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Volumn 22, Issue 7, 2015, Pages 540-546

The pilus usher controls protein interactions via domain masking and is functional as an oligomer

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; FIMC PROTEIN; FIMD PROTEIN; FIMH PROTEIN; OLIGOMER; OUTER MEMBRANE PROTEIN; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; FIMBRIA PROTEIN; FIMD PROTEIN, E COLI;

EID: 84936847500     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3044     Document Type: Article
Times cited : (29)

References (51)
  • 1
    • 37349093031 scopus 로고    scopus 로고
    • Evolution of the chaperone/usher assembly pathway: Fimbrial classification goes Greek
    • Nuccio, S.P. & Baumler, A.J. Evolution of the chaperone/usher assembly pathway: fimbrial classification goes Greek. Microbiol. Mol. Biol. Rev. 71, 551-575 (2007).
    • (2007) Microbiol. Mol. Biol. Rev , vol.71 , pp. 551-575
    • Nuccio, S.P.1    Baumler, A.J.2
  • 2
    • 77950384104 scopus 로고    scopus 로고
    • Adhesive organelles of gram-negative pathogens assembled with the classical chaperone/usher machinery: Structure and function from a clinical standpoint
    • Zav'yalov, V., Zavialov, A., Zav'yalova, G. & Korpela, T. Adhesive organelles of Gram-negative pathogens assembled with the classical chaperone/usher machinery: structure and function from a clinical standpoint. FEMS Microbiol. Rev. 34, 317-378 (2010).
    • (2010) FEMS Microbiol. Rev , vol.34 , pp. 317-378
    • Zav'Yalov, V.1    Zavialov, A.2    Zav'Yalova, G.3    Korpela, T.4
  • 3
    • 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
  • 4
    • 84866938204 scopus 로고    scopus 로고
    • Surface organelles assembled by secretion systems of gram-negative bacteria: Diversity in structure and function
    • Thanassi, D.G., Bliska, J.B. & Christie, P.J. Surface organelles assembled by secretion systems of Gram-negative bacteria: diversity in structure and function. FEMS Microbiol. Rev. 36, 1046-1082 (2012).
    • (2012) FEMS Microbiol. Rev , vol.36 , pp. 1046-1082
    • Thanassi, D.G.1    Bliska, J.B.2    Christie, P.J.3
  • 5
    • 0032553579 scopus 로고    scopus 로고
    • Induction and evasion of host defenses by type 1-piliated uropathogenic escherichia coli
    • Mulvey, M.A. et al. Induction and evasion of host defenses by type 1-piliated uropathogenic Escherichia coli. Science 282, 1494-1497 (1998).
    • (1998) Science , vol.282 , pp. 1494-1497
    • Mulvey, M.A.1
  • 6
    • 0028172870 scopus 로고
    • The gal(alpha1-4)gal-specific tip adhesin of escherichia coli p-fimbriae is needed for pyelonephritis to occur in the normal urinary tract
    • Roberts, J.A. et al. The Gal(alpha1-4)Gal-specific tip adhesin of Escherichia coli P-fimbriae is needed for pyelonephritis to occur in the normal urinary tract. Proc. Natl. Acad. Sci. USA 91, 11889-11893 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11889-11893
    • Roberts, J.A.1
  • 7
    • 0028945986 scopus 로고
    • Fimh adhesin of type-1 pili is assembled into a fibrillar tip structure in the enterobacteriaceae
    • Jones, C.H. et al. FimH adhesin of type-1 pili is assembled into a fibrillar tip structure in the Enterobacteriaceae. Proc. Natl. Acad. Sci. USA 92, 2081-2085 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2081-2085
    • Jones, C.H.1
  • 8
    • 0036428752 scopus 로고    scopus 로고
    • Exploring the 3D molecular architecture of escherichia coli type 1 pili
    • Hahn, E. et al. Exploring the 3D molecular architecture of Escherichia coli type 1 pili. J. Mol. Biol. 323, 845-857 (2002).
    • (2002) J. Mol. Biol , vol.323 , pp. 845-857
    • Hahn, E.1
  • 10
    • 0033551911 scopus 로고    scopus 로고
    • X-ray structure of the fimc-fimh chaperone-Adhesin complex from uropathogenic escherichia coli
    • Choudhury, D. et al. X-ray structure of the FimC-FimH chaperone-Adhesin complex from uropathogenic Escherichia coli. Science 285, 1061-1066 (1999).
    • (1999) Science , vol.285 , pp. 1061-1066
    • Choudhury, D.1
  • 11
    • 0039843096 scopus 로고    scopus 로고
    • Structural basis of chaperone function and pilus biogenesis
    • Sauer, F.G. et al. Structural basis of chaperone function and pilus biogenesis. Science 285, 1058-1061 (1999).
    • (1999) Science , vol.285 , pp. 1058-1061
    • Sauer, F.G.1
  • 12
    • 0038820383 scopus 로고    scopus 로고
    • Structure and biogenesis of the capsular f1 antigen from yersinia pestis: Preserved folding energy drives fiber formation
    • Zavialov, A.V. et al. Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation. Cell 113, 587-596 (2003).
    • (2003) Cell , vol.113 , pp. 587-596
    • Zavialov, A.V.1
  • 13
    • 42349106617 scopus 로고    scopus 로고
    • Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst
    • Nishiyama, M., Ishikawa, T., Rechsteiner, H. & Glockshuber, R. Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst. Science 320, 376-379 (2008).
    • (2008) Science , vol.320 , pp. 376-379
    • Nishiyama, M.1    Ishikawa, T.2    Rechsteiner, H.3    Glockshuber, R.4
  • 14
    • 0037112164 scopus 로고    scopus 로고
    • Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation
    • Sauer, F.G., Pinkner, J.S., Waksman, G. & Hultgren, S.J. Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation. Cell 111, 543-551 (2002).
    • (2002) Cell , vol.111 , pp. 543-551
    • Sauer, F.G.1    Pinkner, J.S.2    Waksman, G.3    Hultgren, S.J.4
  • 15
    • 51349128736 scopus 로고    scopus 로고
    • Unraveling the molecular basis of subunit specificity in p pilus assembly by mass spectrometry
    • Rose, R.J. et al. Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry. Proc. Natl. Acad. Sci. USA 105, 12873-12878 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 12873-12878
    • Rose, R.J.1
  • 16
    • 74649085109 scopus 로고    scopus 로고
    • The outer membrane usher guarantees the formation of functional pili by selectively catalyzing donor-strand exchange between subunits that are adjacent in the mature pilus
    • Nishiyama, M. & Glockshuber, R. The outer membrane usher guarantees the formation of functional pili by selectively catalyzing donor-strand exchange between subunits that are adjacent in the mature pilus. J. Mol. Biol. 396, 1-8 (2010).
    • (2010) J. Mol. Biol , vol.396 , pp. 1-8
    • Nishiyama, M.1    Glockshuber, R.2
  • 17
    • 77950192168 scopus 로고    scopus 로고
    • The differential affinity of the usher for chaperone-subunit complexes is required for assembly of complete pili
    • Li, Q. et al. The differential affinity of the usher for chaperone-subunit complexes is required for assembly of complete pili. Mol. Microbiol. 76, 159-172 (2010).
    • (2010) Mol. Microbiol , vol.76 , pp. 159-172
    • Li, Q.1
  • 18
    • 0032522714 scopus 로고    scopus 로고
    • Ramifications of kinetic partitioning on usher-mediated pilus biogenesis
    • Saulino, E.T., Thanassi, D.G., Pinkner, J.S. & Hultgren, S.J. Ramifications of kinetic partitioning on usher-mediated pilus biogenesis. EMBO J. 17, 2177-2185 (1998).
    • (1998) EMBO J , vol.17 , pp. 2177-2185
    • Saulino, E.T.1    Thanassi, D.G.2    Pinkner, J.S.3    Hultgren, S.J.4
  • 19
    • 84862239241 scopus 로고    scopus 로고
    • Domain activities of papc usher reveal the mechanism of action of an escherichia coli molecular machine
    • Volkan, E. et al. Domain activities of PapC usher reveal the mechanism of action of an Escherichia coli molecular machine. Proc. Natl. Acad. Sci. USA 109, 9563-9568 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 9563-9568
    • Volkan, E.1
  • 20
    • 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
  • 21
    • 21844451873 scopus 로고    scopus 로고
    • Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform fimd
    • Nishiyama, M. et al. Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD. EMBO J. 24, 2075-2086 (2005).
    • (2005) EMBO J , vol.24 , pp. 2075-2086
    • Nishiyama, M.1
  • 22
    • 66149150292 scopus 로고    scopus 로고
    • Insights into pilus assembly and secretion from the structure and functional characterization of usher papc
    • Huang, Y., Smith, B.S., Chen, L.X., Baxter, R.H. & Deisenhofer, J. Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC. Proc. Natl. Acad. Sci. USA 106, 7403-7407 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7403-7407
    • Huang, Y.1    Smith, B.S.2    Chen, L.X.3    Baxter, R.H.4    Deisenhofer, J.5
  • 23
    • 79957929732 scopus 로고    scopus 로고
    • Crystal structure of the fimd usher bound to its cognate fimc-fimh substrate
    • Phan, G. et al. Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate. Nature 474, 49-53 (2011).
    • (2011) Nature , vol.474 , pp. 49-53
    • Phan, G.1
  • 24
    • 3843050179 scopus 로고    scopus 로고
    • The usher n terminus is the initial targeting site for chaperone-subunit complexes and participates in subsequent pilus biogenesis events
    • Ng, T.W., Akman, L., Osisami, M. & Thanassi, D.G. The usher N terminus is the initial targeting site for chaperone-subunit complexes and participates in subsequent pilus biogenesis events. J. Bacteriol. 186, 5321-5331 (2004).
    • (2004) J. Bacteriol , vol.186 , pp. 5321-5331
    • Ng, T.W.1    Akman, L.2    Osisami, M.3    Thanassi, D.G.4
  • 25
    • 77957244767 scopus 로고    scopus 로고
    • Conserved hydrophobic clusters on the surface of the caf1a usher c-terminal domain are important for f1 antigen assembly
    • Dubnovitsky, A.P. et al. Conserved hydrophobic clusters on the surface of the Caf1A usher C-terminal domain are important for F1 antigen assembly. J. Mol. Biol. 403, 243-259 (2010).
    • (2010) J. Mol. Biol , vol.403 , pp. 243-259
    • Dubnovitsky, A.P.1
  • 26
    • 39649123737 scopus 로고    scopus 로고
    • Crystal structure of the ternary fimc-fimf(t)-fimd(n) complex indicates conserved pilus chaperone-subunit complex recognition by the usher fimd
    • Eidam, O., Dworkowski, F.S., Glockshuber, R., Grutter, M.G. & Capitani, G. Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD. FEBS Lett. 582, 651-655 (2008).
    • (2008) FEBS Lett , vol.582 , pp. 651-655
    • Eidam, O.1    Dworkowski, F.S.2    Glockshuber, R.3    Grutter, M.G.4    Capitani, G.5
  • 27
    • 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
  • 28
    • 33645300368 scopus 로고    scopus 로고
    • Analysis of the requirements for pilus biogenesis at the outer membrane usher and the function of the usher c-terminus
    • So, S.S. & Thanassi, D.G. Analysis of the requirements for pilus biogenesis at the outer membrane usher and the function of the usher C-terminus. Mol. Microbiol. 60, 364-375 (2006).
    • (2006) Mol. Microbiol , vol.60 , pp. 364-375
    • So, S.S.1    Thanassi, D.G.2
  • 29
    • 34247372309 scopus 로고    scopus 로고
    • Recognition of the n-terminal lectin domain of fimh adhesin by the usher fimd is required for type 1 pilus biogenesis
    • Munera, D., Hultgren, S. & Fernandez, L.A. Recognition of the N-terminal lectin domain of FimH adhesin by the usher FimD is required for type 1 pilus biogenesis. Mol. Microbiol. 64, 333-346 (2007).
    • (2007) Mol. Microbiol , vol.64 , pp. 333-346
    • Munera, D.1    Hultgren, S.2    Fernandez, L.A.3
  • 30
    • 0032539855 scopus 로고    scopus 로고
    • The papc usher forms an oligomeric channel: Implications for pilus biogenesis across the outer membrane
    • Thanassi, D.G. et al. The PapC usher forms an oligomeric channel: implications for pilus biogenesis across the outer membrane. Proc. Natl. Acad. Sci. USA 95, 3146-3151 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3146-3151
    • Thanassi, D.G.1
  • 31
    • 9244243105 scopus 로고    scopus 로고
    • The outer membrane usher forms a twin-pore secretion complex
    • Li, H. et al. The outer membrane usher forms a twin-pore secretion complex. J. Mol. Biol. 344, 1397-1407 (2004).
    • (2004) J. Mol. Biol , vol.344 , pp. 1397-1407
    • Li, H.1
  • 32
    • 84874110023 scopus 로고    scopus 로고
    • Dissection of pilus tip assembly by the fimd usher monomer
    • Allen, W.J., Phan, G., Hultgren, S.J. & Waksman, G. Dissection of pilus tip assembly by the FimD usher monomer. J. Mol. Biol. 425, 958-967 (2013).
    • (2013) J. Mol. Biol , vol.425 , pp. 958-967
    • Allen, W.J.1    Phan, G.2    Hultgren, S.J.3    Waksman, G.4
  • 33
    • 73149104141 scopus 로고    scopus 로고
    • An enhanced system for unnatural amino acid mutagenesis in e. Coli
    • Young, T.S., Ahmad, I., Yin, J.A. & Schultz, P.G. An enhanced system for unnatural amino acid mutagenesis in E. coli. J. Mol. Biol. 395, 361-374 (2010).
    • (2010) J. Mol. Biol , vol.395 , pp. 361-374
    • Young, T.S.1    Ahmad, I.2    Yin, J.A.3    Schultz, P.G.4
  • 34
    • 0037143649 scopus 로고    scopus 로고
    • Addition of a photocrosslinking amino acid to the genetic code of escherichia coli
    • Chin, J.W., Martin, A.B., King, D.S., Wang, L. & Schultz, P.G. Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli. Proc. Natl. Acad. Sci. USA 99, 11020-11024 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11020-11024
    • Chin, J.W.1    Martin, A.B.2    King, D.S.3    Wang, L.4    Schultz, P.G.5
  • 35
    • 58249085344 scopus 로고    scopus 로고
    • Fluorescence approaches to quantifying biomolecular interactions
    • Royer, C.A. & Scarlata, S.F. Fluorescence approaches to quantifying biomolecular interactions. Methods Enzymol. 450, 79-106 (2008).
    • (2008) Methods Enzymol , vol.450 , pp. 79-106
    • Royer, C.A.1    Scarlata, S.F.2
  • 36
    • 84863810994 scopus 로고    scopus 로고
    • The role of chaperone-subunit usher domain interactions in the mechanism of bacterial pilus biogenesis revealed by esi-ms
    • Morrissey, B. et al. The role of chaperone-subunit usher domain interactions in the mechanism of bacterial pilus biogenesis revealed by ESI-MS. Mol. Cell. Proteomics 11, M111.015289 (2012).
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. M111015289
    • Morrissey, B.1
  • 37
    • 73649132280 scopus 로고    scopus 로고
    • Modulating effects of the plug, helix and n-And c-terminal domains on channel properties of the papc usher
    • Mapingire, O.S., Henderson, N.S., Duret, G., Thanassi, D.G. & Delcour, A.H. Modulating effects of the plug, helix and N-And C-terminal domains on channel properties of the PapC usher. J. Biol. Chem. 284, 36324-36333 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 36324-36333
    • Mapingire, O.S.1    Henderson, N.S.2    Duret, G.3    Thanassi, D.G.4    Delcour, A.H.5
  • 38
    • 62149091092 scopus 로고    scopus 로고
    • Caf1a usher possesses a caf1 subunit-like domain that is crucial for caf1 fibre secretion
    • Yu, X. et al. Caf1A usher possesses a Caf1 subunit-like domain that is crucial for Caf1 fibre secretion. Biochem. J. 418, 541-551 (2009).
    • (2009) Biochem. J , vol.418 , pp. 541-551
    • Yu, X.1
  • 39
    • 79551663696 scopus 로고    scopus 로고
    • Function of the usher n-terminus in catalysing pilus assembly
    • Henderson, N.S., Ng, T.W., Talukder, I. & Thanassi, D.G. Function of the usher N-terminus in catalysing pilus assembly. Mol. Microbiol. 79, 954-967 (2011).
    • (2011) Mol. Microbiol , vol.79 , pp. 954-967
    • Henderson, N.S.1    Ng, T.W.2    Talukder, I.3    Thanassi, D.G.4
  • 40
    • 18844384961 scopus 로고    scopus 로고
    • Protein secretion in the absence of atp: The autotransporter, two-partner secretion, and chaperone/usher pathways of gram-negative bacteria
    • Thanassi, D.G., Stathopoulos, C., Karkal, A. & Li, H. Protein secretion in the absence of ATP: the autotransporter, two-partner secretion, and chaperone/usher pathways of Gram-negative bacteria. Mol. Membr. Biol. 22, 63-72 (2005).
    • (2005) Mol. Membr. Biol , vol.22 , pp. 63-72
    • Thanassi, D.G.1    Stathopoulos, C.2    Karkal, A.3    Li, H.4
  • 41
    • 79953022888 scopus 로고    scopus 로고
    • The oligomeric state and arrangement of the active bacterial translocon
    • Deville, K. et al. The oligomeric state and arrangement of the active bacterial translocon. J. Biol. Chem. 286, 4659-4669 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 4659-4669
    • Deville, K.1
  • 42
    • 0242669353 scopus 로고    scopus 로고
    • Protein insertion into the mitochondrial inner membrane by a twin-pore translocase
    • Rehling, P. et al. Protein insertion into the mitochondrial inner membrane by a twin-pore translocase. Science 299, 1747-1751 (2003).
    • (2003) Science , vol.299 , pp. 1747-1751
    • Rehling, P.1
  • 43
    • 0035844870 scopus 로고    scopus 로고
    • Tom40, the pore-forming component of the protein-conducting tom channel in the outer membrane of mitochondria
    • Ahting, U. et al. Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria. J. Cell Biol. 153, 1151-1160 (2001).
    • (2001) J. Cell Biol , vol.153 , pp. 1151-1160
    • Ahting, U.1
  • 44
    • 84883742434 scopus 로고    scopus 로고
    • Allosteric mechanism of water-channel gating by ca2+-calmodulin
    • Reichow, S.L. et al. Allosteric mechanism of water-channel gating by Ca2+-calmodulin. Nat. Struct. Mol. Biol. 20, 1085-1092 (2013).
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 1085-1092
    • Reichow, S.L.1
  • 45
    • 84858238365 scopus 로고    scopus 로고
    • Two copies of the secy channel and acidic lipids are necessary to activate the seca translocation atpase
    • Dalal, K., Chan, C.S., Sligar, S.G. & Duong, F. Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase. Proc. Natl. Acad. Sci. USA 109, 4104-4109 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 4104-4109
    • Dalal, K.1    Chan, C.S.2    Sligar, S.G.3    Duong, F.4
  • 46
    • 84880361227 scopus 로고    scopus 로고
    • Stoichiometry of secyeg in the active translocase of escherichia coli varies with precursor species
    • Mao, C. et al. Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species. Proc. Natl. Acad. Sci. USA 110, 11815-11820 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 11815-11820
    • Mao, C.1
  • 47
    • 16544395270 scopus 로고    scopus 로고
    • Site-directed, ligase-independent mutagenesis (slim a single-tube methodology approaching 100% efficiency in 4 h
    • Chiu, J., March, P.E., Lee, R. & Tillett, D. Site-directed, Ligase-Independent Mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4 h. Nucleic Acids Res. 32, e174 (2004).
    • (2004) Nucleic Acids Res , vol.32 , pp. e174
    • Chiu, J.1    March, P.E.2    Lee, R.3    Tillett, D.4
  • 48
    • 42249087464 scopus 로고    scopus 로고
    • Site-directed, ligase-independent mutagenesis (slim for highly efficient mutagenesis of plasmids greater than 8kb
    • Chiu, J., Tillett, D., Dawes, I.W. & March, P.E. Site-directed, Ligase-Independent Mutagenesis (SLIM) for highly efficient mutagenesis of plasmids greater than 8kb. J. Microbiol. Methods 73, 195-198 (2008).
    • (2008) J. Microbiol. Methods , vol.73 , pp. 195-198
    • Chiu, J.1    Tillett, D.2    Dawes, I.W.3    March, P.E.4
  • 49
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. & Mann, M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858 (1996).
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 50
    • 27544511899 scopus 로고    scopus 로고
    • Inspect: Identification of posttranslationally modified peptides from tandem mass spectra
    • Tanner, S. et al. InsPecT: identification of posttranslationally modified peptides from tandem mass spectra. Anal. Chem. 77, 4626-4639 (2005).
    • (2005) Anal. Chem , vol.77 , pp. 4626-4639
    • Tanner, S.1
  • 51
    • 84879323488 scopus 로고    scopus 로고
    • Purification of the outer membrane usher protein and periplasmic chaperone-subunit complexes from the p and type 1 pilus systems
    • Henderson, N.S. & Thanassi, D.G. Purification of the outer membrane usher protein and periplasmic chaperone-subunit complexes from the P and type 1 pilus systems. Methods Mol. Biol. 966, 37-52 (2013).
    • (2013) Methods Mol. Biol , vol.966 , pp. 37-52
    • Henderson, N.S.1    Thanassi, D.G.2


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