein B from Neisseria meningitidis suggests roles in iron acquisition and neutralization of host defences. Acta Crystallographica. Section F, Structural Biology Communications 70:Pt. 10 (2014), 1312–1317, 10.1107/s2053230x14019372.
    • (2014) Acta Crystallographica. Section F, Structural Biology Communications , vol.70 , pp. 1312-1317
    • Brooks, C.L.1    Arutyunova, E.2    Lemieux, M.J.3
  • 21
    • 29644440332 scopus 로고    scopus 로고
    • Identification of Borrelia burgdorferi outer surface proteins
    • Brooks, C.S., Vuppala, S.R., Jett, A.M., Akins, D.R., Identification of Borrelia burgdorferi outer surface proteins. Infection and Immunity 74:1 (2006), 296–304, 10.1128/iai.74.1.296-304.2006.
    • (2006) Infection and Immunity , vol.74 , Issue.1 , pp. 296-304
    • Brooks, C.S.1    Vuppala, S.R.2    Jett, A.M.3    Akins, D.R.4
  • 22
    • 84928208108 scopus 로고    scopus 로고
    • The molecular mechanism of bacterial lipoprotein modification—How, when and why?
    • Buddelmeijer, N., The molecular mechanism of bacterial lipoprotein modification—How, when and why?. FEMS Microbiology Reviews 39:2 (2015), 246–261, 10.1093/femsre/fuu006.
    • (2015) FEMS Microbiology Reviews , vol.39 , Issue.2 , pp. 246-261
    • Buddelmeijer, N.1
  • 23
    • 63049110964 scopus 로고    scopus 로고
    • The Rcs two-component system regulates expression of lysozyme inhibitors and is induced by exposure to lysozyme
    • Callewaert, L., Vanoirbeek, K.G., Lurquin, I., Michiels, C.W., Aertsen, A., The Rcs two-component system regulates expression of lysozyme inhibitors and is induced by exposure to lysozyme. Journal of Bacteriology 191:6 (2009), 1979–1981, 10.1128/jb.01549-08.
    • (2009) Journal of Bacteriology , vol.191 , Issue.6 , pp. 1979-1981
    • Callewaert, L.1    Vanoirbeek, K.G.2    Lurquin, I.3    Michiels, C.W.4    Aertsen, A.5
  • 24
  • 25
    • 84892898063 scopus 로고    scopus 로고
    • Proteomic profiling of the surface-exposed cell envelope proteins of Caulobacter crescentus
    • Cao, Y., Bazemore-Walker, C.R., Proteomic profiling of the surface-exposed cell envelope proteins of Caulobacter crescentus. Journal of Proteomics 97 (2014), 187–194, 10.1016/j.jprot.2013.08.011.
    • (2014) Journal of Proteomics , vol.97 , pp. 187-194
    • Cao, Y.1    Bazemore-Walker, C.R.2
  • 26
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban, M.J., Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. Journal of Molecular Biology 104:3 (1976), 541–555.
    • (1976) Journal of Molecular Biology , vol.104 , Issue.3 , pp. 541-555
    • Casadaban, M.J.1
  • 27
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban, M.J., Cohen, S.N., Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. Journal of Molecular Biology 138:2 (1980), 179–207.
    • (1980) Journal of Molecular Biology , vol.138 , Issue.2 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 29
    • 84855394288 scopus 로고    scopus 로고
    • Probing the Borrelia burgdorferi surface lipoprotein secretion pathway using a conditionally folding protein domain
    • Chen, S., Zuckert, W.R., Probing the Borrelia burgdorferi surface lipoprotein secretion pathway using a conditionally folding protein domain. Journal of Bacteriology 193:23 (2011), 6724–6732, 10.1128/jb.06042-11.
    • (2011) Journal of Bacteriology , vol.193 , Issue.23 , pp. 6724-6732
    • Chen, S.1    Zuckert, W.R.2
  • 31
    • 84919922342 scopus 로고    scopus 로고
    • Detecting envelope stress by monitoring beta-barrel assembly
    • Cho, S.H., Szewczyk, J., Pesavento, C., Zietek, M., Banzhaf, M., Roszczenko, P.,.. Collet, J.F., Detecting envelope stress by monitoring beta-barrel assembly. Cell 159:7 (2014), 1652–1664, 10.1016/j.cell.2014.11.045.
    • (2014) Cell , vol.159 , Issue.7 , pp. 1652-1664
    • Cho, S.H.1    Szewczyk, J.2    Pesavento, C.3    Zietek, M.4    Banzhaf, M.5    Roszczenko, P.6    Collet, J.F.7
  • 32
    • 0025608125 scopus 로고
    • Identification of seven surface-exposed Brucella outer membrane proteins by use of monoclonal antibodies: Immunogold labeling for electron microscopy and enzyme-linked immunosorbent assay
    • Cloeckaert, A., de Wergifosse, P., Dubray, G., Limet, J.N., Identification of seven surface-exposed Brucella outer membrane proteins by use of monoclonal antibodies: Immunogold labeling for electron microscopy and enzyme-linked immunosorbent assay. Infection and Immunity 58:12 (1990), 3980–3987.
    • (1990) Infection and Immunity , vol.58 , Issue.12 , pp. 3980-3987
    • Cloeckaert, A.1    de Wergifosse, P.2    Dubray, G.3    Limet, J.N.4
  • 34
    • 0028073695 scopus 로고
    • Iron piracy: Acquisition of transferrin-bound iron by bacterial pathogens
    • Cornelissen, C.N., Sparling, P.F., Iron piracy: Acquisition of transferrin-bound iron by bacterial pathogens. Molecular Microbiology 14:5 (1994), 843–850.
    • (1994) Molecular Microbiology , vol.14 , Issue.5 , pp. 843-850
    • Cornelissen, C.N.1    Sparling, P.F.2
  • 35
    • 0029913326 scopus 로고    scopus 로고
    • Binding and surface exposure characteristics of the gonococcal transferrin receptor are dependent on both transferrin-binding proteins
    • Cornelissen, C.N., Sparling, P.F., Binding and surface exposure characteristics of the gonococcal transferrin receptor are dependent on both transferrin-binding proteins. Journal of Bacteriology 178:5 (1996), 1437–1444.
    • (1996) Journal of Bacteriology , vol.178 , Issue.5 , pp. 1437-1444
    • Cornelissen, C.N.1    Sparling, P.F.2
  • 37
    • 0035903666 scopus 로고    scopus 로고
    • Subtilisin-like autotransporter serves as maturation protease in a bacterial secretion pathway
    • Coutte, L., Antoine, R., Drobecq, H., Locht, C., Jacob-Dubuisson, F., Subtilisin-like autotransporter serves as maturation protease in a bacterial secretion pathway. The EMBO Journal 20:18 (2001), 5040–5048, 10.1093/emboj/20.18.5040.
    • (2001) The EMBO Journal , vol.20 , Issue.18 , pp. 5040-5048
    • Coutte, L.1    Antoine, R.2    Drobecq, H.3    Locht, C.4    Jacob-Dubuisson, F.5
  • 39
    • 79951809756 scopus 로고    scopus 로고
    • The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli
    • Cowles, C.E., Li, Y., Semmelhack, M.F., Cristea, I.M., Silhavy, T.J., The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli. Molecular Microbiology 79:5 (2011), 1168–1181, 10.1111/j.1365-2958.2011.07539.x.
    • (2011) Molecular Microbiology , vol.79 , Issue.5 , pp. 1168-1181
    • Cowles, C.E.1    Li, Y.2    Semmelhack, M.F.3    Cristea, I.M.4    Silhavy, T.J.5
  • 40
    • 0242417007 scopus 로고    scopus 로고
    • LipL21 is a novel surface-exposed lipoprotein of pathogenic Leptospira species
    • Cullen, P.A., Haake, D.A., Bulach, D.M., Zuerner, R.L., Adler, B., LipL21 is a novel surface-exposed lipoprotein of pathogenic Leptospira species. Infection and Immunity 71:5 (2003), 2414–2421.
    • (2003) Infection and Immunity , vol.71 , Issue.5 , pp. 2414-2421
    • Cullen, P.A.1    Haake, D.A.2    Bulach, D.M.3    Zuerner, R.L.4    Adler, B.5
  • 44
    • 0023375651 scopus 로고
    • Export and secretion of the lipoprotein pullulanase by Klebsiella pneumoniae
    • d'Enfert, C., Chapon, C., Pugsley, A.P., Export and secretion of the lipoprotein pullulanase by Klebsiella pneumoniae. Molecular Microbiology 1:1 (1987), 107–116.
    • (1987) Molecular Microbiology , vol.1 , Issue.1 , pp. 107-116
    • d'Enfert, C.1    Chapon, C.2    Pugsley, A.P.3
  • 45
    • 0023441713 scopus 로고
    • Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase
    • d'Enfert, C., Ryter, A., Pugsley, A.P., Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase. The EMBO Journal 6:11 (1987), 3531–3538.
    • (1987) The EMBO Journal , vol.6 , Issue.11 , pp. 3531-3538
    • d'Enfert, C.1    Ryter, A.2    Pugsley, A.P.3
  • 46
    • 34447283105 scopus 로고    scopus 로고
    • Identification of transferrin-binding domains in TbpB expressed by Neisseria gonorrhoeae
    • DeRocco, A.J., Cornelissen, C.N., Identification of transferrin-binding domains in TbpB expressed by Neisseria gonorrhoeae. Infection and Immunity 75:7 (2007), 3220–3232, 10.1128/iai.00072-07.
    • (2007) Infection and Immunity , vol.75 , Issue.7 , pp. 3220-3232
    • DeRocco, A.J.1    Cornelissen, C.N.2
  • 47
    • 0021800753 scopus 로고
    • Inhibition of prolipoprotein signal peptidase by globomycin
    • Dev, I.K., Harvey, R.J., Ray, P.H., Inhibition of prolipoprotein signal peptidase by globomycin. The Journal of Biological Chemistry 260:10 (1985), 5891–5894.
    • (1985) The Journal of Biological Chemistry , vol.260 , Issue.10 , pp. 5891-5894
    • Dev, I.K.1    Harvey, R.J.2    Ray, P.H.3
  • 48
    • 27844443566 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea
    • Dilks, K., Gimenez, M.I., Pohlschroder, M., Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea. Journal of Bacteriology 187:23 (2005), 8104–8113, 10.1128/jb.187.23.8104-8113.2005.
    • (2005) Journal of Bacteriology , vol.187 , Issue.23 , pp. 8104-8113
    • Dilks, K.1    Gimenez, M.I.2    Pohlschroder, M.3
  • 49
    • 33750892424 scopus 로고    scopus 로고
    • Wza the translocon for E. coli capsular polysaccharides defines a new class of membrane protein
    • Dong, C., Beis, K., Nesper, J., Brunkan-Lamontagne, A.L., Clarke, B.R., Whitfield, C., Naismith, J.H., Wza the translocon for E. coli capsular polysaccharides defines a new class of membrane protein. Nature 444:7116 (2006), 226–229, 10.1038/nature05267.
    • (2006) Nature , vol.444 , Issue.7116 , pp. 226-229
    • Dong, C.1    Beis, K.2    Nesper, J.3    Brunkan-Lamontagne, A.L.4    Clarke, B.R.5    Whitfield, C.6    Naismith, J.H.7
  • 51
    • 84953213332 scopus 로고    scopus 로고
    • Structural basis of pullulanase membrane binding and secretion revealed by X-ray crystallography, molecular dynamics and biochemical analysis
    • East, A., Mechaly, A.E., Huysmans, G.H., Bernarde, C., Tello-Manigne, D., Nadeau, N.,.. Francetic, O., Structural basis of pullulanase membrane binding and secretion revealed by X-ray crystallography, molecular dynamics and biochemical analysis. Structure 24:1 (2016), 92–104, 10.1016/j.str.2015.10.023.
    • (2016) Structure , vol.24 , Issue.1 , pp. 92-104
    • East, A.1    Mechaly, A.E.2    Huysmans, G.H.3    Bernarde, C.4    Tello-Manigne, D.5    Nadeau, N.6    Francetic, O.7
  • 52
    • 58649086297 scopus 로고    scopus 로고
    • Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly
    • Epstein, E.A., Reizian, M.A., Chapman, M.R., Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly. Journal of Bacteriology 191:2 (2009), 608–615, 10.1128/jb.01244-08.
    • (2009) Journal of Bacteriology , vol.191 , Issue.2 , pp. 608-615
    • Epstein, E.A.1    Reizian, M.A.2    Chapman, M.R.3
  • 53
    • 77957342591 scopus 로고    scopus 로고
    • Antimicrobial peptides activate the Rcs regulon through the outer membrane lipoprotein RcsF
    • Farris, C., Sanowar, S., Bader, M.W., Pfuetzner, R., Miller, S.I., Antimicrobial peptides activate the Rcs regulon through the outer membrane lipoprotein RcsF. Journal of Bacteriology 192:19 (2010), 4894–4903, 10.1128/jb.00505-10.
    • (2010) Journal of Bacteriology , vol.192 , Issue.19 , pp. 4894-4903
    • Farris, C.1    Sanowar, S.2    Bader, M.W.3    Pfuetzner, R.4    Miller, S.I.5
  • 55
    • 84902172649 scopus 로고    scopus 로고
    • Identification of a Haemophilus influenzae factor H-Binding lipoprotein involved in serum resistance
    • Fleury, C., Su, Y.C., Hallstrom, T., Sandblad, L., Zipfel, P.F., Riesbeck, K., Identification of a Haemophilus influenzae factor H-Binding lipoprotein involved in serum resistance. Journal of Immunology 192:12 (2014), 5913–5923, 10.4049/jimmunol.1303449.
    • (2014) Journal of Immunology , vol.192 , Issue.12 , pp. 5913-5923
    • Fleury, C.1    Su, Y.C.2    Hallstrom, T.3    Sandblad, L.4    Zipfel, P.F.5    Riesbeck, K.6
  • 56
    • 84905715131 scopus 로고    scopus 로고
    • Identification of Coxiella burnetii surface-exposed and cell envelope associated proteins using a combined bioinformatics plus proteomics strategy
    • Flores-Ramirez, G., Jankovicova, B., Bilkova, Z., Miernyk, J.A., Skultety, L., Identification of Coxiella burnetii surface-exposed and cell envelope associated proteins using a combined bioinformatics plus proteomics strategy. Proteomics 14:16 (2014), 1868–1881, 10.1002/pmic.201300338.
    • (2014) Proteomics , vol.14 , Issue.16 , pp. 1868-1881
    • Flores-Ramirez, G.1    Jankovicova, B.2    Bilkova, Z.3    Miernyk, J.A.4    Skultety, L.5
  • 57
    • 3843095033 scopus 로고    scopus 로고
    • Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway
    • Froderberg, L., Houben, E.N., Baars, L., Luirink, J., de Gier, J.W., Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway. The Journal of Biological Chemistry 279:30 (2004), 31026–31032, 10.1074/jbc.M403229200.
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.30 , pp. 31026-31032
    • Froderberg, L.1    Houben, E.N.2    Baars, L.3    Luirink, J.4    de Gier, J.W.5
  • 58
    • 0037044719 scopus 로고    scopus 로고
    • Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals
    • Fukuda, A., Matsuyama, S., Hara, T., Nakayama, J., Nagasawa, H., Tokuda, H., Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals. The Journal of Biological Chemistry 277:45 (2002), 43512–43518, 10.1074/jbc.M206816200.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 43512-43518
    • Fukuda, A.1    Matsuyama, S.2    Hara, T.3    Nakayama, J.4    Nagasawa, H.5    Tokuda, H.6
  • 59
    • 0026010463 scopus 로고
    • The protein sequence responsible for lipoprotein membrane localization in Escherichia coli exhibits remarkable specificity
    • Gennity, J.M., Inouye, M., The protein sequence responsible for lipoprotein membrane localization in Escherichia coli exhibits remarkable specificity. The Journal of Biological Chemistry 266:25 (1991), 16458–16464.
    • (1991) The Journal of Biological Chemistry , vol.266 , Issue.25 , pp. 16458-16464
    • Gennity, J.M.1    Inouye, M.2
  • 60
    • 36549088956 scopus 로고    scopus 로고
    • Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins
    • Gimenez, M.I., Dilks, K., Pohlschroder, M., Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins. Molecular Microbiology 66:6 (2007), 1597–1606, 10.1111/j.1365-2958.2007.06034.x.
    • (2007) Molecular Microbiology , vol.66 , Issue.6 , pp. 1597-1606
    • Gimenez, M.I.1    Dilks, K.2    Pohlschroder, M.3
  • 61
    • 84946837764 scopus 로고    scopus 로고
    • Escherichia coli lipoprotein binds human plasminogen via an intramolecular domain
    • Gonzalez, T., Gaultney, R.A., Floden, A.M., Brissette, C.A., Escherichia coli lipoprotein binds human plasminogen via an intramolecular domain. Frontiers in Microbiology, 6, 2015, 1095, 10.3389/fmicb.2015.01095.
    • (2015) Frontiers in Microbiology , vol.6 , pp. 1095
    • Gonzalez, T.1    Gaultney, R.A.2    Floden, A.M.3    Brissette, C.A.4
  • 63
    • 84879889804 scopus 로고    scopus 로고
    • Autotransporter secretion: Varying on a theme
    • Grijpstra, J., Arenas, J., Rutten, L., Tommassen, J., Autotransporter secretion: Varying on a theme. Research in Microbiology 164:6 (2013), 562–582, 10.1016/j.resmic.2013.03.010.
    • (2013) Research in Microbiology , vol.164 , Issue.6 , pp. 562-582
    • Grijpstra, J.1    Arenas, J.2    Rutten, L.3    Tommassen, J.4
  • 64
    • 84960117472 scopus 로고    scopus 로고
    • Structural basis of outer membrane protein insertion by the BAM complex
    • Gu, Y., Li, H., Dong, H., Zeng, Y., Zhang, Z., Paterson, N.G.,.. Dong, C., Structural basis of outer membrane protein insertion by the BAM complex. Nature 531:7592 (2016), 64–69, 10.1038/nature17199.
    • (2016) Nature , vol.531 , Issue.7592 , pp. 64-69
    • Gu, Y.1    Li, H.2    Dong, H.3    Zeng, Y.4    Zhang, Z.5    Paterson, N.G.6    Dong, C.7
  • 65
    • 0026111879 scopus 로고
    • Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli
    • Gupta, S.D., Wu, H.C., Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli. FEMS Microbiology Letters 62:1 (1991), 37–41.
    • (1991) FEMS Microbiology Letters , vol.62 , Issue.1 , pp. 37-41
    • Gupta, S.D.1    Wu, H.C.2
  • 66
    • 0141890241 scopus 로고    scopus 로고
    • Mechanism underlying the inner membrane retention of Escherichia coli lipoproteins caused by Lol avoidance signals
    • Hara, T., Matsuyama, S., Tokuda, H., Mechanism underlying the inner membrane retention of Escherichia coli lipoproteins caused by Lol avoidance signals. The Journal of Biological Chemistry 278:41 (2003), 40408–40414, 10.1074/jbc.M307836200.
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.41 , pp. 40408-40414
    • Hara, T.1    Matsuyama, S.2    Tokuda, H.3
  • 67
    • 84898670675 scopus 로고    scopus 로고
    • Roles of the protruding loop of factor B essential for the localization of lipoproteins (LolB) in the anchoring of bacterial triacylated proteins to the outer membrane
    • Hayashi, Y., Tsurumizu, R., Tsukahara, J., Takeda, K., Narita, S., Mori, M.,.. Tokuda, H., Roles of the protruding loop of factor B essential for the localization of lipoproteins (LolB) in the anchoring of bacterial triacylated proteins to the outer membrane. The Journal of Biological Chemistry 289:15 (2014), 10530–10539, 10.1074/jbc.M113.539270.
    • (2014) The Journal of Biological Chemistry , vol.289 , Issue.15 , pp. 10530-10539
    • Hayashi, Y.1    Tsurumizu, R.2    Tsukahara, J.3    Takeda, K.4    Narita, S.5    Mori, M.6    Tokuda, H.7
  • 69
    • 84991449813 scopus 로고    scopus 로고
    • Slam is an outer membrane protein that is required for the surface display of lipidated virulence factors in Neisseria
    • Hooda, Y., Lai, C.C.-L., Judd, A., Buckwalter, C.M., Shin, H.E., Gray-Owen, S.D., Moraes, T.F., Slam is an outer membrane protein that is required for the surface display of lipidated virulence factors in Neisseria. Nature Microbiology, 1, 2016, 16009, 10.1038/nmicrobiol.2016.9.
    • (2016) Nature Microbiology , vol.1 , pp. 16009
    • Hooda, Y.1    Lai, C.C.-L.2    Judd, A.3    Buckwalter, C.M.4    Shin, H.E.5    Gray-Owen, S.D.6    Moraes, T.F.7
  • 70
    • 46249094238 scopus 로고    scopus 로고
    • Borrelia burgdorferi surface-localized proteins expressed during persistent murine infection are conserved among diverse Borrelia spp
    • Hughes, J.L., Nolder, C.L., Nowalk, A.J., Clifton, D.R., Howison, R.R., Schmit, V.L.,.. Carroll, J.A., Borrelia burgdorferi surface-localized proteins expressed during persistent murine infection are conserved among diverse Borrelia spp. Infection and Immunity 76:6 (2008), 2498–2511, 10.1128/iai.01583-07.
    • (2008) Infection and Immunity , vol.76 , Issue.6 , pp. 2498-2511
    • Hughes, J.L.1    Nolder, C.L.2    Nowalk, A.J.3    Clifton, D.R.4    Howison, R.R.5    Schmit, V.L.6    Carroll, J.A.7
  • 71
    • 0019309069 scopus 로고
    • Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin
    • Hussain, M., Ichihara, S., Mizushima, S., Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin. The Journal of Biological Chemistry 255:8 (1980), 3707–3712.
    • (1980) The Journal of Biological Chemistry , vol.255 , Issue.8 , pp. 3707-3712
    • Hussain, M.1    Ichihara, S.2    Mizushima, S.3
  • 72
    • 73149118024 scopus 로고    scopus 로고
    • Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane
    • Ieva, R., Bernstein, H.D., Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane. Proceedings of the National Academy of Sciences of the United States of America 106:45 (2009), 19120–19125, 10.1073/pnas.0907912106.
    • (2009) Proceedings of the National Academy of Sciences of the United States of America , vol.106 , Issue.45 , pp. 19120-19125
    • Ieva, R.1    Bernstein, H.D.2
  • 74
    • 0035103994 scopus 로고    scopus 로고
    • JlpA, a novel surface-exposed lipoprotein specific to Campylobacter jejuni, mediates adherence to host epithelial cells
    • Jin, S., Joe, A., Lynett, J., Hani, E.K., Sherman, P., Chan, V.L., JlpA, a novel surface-exposed lipoprotein specific to Campylobacter jejuni, mediates adherence to host epithelial cells. Molecular Microbiology 39:5 (2001), 1225–1236.
    • (2001) Molecular Microbiology , vol.39 , Issue.5 , pp. 1225-1236
    • Jin, S.1    Joe, A.2    Lynett, J.3    Hani, E.K.4    Sherman, P.5    Chan, V.L.6
  • 75
    • 84905657805 scopus 로고    scopus 로고
    • The cross-talk between spirochetal lipoproteins and immunity
    • Kelesidis, T., The cross-talk between spirochetal lipoproteins and immunity. Frontiers in Immunology, 5, 2014, 310, 10.3389/fimmu.2014.00310.
    • (2014) Frontiers in Immunology , vol.5 , pp. 310
    • Kelesidis, T.1
  • 77
    • 84948706537 scopus 로고    scopus 로고
    • A meningococcal vaccine antigen engineered to increase thermal stability and stabilize protective epitopes
    • Konar, M., Pajon, R., Beernink, P.T., A meningococcal vaccine antigen engineered to increase thermal stability and stabilize protective epitopes. Proceedings of the National Academy of Sciences of the United States of America 112:48 (2015), 14823–14828, 10.1073/pnas.1507829112.
    • (2015) Proceedings of the National Academy of Sciences of the United States of America , vol.112 , Issue.48 , pp. 14823-14828
    • Konar, M.1    Pajon, R.2    Beernink, P.T.3
  • 79
    • 46049115447 scopus 로고    scopus 로고
    • Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices
    • Koropatkin, N.M., Martens, E.C., Gordon, J.I., Smith, T.J., Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices. Structure 16:7 (2008), 1105–1115, 10.1016/j.str.2008.03.017.
    • (2008) Structure , vol.16 , Issue.7 , pp. 1105-1115
    • Koropatkin, N.M.1    Martens, E.C.2    Gordon, J.I.3    Smith, T.J.4
  • 80
    • 0038690451 scopus 로고    scopus 로고
    • Insight into the structure and function of the transferrin receptor from Neisseria meningitidis using microcalorimetric techniques
    • Krell, T., Renauld-Mongenie, G., Nicolai, M.C., Fraysse, S., Chevalier, M., Berard, Y.,.. Lissolo, L., Insight into the structure and function of the transferrin receptor from Neisseria meningitidis using microcalorimetric techniques. The Journal of Biological Chemistry 278:17 (2003), 14712–14722, 10.1074/jbc.M204461200.
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.17 , pp. 14712-14722
    • Krell, T.1    Renauld-Mongenie, G.2    Nicolai, M.C.3    Fraysse, S.4    Chevalier, M.5    Berard, Y.6    Lissolo, L.7
  • 81
    • 0035283085 scopus 로고    scopus 로고
    • Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi
    • Kumaran, D., Eswaramoorthy, S., Luft, B.J., Koide, S., Dunn, J.J., Lawson, C.L., Swaminathan, S., Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi. The EMBO Journal 20:5 (2001), 971–978, 10.1093/emboj/20.5.971.
    • (2001) The EMBO Journal , vol.20 , Issue.5 , pp. 971-978
    • Kumaran, D.1    Eswaramoorthy, S.2    Luft, B.J.3    Koide, S.4    Dunn, J.J.5    Lawson, C.L.6    Swaminathan, S.7
  • 82
    • 79958125256 scopus 로고    scopus 로고
    • Surface localization determinants of Borrelia OspC/Vsp family lipoproteins
    • Kumru, O.S., Schulze, R.J., Rodnin, M.V., Ladokhin, A.S., Zuckert, W.R., Surface localization determinants of Borrelia OspC/Vsp family lipoproteins. Journal of Bacteriology 193:11 (2011), 2814–2825, 10.1128/jb.00015-11.
    • (2011) Journal of Bacteriology , vol.193 , Issue.11 , pp. 2814-2825
    • Kumru, O.S.1    Schulze, R.J.2    Rodnin, M.V.3    Ladokhin, A.S.4    Zuckert, W.R.5
  • 83
    • 84859739265 scopus 로고    scopus 로고
    • Novel bacterial lipoprotein structures conserved in low-GC content gram-positive bacteria are recognized by Toll-like receptor 2
    • Kurokawa, K., Ryu, K.H., Ichikawa, R., Masuda, A., Kim, M.S., Lee, H.,.. Lee, B.L., Novel bacterial lipoprotein structures conserved in low-GC content gram-positive bacteria are recognized by Toll-like receptor 2. The Journal of Biological Chemistry 287:16 (2012), 13170–13181, 10.1074/jbc.M111.292235.
    • (2012) The Journal of Biological Chemistry , vol.287 , Issue.16 , pp. 13170-13181
    • Kurokawa, K.1    Ryu, K.H.2    Ichikawa, R.3    Masuda, A.4    Kim, M.S.5    Lee, H.6    Lee, B.L.7
  • 84
    • 84896734943 scopus 로고    scopus 로고
    • A discrete genetic locus confers xyloglucan metabolism in select human gut Bacteroidetes
    • Larsbrink, J., Rogers, T.E., Hemsworth, G.R., McKee, L.S., Tauzin, A.S., Spadiut, O.,.. Brumer, H., A discrete genetic locus confers xyloglucan metabolism in select human gut Bacteroidetes. Nature 506:7489 (2014), 498–502, 10.1038/nature12907.
    • (2014) Nature , vol.506 , Issue.7489 , pp. 498-502
    • Larsbrink, J.1    Rogers, T.E.2    Hemsworth, G.R.3    McKee, L.S.4    Tauzin, A.S.5    Spadiut, O.6    Brumer, H.7
  • 85
    • 40449091818 scopus 로고    scopus 로고
    • The Rcs phosphorelay is a cell envelope stress response activated by peptidoglycan stress and contributes to intrinsic antibiotic resistance
    • Laubacher, M.E., Ades, S.E., The Rcs phosphorelay is a cell envelope stress response activated by peptidoglycan stress and contributes to intrinsic antibiotic resistance. Journal of Bacteriology 190:6 (2008), 2065–2074, 10.1128/jb.01740-07.
    • (2008) Journal of Bacteriology , vol.190 , Issue.6 , pp. 2065-2074
    • Laubacher, M.E.1    Ades, S.E.2
  • 86
    • 78649909904 scopus 로고    scopus 로고
    • Phosphate starvation triggers production and secretion of an extracellular lipoprotein in Caulobacter crescentus
    • Le Blastier, S., Hamels, A., Cabeen, M., Schille, L., Tilquin, F., Dieu, M.,.. Matroule, J.Y., Phosphate starvation triggers production and secretion of an extracellular lipoprotein in Caulobacter crescentus. PLoS One, 5(12), 2010, e14198, 10.1371/journal.pone.0014198.
    • (2010) PLoS One , vol.5 , Issue.12 , pp. e14198
    • Le Blastier, S.1    Hamels, A.2    Cabeen, M.3    Schille, L.4    Tilquin, F.5    Dieu, M.6    Matroule, J.Y.7
  • 87
    • 75149192610 scopus 로고    scopus 로고
    • Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins
    • Lenhart, T.R., Akins, D.R., Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins. Molecular Microbiology 75:3 (2010), 692–709, 10.1111/j.1365-2958.2009.07015.x.
    • (2010) Molecular Microbiology , vol.75 , Issue.3 , pp. 692-709
    • Lenhart, T.R.1    Akins, D.R.2
  • 88
    • 27444447753 scopus 로고    scopus 로고
    • Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages
    • Leuzzi, R., Serino, L., Scarselli, M., Savino, S., Fontana, M.R., Monaci, E.,.. Pizza, M., Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages. Molecular Microbiology 58:3 (2005), 669–681, 10.1111/j.1365-2958.2005.04859.x.
    • (2005) Molecular Microbiology , vol.58 , Issue.3 , pp. 669-681
    • Leuzzi, R.1    Serino, L.2    Scarselli, M.3    Savino, S.4    Fontana, M.R.5    Monaci, E.6    Pizza, M.7
  • 89
    • 79955767087 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC
    • Leverrier, P., Declercq, J.P., Denoncin, K., Vertommen, D., Hiniker, A., Cho, S.H., Collet, J.F., Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC. The Journal of Biological Chemistry 286:19 (2011), 16734–16742, 10.1074/jbc.M111.224865.
    • (2011) The Journal of Biological Chemistry , vol.286 , Issue.19 , pp. 16734-16742
    • Leverrier, P.1    Declercq, J.P.2    Denoncin, K.3    Vertommen, D.4    Hiniker, A.5    Cho, S.H.6    Collet, J.F.7
  • 90
    • 51549111175 scopus 로고    scopus 로고
    • Novel inner membrane retention signals in Pseudomonas aeruginosa lipoproteins
    • Lewenza, S., Mhlanga, M.M., Pugsley, A.P., Novel inner membrane retention signals in Pseudomonas aeruginosa lipoproteins. Journal of Bacteriology 190:18 (2008), 6119–6125, 10.1128/jb.00603-08.
    • (2008) Journal of Bacteriology , vol.190 , Issue.18 , pp. 6119-6125
    • Lewenza, S.1    Mhlanga, M.M.2    Pugsley, A.P.3
  • 91
    • 0031866123 scopus 로고    scopus 로고
    • Identification and molecular analysis of lbpBA, which encodes the two-component meningococcal lactoferrin receptor
    • Lewis, L.A., Rohde, K., Gipson, M., Behrens, B., Gray, E., Toth, S.I.,.. Dyer, D.W., Identification and molecular analysis of lbpBA, which encodes the two-component meningococcal lactoferrin receptor. Infection and Immunity 66:6 (1998), 3017–3023.
    • (1998) Infection and Immunity , vol.66 , Issue.6 , pp. 3017-3023
    • Lewis, L.A.1    Rohde, K.2    Gipson, M.3    Behrens, B.4    Gray, E.5    Toth, S.I.6    Dyer, D.W.7
  • 92
    • 84899550455 scopus 로고    scopus 로고
    • Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources
    • Li, G.W., Burkhardt, D., Gross, C., Weissman, J.S., Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources. Cell 157:3 (2014), 624–635, 10.1016/j.cell.2014.02.033.
    • (2014) Cell , vol.157 , Issue.3 , pp. 624-635
    • Li, G.W.1    Burkhardt, D.2    Gross, C.3    Weissman, J.S.4
  • 94
    • 22144492215 scopus 로고    scopus 로고
    • Determining the functionality of putative Tat-dependent signal peptides in Streptomyces coelicolor A3(2) by using two different reporter proteins
    • Li, H., Jacques, P.E., Ghinet, M.G., Brzezinski, R., Morosoli, R., Determining the functionality of putative Tat-dependent signal peptides in Streptomyces coelicolor A3(2) by using two different reporter proteins. Microbiology 151:Pt. 7 (2005), 2189–2198, 10.1099/mic.0.27893-0.
    • (2005) Microbiology , vol.151 , pp. 2189-2198
    • Li, H.1    Jacques, P.E.2    Ghinet, M.G.3    Brzezinski, R.4    Morosoli, R.5
  • 95
    • 84887218070 scopus 로고    scopus 로고
    • Outer membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: Paradigm deviations in H. pylori
    • Liechti, G., Goldberg, J.B., Outer membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: Paradigm deviations in H. pylori. Frontiers in Cellular and Infection Microbiology, 2, 2012, 29, 10.3389/fcimb.2012.00029.
    • (2012) Frontiers in Cellular and Infection Microbiology , vol.2 , pp. 29
    • Liechti, G.1    Goldberg, J.B.2
  • 98
    • 0036091972 scopus 로고    scopus 로고
    • DOLOP—Database of bacterial lipoproteins
    • Madan Babu, M., Sankaran, K., DOLOP—Database of bacterial lipoproteins. Bioinformatics 18:4 (2002), 641–643.
    • (2002) Bioinformatics , vol.18 , Issue.4 , pp. 641-643
    • Madan Babu, M.1    Sankaran, K.2
  • 99
    • 25144451503 scopus 로고    scopus 로고
    • The Rcs phosphorelay: A complex signal transduction system
    • Majdalani, N., Gottesman, S., The Rcs phosphorelay: A complex signal transduction system. Annual Review of Microbiology 59 (2005), 379–405, 10.1146/annurev.micro.59.050405.101230.
    • (2005) Annual Review of Microbiology , vol.59 , pp. 379-405
    • Majdalani, N.1    Gottesman, S.2
  • 100
    • 80051555789 scopus 로고    scopus 로고
    • The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation
    • Manfredi, P., Renzi, F., Mally, M., Sauteur, L., Schmaler, M., Moes, S.,.. Cornelis, G.R., The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation. Molecular Microbiology 81:4 (2011), 1050–1060, 10.1111/j.1365-2958.2011.07750.x.
    • (2011) Molecular Microbiology , vol.81 , Issue.4 , pp. 1050-1060
    • Manfredi, P.1    Renzi, F.2    Mally, M.3    Sauteur, L.4    Schmaler, M.5    Moes, S.6    Cornelis, G.R.7
  • 101
    • 0019004444 scopus 로고
    • Outer membrane of Escherichia coli: Properties of the F sex factor traT protein which is involved in surface exclusion
    • Manning, P.A., Beutin, L., Achtman, M., Outer membrane of Escherichia coli: Properties of the F sex factor traT protein which is involved in surface exclusion. Journal of Bacteriology 142:1 (1980), 285–294.
    • (1980) Journal of Bacteriology , vol.142 , Issue.1 , pp. 285-294
    • Manning, P.A.1    Beutin, L.2    Achtman, M.3
  • 102
    • 84953299648 scopus 로고    scopus 로고
    • Crystal structure of E. coli lipoprotein diacylglyceryl transferase
    • Mao, G., Zhao, Y., Kang, X., Li, Z., Zhang, Y., Wang, X.,.. Zhang, X.C., Crystal structure of E. coli lipoprotein diacylglyceryl transferase. Nature Communications, 7, 2016, 10198, 10.1038/ncomms10198.
    • (2016) Nature Communications , vol.7 , pp. 10198
    • Mao, G.1    Zhao, Y.2    Kang, X.3    Li, Z.4    Zhang, Y.5    Wang, X.6    Zhang, X.C.7
  • 103
    • 74249119955 scopus 로고    scopus 로고
    • NMR dynamics and antibody recognition of the meningococcal lipidated outer membrane protein LP2086 in micellar solution
    • Mascioni, A., Moy, F.J., McNeil, L.K., Murphy, E., Bentley, B.E., Camarda, R.,.. Tsao, D.H., NMR dynamics and antibody recognition of the meningococcal lipidated outer membrane protein LP2086 in micellar solution. Biochimica et Biophysica Acta 1798:2 (2010), 87–93, 10.1016/j.bbamem.2009.09.021.
    • (2010) Biochimica et Biophysica Acta , vol.1798 , Issue.2 , pp. 87-93
    • Mascioni, A.1    Moy, F.J.2    McNeil, L.K.3    Murphy, E.4    Bentley, B.E.5    Camarda, R.6    Tsao, D.H.7
  • 106
    • 33845968454 scopus 로고    scopus 로고
    • LipL46 is a novel surface-exposed lipoprotein expressed during leptospiral dissemination in the mammalian host
    • Matsunaga, J., Werneid, K., Zuerner, R.L., Frank, A., Haake, D.A., LipL46 is a novel surface-exposed lipoprotein expressed during leptospiral dissemination in the mammalian host. Microbiology 152:Pt. 12 (2006), 3777–3786, 10.1099/mic.0.29162-0.
    • (2006) Microbiology , vol.152 , pp. 3777-3786
    • Matsunaga, J.1    Werneid, K.2    Zuerner, R.L.3    Frank, A.4    Haake, D.A.5
  • 107
    • 0028981022 scopus 로고
    • A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane
    • Matsuyama, S., Tajima, T., Tokuda, H., A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane. The EMBO Journal 14:14 (1995), 3365–3372.
    • (1995) The EMBO Journal , vol.14 , Issue.14 , pp. 3365-3372
    • Matsuyama, S.1    Tajima, T.2    Tokuda, H.3
  • 108
    • 0030663775 scopus 로고    scopus 로고
    • A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli
    • Matsuyama, S., Yokota, N., Tokuda, H., A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli. The EMBO Journal 16:23 (1997), 6947–6955, 10.1093/emboj/16.23.6947.
    • (1997) The EMBO Journal , vol.16 , Issue.23 , pp. 6947-6955
    • Matsuyama, S.1    Yokota, N.2    Tokuda, H.3
  • 110
  • 111
    • 0035850777 scopus 로고    scopus 로고
    • Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB
    • Miyamoto, A., Matsuyama, S., Tokuda, H., Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB. Biochemical and Biophysical Research Communications 287:5 (2001), 1125–1128, 10.1006/bbrc.2001.5705.
    • (2001) Biochemical and Biophysical Research Communications , vol.287 , Issue.5 , pp. 1125-1128
    • Miyamoto, A.1    Matsuyama, S.2    Tokuda, H.3
  • 112
    • 84871722765 scopus 로고    scopus 로고
    • Functional differentiation of structurally similar membrane subunits of the ABC transporter LolCDE complex
    • Mizutani, M., Mukaiyama, K., Xiao, J., Mori, M., Satou, R., Narita, S.,.. Tokuda, H., Functional differentiation of structurally similar membrane subunits of the ABC transporter LolCDE complex. FEBS Letters 587:1 (2013), 23–29, 10.1016/j.febslet.2012.11.009.
    • (2013) FEBS Letters , vol.587 , Issue.1 , pp. 23-29
    • Mizutani, M.1    Mukaiyama, K.2    Xiao, J.3    Mori, M.4    Satou, R.5    Narita, S.6    Tokuda, H.7
  • 113
    • 84925222674 scopus 로고    scopus 로고
    • The negatively charged regions of lactoferrin binding protein B, an adaptation against anti-microbial peptides
    • Morgenthau, A., Beddek, A., Schryvers, A.B., The negatively charged regions of lactoferrin binding protein B, an adaptation against anti-microbial peptides. PLoS One, 9(1), 2014, e86243, 10.1371/journal.pone.0086243.
    • (2014) PLoS One , vol.9 , Issue.1 , pp. e86243
    • Morgenthau, A.1    Beddek, A.2    Schryvers, A.B.3
  • 114
    • 84889573712 scopus 로고    scopus 로고
    • Bacterial receptors for host transferrin and lactoferrin: Molecular mechanisms and role in host-microbe interactions
    • Morgenthau, A., Pogoutse, A., Adamiak, P., Moraes, T.F., Schryvers, A.B., Bacterial receptors for host transferrin and lactoferrin: Molecular mechanisms and role in host-microbe interactions. Future Microbiology 8:12 (2013), 1575–1585, 10.2217/fmb.13.125.
    • (2013) Future Microbiology , vol.8 , Issue.12 , pp. 1575-1585
    • Morgenthau, A.1    Pogoutse, A.2    Adamiak, P.3    Moraes, T.F.4    Schryvers, A.B.5
  • 115
    • 0026063242 scopus 로고
    • Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II)
    • Munoa, F.J., Miller, K.W., Beers, R., Graham, M., Wu, H.C., Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II). The Journal of Biological Chemistry 266:26 (1991), 17667–17672.
    • (1991) The Journal of Biological Chemistry , vol.266 , Issue.26 , pp. 17667-17672
    • Munoa, F.J.1    Miller, K.W.2    Beers, R.3    Graham, M.4    Wu, H.C.5
  • 116
    • 84882801196 scopus 로고    scopus 로고
    • Understanding the lid movements of LolA in Escherichia coli using molecular dynamics simulation and in silico point mutation
    • Murahari, P., Anishetty, S., Pennathur, G., Understanding the lid movements of LolA in Escherichia coli using molecular dynamics simulation and in silico point mutation. Computational Biology and Chemistry 47 (2013), 71–80, 10.1016/j.compbiolchem.2013.06.005.
    • (2013) Computational Biology and Chemistry , vol.47 , pp. 71-80
    • Murahari, P.1    Anishetty, S.2    Pennathur, G.3
  • 118
    • 34250351484 scopus 로고    scopus 로고
    • Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins
    • Narita, S., Tokuda, H., Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins. The Journal of Biological Chemistry 282:18 (2007), 13372–13378, 10.1074/jbc.M611839200.
    • (2007) The Journal of Biological Chemistry , vol.282 , Issue.18 , pp. 13372-13378
    • Narita, S.1    Tokuda, H.2
  • 119
    • 77954692040 scopus 로고    scopus 로고
    • Sorting of bacterial lipoproteins to the outer membrane by the Lol system
    • Narita, S., Tokuda, H., Sorting of bacterial lipoproteins to the outer membrane by the Lol system. Methods in Molecular Biology 619 (2010), 117–129, 10.1007/978-1-60327-412-8_7.
    • (2010) Methods in Molecular Biology , vol.619 , pp. 117-129
    • Narita, S.1    Tokuda, H.2
  • 120
    • 80052551712 scopus 로고    scopus 로고
    • Overexpression of LolCDE allows deletion of the Escherichia coli gene encoding apolipoprotein N-acyltransferase
    • Narita, S., Tokuda, H., Overexpression of LolCDE allows deletion of the Escherichia coli gene encoding apolipoprotein N-acyltransferase. Journal of Bacteriology 193:18 (2011), 4832–4840, 10.1128/jb.05013-11.
    • (2011) Journal of Bacteriology , vol.193 , Issue.18 , pp. 4832-4840
    • Narita, S.1    Tokuda, H.2
  • 121
    • 84902268313 scopus 로고    scopus 로고
    • Type II secretion system: A magic beanstalk or a protein escalator
    • Nivaskumar, M., Francetic, O., Type II secretion system: A magic beanstalk or a protein escalator. Biochimica et Biophysica Acta 1843:8 (2014), 1568–1577, 10.1016/j.bbamcr.2013.12.020.
    • (2014) Biochimica et Biophysica Acta , vol.1843 , Issue.8 , pp. 1568-1577
    • Nivaskumar, M.1    Francetic, O.2
  • 122
    • 84857783784 scopus 로고    scopus 로고
    • Structural basis for iron piracy by pathogenic Neisseria
    • Noinaj, N., Easley, N.C., Oke, M., Mizuno, N., Gumbart, J., Boura, E.,.. Buchanan, S.K., Structural basis for iron piracy by pathogenic Neisseria. Nature 483:7387 (2012), 53–58, 10.1038/nature10823.
    • (2012) Nature , vol.483 , Issue.7387 , pp. 53-58
    • Noinaj, N.1    Easley, N.C.2    Oke, M.3    Mizuno, N.4    Gumbart, J.5    Boura, E.6    Buchanan, S.K.7
  • 123
    • 54449086634 scopus 로고    scopus 로고
    • Opening and closing of the hydrophobic cavity of LolA coupled to lipoprotein binding and release
    • Oguchi, Y., Takeda, K., Watanabe, S., Yokota, N., Miki, K., Tokuda, H., Opening and closing of the hydrophobic cavity of LolA coupled to lipoprotein binding and release. The Journal of Biological Chemistry 283:37 (2008), 25414–25420, 10.1074/jbc.M804736200.
    • (2008) The Journal of Biological Chemistry , vol.283 , Issue.37 , pp. 25414-25420
    • Oguchi, Y.1    Takeda, K.2    Watanabe, S.3    Yokota, N.4    Miki, K.5    Tokuda, H.6
  • 124
    • 65249085615 scopus 로고    scopus 로고
    • Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB
    • Okuda, S., Tokuda, H., Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB. Proceedings of the National Academy of Sciences of the United States of America 106:14 (2009), 5877–5882, 10.1073/pnas.0900896106.
    • (2009) Proceedings of the National Academy of Sciences of the United States of America , vol.106 , Issue.14 , pp. 5877-5882
    • Okuda, S.1    Tokuda, H.2
  • 125
    • 80053280679 scopus 로고    scopus 로고
    • Lipoprotein sorting in bacteria
    • Okuda, S., Tokuda, H., Lipoprotein sorting in bacteria. Annual Review of Microbiology 65 (2011), 239–259, 10.1146/annurev-micro-090110-102859.
    • (2011) Annual Review of Microbiology , vol.65 , pp. 239-259
    • Okuda, S.1    Tokuda, H.2
  • 126
    • 44749084464 scopus 로고    scopus 로고
    • A short helix in the C-terminal region of LolA is important for the specific membrane localization of lipoproteins
    • Okuda, S., Watanabe, S., Tokuda, H., A short helix in the C-terminal region of LolA is important for the specific membrane localization of lipoproteins. FEBS Letters 582:15 (2008), 2247–2251, 10.1016/j.febslet.2008.05.022.
    • (2008) FEBS Letters , vol.582 , Issue.15 , pp. 2247-2251
    • Okuda, S.1    Watanabe, S.2    Tokuda, H.3
  • 127
    • 84861220038 scopus 로고    scopus 로고
    • Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane
    • Pailler, J., Aucher, W., Pires, M., Buddelmeijer, N., Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane. Journal of Bacteriology 194:9 (2012), 2142–2151, 10.1128/JB.06641-11.
    • (2012) Journal of Bacteriology , vol.194 , Issue.9 , pp. 2142-2151
    • Pailler, J.1    Aucher, W.2    Pires, M.3    Buddelmeijer, N.4
  • 128
    • 0036274609 scopus 로고    scopus 로고
    • A putative three-dimensional targeting motif of polygalacturonase (PehA), a protein secreted through the type II (GSP) pathway in Erwinia carotovora
    • Palomaki, T., Pickersgill, R., Riekki, R., Romantschuk, M., Saarilahti, H.T., A putative three-dimensional targeting motif of polygalacturonase (PehA), a protein secreted through the type II (GSP) pathway in Erwinia carotovora. Molecular Microbiology 43:3 (2002), 585–596.
    • (2002) Molecular Microbiology , vol.43 , Issue.3 , pp. 585-596
    • Palomaki, T.1    Pickersgill, R.2    Riekki, R.3    Romantschuk, M.4    Saarilahti, H.T.5
  • 130
    • 84907813636 scopus 로고    scopus 로고
    • Substrate recognition by the bacterial type II secretion system: More than a simple interaction
    • Pineau, C., Guschinskaya, N., Robert, X., Gouet, P., Ballut, L., Shevchik, V.E., Substrate recognition by the bacterial type II secretion system: More than a simple interaction. Molecular Microbiology 94:1 (2014), 126–140, 10.1111/mmi.12744.
    • (2014) Molecular Microbiology , vol.94 , Issue.1 , pp. 126-140
    • Pineau, C.1    Guschinskaya, N.2    Robert, X.3    Gouet, P.4    Ballut, L.5    Shevchik, V.E.6
  • 131
    • 0034629284 scopus 로고    scopus 로고
    • Identification of vaccine candidates against serogroup B meningococcus by whole-genome sequencing
    • Pizza, M., Scarlato, V., Masignani, V., Giuliani, M.M., Arico, B., Comanducci, M.,.. Rappuoli, R., Identification of vaccine candidates against serogroup B meningococcus by whole-genome sequencing. Science 287:5459 (2000), 1816–1820.
    • (2000) Science , vol.287 , Issue.5459 , pp. 1816-1820
    • Pizza, M.1    Scarlato, V.2    Masignani, V.3    Giuliani, M.M.4    Arico, B.5    Comanducci, M.6    Rappuoli, R.7
  • 132
    • 84879593927 scopus 로고    scopus 로고
    • The outer surface lipoprotein VolA mediates utilization of exogenous lipids by Vibrio cholerae
    • Pride, A.C., Herrera, C.M., Guan, Z., Giles, D.K., Trent, M.S., The outer surface lipoprotein VolA mediates utilization of exogenous lipids by Vibrio cholerae. MBio 4:3 (2013), e00305–e00313, 10.1128/mBio.00305-13.
    • (2013) MBio , vol.4 , Issue.3 , pp. e00305-e00313
    • Pride, A.C.1    Herrera, C.M.2    Guan, Z.3    Giles, D.K.4    Trent, M.S.5
  • 133
    • 0022633064 scopus 로고
    • Extracellular pullulanase of Klebsiella pneumoniae is a lipoprotein
    • Pugsley, A.P., Chapon, C., Schwartz, M., Extracellular pullulanase of Klebsiella pneumoniae is a lipoprotein. Journal of Bacteriology 166:3 (1986), 1083–1088.
    • (1986) Journal of Bacteriology , vol.166 , Issue.3 , pp. 1083-1088
    • Pugsley, A.P.1    Chapon, C.2    Schwartz, M.3
  • 134
    • 84897477890 scopus 로고    scopus 로고
    • Outer surface proteins of Borrelia: Peerless immune evasion tools
    • Pulzova, L., Bhide, M., Outer surface proteins of Borrelia: Peerless immune evasion tools. Current Protein & Peptide Science 15:1 (2014), 75–88.
    • (2014) Current Protein & Peptide Science , vol.15 , Issue.1 , pp. 75-88
    • Pulzova, L.1    Bhide, M.2
  • 135
    • 84907101187 scopus 로고    scopus 로고
    • FipB, an essential virulence factor of Francisella tularensis subsp. tularensis, has dual roles in disulfide bond formation
    • Qin, A., Zhang, Y., Clark, M.E., Rabideau, M.M., Millan Barea, L.R., Mann, B.J., FipB, an essential virulence factor of Francisella tularensis subsp. tularensis, has dual roles in disulfide bond formation. Journal of Bacteriology 196:20 (2014), 3571–3581, 10.1128/jb.01359-13.
    • (2014) Journal of Bacteriology , vol.196 , Issue.20 , pp. 3571-3581
    • Qin, A.1    Zhang, Y.2    Clark, M.E.3    Rabideau, M.M.4    Millan Barea, L.R.5    Mann, B.J.6
  • 136
    • 77955556470 scopus 로고    scopus 로고
    • Hydrophobic surface patches on LolA of Pseudomonas aeruginosa are essential for lipoprotein binding
    • Remans, K., Pauwels, K., van Ulsen, P., Buts, L., Cornelis, P., Tommassen, J.,.. Van Gelder, P., Hydrophobic surface patches on LolA of Pseudomonas aeruginosa are essential for lipoprotein binding. Journal of Molecular Biology 401:5 (2010), 921–930, 10.1016/j.jmb.2010.06.067.
    • (2010) Journal of Molecular Biology , vol.401 , Issue.5 , pp. 921-930
    • Remans, K.1    Pauwels, K.2    van Ulsen, P.3    Buts, L.4    Cornelis, P.5    Tommassen, J.6    Van Gelder, P.7
  • 137
    • 79959826593 scopus 로고    scopus 로고
    • The N-glycan glycoprotein deglycosylation complex (Gpd) from Capnocytophaga canimorsus deglycosylates human IgG
    • Renzi, F., Manfredi, P., Mally, M., Moes, S., Jeno, P., Cornelis, G.R., The N-glycan glycoprotein deglycosylation complex (Gpd) from Capnocytophaga canimorsus deglycosylates human IgG. PLoS Pathogens, 7(6), 2011, e1002118, 10.1371/journal.ppat.1002118.
    • (2011) PLoS Pathogens , vol.7 , Issue.6 , pp. e1002118
    • Renzi, F.1    Manfredi, P.2    Mally, M.3    Moes, S.4    Jeno, P.5    Cornelis, G.R.6
  • 138
    • 84857644824 scopus 로고    scopus 로고
    • The Bam machine: A molecular cooper
    • Ricci, D.P., Silhavy, T.J., The Bam machine: A molecular cooper. Biochimica et Biophysica Acta 1818:4 (2012), 1067–1084, 10.1016/j.bbamem.2011.08.020.
    • (2012) Biochimica et Biophysica Acta , vol.1818 , Issue.4 , pp. 1067-1084
    • Ricci, D.P.1    Silhavy, T.J.2
  • 139
    • 12544257510 scopus 로고    scopus 로고
    • Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli
    • Robichon, C., Vidal-Ingigliardi, D., Pugsley, A.P., Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. The Journal of Biological Chemistry 280:2 (2005), 974–983, 10.1074/jbc.M411059200.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.2 , pp. 974-983
    • Robichon, C.1    Vidal-Ingigliardi, D.2    Pugsley, A.P.3
  • 140
    • 79956292587 scopus 로고    scopus 로고
    • A disulfide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RCSF
    • Rogov, V.V., Rogova, N.Y., Bernhard, F., Lohr, F., Dotsch, V., A disulfide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RCSF. The Journal of Biological Chemistry 286:21 (2011), 18775–18783, 10.1074/jbc.M111.230185.
    • (2011) The Journal of Biological Chemistry , vol.286 , Issue.21 , pp. 18775-18783
    • Rogov, V.V.1    Rogova, N.Y.2    Bernhard, F.3    Lohr, F.4    Dotsch, V.5
  • 141
    • 84873633107 scopus 로고    scopus 로고
    • Lipidation of the autotransporter NalP of Neisseria meningitidis is required for its function in the release of cell-surface-exposed proteins
    • Roussel-Jazede, V., Grijpstra, J., van Dam, V., Tommassen, J., van Ulsen, P., Lipidation of the autotransporter NalP of Neisseria meningitidis is required for its function in the release of cell-surface-exposed proteins. Microbiology 159:Pt. 2 (2013), 286–295, 10.1099/mic.0.063982-0.
    • (2013) Microbiology , vol.159 , pp. 286-295
    • Roussel-Jazede, V.1    Grijpstra, J.2    van Dam, V.3    Tommassen, J.4    van Ulsen, P.5
  • 142
    • 77953924496 scopus 로고    scopus 로고
    • NalP-mediated proteolytic release of lactoferrin-binding protein B from the meningococcal cell surface
    • Roussel-Jazede, V., Jongerius, I., Bos, M.P., Tommassen, J., van Ulsen, P., NalP-mediated proteolytic release of lactoferrin-binding protein B from the meningococcal cell surface. Infection and Immunity 78:7 (2010), 3083–3089, 10.1128/iai.01193-09.
    • (2010) Infection and Immunity , vol.78 , Issue.7 , pp. 3083-3089
    • Roussel-Jazede, V.1    Jongerius, I.2    Bos, M.P.3    Tommassen, J.4    van Ulsen, P.5
  • 143
    • 0037008715 scopus 로고    scopus 로고
    • Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis
    • Sabarth, N., Lamer, S., Zimny-Arndt, U., Jungblut, P.R., Meyer, T.F., Bumann, D., Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis. The Journal of Biological Chemistry 277:31 (2002), 27896–27902, 10.1074/jbc.M204473200.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.31 , pp. 27896-27902
    • Sabarth, N.1    Lamer, S.2    Zimny-Arndt, U.3    Jungblut, P.R.4    Meyer, T.F.5    Bumann, D.6
  • 146
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol
    • Sankaran, K., Wu, H.C., Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. The Journal of Biological Chemistry 269:31 (1994), 19701–19706.
    • (1994) The Journal of Biological Chemistry , vol.269 , Issue.31 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 147
    • 70350749405 scopus 로고    scopus 로고
    • Assessment of vaccine potential of the Neisseria-specific protein NMB0938
    • Sardinas, G., Climent, Y., Rodriguez, Y., Gonzalez, S., Garcia, D., Cobas, K.,.. Yero, D., Assessment of vaccine potential of the Neisseria-specific protein NMB0938. Vaccine 27:49 (2009), 6910–6917, 10.1016/j.vaccine.2009.09.005.
    • (2009) Vaccine , vol.27 , Issue.49 , pp. 6910-6917
    • Sardinas, G.1    Climent, Y.2    Rodriguez, Y.3    Gonzalez, S.4    Garcia, D.5    Cobas, K.6    Yero, D.7
  • 148
    • 0029816618 scopus 로고    scopus 로고
    • Identification of two regions of Klebsiella oxytoca pullulanase that together are capable of promoting beta-lactamase secretion by the general secretory pathway
    • Sauvonnet, N., Pugsley, A.P., Identification of two regions of Klebsiella oxytoca pullulanase that together are capable of promoting beta-lactamase secretion by the general secretory pathway. Molecular Microbiology 22:1 (1996), 1–7.
    • (1996) Molecular Microbiology , vol.22 , Issue.1 , pp. 1-7
    • Sauvonnet, N.1    Pugsley, A.P.2
  • 149
    • 67249113222 scopus 로고    scopus 로고
    • Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates
    • Schneider, M.C., Prosser, B.E., Caesar, J.J., Kugelberg, E., Li, S., Zhang, Q.,.. Lea, S.M., Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates. Nature 458:7240 (2009), 890–893, 10.1038/nature07769.
    • (2009) Nature , vol.458 , Issue.7240 , pp. 890-893
    • Schneider, M.C.1    Prosser, B.E.2    Caesar, J.J.3    Kugelberg, E.4    Li, S.5    Zhang, Q.6    Lea, S.M.7
  • 150
    • 77952816250 scopus 로고    scopus 로고
    • Translocation of Borrelia burgdorferi surface lipoprotein OspA through the outer membrane requires an unfolded conformation and can initiate at the C-terminus
    • Schulze, R.J., Chen, S., Kumru, O.S., Zuckert, W.R., Translocation of Borrelia burgdorferi surface lipoprotein OspA through the outer membrane requires an unfolded conformation and can initiate at the C-terminus. Molecular Microbiology 76:5 (2010), 1266–1278, 10.1111/j.1365-2958.2010.07172.x.
    • (2010) Molecular Microbiology , vol.76 , Issue.5 , pp. 1266-1278
    • Schulze, R.J.1    Chen, S.2    Kumru, O.S.3    Zuckert, W.R.4
  • 151
    • 33645077876 scopus 로고    scopus 로고
    • Borrelia burgdorferi lipoproteins are secreted to the outer surface by default
    • Schulze, R.J., Zuckert, W.R., Borrelia burgdorferi lipoproteins are secreted to the outer surface by default. Molecular Microbiology 59:5 (2006), 1473–1484, 10.1111/j.1365-2958.2006.05039.x.
    • (2006) Molecular Microbiology , vol.59 , Issue.5 , pp. 1473-1484
    • Schulze, R.J.1    Zuckert, W.R.2
  • 153
    • 0034651753 scopus 로고    scopus 로고
    • YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase
    • Scotti, P.A., Urbanus, M.L., Brunner, J., de Gier, J.W., von Heijne, G., van der Does, C.,.. Luirink, J., YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase. The EMBO Journal 19:4 (2000), 542–549, 10.1093/emboj/19.4.542.
    • (2000) The EMBO Journal , vol.19 , Issue.4 , pp. 542-549
    • Scotti, P.A.1    Urbanus, M.L.2    Brunner, J.3    de Gier, J.W.4    von Heijne, G.5    van der Does, C.6    Luirink, J.7
  • 154
    • 84866178763 scopus 로고    scopus 로고
    • Surface proteome analysis and characterization of surface cell antigen (Sca) or autotransporter family of Rickettsia typhi
    • Sears, K.T., Ceraul, S.M., Gillespie, J.J., Allen, E.D. Jr., Popov, V.L., Ammerman, N.C.,.. Azad, A.F., Surface proteome analysis and characterization of surface cell antigen (Sca) or autotransporter family of Rickettsia typhi. PLoS Pathogens, 8(8), 2012, e1002856, 10.1371/journal.ppat.1002856.
    • (2012) PLoS Pathogens , vol.8 , Issue.8 , pp. e1002856
    • Sears, K.T.1    Ceraul, S.M.2    Gillespie, J.J.3    Allen, E.D.4    Popov, V.L.5    Ammerman, N.C.6    Azad, A.F.7
  • 155
    • 84929317723 scopus 로고    scopus 로고
    • Neisseria meningitidis factor H-binding protein fHbp: A key virulence factor and vaccine antigen
    • Seib, K.L., Scarselli, M., Comanducci, M., Toneatto, D., Masignani, V., Neisseria meningitidis factor H-binding protein fHbp: A key virulence factor and vaccine antigen. Expert Review of Vaccines 14:6 (2015), 841–859, 10.1586/14760584.2015.1016915.
    • (2015) Expert Review of Vaccines , vol.14 , Issue.6 , pp. 841-859
    • Seib, K.L.1    Scarselli, M.2    Comanducci, M.3    Toneatto, D.4    Masignani, V.5
  • 159
    • 0030013042 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of the gene encoding LipL41, a surface-exposed lipoprotein of pathogenic Leptospira species
    • Shang, E.S., Summers, T.A., Haake, D.A., Molecular cloning and sequence analysis of the gene encoding LipL41, a surface-exposed lipoprotein of pathogenic Leptospira species. Infection and Immunity 64:6 (1996), 2322–2330.
    • (1996) Infection and Immunity , vol.64 , Issue.6 , pp. 2322-2330
    • Shang, E.S.1    Summers, T.A.2    Haake, D.A.3
  • 160
    • 0033802036 scopus 로고    scopus 로고
    • Characterization of four outer membrane proteins involved in binding starch to the cell surface of Bacteroides thetaiotaomicron
    • Shipman, J.A., Berleman, J.E., Salyers, A.A., Characterization of four outer membrane proteins involved in binding starch to the cell surface of Bacteroides thetaiotaomicron. Journal of Bacteriology 182:19 (2000), 5365–5372.
    • (2000) Journal of Bacteriology , vol.182 , Issue.19 , pp. 5365-5372
    • Shipman, J.A.1    Berleman, J.E.2    Salyers, A.A.3
  • 161
    • 77952528533 scopus 로고    scopus 로고
    • Twin arginine translocase pathway and fast-folding lipoprotein biosynthesis in E. coli: Interesting implications and applications
    • Shruthi, H., Anand, P., Murugan, V., Sankaran, K., Twin arginine translocase pathway and fast-folding lipoprotein biosynthesis in E. coli: Interesting implications and applications. Molecular BioSystems 6:6 (2010), 999–1007, 10.1039/b916510j.
    • (2010) Molecular BioSystems , vol.6 , Issue.6 , pp. 999-1007
    • Shruthi, H.1    Anand, P.2    Murugan, V.3    Sankaran, K.4
  • 162
    • 77954457475 scopus 로고    scopus 로고
    • TAT-pathway-dependent lipoproteins as a niche-based adaptation in prokaryotes
    • Shruthi, H., Babu, M.M., Sankaran, K., TAT-pathway-dependent lipoproteins as a niche-based adaptation in prokaryotes. Journal of Molecular Evolution 70:4 (2010), 359–370, 10.1007/s00239-010-9334-2.
    • (2010) Journal of Molecular Evolution , vol.70 , Issue.4 , pp. 359-370
    • Shruthi, H.1    Babu, M.M.2    Sankaran, K.3
  • 163
    • 0034674154 scopus 로고    scopus 로고
    • Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution
    • Shu, W., Liu, J., Ji, H., Lu, M., Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution. Journal of Molecular Biology 299:4 (2000), 1101–1112, 10.1006/jmbi.2000.3776.
    • (2000) Journal of Molecular Biology , vol.299 , Issue.4 , pp. 1101-1112
    • Shu, W.1    Liu, J.2    Ji, H.3    Lu, M.4
  • 164
    • 43649087706 scopus 로고    scopus 로고
    • Pbp, a cell-surface exposed plasminogen binding protein of Bacteroides fragilis
    • Sijbrandi, R., Stork, M., Luirink, J., Otto, B.R., Pbp, a cell-surface exposed plasminogen binding protein of Bacteroides fragilis. Microbes and Infection 10:5 (2008), 514–521, 10.1016/j.micinf.2008.01.015.
    • (2008) Microbes and Infection , vol.10 , Issue.5 , pp. 514-521
    • Sijbrandi, R.1    Stork, M.2    Luirink, J.3    Otto, B.R.4
  • 165
    • 39749175060 scopus 로고    scopus 로고
    • Membrane localization and topology of the Yersinia pestis YscJ lipoprotein
    • Silva-Herzog, E., Ferracci, F., Jackson, M.W., Joseph, S.S., Plano, G.V., Membrane localization and topology of the Yersinia pestis YscJ lipoprotein. Microbiology 154:Pt. 2 (2008), 593–607, 10.1099/mic.0.2007/013045-0.
    • (2008) Microbiology , vol.154 , pp. 593-607
    • Silva-Herzog, E.1    Ferracci, F.2    Jackson, M.W.3    Joseph, S.S.4    Plano, G.V.5
  • 167
    • 34948827356 scopus 로고    scopus 로고
    • Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
    • Sklar, J.G., Wu, T., Kahne, D., Silhavy, T.J., Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes & Development 21:19 (2007), 2473–2484, 10.1101/gad.1581007.
    • (2007) Genes & Development , vol.21 , Issue.19 , pp. 2473-2484
    • Sklar, J.G.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 168
    • 77952372626 scopus 로고    scopus 로고
    • Improved accuracy of cell surface shaving proteomics in Staphylococcus aureus using a false-positive control
    • Solis, N., Larsen, M.R., Cordwell, S.J., Improved accuracy of cell surface shaving proteomics in Staphylococcus aureus using a false-positive control. Proteomics 10:10 (2010), 2037–2049, 10.1002/pmic.200900564.
    • (2010) Proteomics , vol.10 , Issue.10 , pp. 2037-2049
    • Solis, N.1    Larsen, M.R.2    Cordwell, S.J.3
  • 169
    • 0028233079 scopus 로고
    • Identification and characterization of a chromosomal virulence gene, vacJ, required for intercellular spreading of Shigella flexneri
    • Suzuki, T., Murai, T., Fukuda, I., Tobe, T., Yoshikawa, M., Sasakawa, C., Identification and characterization of a chromosomal virulence gene, vacJ, required for intercellular spreading of Shigella flexneri. Molecular Microbiology 11:1 (1994), 31–41.
    • (1994) Molecular Microbiology , vol.11 , Issue.1 , pp. 31-41
    • Suzuki, T.1    Murai, T.2    Fukuda, I.3    Tobe, T.4    Yoshikawa, M.5    Sasakawa, C.6
  • 170
    • 0038602740 scopus 로고    scopus 로고
    • Crystal structures of bacterial lipoprotein localization factors, LolA and LolB
    • Takeda, K., Miyatake, H., Yokota, N., Matsuyama, S., Tokuda, H., Miki, K., Crystal structures of bacterial lipoprotein localization factors, LolA and LolB. The EMBO Journal 22:13 (2003), 3199–3209, 10.1093/emboj/cdg324.
    • (2003) The EMBO Journal , vol.22 , Issue.13 , pp. 3199-3209
    • Takeda, K.1    Miyatake, H.2    Yokota, N.3    Matsuyama, S.4    Tokuda, H.5    Miki, K.6
  • 171
    • 27144449975 scopus 로고    scopus 로고
    • Mechanisms underlying energy-independent transfer of lipoproteins from LolA to LolB, which have similar unclosed {beta}-barrel structures
    • Taniguchi, N., Matsuyama, S., Tokuda, H., Mechanisms underlying energy-independent transfer of lipoproteins from LolA to LolB, which have similar unclosed {beta}-barrel structures. The Journal of Biological Chemistry 280:41 (2005), 34481–34488, 10.1074/jbc.M507388200.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.41 , pp. 34481-34488
    • Taniguchi, N.1    Matsuyama, S.2    Tokuda, H.3
  • 172
    • 0035861554 scopus 로고    scopus 로고
    • Lipoprotein sorting signals evaluated as the LolA-dependent release of lipoproteins from the cytoplasmic membrane of Escherichia coli
    • Terada, M., Kuroda, T., Matsuyama, S.I., Tokuda, H., Lipoprotein sorting signals evaluated as the LolA-dependent release of lipoproteins from the cytoplasmic membrane of Escherichia coli. The Journal of Biological Chemistry 276:50 (2001), 47690–47694, 10.1074/jbc.M109307200.
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.50 , pp. 47690-47694
    • Terada, M.1    Kuroda, T.2    Matsuyama, S.I.3    Tokuda, H.4
  • 173
    • 0032773958 scopus 로고    scopus 로고
    • Outer membrane proteins Omp10, Omp16, and Omp19 of Brucella spp. are lipoproteins
    • Tibor, A., Decelle, B., Letesson, J.J., Outer membrane proteins Omp10, Omp16, and Omp19 of Brucella spp. are lipoproteins. Infection and Immunity 67:9 (1999), 4960–4962.
    • (1999) Infection and Immunity , vol.67 , Issue.9 , pp. 4960-4962
    • Tibor, A.1    Decelle, B.2    Letesson, J.J.3
  • 174
    • 84995334089 scopus 로고    scopus 로고
    • Chapter 4: Bacterial lipoproteins: Biogenesis, virulence/pathogenicity and trafficking
    • H. Remaut R. Fronzes Caister Academic Press Norfolk, UK
    • Tokuda, H., Sander, P., Lee, B., Okuda, S., Grau, T., Tschumi, A.,.. Nakayama, H., Chapter 4: Bacterial lipoproteins: Biogenesis, virulence/pathogenicity and trafficking. Remaut, H., Fronzes, R., (eds.) Bacterial membranes: Structural and molecular biology, 2013, Caister Academic Press, Norfolk, UK, 133–178.
    • (2013) Bacterial membranes: Structural and molecular biology , pp. 133-178
    • Tokuda, H.1    Sander, P.2    Lee, B.3    Okuda, S.4    Grau, T.5    Tschumi, A.6    Nakayama, H.7
  • 177
    • 68749109764 scopus 로고    scopus 로고
    • Dissection of LolB function—Lipoprotein binding, membrane targeting and incorporation of lipoproteins into lipid bilayers
    • Tsukahara, J., Mukaiyama, K., Okuda, S., Narita, S., Tokuda, H., Dissection of LolB function—Lipoprotein binding, membrane targeting and incorporation of lipoproteins into lipid bilayers. The FEBS Journal 276:16 (2009), 4496–4504, 10.1111/j.1742-4658.2009.07156.x.
    • (2009) The FEBS Journal , vol.276 , Issue.16 , pp. 4496-4504
    • Tsukahara, J.1    Mukaiyama, K.2    Okuda, S.3    Narita, S.4    Tokuda, H.5
  • 178
    • 69949150584 scopus 로고    scopus 로고
    • Real time analysis of lipoprotein transfer from LolA to LolB by means of surface plasmon resonance
    • Tsukahara, J., Narita, S., Tokuda, H., Real time analysis of lipoprotein transfer from LolA to LolB by means of surface plasmon resonance. FEBS Letters 583:18 (2009), 2987–2990, 10.1016/j.febslet.2009.08.032.
    • (2009) FEBS Letters , vol.583 , Issue.18 , pp. 2987-2990
    • Tsukahara, J.1    Narita, S.2    Tokuda, H.3
  • 179
    • 0036077230 scopus 로고    scopus 로고
    • Autotransported serine protease A of Neisseria meningitidis: An immunogenic, surface-exposed outer membrane, and secreted protein
    • Turner, D.P., Wooldridge, K.G., Ala'Aldeen, D.A., Autotransported serine protease A of Neisseria meningitidis: An immunogenic, surface-exposed outer membrane, and secreted protein. Infection and Immunity 70:8 (2002), 4447–4461.
    • (2002) Infection and Immunity , vol.70 , Issue.8 , pp. 4447-4461
    • Turner, D.P.1    Wooldridge, K.G.2    Ala'Aldeen, D.A.3
  • 181
    • 84959036430 scopus 로고    scopus 로고
    • Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin
    • Vogeley, L., El Arnaout, T., Bailey, J., Stansfeld, P.J., Boland, C., Caffrey, M., Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin. Science 351:6275 (2016), 876–880, 10.1126/science.aad3747.
    • (2016) Science , vol.351 , Issue.6275 , pp. 876-880
    • Vogeley, L.1    El Arnaout, T.2    Bailey, J.3    Stansfeld, P.J.4    Boland, C.5    Caffrey, M.6
  • 182
    • 0024393453 scopus 로고
    • The structure of signal peptides from bacterial lipoproteins
    • von Heijne, G., The structure of signal peptides from bacterial lipoproteins. Protein Engineering 2:7 (1989), 531–534.
    • (1989) Protein Engineering , vol.2 , Issue.7 , pp. 531-534
    • von Heijne, G.1
  • 183
    • 84902007682 scopus 로고    scopus 로고
    • Analysis of surface-exposed outer membrane proteins in Helicobacter pylori
    • Voss, B.J., Gaddy, J.A., McDonald, W.H., Cover, T.L., Analysis of surface-exposed outer membrane proteins in Helicobacter pylori. Journal of Bacteriology 196:13 (2014), 2455–2471, 10.1128/jb.01768-14.
    • (2014) Journal of Bacteriology , vol.196 , Issue.13 , pp. 2455-2471
    • Voss, B.J.1    Gaddy, J.A.2    McDonald, W.H.3    Cover, T.L.4
  • 184
    • 67650177056 scopus 로고    scopus 로고
    • Identification of uropathogenic Escherichia coli surface proteins by shotgun proteomics
    • Walters, M.S., Mobley, H.L., Identification of uropathogenic Escherichia coli surface proteins by shotgun proteomics. Journal of Microbiological Methods 78:2 (2009), 131–135, 10.1016/j.mimet.2009.04.013.
    • (2009) Journal of Microbiological Methods , vol.78 , Issue.2 , pp. 131-135
    • Walters, M.S.1    Mobley, H.L.2
  • 185
    • 54449093948 scopus 로고    scopus 로고
    • Introduction of a lethal redox switch that controls the opening and closing of the hydrophobic cavity in LolA
    • Watanabe, S., Oguchi, Y., Takeda, K., Miki, K., Tokuda, H., Introduction of a lethal redox switch that controls the opening and closing of the hydrophobic cavity in LolA. The Journal of Biological Chemistry 283:37 (2008), 25421–25427, 10.1074/jbc.M804737200.
    • (2008) The Journal of Biological Chemistry , vol.283 , Issue.37 , pp. 25421-25427
    • Watanabe, S.1    Oguchi, Y.2    Takeda, K.3    Miki, K.4    Tokuda, H.5
  • 186
    • 84943328664 scopus 로고    scopus 로고
    • Identification of BamC on the surface of E. coli
    • Webb, C.T., Lithgow, T., Identification of BamC on the surface of E. coli. Methods in Molecular Biology 1329 (2015), 215–225, 10.1007/978-1-4939-2871-2_17.
    • (2015) Methods in Molecular Biology , vol.1329 , pp. 215-225
    • Webb, C.T.1    Lithgow, T.2
  • 187
    • 84865523255 scopus 로고    scopus 로고
    • Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC
    • Webb, C.T., Selkrig, J., Perry, A.J., Noinaj, N., Buchanan, S.K., Lithgow, T., Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC. Journal of Molecular Biology 422:4 (2012), 545–555, 10.1016/j.jmb.2012.05.035.
    • (2012) Journal of Molecular Biology , vol.422 , Issue.4 , pp. 545-555
    • Webb, C.T.1    Selkrig, J.2    Perry, A.J.3    Noinaj, N.4    Buchanan, S.K.5    Lithgow, T.6
  • 188
    • 33746356503 scopus 로고    scopus 로고
    • Biosynthesis and assembly of capsular polysaccharides in Escherichia coli
    • Whitfield, C., Biosynthesis and assembly of capsular polysaccharides in Escherichia coli. Annual Review of Biochemistry 75 (2006), 39–68, 10.1146/annurev.biochem.75.103004.142545.
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 39-68
    • Whitfield, C.1
  • 189
    • 84922640624 scopus 로고    scopus 로고
    • Analysis of the outer membrane proteome and secretome of Bacteroides fragilis reveals a multiplicity of secretion mechanisms
    • Wilson, M.M., Anderson, D.E., Bernstein, H.D., Analysis of the outer membrane proteome and secretome of Bacteroides fragilis reveals a multiplicity of secretion mechanisms. PLoS One, 10(2), 2015, e0117732, 10.1371/journal.pone.0117732.
    • (2015) PLoS One , vol.10 , Issue.2 , pp. e0117732
    • Wilson, M.M.1    Anderson, D.E.2    Bernstein, H.D.3
  • 190
    • 84958769895 scopus 로고    scopus 로고
    • Surface-exposed lipoproteins: An emerging secretion phenomenon in gram-negative bacteria
    • Wilson, M.M., Bernstein, H.D., Surface-exposed lipoproteins: An emerging secretion phenomenon in gram-negative bacteria. Trends in Microbiology 24:3 (2016), 198–208, 10.1016/j.tim.2015.11.006.
    • (2016) Trends in Microbiology , vol.24 , Issue.3 , pp. 198-208
    • Wilson, M.M.1    Bernstein, H.D.2
  • 191
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu, T., Malinverni, J., Ruiz, N., Kim, S., Silhavy, T.J., Kahne, D., Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121:2 (2005), 235–245, 10.1016/j.cell.2005.02.015.
    • (2005) Cell , vol.121 , Issue.2 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5    Kahne, D.6
  • 192
    • 0032515092 scopus 로고    scopus 로고
    • Identification and subcellular localization of a novel Cu, Zn superoxide dismutase of Mycobacterium tuberculosis
    • Wu, C.H., Tsai-Wu, J.J., Huang, Y.T., Lin, C.Y., Lioua, G.G., Lee, F.J., Identification and subcellular localization of a novel Cu, Zn superoxide dismutase of Mycobacterium tuberculosis. FEBS Letters 439:1–2 (1998), 192–196.
    • (1998) FEBS Letters , vol.439 , Issue.1-2 , pp. 192-196
    • Wu, C.H.1    Tsai-Wu, J.J.2    Huang, Y.T.3    Lin, C.Y.4    Lioua, G.G.5    Lee, F.J.6
  • 193
    • 0033787084 scopus 로고    scopus 로고
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes
    • Yakushi, T., Masuda, K., Narita, S., Matsuyama, S., Tokuda, H., A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nature Cell Biology 2:4 (2000), 212–218, 10.1038/35008635.
    • (2000) Nature Cell Biology , vol.2 , Issue.4 , pp. 212-218
    • Yakushi, T.1    Masuda, K.2    Narita, S.3    Matsuyama, S.4    Tokuda, H.5
  • 194
    • 0032484007 scopus 로고    scopus 로고
    • LolA-dependent release of a lipid-modified protein from the inner membrane of Escherichia coli requires nucleoside triphosphate
    • Yakushi, T., Yokota, N., Matsuyama, S., Tokuda, H., LolA-dependent release of a lipid-modified protein from the inner membrane of Escherichia coli requires nucleoside triphosphate. The Journal of Biological Chemistry 273:49 (1998), 32576–32581.
    • (1998) The Journal of Biological Chemistry , vol.273 , Issue.49 , pp. 32576-32581
    • Yakushi, T.1    Yokota, N.2    Matsuyama, S.3    Tokuda, H.4
  • 195
    • 0024279918 scopus 로고
    • A single amino acid determinant of the membrane localization of lipoproteins in E. coli
    • Yamaguchi, K., Yu, F., Inouye, M., A single amino acid determinant of the membrane localization of lipoproteins in E. coli. Cell 53:3 (1988), 423–432.
    • (1988) Cell , vol.53 , Issue.3 , pp. 423-432
    • Yamaguchi, K.1    Yu, F.2    Inouye, M.3
  • 197
    • 49449107199 scopus 로고    scopus 로고
    • Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state
    • Zuber, B., Chami, M., Houssin, C., Dubochet, J., Griffiths, G., Daffe, M., Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state. Journal of Bacteriology 190:16 (2008), 5672–5680, 10.1128/JB.01919-07.
    • (2008) Journal of Bacteriology , vol.190 , Issue.16 , pp. 5672-5680
    • Zuber, B.1    Chami, M.2    Houssin, C.3    Dubochet, J.4    Griffiths, G.5    Daffe, M.6
  • 198
    • 84902276774 scopus 로고    scopus 로고
    • Secretion of bacterial lipoproteins: Through the cytoplasmic membrane, the periplasm and beyond
    • Zuckert, W.R., Secretion of bacterial lipoproteins: Through the cytoplasmic membrane, the periplasm and beyond. Biochimica et Biophysica Acta 1843:8 (2014), 1509–1516, 10.1016/j.bbamcr.2014.04.022.
    • (2014) Biochimica et Biophysica Acta , vol.1843 , Issue.8 , pp. 1509-1516
    • Zuckert, W.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.