메뉴 건너뛰기




Volumn 1, Issue 8, 2016, Pages

Protein folding in the cell envelope of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; ESCHERICHIA COLI PROTEIN;

EID: 84991211421     PISSN: None     EISSN: 20585276     Source Type: Journal    
DOI: 10.1038/nmicrobiol.2016.107     Document Type: Article
Times cited : (68)

References (172)
  • 1
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A. & Chan, H. S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4, 10-19 (1997).
    • (1997) Nature Struct. Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 2
    • 84936137605 scopus 로고    scopus 로고
    • Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape
    • Yu, H. et al. Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape. Proc. Natl Acad. Sci. USA 112, 8308-8313 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 8308-8313
    • Yu, H.1
  • 3
    • 84876281768 scopus 로고    scopus 로고
    • Unusual biophysics of intrinsically disordered proteins
    • Uversky, V. N. Unusual biophysics of intrinsically disordered proteins. Biochim. Biophys. Acta 1834, 932-951 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 932-951
    • Uversky, V.N.1
  • 4
    • 84875826727 scopus 로고    scopus 로고
    • Intrinsically disordered proteins undergo and assist folding transitions in the proteome
    • Kovacs, D., Szabo, B., Pancsa, R. & Tompa, P. Intrinsically disordered proteins undergo and assist folding transitions in the proteome. Arch. Biochem. Biophys. 531, 80-89 (2013).
    • (2013) Arch. Biochem. Biophys , vol.531 , pp. 80-89
    • Kovacs, D.1    Szabo, B.2    Pancsa, R.3    Tompa, P.4
  • 5
    • 84928253866 scopus 로고    scopus 로고
    • Proteome-wide subcellular topologies of E. Coli polypeptides database (STEPdb)
    • Orfanoudaki, G. & Economou, A. Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb). Mol. Cell Proteomics 13, 3674-3687 (2014).
    • (2014) Mol. Cell Proteomics , vol.13 , pp. 3674-3687
    • Orfanoudaki, G.1    Economou, A.2
  • 7
    • 84874592097 scopus 로고    scopus 로고
    • The Escherichia coli peripheral inner membrane proteome
    • Papanastasiou, M. et al. The Escherichia coli peripheral inner membrane proteome. Mol. Cell. Proteomics 12, 599-610 (2013).
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 599-610
    • Papanastasiou, M.1
  • 8
    • 84953224091 scopus 로고    scopus 로고
    • Rapid label-free quantitative analysis of the E. Coli BL21(DE3) inner membrane proteome
    • Papanastasiou, M. et al. Rapid label-free quantitative analysis of the E. coli BL21(DE3) inner membrane proteome. Proteomics 16, 85-97 (2016).
    • (2016) Proteomics , vol.16 , pp. 85-97
    • Papanastasiou, M.1
  • 10
    • 79955027962 scopus 로고    scopus 로고
    • Sorting of an integral outer membrane protein via the lipoprotein-specific Lol pathway and a dedicated lipoprotein pilotin
    • Collin, S., Guilvout, I., Nickerson, N. N. & Pugsley, A. P. Sorting of an integral outer membrane protein via the lipoprotein-specific Lol pathway and a dedicated lipoprotein pilotin. Mol. Microbiol. 80, 655-665 (2011).
    • (2011) Mol. Microbiol , vol.80 , pp. 655-665
    • Collin, S.1    Guilvout, I.2    Nickerson, N.N.3    Pugsley, A.P.4
  • 11
    • 84919351502 scopus 로고    scopus 로고
    • Structure of the nonameric bacterial amyloid secretion channel
    • Cao, B. et al. Structure of the nonameric bacterial amyloid secretion channel. Proc. Natl Acad. Sci. USA 111, E5439-E5444 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111
    • Cao, B.1
  • 12
    • 84879888089 scopus 로고    scopus 로고
    • Protein translocation across the inner membrane of Gram-negative bacteria: The Sec and Tat dependent protein transport pathways
    • Kudva, R. et al. Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways. Res. Microbiol. 164, 505-534 (2013).
    • (2013) Res. Microbiol , vol.164 , pp. 505-534
    • Kudva, R.1
  • 13
    • 84879879193 scopus 로고    scopus 로고
    • The Sec-dependent pathway
    • Beckwith, J. The Sec-dependent pathway. Res. Microbiol. 164, 497-504 (2013).
    • (2013) Res. Microbiol , vol.164 , pp. 497-504
    • Beckwith, J.1
  • 14
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A. & Hayer-Hartl, M. Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332 (2011).
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 15
    • 67650661943 scopus 로고    scopus 로고
    • The perspectives of studying multi-domain protein folding
    • Fitter, J. The perspectives of studying multi-domain protein folding. Cell. Mol. Life Sci. 66, 1672-1681 (2009).
    • (2009) Cell. Mol. Life Sci , vol.66 , pp. 1672-1681
    • Fitter, J.1
  • 16
    • 84938675284 scopus 로고    scopus 로고
    • How co-translational folding of multi-domain protein is affected by elongation schedule: Molecular simulations
    • Tanaka, T., Hori, N. & Takada, S. How co-translational folding of multi-domain protein is affected by elongation schedule: molecular simulations. PLoS Comput. Biol. 11, e1004356 (2015).
    • (2015) PLoS Comput. Biol , vol.11
    • Tanaka, T.1    Hori, N.2    Takada, S.3
  • 18
    • 84887620404 scopus 로고    scopus 로고
    • What is the total number of protein molecules per cell volume? A call to rethink some published values
    • Milo, R. What is the total number of protein molecules per cell volume? A call to rethink some published values. Bioessays 35, 1050-1055 (2013).
    • (2013) Bioessays , vol.35 , pp. 1050-1055
    • Milo, R.1
  • 19
  • 20
    • 84930660167 scopus 로고    scopus 로고
    • Macromolecular crowding: Macromolecules friend or foe
    • Mittal, S., Chowhan, R. K. & Singh, L. R. Macromolecular crowding: macromolecules friend or foe. Biochim. Biophys. Acta 1850, 1822-1831 (2015).
    • (2015) Biochim. Biophys. Acta , vol.1850 , pp. 1822-1831
    • Mittal, S.1    Chowhan, R.K.2    Singh, L.R.3
  • 21
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
    • Zhou, H. X., Rivas, G. & Minton, A. P. Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu. Rev. Biophys. 37, 375-397 (2008).
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 22
    • 84874084196 scopus 로고    scopus 로고
    • Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion
    • Ye, C., Chai, Q., Zhong, M. & Wei, Y. Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion. Protein Sci. 22, 239-245 (2013).
    • (2013) Protein Sci , vol.22 , pp. 239-245
    • Ye, C.1    Chai, Q.2    Zhong, M.3    Wei, Y.4
  • 23
    • 0034674154 scopus 로고    scopus 로고
    • Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 Å resolution
    • Shu, W., Liu, J., Ji, H. & Lu, M. Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 Å resolution. J. Mol. Biol. 299, 1101-1112 (2000).
    • (2000) J. Mol. Biol , vol.299 , pp. 1101-1112
    • Shu, W.1    Liu, J.2    Ji, H.3    Lu, M.4
  • 24
    • 4143114616 scopus 로고    scopus 로고
    • Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation
    • Walton, T. A. & Sousa, M. C. Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol. Cell. 15, 367-374 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 367-374
    • Walton, T.A.1    Sousa, M.C.2
  • 25
    • 38549132443 scopus 로고    scopus 로고
    • Electrostatic contribution to the thermodynamic and kinetic stability of the homotrimeric coiled coil Lpp-56: A computational study
    • Bjelic, S., Wieninger, S., Jelesarov, I. & Karshikoff, A. Electrostatic contribution to the thermodynamic and kinetic stability of the homotrimeric coiled coil Lpp-56: a computational study. Proteins 70, 810-822 (2008).
    • (2008) Proteins , vol.70 , pp. 810-822
    • Bjelic, S.1    Wieninger, S.2    Jelesarov, I.3    Karshikoff, A.4
  • 26
    • 0038247520 scopus 로고    scopus 로고
    • Solution structure of Apo Cu, Zn superoxide dismutase: Role of metal ions in protein folding
    • Banci, L., Bertini, I., Cramaro, F., Del Conte, R. & Viezzoli, M. S. Solution structure of Apo Cu, Zn superoxide dismutase: role of metal ions in protein folding. Biochemistry 42, 9543-9553 (2003).
    • (2003) Biochemistry , vol.42 , pp. 9543-9553
    • Banci, L.1    Bertini, I.2    Cramaro, F.3    Del Conte, R.4    Viezzoli, M.S.5
  • 27
    • 69149083388 scopus 로고    scopus 로고
    • Predicting weakly stable regions, oligomerization state, and protein-protein interfaces in transmembrane domains of outer membrane proteins
    • Naveed, H., Jackups, R. Jr & Liang, J. Predicting weakly stable regions, oligomerization state, and protein-protein interfaces in transmembrane domains of outer membrane proteins. Proc. Natl Acad. Sci. USA 106, 12735-12740 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 12735-12740
    • Naveed, H.1    Jackups, R.2    Liang, J.3
  • 28
    • 0027456615 scopus 로고
    • Folding and assembly of bacterial alkaline phosphatase in vitro and in vivo
    • Akiyama, Y. & Ito, K. Folding and assembly of bacterial alkaline phosphatase in vitro and in vivo. J. Biol. Chem. 268, 8146-8150 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 8146-8150
    • Akiyama, Y.1    Ito, K.2
  • 29
    • 0242490833 scopus 로고    scopus 로고
    • Assembly of TolC, a structurally unique and multifunctional outer membrane protein of Escherichia coli K-12
    • Werner, J., Augustus, A. M. & Misra, R. Assembly of TolC, a structurally unique and multifunctional outer membrane protein of Escherichia coli K-12. J. Bacteriol. 185, 6540-6547 (2003).
    • (2003) J. Bacteriol , vol.185 , pp. 6540-6547
    • Werner, J.1    Augustus, A.M.2    Misra, R.3
  • 30
    • 0030045746 scopus 로고    scopus 로고
    • Folding and membrane insertion of the trimeric β-barrel protein OmpF
    • Surrey, T., Schmid, A. & Jahnig, F. Folding and membrane insertion of the trimeric β-barrel protein OmpF. Biochemistry 35, 2283-2288 (1996).
    • (1996) Biochemistry , vol.35 , pp. 2283-2288
    • Surrey, T.1    Schmid, A.2    Jahnig, F.3
  • 31
    • 84939131090 scopus 로고    scopus 로고
    • Assembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA
    • Dunstan, R. A. et al. Assembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA. Mol. Microbiol. 97, 616-629 (2015).
    • (2015) Mol. Microbiol , vol.97 , pp. 616-629
    • Dunstan, R.A.1
  • 32
    • 34547634728 scopus 로고    scopus 로고
    • PH of the cytoplasm and periplasm of Escherichia coli: Rapid measurement by green fluorescent protein fluorimetry
    • Wilks, J. C. & Slonczewski, J. L. pH of the cytoplasm and periplasm of Escherichia coli: rapid measurement by green fluorescent protein fluorimetry. J. Bacteriol. 189, 5601-5607 (2007).
    • (2007) J. Bacteriol , vol.189 , pp. 5601-5607
    • Wilks, J.C.1    Slonczewski, J.L.2
  • 33
    • 84904480100 scopus 로고    scopus 로고
    • A primary role for disulfide formation in the productive folding of prokaryotic Cu, Zn-superoxide dismutase
    • Sakurai, Y., Anzai, I. & Furukawa, Y. A primary role for disulfide formation in the productive folding of prokaryotic Cu, Zn-superoxide dismutase. J. Biol. Chem. 289, 20139-20149 (2014).
    • (2014) J. Biol. Chem , vol.289 , pp. 20139-20149
    • Sakurai, Y.1    Anzai, I.2    Furukawa, Y.3
  • 34
    • 34548497885 scopus 로고    scopus 로고
    • Control of DegP-dependent degradation of c-type cytochromes by heme and the cytochrome c maturation system in Escherichia coli
    • Gao, T. & O'Brian, M. R. Control of DegP-dependent degradation of c-type cytochromes by heme and the cytochrome c maturation system in Escherichia coli. J. Bacteriol. 189, 6253-6259 (2007).
    • (2007) J. Bacteriol , vol.189 , pp. 6253-6259
    • Gao, T.1    O'Brian, M.R.2
  • 35
    • 0032562651 scopus 로고    scopus 로고
    • The structure of glutamine-binding protein complexed with glutamine at 1.94 Å resolution: Comparisons with other amino acid binding proteins
    • Sun, Y. J., Rose, J., Wang, B. C. & Hsiao, C. D. The structure of glutamine-binding protein complexed with glutamine at 1.94 Å resolution: comparisons with other amino acid binding proteins. J. Mol. Biol. 278, 219-229 (1998).
    • (1998) J. Mol. Biol , vol.278 , pp. 219-229
    • Sun, Y.J.1    Rose, J.2    Wang, B.C.3    Hsiao, C.D.4
  • 37
    • 0036005637 scopus 로고    scopus 로고
    • Role of cofactors in protein folding
    • Wittung-Stafshede, P. Role of cofactors in protein folding. Acc. Chem. Res. 35, 201-208 (2002).
    • (2002) Acc. Chem. Res , vol.35 , pp. 201-208
    • Wittung-Stafshede, P.1
  • 38
    • 54549088946 scopus 로고    scopus 로고
    • Protein-folding location can regulate manganese-binding versus copper- or zinc-binding
    • Tottey, S. et al. Protein-folding location can regulate manganese-binding versus copper- or zinc-binding. Nature 455, 1138-1142 (2008).
    • (2008) Nature , vol.455 , pp. 1138-1142
    • Tottey, S.1
  • 39
    • 84902295043 scopus 로고    scopus 로고
    • Equilibrium folding of pro-HlyA from Escherichia coli reveals a stable calcium ion dependent folding intermediate
    • Thomas, S., Bakkes, P. J., Smits, S. H. & Schmitt, L. Equilibrium folding of pro-HlyA from Escherichia coli reveals a stable calcium ion dependent folding intermediate. Biochim. Biophys. Acta 1844, 1500-1510 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1844 , pp. 1500-1510
    • Thomas, S.1    Bakkes, P.J.2    Smits, S.H.3    Schmitt, L.4
  • 40
    • 24344509845 scopus 로고    scopus 로고
    • The role of calcium in the conformational dynamics and thermal stability of the d-galactose/d-glucose-binding protein from Escherichia coli
    • Herman, P. et al. The role of calcium in the conformational dynamics and thermal stability of the d-galactose/d-glucose-binding protein from Escherichia coli. Proteins 61, 184-195 (2005).
    • (2005) Proteins , vol.61 , pp. 184-195
    • Herman, P.1
  • 41
    • 84917742907 scopus 로고    scopus 로고
    • Molecular simulations of metal-coupled protein folding
    • Li, W., Wang, J., Zhang, J. & Wang, W. Molecular simulations of metal-coupled protein folding. Curr. Opin. Struct. Biol. 30, 25-31 (2015).
    • (2015) Curr. Opin. Struct. Biol , vol.30 , pp. 25-31
    • Li, W.1    Wang, J.2    Zhang, J.3    Wang, W.4
  • 42
    • 33645506272 scopus 로고    scopus 로고
    • Cofactor effects on the protein folding reaction: Acceleration of α-lactalbumin refolding by metal ions
    • Bushmarina, N. A., Blanchet, C. E., Vernier, G. & Forge, V. Cofactor effects on the protein folding reaction: acceleration of α-lactalbumin refolding by metal ions. Protein Sci. 15, 659-671 (2006).
    • (2006) Protein Sci , vol.15 , pp. 659-671
    • Bushmarina, N.A.1    Blanchet, C.E.2    Vernier, G.3    Forge, V.4
  • 43
    • 84899126341 scopus 로고    scopus 로고
    • Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA
    • Gessmann, D. et al. Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA. Proc. Natl Acad. Sci. USA 111, 5878-5883 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 5878-5883
    • Gessmann, D.1
  • 44
    • 84944699383 scopus 로고    scopus 로고
    • Lipids assist the membrane insertion of a BAM-independent outer membrane protein
    • Huysmans, G. H., Guilvout, I., Chami, M., Nickerson, N. N. & Pugsley, A. P. Lipids assist the membrane insertion of a BAM-independent outer membrane protein. Sci. Rep. 5, 15068 (2015).
    • (2015) Sci. Rep , vol.5
    • Huysmans, G.H.1    Guilvout, I.2    Chami, M.3    Nickerson, N.N.4    Pugsley, A.P.5
  • 45
    • 84901828074 scopus 로고    scopus 로고
    • Feeling the hidden mechanical forces in lipid bilayer is an original sense
    • Anishkin, A., Loukin, S. H., Teng, J. & Kung, C. Feeling the hidden mechanical forces in lipid bilayer is an original sense. Proc. Natl Acad. Sci. USA 111, 7898-7905 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 7898-7905
    • Anishkin, A.1    Loukin, S.H.2    Teng, J.3    Kung, C.4
  • 46
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie, J. U. Solving the membrane protein folding problem. Nature 438, 581-589 (2005).
    • (2005) Nature , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 47
    • 55549120907 scopus 로고    scopus 로고
    • Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro
    • Burgess, N. K., Dao, T. P., Stanley, A. M. & Fleming, K. G. Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro. J. Biol. Chem. 283, 26748-26758 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 26748-26758
    • Burgess, N.K.1    Dao, T.P.2    Stanley, A.M.3    Fleming, K.G.4
  • 48
    • 84902343087 scopus 로고    scopus 로고
    • Co-translational protein targeting to the bacterial membrane
    • Saraogi, I. & Shan, S. O. Co-translational protein targeting to the bacterial membrane. Biochim. Biophys. Acta 1843, 1433-1441 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1433-1441
    • Saraogi, I.1    Shan, S.O.2
  • 50
    • 17644386832 scopus 로고    scopus 로고
    • Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation
    • Huber, D. et al. Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation. J. Bacteriol. 187, 2983-2991 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 2983-2991
    • Huber, D.1
  • 51
    • 84863039852 scopus 로고    scopus 로고
    • Novel proteomic tools reveal essential roles of SRP and importance of proper membrane protein biogenesis
    • Zhang, D., Sweredoski, M. J., Graham, R. L., Hess, S. & Shan, S. O. Novel proteomic tools reveal essential roles of SRP and importance of proper membrane protein biogenesis. Mol. Cell. Proteomics 11, M111.011585 (2012).
    • (2012) Mol. Cell. Proteomics , vol.11
    • Zhang, D.1    Sweredoski, M.J.2    Graham, R.L.3    Hess, S.4    Shan, S.O.5
  • 52
  • 53
    • 84870859321 scopus 로고    scopus 로고
    • Breaking on through to the other side: Protein export through the bacterial Sec system
    • Chatzi, K. E., Sardis, M. F., Karamanou, S. & Economou, A. Breaking on through to the other side: protein export through the bacterial Sec system. Biochem. J. 449, 25-37 (2013).
    • (2013) Biochem. J , vol.449 , pp. 25-37
    • Chatzi, K.E.1    Sardis, M.F.2    Karamanou, S.3    Economou, A.4
  • 54
    • 70450171353 scopus 로고    scopus 로고
    • Signal peptides are allosteric activators of the protein translocase
    • Gouridis, G., Karamanou, S., Gelis, I., Kalodimos, C. G. & Economou, A. Signal peptides are allosteric activators of the protein translocase. Nature 462, 363-367 (2009).
    • (2009) Nature , vol.462 , pp. 363-367
    • Gouridis, G.1    Karamanou, S.2    Gelis, I.3    Kalodimos, C.G.4    Economou, A.5
  • 55
    • 0027458691 scopus 로고
    • SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli
    • Matsuyama, S., Fujita, Y. & Mizushima, S. SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli. Embo J. 12, 265-270 (1993).
    • (1993) Embo J , vol.12 , pp. 265-270
    • Matsuyama, S.1    Fujita, Y.2    Mizushima, S.3
  • 56
    • 70149110001 scopus 로고    scopus 로고
    • Detecting folding intermediates of a protein as it passes through the bacterial translocation channel
    • Kadokura, H. & Beckwith, J. Detecting folding intermediates of a protein as it passes through the bacterial translocation channel. Cell 138, 1164-1173 (2009).
    • (2009) Cell , vol.138 , pp. 1164-1173
    • Kadokura, H.1    Beckwith, J.2
  • 58
    • 84941670513 scopus 로고    scopus 로고
    • Type III secretion systems: The bacterial flagellum and the injectisome
    • Diepold, A. & Armitage, J. P. Type III secretion systems: the bacterial flagellum and the injectisome. Philos. Trans. R. Soc. Lond. B Biol. Sci. 370, 20150020 (2015).
    • (2015) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.370
    • Diepold, A.1    Armitage, J.P.2
  • 59
    • 84902267629 scopus 로고    scopus 로고
    • Protein transport by the bacterial Tat pathway
    • Patel, R., Smith, S. M. & Robinson, C. Protein transport by the bacterial Tat pathway. Biochim. Biophys. Acta 1843, 1620-1628 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1620-1628
    • Patel, R.1    Smith, S.M.2    Robinson, C.3
  • 60
    • 3142550604 scopus 로고    scopus 로고
    • Sequence analysis of bacterial redox enzyme maturation proteins (REMPs)
    • Turner, R. J., Papish, A. L. & Sargent, F. Sequence analysis of bacterial redox enzyme maturation proteins (REMPs). Can. J. Microbiol. 50, 225-238 (2004).
    • (2004) Can. J. Microbiol , vol.50 , pp. 225-238
    • Turner, R.J.1    Papish, A.L.2    Sargent, F.3
  • 61
    • 84929314375 scopus 로고    scopus 로고
    • Secretion systems in Gram-negative bacteria: Structural and mechanistic insights
    • Costa, T. R. et al. Secretion systems in Gram-negative bacteria: structural and mechanistic insights. Nature Rev. Microbiol. 13, 343-359 (2015).
    • (2015) Nature Rev. Microbiol , vol.13 , pp. 343-359
    • Costa, T.R.1
  • 62
    • 8844241421 scopus 로고    scopus 로고
    • Type i secretion in Gram-negative bacteria
    • Delepelaire, P. Type I secretion in Gram-negative bacteria. Biochim. Biophys. Acta 1694, 149-161 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 149-161
    • Delepelaire, P.1
  • 63
    • 84858226936 scopus 로고    scopus 로고
    • Type v secretion: Mechanism(s) of autotransport through the bacterial outer membrane
    • Leo, J. C., Grin, I. & Linke, D. Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane. Philos. Trans. R. Soc. Lond. B Biol. Sci. 367, 1088-1101 (2012).
    • (2012) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.367 , pp. 1088-1101
    • Leo, J.C.1    Grin, I.2    Linke, D.3
  • 64
    • 84902251736 scopus 로고    scopus 로고
    • Mechanism and structure of the bacterial type IV secretion systems
    • Christie, P. J., Whitaker, N. & Gonzalez-Rivera, C. Mechanism and structure of the bacterial type IV secretion systems. Biochim. Biophys. Acta 1843, 1578-1591 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1578-1591
    • Christie, P.J.1    Whitaker, N.2    Gonzalez-Rivera, C.3
  • 65
    • 77957116092 scopus 로고    scopus 로고
    • Type IV secretion systems: Versatility and diversity in function
    • Wallden, K., Rivera-Calzada, A. & Waksman, G. Type IV secretion systems: versatility and diversity in function. Cell Microbiol. 12, 1203-1212 (2010).
    • (2010) Cell Microbiol , vol.12 , pp. 1203-1212
    • Wallden, K.1    Rivera-Calzada, A.2    Waksman, G.3
  • 66
    • 84955388560 scopus 로고    scopus 로고
    • Aim load, fire: The type VI secretion system, a bacterial nanoweapon
    • Cianfanelli, F. R., Monlezun, L. & Coulthurst, S. J. Aim, load, fire: the type VI secretion system, a bacterial nanoweapon. Trends Microbiol. 24, 51-62 (2016).
    • (2016) Trends Microbiol , vol.24 , pp. 51-62
    • Cianfanelli, F.R.1    Monlezun, L.2    Coulthurst, S.J.3
  • 68
    • 35348892037 scopus 로고    scopus 로고
    • Type VII secretion - Mycobacteria show the way
    • Abdallah, A. M. et al. Type VII secretion - mycobacteria show the way. Nature Rev. Microbiol. 5, 883-891 (2007).
    • (2007) Nature Rev. Microbiol , vol.5 , pp. 883-891
    • Abdallah, A.M.1
  • 69
    • 80053280679 scopus 로고    scopus 로고
    • Lipoprotein sorting in bacteria
    • Okuda, S. & Tokuda, H. Lipoprotein sorting in bacteria. Annu. Rev. Microbiol. 65, 239-659 (2011).
    • (2011) Annu. Rev. Microbiol , vol.65 , pp. 239-659
    • Okuda, S.1    Tokuda, H.2
  • 70
    • 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. Proc. Natl Acad. Sci. USA 106, 5877-5882 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 5877-5882
    • Okuda, S.1    Tokuda, H.2
  • 72
    • 57649242773 scopus 로고    scopus 로고
    • Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp
    • Jarchow, S., Luck, C., Gorg, A. & Skerra, A. Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp. Proteomics 8, 4987-4994 (2008).
    • (2008) Proteomics , vol.8 , pp. 4987-4994
    • Jarchow, S.1    Luck, C.2    Gorg, A.3    Skerra, A.4
  • 73
    • 2642652226 scopus 로고    scopus 로고
    • Selection for a periplasmic factor improving phage display and functional periplasmic expression
    • Bothmann, H. & Pluckthun, A. Selection for a periplasmic factor improving phage display and functional periplasmic expression. Nature Biotechnol. 16, 376-380 (1998).
    • (1998) Nature Biotechnol , vol.16 , pp. 376-380
    • Bothmann, H.1    Pluckthun, A.2
  • 74
    • 84887429368 scopus 로고    scopus 로고
    • Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp
    • Burmann, B. M., Wang, C. & Hiller, S. Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp. Nature Struct. Mol. Biol. 20, 1265-1272 (2013).
    • (2013) Nature Struct. Mol. Biol , vol.20 , pp. 1265-1272
    • Burmann, B.M.1    Wang, C.2    Hiller, S.3
  • 75
    • 0038831330 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis, trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro
    • Ramm, K. & Pluckthun, A. The periplasmic Escherichia coli peptidylprolyl cis, trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro. J. Biol. Chem. 275, 17106-17113 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 17106-17113
    • Ramm, K.1    Pluckthun, A.2
  • 76
    • 0039423955 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis, trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines
    • Bothmann, H. & Pluckthun, A. The periplasmic Escherichia coli peptidylprolyl cis, trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines. J. Biol. Chem. 275, 17100-17105 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 17100-17105
    • Bothmann, H.1    Pluckthun, A.2
  • 77
    • 75149136165 scopus 로고    scopus 로고
    • The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity
    • Weininger, U., Jakob, R. P., Kovermann, M., Balbach, J. & Schmid, F. X. The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity. Protein Sci. 19, 6-18 (2010).
    • (2010) Protein Sci , vol.19 , pp. 6-18
    • Weininger, U.1    Jakob, R.P.2    Kovermann, M.3    Balbach, J.4    Schmid, F.X.5
  • 78
    • 84905382347 scopus 로고    scopus 로고
    • Dynamic interaction of the sec translocon with the chaperone PpiD
    • Sachelaru, I., Petriman, N. A., Kudva, R. & Koch, H. G. Dynamic interaction of the sec translocon with the chaperone PpiD. J. Biol. Chem. 289, 21706-21715 (2014).
    • (2014) J. Biol. Chem , vol.289 , pp. 21706-21715
    • Sachelaru, I.1    Petriman, N.A.2    Kudva, R.3    Koch, H.G.4
  • 79
    • 43949125856 scopus 로고    scopus 로고
    • The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon
    • Antonoaea, R., Furst, M., Nishiyama, K. & Muller, M. The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon. Biochemistry 47, 5649-5656 (2008).
    • (2008) Biochemistry , vol.47 , pp. 5649-5656
    • Antonoaea, R.1    Furst, M.2    Nishiyama, K.3    Muller, M.4
  • 80
    • 27744565064 scopus 로고    scopus 로고
    • Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli
    • Justice, S. S. et al. Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli. J. Bacteriol. 187, 7680-6 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 7680-7686
    • Justice, S.S.1
  • 81
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess, C., Beil, A. & Ehrmann, M. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97, 339-347 (1999).
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 82
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • Krojer, T. et al. Structural basis for the regulated protease and chaperone function of DegP. Nature 453, 885-890 (2008).
    • (2008) Nature , vol.453 , pp. 885-890
    • Krojer, T.1
  • 83
    • 34447644224 scopus 로고    scopus 로고
    • Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock
    • Skorko-Glonek, J., Laskowska, E., Sobiecka-Szkatula, A. & Lipinska, B. Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock. Arch. Biochem. Biophys. 464, 80-89 (2007).
    • (2007) Arch. Biochem. Biophys , vol.464 , pp. 80-89
    • Skorko-Glonek, J.1    Laskowska, E.2    Sobiecka-Szkatula, A.3    Lipinska, B.4
  • 84
    • 84894281306 scopus 로고    scopus 로고
    • DegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in the Gram-negative bacterium Escherichia coli
    • Ge, X. et al. DegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in the Gram-negative bacterium Escherichia coli. Febs J. 281, 1226-1240 (2014).
    • (2014) Febs J , vol.281 , pp. 1226-1240
    • Ge, X.1
  • 85
    • 84878877273 scopus 로고    scopus 로고
    • Disulfide bond formation in the bacterial periplasm: Major achievements and challenges ahead
    • Denoncin, K. & Collet, J. F. Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead. Antioxid. Redox Signal. 19, 63-71 (2013).
    • (2013) Antioxid. Redox Signal , vol.19 , pp. 63-71
    • Denoncin, K.1    Collet, J.F.2
  • 86
    • 84875037470 scopus 로고    scopus 로고
    • Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm
    • Moon, C. P., Zaccai, N. R., Fleming, P. J., Gessmann, D. & Fleming, K. G. Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm. Proc. Natl Acad. Sci. USA 110, 4285-4290 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 4285-4290
    • Moon, C.P.1    Zaccai, N.R.2    Fleming, P.J.3    Gessmann, D.4    Fleming, K.G.5
  • 87
    • 84875065984 scopus 로고    scopus 로고
    • Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS
    • Dunstan, R. A. et al. Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS. PLoS Pathog. 9, e1003117 (2013).
    • (2013) PLoS Pathog , vol.9
    • Dunstan, R.A.1
  • 88
    • 84939268636 scopus 로고    scopus 로고
    • A novel pathway for outer membrane protein biogenesis in Gram-negative bacteria
    • Jeeves, M. & Knowles, T. J. A novel pathway for outer membrane protein biogenesis in Gram-negative bacteria. Mol. Microbiol. 97, 607-611 (2015).
    • (2015) Mol. Microbiol , vol.97 , pp. 607-611
    • Jeeves, M.1    Knowles, T.J.2
  • 89
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity
    • Behrens, S., Maier, R., de Cock, H., Schmid, F. X. & Gross, C. A. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. Embo J. 20, 285-294 (2001).
    • (2001) Embo J , vol.20 , pp. 285-294
    • Behrens, S.1    Maier, R.2    De Cock, H.3    Schmid, F.X.4    Gross, C.A.5
  • 90
    • 1542571983 scopus 로고    scopus 로고
    • The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins
    • Bitto, E. & McKay, D. B. The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins. J. Biol. Chem. 278, 49316-49322 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 49316-49322
    • Bitto, E.1    McKay, D.B.2
  • 91
    • 84914094309 scopus 로고    scopus 로고
    • Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: What have we learned to date? Arch
    • McMorran, L. M., Brockwell, D. J. & Radford, S. E. Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date? Arch. Biochem. Biophys. 564, 265-280 (2014).
    • (2014) Biochem. Biophys , vol.564 , pp. 265-280
    • McMorran, L.M.1    Brockwell, D.J.2    Radford, S.E.3
  • 92
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • Chen, R. & Henning, U. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol. Microbiol. 19, 1287-1294 (1996).
    • (1996) Mol. Microbiol , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 93
    • 70350520053 scopus 로고    scopus 로고
    • The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential
    • Patel, G. J., Behrens-Kneip, S., Holst, O. & Kleinschmidt, J. H. The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential. Biochemistry 48, 10235-10245 (2009).
    • (2009) Biochemistry , vol.48 , pp. 10235-10245
    • Patel, G.J.1    Behrens-Kneip, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 94
    • 84943450201 scopus 로고    scopus 로고
    • Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins
    • Thoma, J., Burmann, B. M., Hiller, S. & Muller, D. J. Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins. Nature Struct. Mol. Biol. 22, 795-802 (2015).
    • (2015) Nature Struct. Mol. Biol , vol.22 , pp. 795-802
    • Thoma, J.1    Burmann, B.M.2    Hiller, S.3    Muller, D.J.4
  • 95
    • 84880965951 scopus 로고    scopus 로고
    • Role for Skp in LptD assembly in Escherichia coli
    • Schwalm, J., Mahoney, T. F., Soltes, G. R. & Silhavy, T. J. Role for Skp in LptD assembly in Escherichia coli. J. Bacteriol. 195, 3734-3742 (2013).
    • (2013) J. Bacteriol , vol.195 , pp. 3734-3742
    • Schwalm, J.1    Mahoney, T.F.2    Soltes, G.R.3    Silhavy, T.J.4
  • 96
    • 84884305905 scopus 로고    scopus 로고
    • Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli
    • Narita, S., Masui, C., Suzuki, T., Dohmae, N. & Akiyama, Y. Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli. Proc. Natl Acad. Sci. USA 110, E3612-E3621 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110
    • Narita, S.1    Masui, C.2    Suzuki, T.3    Dohmae, N.4    Akiyama, Y.5
  • 97
    • 77952363712 scopus 로고    scopus 로고
    • Reconstitution of outer membrane protein assembly from purified components
    • Hagan, C. L., Kim, S. & Kahne, D. Reconstitution of outer membrane protein assembly from purified components. Science 328, 890-892 (2010).
    • (2010) Science , vol.328 , pp. 890-892
    • Hagan, C.L.1    Kim, S.2    Kahne, D.3
  • 98
    • 0042878499 scopus 로고    scopus 로고
    • Membrane protein folding on the example of outer membrane protein A of Escherichia coli
    • Kleinschmidt, J. H. Membrane protein folding on the example of outer membrane protein A of Escherichia coli. Cell. Mol. Life Sci. 60, 1547-1558 (2003).
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 1547-1558
    • Kleinschmidt, J.H.1
  • 99
    • 67650711063 scopus 로고    scopus 로고
    • Folding and trimerization of signal sequence-less mature TolC in the cytoplasm of Escherichia coli
    • Masi, M., Duret, G., Delcour, A. H. & Misra, R. Folding and trimerization of signal sequence-less mature TolC in the cytoplasm of Escherichia coli. Microbiology 155, 1847-1857 (2009).
    • (2009) Microbiology , vol.155 , pp. 1847-1857
    • Masi, M.1    Duret, G.2    Delcour, A.H.3    Misra, R.4
  • 101
    • 84904181910 scopus 로고    scopus 로고
    • Lateral opening and exit pore formation are required for BamA function
    • Noinaj, N., Kuszak, A. J., Balusek, C., Gumbart, J. C. & Buchanan, S. K. Lateral opening and exit pore formation are required for BamA function. Structure 22, 1055-1062 (2014).
    • (2014) Structure , vol.22 , pp. 1055-1062
    • Noinaj, N.1    Kuszak, A.J.2    Balusek, C.3    Gumbart, J.C.4    Buchanan, S.K.5
  • 102
    • 84924962448 scopus 로고    scopus 로고
    • The β-barrel membrane protein insertase machinery from Gram-negative bacteria
    • Noinaj, N., Rollauer, S. E. & Buchanan, S. K. The β-barrel membrane protein insertase machinery from Gram-negative bacteria. Curr. Opin. Struct. Biol. 31, 35-42 (2015).
    • (2015) Curr. Opin. Struct. Biol , vol.31 , pp. 35-42
    • Noinaj, N.1    Rollauer, S.E.2    Buchanan, S.K.3
  • 103
    • 84960117472 scopus 로고    scopus 로고
    • Structural basis of outer membrane protein insertion by the BAM complex
    • Gu, Y. et al. Structural basis of outer membrane protein insertion by the BAM complex. Nature 531, 64-69 (2016).
    • (2016) Nature , vol.531 , pp. 64-69
    • Gu, Y.1
  • 104
    • 84860719904 scopus 로고    scopus 로고
    • Discovery of an archetypal protein transport system in bacterial outer membranes
    • Selkrig, J. et al. Discovery of an archetypal protein transport system in bacterial outer membranes. Nature Struct. Mol. Biol. 19, 506-510 (2012).
    • (2012) Nature Struct. Mol. Biol , vol.19 , pp. 506-510
    • Selkrig, J.1
  • 105
    • 84902327125 scopus 로고    scopus 로고
    • Assembly of β-barrel proteins into bacterial outer membranes
    • Selkrig, J., Leyton, D. L., Webb, C. T. & Lithgow, T. Assembly of β-barrel proteins into bacterial outer membranes. Biochim. Biophys. Acta 1843, 1542-1550 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1542-1550
    • Selkrig, J.1    Leyton, D.L.2    Webb, C.T.3    Lithgow, T.4
  • 107
    • 70350470007 scopus 로고    scopus 로고
    • Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae
    • Ruiz-Perez, F. et al. Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae. J. Bacteriol. 191, 6571-6583 (2009).
    • (2009) J. Bacteriol , vol.191 , pp. 6571-6583
    • Ruiz-Perez, F.1
  • 108
    • 33744746602 scopus 로고    scopus 로고
    • The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation
    • Rutherford, N., Charbonneau, M. E., Berthiaume, F., Betton, J. M. & Mourez, M. The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation. J. Bacteriol. 188, 4111-4116 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 4111-4116
    • Rutherford, N.1    Charbonneau, M.E.2    Berthiaume, F.3    Betton, J.M.4    Mourez, M.5
  • 109
    • 84939171436 scopus 로고    scopus 로고
    • Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes
    • Shen, H. H. et al. Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes. Nature Commun. 5, 5078 (2014).
    • (2014) Nature Commun , vol.5 , pp. 5078
    • Shen, H.H.1
  • 110
    • 84887430811 scopus 로고    scopus 로고
    • The structural basis of autotransporter translocation by TamA
    • Gruss, F. et al. The structural basis of autotransporter translocation by TamA. Nature Struct. Mol. Biol. 20, 1318-1320 (2013).
    • (2013) Nature Struct. Mol. Biol , vol.20 , pp. 1318-1320
    • Gruss, F.1
  • 111
    • 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. Proc. Natl Acad. Sci. USA 106, 19120-19125 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 19120-19125
    • Ieva, R.1    Bernstein, H.D.2
  • 112
    • 79961138396 scopus 로고    scopus 로고
    • The essential β-barrel assembly machinery complex components BamD and BamA are required for autotransporter biogenesis
    • Rossiter, A. E. et al. The essential β-barrel assembly machinery complex components BamD and BamA are required for autotransporter biogenesis. J. Bacteriol. 193, 4250-4253 (2011).
    • (2011) J. Bacteriol , vol.193 , pp. 4250-4253
    • Rossiter, A.E.1
  • 113
    • 84860134831 scopus 로고    scopus 로고
    • Autotransporters: The cellular environment reshapes a folding mechanism to promote protein transport
    • Braselmann, E. & Clark, P. L. Autotransporters: the cellular environment reshapes a folding mechanism to promote protein transport. J. Phys. Chem. Lett. 3, 1063-1071 (2012).
    • (2012) J. Phys. Chem. Lett , vol.3 , pp. 1063-1071
    • Braselmann, E.1    Clark, P.L.2
  • 114
    • 84890278171 scopus 로고    scopus 로고
    • Stepwise folding of an autotransporter passenger domain is not essential for its secretion
    • Kang'ethe, W. & Bernstein, H. D. Stepwise folding of an autotransporter passenger domain is not essential for its secretion. J. Biol. Chem. 288, 35028-35038 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 35028-35038
    • Kang'Ethe, W.1    Bernstein, H.D.2
  • 115
    • 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. Mol. Microbiol. 97, 205-215 (2015).
    • (2015) Mol. Microbiol , vol.97 , pp. 205-215
    • Bernstein, H.D.1
  • 116
    • 84960466600 scopus 로고    scopus 로고
    • Bacterial amyloid formation: Structural insights into curli biogensis
    • Van Gerven, N., Klein, R. D., Hultgren, S. J. & Remaut, H. Bacterial amyloid formation: structural insights into curli biogensis. Trends Microbiol. 23, 693-706 (2015).
    • (2015) Trends Microbiol , vol.23 , pp. 693-706
    • Van Gerven, N.1    Klein, R.D.2    Hultgren, S.J.3    Remaut, H.4
  • 118
    • 33645055929 scopus 로고    scopus 로고
    • Secretion of curli fibre subunits is mediated by the outer membrane-localized CsgG protein
    • Robinson, L. S., Ashman, E. M., Hultgren, S. J. & Chapman, M. R. Secretion of curli fibre subunits is mediated by the outer membrane-localized CsgG protein. Mol. Microbiol. 59, 870-881 (2006).
    • (2006) Mol. Microbiol , vol.59 , pp. 870-881
    • Robinson, L.S.1    Ashman, E.M.2    Hultgren, S.J.3    Chapman, M.R.4
  • 119
    • 84860171314 scopus 로고    scopus 로고
    • The E. Coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism
    • Shu, Q. et al. The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. Proc. Natl Acad. Sci. USA 109, 6502-6507 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 6502-6507
    • Shu, Q.1
  • 120
    • 84921858909 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG
    • Goyal, P. et al. Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG. Nature 516, 250-253 (2014).
    • (2014) Nature , vol.516 , pp. 250-253
    • Goyal, P.1
  • 121
    • 84902314008 scopus 로고    scopus 로고
    • The molecular dissection of the chaperone-usher pathway
    • Geibel, S. & Waksman, G. The molecular dissection of the chaperone-usher pathway. Biochim. Biophys. Acta 1843, 1559-1567 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1559-1567
    • Geibel, S.1    Waksman, G.2
  • 122
    • 78049444220 scopus 로고    scopus 로고
    • Escherichia coli K-12 possesses multiple cryptic but functional chaperone-usher fimbriae with distinct surface specificities
    • Korea, C. G., Badouraly, R., Prevost, M. C., Ghigo, J. M. & Beloin, C. Escherichia coli K-12 possesses multiple cryptic but functional chaperone-usher fimbriae with distinct surface specificities. Environ. Microbiol. 12, 1957-1977 (2010).
    • (2010) Environ. Microbiol , vol.12 , pp. 1957-1977
    • Korea, C.G.1    Badouraly, R.2    Prevost, M.C.3    Ghigo, J.M.4    Beloin, C.5
  • 123
    • 43049171700 scopus 로고    scopus 로고
    • Fiber formation across the bacterial outer membrane by the chaperone/usher pathway
    • Remaut, H. et al. Fiber formation across the bacterial outer membrane by the chaperone/usher pathway. Cell 133, 640-652 (2008).
    • (2008) Cell , vol.133 , pp. 640-652
    • Remaut, H.1
  • 124
    • 84864261756 scopus 로고    scopus 로고
    • Quality control of disulfide bond formation in pilus subunits by the chaperone FimC
    • Crespo, M. D. et al. Quality control of disulfide bond formation in pilus subunits by the chaperone FimC. Nature Chem. Biol. 8, 707-713 (2012).
    • (2012) Nature Chem. Biol , vol.8 , pp. 707-713
    • Crespo, M.D.1
  • 125
    • 10744220460 scopus 로고    scopus 로고
    • Vesicle-mediated export and assembly of pore-forming oligomers of the enterobacterial ClyA cytotoxin
    • Wai, S. N. et al. Vesicle-mediated export and assembly of pore-forming oligomers of the enterobacterial ClyA cytotoxin. Cell 115, 25-35 (2003).
    • (2003) Cell , vol.115 , pp. 25-35
    • Wai, S.N.1
  • 126
    • 84863533501 scopus 로고    scopus 로고
    • A protein export pathway involving Escherichia coli porins
    • Prehna, G. et al. A protein export pathway involving Escherichia coli porins. Structure 20, 1154-1166 (2012).
    • (2012) Structure , vol.20 , pp. 1154-1166
    • Prehna, G.1
  • 127
    • 34748828756 scopus 로고    scopus 로고
    • Global proteomic profiling of native outer membrane vesicles derived from Escherichia coli
    • Lee, E. Y. et al. Global proteomic profiling of native outer membrane vesicles derived from Escherichia coli. Proteomics 7, 3143-3153 (2007).
    • (2007) Proteomics , vol.7 , pp. 3143-3153
    • Lee, E.Y.1
  • 128
    • 84941877295 scopus 로고    scopus 로고
    • Outer-membrane vesicles from Gram-negative bacteria: Biogenesis and functions
    • Schwechheimer, C. & Kuehn, M. J. Outer-membrane vesicles from Gram-negative bacteria: biogenesis and functions. Nature Rev. Microbiol. 13, 605-619 (2015).
    • (2015) Nature Rev. Microbiol , vol.13 , pp. 605-619
    • Schwechheimer, C.1    Kuehn, M.J.2
  • 129
    • 84886681946 scopus 로고    scopus 로고
    • A non-classical assembly pathway of Escherichia coli pore-forming toxin cytolysin A
    • Fahie, M. et al. A non-classical assembly pathway of Escherichia coli pore-forming toxin cytolysin A. J. Biol. Chem. 288, 31042-31051 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 31042-31051
    • Fahie, M.1
  • 130
    • 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. Biochim. Biophys. Acta 1843, 1568-1577 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1568-1577
    • Nivaskumar, M.1    Francetic, O.2
  • 131
    • 0034671617 scopus 로고    scopus 로고
    • Expression of the endogenous type II secretion pathway in Escherichia coli leads to chitinase secretion
    • Francetic, O., Belin, D., Badaut, C. & Pugsley, A. P. Expression of the endogenous type II secretion pathway in Escherichia coli leads to chitinase secretion. Embo J. 19, 6697-6703 (2000).
    • (2000) Embo J , vol.19 , pp. 6697-6703
    • Francetic, O.1    Belin, D.2    Badaut, C.3    Pugsley, A.P.4
  • 132
    • 78449293752 scopus 로고    scopus 로고
    • Swimming against the tide: Progress and challenges in our understanding of colicin translocation
    • Kleanthous, C. Swimming against the tide: progress and challenges in our understanding of colicin translocation. Nature Rev. Microbiol. 8, 843-848 (2010).
    • (2010) Nature Rev. Microbiol , vol.8 , pp. 843-848
    • Kleanthous, C.1
  • 133
    • 84870167740 scopus 로고    scopus 로고
    • Pathways of colicin import: Utilization of BtuB, OmpF porin and the TolC drug-export protein
    • Zakharov, S. D., Sharma, O., Zhalnina, M., Yamashita, E. & Cramer, W. A. Pathways of colicin import: utilization of BtuB, OmpF porin and the TolC drug-export protein. Biochem. Soc. Trans. 40, 1463-1468 (2012).
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 1463-1468
    • Zakharov, S.D.1    Sharma, O.2    Zhalnina, M.3    Yamashita, E.4    Cramer, W.A.5
  • 134
    • 84879672979 scopus 로고    scopus 로고
    • Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF
    • Housden, N. G. et al. Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF. Science 340, 1570-1574 (2013).
    • (2013) Science , vol.340 , pp. 1570-1574
    • Housden, N.G.1
  • 135
    • 54449087613 scopus 로고    scopus 로고
    • Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli
    • Zeth, K., Romer, C., Patzer, S. I. & Braun, V. Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli. J. Biol. Chem. 283, 25324-25331 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 25324-25331
    • Zeth, K.1    Romer, C.2    Patzer, S.I.3    Braun, V.4
  • 136
    • 47749139311 scopus 로고    scopus 로고
    • Periplasmic chaperone FkpA is essential for imported colicin M toxicity
    • Hullmann, J., Patzer, S. I., Romer, C., Hantke, K. & Braun, V. Periplasmic chaperone FkpA is essential for imported colicin M toxicity. Mol. Microbiol. 69, 926-937 (2008).
    • (2008) Mol. Microbiol , vol.69 , pp. 926-937
    • Hullmann, J.1    Patzer, S.I.2    Romer, C.3    Hantke, K.4    Braun, V.5
  • 137
    • 84920502297 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2014
    • Walsh, G. Biopharmaceutical benchmarks 2014. Nature Biotechnol. 32, 992-1000 (2014).
    • (2014) Nature Biotechnol , vol.32 , pp. 992-1000
    • Walsh, G.1
  • 138
    • 84937411096 scopus 로고    scopus 로고
    • Production of biopharmaceuticals in E. Coli: Current scenario and future perspectives
    • Baeshen, M. N. et al. Production of biopharmaceuticals in E. coli: current scenario and future perspectives. J. Microbiol. Biotechnol. 25, 953-962 (2015).
    • (2015) J. Microbiol. Biotechnol , vol.25 , pp. 953-962
    • Baeshen, M.N.1
  • 139
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • Choi, J. H. & Lee, S. Y. Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl. Microbiol. Biotechnol. 64, 625-635 (2004).
    • (2004) Appl. Microbiol. Biotechnol , vol.64 , pp. 625-635
    • Choi, J.H.1    Lee, S.Y.2
  • 140
    • 33745931632 scopus 로고    scopus 로고
    • A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli
    • Schlapschy, M., Grimm, S. & Skerra, A. A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli. Protein Eng. Des. Sel. 19, 385-390 (2006).
    • (2006) Protein Eng. Des. Sel , vol.19 , pp. 385-390
    • Schlapschy, M.1    Grimm, S.2    Skerra, A.3
  • 141
    • 62149096127 scopus 로고    scopus 로고
    • Use of folding modulators to improve heterologous protein production in Escherichia coli
    • Kolaj, O., Spada, S., Robin, S. & Wall, J. G. Use of folding modulators to improve heterologous protein production in Escherichia coli. Microb. Cell. Fact. 8, 9 (2009).
    • (2009) Microb. Cell. Fact , vol.8 , pp. 9
    • Kolaj, O.1    Spada, S.2    Robin, S.3    Wall, J.G.4
  • 143
    • 77955068108 scopus 로고    scopus 로고
    • Bacterial surface proteins and vaccines
    • Grandi, G. Bacterial surface proteins and vaccines. F1000 Biol. Rep. 2, 36 (2010).
    • (2010) F1000 Biol. Rep , vol.2 , pp. 36
    • Grandi, G.1
  • 144
    • 85028104443 scopus 로고    scopus 로고
    • Bacterial outer membrane vesicles in disease and preventive medicine
    • Unal, C. M., Schaar, V. & Riesbeck, K. Bacterial outer membrane vesicles in disease and preventive medicine. Semin. Immunopathol. 33, 395-408 (2011).
    • (2011) Semin. Immunopathol , vol.33 , pp. 395-408
    • Unal, C.M.1    Schaar, V.2    Riesbeck, K.3
  • 145
    • 84876001000 scopus 로고    scopus 로고
    • Immunization with Escherichia coli outer membrane vesicles protects bacteria-induced lethality via Th1 and Th17 cell responses
    • Kim, O. Y. et al. Immunization with Escherichia coli outer membrane vesicles protects bacteria-induced lethality via Th1 and Th17 cell responses. J. Immunol. 190, 4092-4102 (2013).
    • (2013) J. Immunol , vol.190 , pp. 4092-4102
    • Kim, O.Y.1
  • 146
    • 78751624924 scopus 로고    scopus 로고
    • Decorating microbes: Surface display of proteins on Escherichia coli
    • van Bloois, E., Winter, R. T., Kolmar, H. & Fraaije, M. W. Decorating microbes: surface display of proteins on Escherichia coli. Trends Biotechnol. 29, 79-86 (2011).
    • (2011) Trends Biotechnol , vol.29 , pp. 79-86
    • Van Bloois, E.1    Winter, R.T.2    Kolmar, H.3    Fraaije, M.W.4
  • 147
    • 84920250270 scopus 로고    scopus 로고
    • Bacterial whole-cell biocatalysts by surface display of enzymes: Toward industrial application
    • Schuurmann, J., Quehl, P., Festel, G. & Jose, J. Bacterial whole-cell biocatalysts by surface display of enzymes: toward industrial application. Appl. Microbiol. Biotechnol. 98, 8031-8046 (2014).
    • (2014) Appl. Microbiol. Biotechnol , vol.98 , pp. 8031-8046
    • Schuurmann, J.1    Quehl, P.2    Festel, G.3    Jose, J.4
  • 150
    • 84902314412 scopus 로고    scopus 로고
    • Everything old is new again: An update on current research on the Cpx envelope stress response
    • Raivio, T. L. Everything old is new again: an update on current research on the Cpx envelope stress response. Biochim. Biophys. Acta. 1843, 1529-1541 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1529-1541
    • Raivio, T.L.1
  • 151
    • 70349664195 scopus 로고    scopus 로고
    • Global analysis of extracytoplasmic stress signaling in Escherichia coli
    • Bury-Mone, S. et al. Global analysis of extracytoplasmic stress signaling in Escherichia coli. PLoS Genet. 5, e1000651 (2009).
    • (2009) PLoS Genet , vol.5
    • Bury-Mone, S.1
  • 152
    • 0035877593 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli σe regulon
    • Dartigalongue, C., Missiakas, D. & Raina, S. Characterization of the Escherichia coli σE regulon. J. Biol. Chem. 276, 20866-20875 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 20866-20875
    • Dartigalongue, C.1    Missiakas, D.2    Raina, S.3
  • 153
    • 80052235693 scopus 로고    scopus 로고
    • Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope
    • Sawa, J. et al. Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope. J. Biol. Chem. 286, 30680-30690 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 30680-30690
    • Sawa, J.1
  • 154
    • 84856708887 scopus 로고    scopus 로고
    • Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ
    • Malet, H. et al. Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ. Nature Struct. Mol. Biol. 19, 152-157 (2012).
    • (2012) Nature Struct. Mol. Biol , vol.19 , pp. 152-157
    • Malet, H.1
  • 155
    • 63049096052 scopus 로고    scopus 로고
    • Characterization of the Cpx regulon in Escherichia coli strain MC4100
    • Price, N. L. & Raivio, T. L. Characterization of the Cpx regulon in Escherichia coli strain MC4100. J. Bacteriol. 191, 1798-1815 (2009).
    • (2009) J. Bacteriol , vol.191 , pp. 1798-1815
    • Price, N.L.1    Raivio, T.L.2
  • 156
    • 79952363991 scopus 로고    scopus 로고
    • Genetic selection designed to stabilize proteins uncovers a chaperone called Spy
    • Quan, S. et al. Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nature Struct. Mol. Biol. 18, 262-269 (2011).
    • (2011) Nature Struct. Mol. Biol , vol.18 , pp. 262-269
    • Quan, S.1
  • 158
    • 84919922342 scopus 로고    scopus 로고
    • Detecting envelope stress by monitoring β-barrel assembly
    • Cho, S. H. et al. Detecting envelope stress by monitoring β-barrel assembly. Cell 159, 1652-1664 (2014).
    • (2014) Cell , vol.159 , pp. 1652-1664
    • Cho, S.H.1
  • 159
    • 0036033555 scopus 로고    scopus 로고
    • A third envelope stress signal transduction pathway in Escherichia coli
    • Raffa, R. G. & Raivio, T. L. A third envelope stress signal transduction pathway in Escherichia coli. Mol. Microbiol. 45, 1599-1611 (2002).
    • (2002) Mol. Microbiol , vol.45 , pp. 1599-1611
    • Raffa, R.G.1    Raivio, T.L.2
  • 160
    • 77955127606 scopus 로고    scopus 로고
    • Managing membrane stress: The phage shock protein (Psp) response, from molecular mechanisms to physiology
    • Joly, N. et al. Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology. FEMS Microbiol. Rev. 34, 797-827 (2010).
    • (2010) FEMS Microbiol. Rev , vol.34 , pp. 797-827
    • Joly, N.1
  • 161
    • 11444262208 scopus 로고    scopus 로고
    • Beyond transcription - New mechanisms for the regulation of molecular chaperones
    • Winter, J. & Jakob, U. Beyond transcription - new mechanisms for the regulation of molecular chaperones. Crit. Rev. Biochem. Mol. Biol. 39, 297-317 (2004).
    • (2004) Crit. Rev. Biochem. Mol. Biol , vol.39 , pp. 297-317
    • Winter, J.1    Jakob, U.2
  • 162
    • 65249182171 scopus 로고    scopus 로고
    • Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding
    • Tapley, T. L. et al. Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. Proc. Natl Acad. Sci. USA 106, 5557-5562 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 5557-5562
    • Tapley, T.L.1
  • 163
    • 46649106145 scopus 로고    scopus 로고
    • Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB
    • Malki, A. et al. Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB. J. Biol. Chem. 283, 13679-13687 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 13679-13687
    • Malki, A.1
  • 165
    • 80052967509 scopus 로고    scopus 로고
    • A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance
    • Zhang, M. et al. A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance. Nature Chem. Biol. 7, 671-677 (2011).
    • (2011) Nature Chem. Biol , vol.7 , pp. 671-677
    • Zhang, M.1
  • 166
    • 4143114616 scopus 로고    scopus 로고
    • Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation
    • Walton, T. A. & Sousa, M. C. Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol. Cell 15, 367-374 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 367-374
    • Walton, T.A.1    Sousa, M.C.2
  • 167
    • 84954392993 scopus 로고    scopus 로고
    • Deuterium labeling together with contrast variation small-angle neutron scattering suggests how Skp captures and releases unfolded outer membrane proteins
    • Zaccai, N. R. et al. Deuterium labeling together with contrast variation small-angle neutron scattering suggests how Skp captures and releases unfolded outer membrane proteins. Methods Enzymol. 566, 159-210 (2016).
    • (2016) Methods Enzymol , vol.566 , pp. 159-210
    • Zaccai, N.R.1
  • 168
    • 84876253260 scopus 로고    scopus 로고
    • Structural and energetic basis of folded-protein transport by the FimD usher
    • Geibel, S., Procko, E., Hultgren, S. J., Baker, D. & Waksman, G. Structural and energetic basis of folded-protein transport by the FimD usher. Nature 496, 243-246 (2013).
    • (2013) Nature , vol.496 , pp. 243-246
    • Geibel, S.1    Procko, E.2    Hultgren, S.J.3    Baker, D.4    Waksman, G.5
  • 169
    • 0034111320 scopus 로고    scopus 로고
    • The Salmonella FlgA protein, a putativeve periplasmic chaperone essential for flagellar P ring formation
    • Nambu, T. & Kutsukake, K. The Salmonella FlgA protein, a putativeve periplasmic chaperone essential for flagellar P ring formation. Microbiology 146, 1171-1178 (2000).
    • (2000) Microbiology , vol.146 , pp. 1171-1178
    • Nambu, T.1    Kutsukake, K.2
  • 170
    • 84864869866 scopus 로고    scopus 로고
    • Cloning, purification, crystallization and preliminary X-ray diffraction studies of Escherichia coli PapD-like protein (EcpD)
    • Pandey, N. K., Pal, R. K., Kashyap, M. & Bhavesh, N. S. Cloning, purification, crystallization and preliminary X-ray diffraction studies of Escherichia coli PapD-like protein (EcpD). Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68, 954-957 (2012).
    • (2012) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.68 , pp. 954-957
    • Pandey, N.K.1    Pal, R.K.2    Kashyap, M.3    Bhavesh, N.S.4
  • 171
    • 84920403296 scopus 로고    scopus 로고
    • Identification of putative substrates for the periplasmic chaperone YfgM in Escherichia coli using quantitative proteomics
    • Gotzke, H. et al. Identification of putative substrates for the periplasmic chaperone YfgM in Escherichia coli using quantitative proteomics. Mol. Cell Proteomics 14, 216-226 (2015).
    • (2015) Mol. Cell Proteomics , vol.14 , pp. 216-226
    • Gotzke, H.1
  • 172
    • 0346366809 scopus 로고    scopus 로고
    • Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
    • Saul, F. A. et al. Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J. Mol. Biol. 335, 595-608 (2004).
    • (2004) J. Mol. Biol , vol.335 , pp. 595-608
    • Saul, F.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.