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Volumn 10, Issue 2, 2010, Pages 277-288

Mass spectrometric characterization of the Campylobacter jejuni adherence factor CadF reveals post-translational processing that removes immunogenicity while retaining fibronectin binding

Author keywords

Campylobacter adherence factor; Campylobacter jejuni; Fibronectin binding; Immunogenicity; Microbiology; Outer membrane proteins

Indexed keywords

BACTERIAL PROTEIN; CADF PROTEIN; FIBRONECTIN; GLYCINE; HEXAHISTIDINE; LEUCINE; MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN A; PHENYLALANINE; SERINE; UNCLASSIFIED DRUG;

EID: 76749149598     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900440     Document Type: Article
Times cited : (28)

References (48)
  • 1
    • 6444243531 scopus 로고    scopus 로고
    • Campylobacter, from obscurity to celebrity
    • Butzler, J. P., Campylobacter, from obscurity to celebrity. Clin. Microbiol. Infect. 2004, 10, 868-876.
    • (2004) Clin. Microbiol. Infect , vol.10 , pp. 868-876
    • Butzler, J.P.1
  • 3
    • 34548028239 scopus 로고    scopus 로고
    • Campylobacter jejuni: Molecular biology and pathogenesis
    • Young, K. T., Davis, L. M., Dirita, V. J., Campylobacter jejuni: molecular biology and pathogenesis. Nat. Rev. Microbiol. 2007, 5, 665-679.
    • (2007) Nat. Rev. Microbiol , vol.5 , pp. 665-679
    • Young, K.T.1    Davis, L.M.2    Dirita, V.J.3
  • 4
    • 27644558148 scopus 로고    scopus 로고
    • Guillain-Barre syndrome
    • Hughes, R. A., Cornblath, D. R., Guillain-Barre syndrome. Lancet 2005, 366, 1653-1666.
    • (2005) Lancet , vol.366 , pp. 1653-1666
    • Hughes, R.A.1    Cornblath, D.R.2
  • 5
    • 9144227738 scopus 로고    scopus 로고
    • Immunoproliferative small intestinal disease associated with Campylobacter jejuni
    • Lecuit, M., Abachin, E., Martin, A., Poyart, C. et al., Immunoproliferative small intestinal disease associated with Campylobacter jejuni. N. Eng. J. Med. 2004, 350, 239-248.
    • (2004) N. Eng. J. Med , vol.350 , pp. 239-248
    • Lecuit, M.1    Abachin, E.2    Martin, A.3    Poyart, C.4
  • 6
    • 34548458056 scopus 로고    scopus 로고
    • The second century of Campylobacter research: Recent advances, new opportunities and old problems
    • Dorrell, N., Wren, B. W., The second century of Campylobacter research: recent advances, new opportunities and old problems. Curr. Opin. Infect. Dis. 2007, 20, 514-518.
    • (2007) Curr. Opin. Infect. Dis , vol.20 , pp. 514-518
    • Dorrell, N.1    Wren, B.W.2
  • 7
    • 0030635485 scopus 로고    scopus 로고
    • Pathogenesis of enteric infection by Campylobacter
    • Ketley, J. M., Pathogenesis of enteric infection by Campylobacter. Microbiology 1997, 143, 5-21.
    • (1997) Microbiology , vol.143 , pp. 5-21
    • Ketley, J.M.1
  • 9
    • 15544387940 scopus 로고    scopus 로고
    • Use of genome-wide expression profiling and mutagenesis to study the intestinal lifestyle of Campylobacter jejuni
    • Stintzi, A., Marlow, D., Palyada, K., Naikare, H. et al., Use of genome-wide expression profiling and mutagenesis to study the intestinal lifestyle of Campylobacter jejuni. Infect. Immun. 2005, 73, 1797-1810.
    • (2005) Infect. Immun , vol.73 , pp. 1797-1810
    • Stintzi, A.1    Marlow, D.2    Palyada, K.3    Naikare, H.4
  • 10
    • 0031573773 scopus 로고    scopus 로고
    • Campylobacter jejuni major outer membrane protein and a 59 kDa protein are involved in binding to fibronectin and INT 407 cell membranes
    • Moser, I., Schroeder, W., Salnikow, J., Campylobacter jejuni major outer membrane protein and a 59 kDa protein are involved in binding to fibronectin and INT 407 cell membranes. FEMS Microbiol. Lett. 1997, 157, 233-238.
    • (1997) FEMS Microbiol. Lett , vol.157 , pp. 233-238
    • Moser, I.1    Schroeder, W.2    Salnikow, J.3
  • 11
    • 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. et al., CapA, an autotransporter protein of Campylobacter jejuni, mediates association with human epithelial cells and colonization of the chicken gut. J. Bacteriol. 2007, 189, 1856-1865.
    • (2007) J. Bacteriol , vol.189 , pp. 1856-1865
    • Ashgar, S.S.1    Oldfield, N.J.2    Wooldridge, K.G.3    Jones, M.A.4
  • 12
    • 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. et al., JlpA, a novel surface-exposed lipoprotein specific to Campylobacter jejuni, mediates adherence to host epithelial cells. Mol. Microbiol. 2001, 39, 1225-1236.
    • (2001) Mol. Microbiol , vol.39 , pp. 1225-1236
    • Jin, S.1    Joe, A.2    Lynett, J.3    Hani, E.K.4
  • 13
    • 34548799195 scopus 로고    scopus 로고
    • Deletion of peb4 gene impairs cell adhesion and biofilm formation in Campylobacter jejuni
    • Asakura, H., Yamasaki, M., Yamamoto, S., Igimi, S., Deletion of peb4 gene impairs cell adhesion and biofilm formation in Campylobacter jejuni. FEMS Microbiol. Lett. 2007, 275, 278-285.
    • (2007) FEMS Microbiol. Lett , vol.275 , pp. 278-285
    • Asakura, H.1    Yamasaki, M.2    Yamamoto, S.3    Igimi, S.4
  • 14
    • 0025994829 scopus 로고
    • Identification, purification, and characterization of major antigenic proteins of Campylobacter jejuni
    • Pei, Z. H., Ellison, R. T., III, Blaser, M. J., Identification, purification, and characterization of major antigenic proteins of Campylobacter jejuni. J. Biol. Chem. 1991, 266, 16363-16369.
    • (1991) J. Biol. Chem , vol.266 , pp. 16363-16369
    • Pei, Z.H.1    Ellison III, R.T.2    Blaser, M.J.3
  • 15
    • 0031885909 scopus 로고    scopus 로고
    • Mutation in the peb1A locus of Campylobacter jejuni reduces interactions with epithelial cells and intestinal colonization of mice
    • Pei, Z., Burucoa, C., Grignon, B., Baqar, S. et al., Mutation in the peb1A locus of Campylobacter jejuni reduces interactions with epithelial cells and intestinal colonization of mice. Infect. Immun. 1998, 66, 938-943.
    • (1998) Infect. Immun , vol.66 , pp. 938-943
    • Pei, Z.1    Burucoa, C.2    Grignon, B.3    Baqar, S.4
  • 16
    • 34247561641 scopus 로고    scopus 로고
    • Structural context for protein N-glycosylation in bacteria: The structure of PEB3, an adhesin from Campylobacter jejuni
    • Rangarajan, E. S., Bhatia, S., Watson, D. C., Munger, C. et al., Structural context for protein N-glycosylation in bacteria: the structure of PEB3, an adhesin from Campylobacter jejuni. Protein Sci. 2007, 16, 990-995.
    • (2007) Protein Sci , vol.16 , pp. 990-995
    • Rangarajan, E.S.1    Bhatia, S.2    Watson, D.C.3    Munger, C.4
  • 17
    • 0030798150 scopus 로고    scopus 로고
    • Konkel, M. E., Garvis, S. G., Tipton, S. L., Anderson, D. E., Jr., Cieplak, W., Jr., Identification and molecular cloning of a gene encoding a fibronectin-binding protein (CadF) from Campylobacter jejuni. Mol. Microbiol. 1997, 24, 953-963.
    • Konkel, M. E., Garvis, S. G., Tipton, S. L., Anderson, D. E., Jr., Cieplak, W., Jr., Identification and molecular cloning of a gene encoding a fibronectin-binding protein (CadF) from Campylobacter jejuni. Mol. Microbiol. 1997, 24, 953-963.
  • 20
    • 34547408814 scopus 로고    scopus 로고
    • Expression patterns and role of the CadF protein in Campylobacter jejuni and Campylobacter coli
    • Krause-Gruszczynska, M., van Alphen, L. B., Oyarzabal, O. A., Alter, T. et al., Expression patterns and role of the CadF protein in Campylobacter jejuni and Campylobacter coli. FEMS Microbiol. Lett. 2007, 274, 9-16.
    • (2007) FEMS Microbiol. Lett , vol.274 , pp. 9-16
    • Krause-Gruszczynska, M.1    van Alphen, L.B.2    Oyarzabal, O.A.3    Alter, T.4
  • 21
    • 0037256265 scopus 로고    scopus 로고
    • Maximal adherence and invasion of INT 407 cells by Campylobacter jejuni requires the CadF outer-membrane protein and microfilament reorganization
    • Monteville, M. R., Yoon, J. E., Konkel, M. E., Maximal adherence and invasion of INT 407 cells by Campylobacter jejuni requires the CadF outer-membrane protein and microfilament reorganization. Microbiology 2003, 149, 153-165.
    • (2003) Microbiology , vol.149 , pp. 153-165
    • Monteville, M.R.1    Yoon, J.E.2    Konkel, M.E.3
  • 22
    • 0033167220 scopus 로고    scopus 로고
    • The absence of cecal colonization of chicks by a mutant of Campylobacter jejuni not expressing bacterial fibronectin-binding protein
    • Ziprin, R. L., Young, C. R., Stanker, L. H., Hume, M. E., Konkel, M. E., The absence of cecal colonization of chicks by a mutant of Campylobacter jejuni not expressing bacterial fibronectin-binding protein. Avian Dis. 1999, 43, 586-589.
    • (1999) Avian Dis , vol.43 , pp. 586-589
    • Ziprin, R.L.1    Young, C.R.2    Stanker, L.H.3    Hume, M.E.4    Konkel, M.E.5
  • 23
    • 23744505064 scopus 로고    scopus 로고
    • Identification of a fibronectin-binding domain within the Campylobacter jejuni CadF protein
    • Konkel, M. E., Christensen, J. E., Keech, A. M., Monteville, M. R. et al., Identification of a fibronectin-binding domain within the Campylobacter jejuni CadF protein. Mol. Microbiol. 2005, 57, 1022-1035.
    • (2005) Mol. Microbiol , vol.57 , pp. 1022-1035
    • Konkel, M.E.1    Christensen, J.E.2    Keech, A.M.3    Monteville, M.R.4
  • 24
    • 0029092071 scopus 로고
    • Conformational analysis of the Campylobacter jejuni porin
    • Bolla, J. M., Loret, E., Zalewski, M., Pages, J. M., Conformational analysis of the Campylobacter jejuni porin. J. Bacteriol. 1995, 177, 4266-4271.
    • (1995) J. Bacteriol , vol.177 , pp. 4266-4271
    • Bolla, J.M.1    Loret, E.2    Zalewski, M.3    Pages, J.M.4
  • 25
    • 34547354204 scopus 로고    scopus 로고
    • Amino acid sequence determination of protein biomarkers of Campylobacter upsaliensis and C. helveticus by "composite" sequence proteomic analysis
    • Fagerquist, C. K., Amino acid sequence determination of protein biomarkers of Campylobacter upsaliensis and C. helveticus by "composite" sequence proteomic analysis. J. Proteome Res. 2007, 6, 2539-2549.
    • (2007) J. Proteome Res , vol.6 , pp. 2539-2549
    • Fagerquist, C.K.1
  • 26
    • 33645835366 scopus 로고    scopus 로고
    • P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae: Defined domains of P159 bind heparin and promote adherence to eukaryote cells
    • Burnett, T. A., Dinkla, K., Rohde, M., Chhatwal, G. S. et al., P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells. Mol. Microbiol. 2006, 60, 669-686.
    • (2006) Mol. Microbiol , vol.60 , pp. 669-686
    • Burnett, T.A.1    Dinkla, K.2    Rohde, M.3    Chhatwal, G.S.4
  • 28
    • 29644440331 scopus 로고    scopus 로고
    • Two domains within the Mycoplasma hyopneumoniae cilium adhesin bind heparin
    • Jenkins, C., Wilton, J. L., Minion, F. C., Falconer, L. et al., Two domains within the Mycoplasma hyopneumoniae cilium adhesin bind heparin. Infect. Immun. 2006, 74, 481-487.
    • (2006) Infect. Immun , vol.74 , pp. 481-487
    • Jenkins, C.1    Wilton, J.L.2    Minion, F.C.3    Falconer, L.4
  • 29
    • 58449115242 scopus 로고    scopus 로고
    • Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein of Mycoplasma hyopneumoniae
    • Wilton, J., Jenkins, C., Cordwell, S. J., Falconer, L. et al., Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein of Mycoplasma hyopneumoniae. Mol. Microbiol. 2009, 71, 566-582.
    • (2009) Mol. Microbiol , vol.71 , pp. 566-582
    • Wilton, J.1    Jenkins, C.2    Cordwell, S.J.3    Falconer, L.4
  • 30
    • 0027584976 scopus 로고
    • Diffuse adherence of enteropathogenic Escherichia coli strains - processing of AIDA-I
    • Benz, I., Schmidt, M. A., Diffuse adherence of enteropathogenic Escherichia coli strains - processing of AIDA-I. Zentralbl. Bakteriol. 1993, 278, 197-208.
    • (1993) Zentralbl. Bakteriol , vol.278 , pp. 197-208
    • Benz, I.1    Schmidt, M.A.2
  • 31
    • 0037027539 scopus 로고    scopus 로고
    • Burnett, T. A., M, A. H., Kuhnert, P., Djordjevic, S. P., Speciating Campylobacter jejuni and Campylobacter coli isolates from poultry and humans using six PCR-based assays. FEMS Microbiol. Lett. 2002, 216, 201-209.
    • Burnett, T. A., M, A. H., Kuhnert, P., Djordjevic, S. P., Speciating Campylobacter jejuni and Campylobacter coli isolates from poultry and humans using six PCR-based assays. FEMS Microbiol. Lett. 2002, 216, 201-209.
  • 32
    • 62849083844 scopus 로고    scopus 로고
    • Differential carbohydrate recognition by Campylobacter jejuni strain 11168: Influences of temperature and growth conditions
    • Day, C. J., Tiralongo, J., Hartnell, R. D., Logue, C. A. et al., Differential carbohydrate recognition by Campylobacter jejuni strain 11168: influences of temperature and growth conditions. PLoS ONE 2009, 4, e4927.
    • (2009) PLoS ONE , vol.4
    • Day, C.J.1    Tiralongo, J.2    Hartnell, R.D.3    Logue, C.A.4
  • 33
    • 0033673225 scopus 로고    scopus 로고
    • Complementing genomics with proteomics: The membrane subproteome of Pseudomonas aeruginosa PAO1
    • Nouwens, A. S., Cordwell, S. J., Larsen, M. R., Molloy, M. P. et al., Complementing genomics with proteomics: the membrane subproteome of Pseudomonas aeruginosa PAO1. Electrophoresis 2000, 21, 3797-3809.
    • (2000) Electrophoresis , vol.21 , pp. 3797-3809
    • Nouwens, A.S.1    Cordwell, S.J.2    Larsen, M.R.3    Molloy, M.P.4
  • 34
    • 38149142479 scopus 로고    scopus 로고
    • Identification of membrane-associated proteins from Campylobacter jejuni strains using complementary proteomics technologies
    • Cordwell, S. J., Len, A. C., Touma, R. G., Scott, N. E. et al., Identification of membrane-associated proteins from Campylobacter jejuni strains using complementary proteomics technologies. Proteomics 2008, 8, 122-139.
    • (2008) Proteomics , vol.8 , pp. 122-139
    • Cordwell, S.J.1    Len, A.C.2    Touma, R.G.3    Scott, N.E.4
  • 35
    • 0036438532 scopus 로고    scopus 로고
    • Acquisition and archiving of information for bacterial proteomics: From sample preparation to database
    • Cordwell, S. J., Acquisition and archiving of information for bacterial proteomics: from sample preparation to database. Methods Enzymol. 2002, 358, 207-227.
    • (2002) Methods Enzymol , vol.358 , pp. 207-227
    • Cordwell, S.J.1
  • 36
    • 0034855145 scopus 로고    scopus 로고
    • Investigation of charge variants of rViscumin by two-dimensional gel electrophoresis and mass spectrometry
    • Lutter, P., Meyer, H. E., Langer, M., Witthohn, K. et al., Investigation of charge variants of rViscumin by two-dimensional gel electrophoresis and mass spectrometry. Electrophoresis 2001, 22, 2888-2897.
    • (2001) Electrophoresis , vol.22 , pp. 2888-2897
    • Lutter, P.1    Meyer, H.E.2    Langer, M.3    Witthohn, K.4
  • 37
    • 0037686474 scopus 로고    scopus 로고
    • Strategy for identifying protein-protein interactions of gel-separated proteins and complexes by mass spectrometry
    • Mackun, K., Downard, K. M., Strategy for identifying protein-protein interactions of gel-separated proteins and complexes by mass spectrometry. Anal. Biochem. 2003, 318, 60-70.
    • (2003) Anal. Biochem , vol.318 , pp. 60-70
    • Mackun, K.1    Downard, K.M.2
  • 38
    • 33746263851 scopus 로고    scopus 로고
    • Use of nitrocellulose membranes for protein characterization by matrix-assisted laser desorption/ionization mass spectrometry
    • Luque-Garcia, J. L., Zhou, G., Sun, T. T., Neubert, T. A., Use of nitrocellulose membranes for protein characterization by matrix-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 2006, 78, 5102-5108.
    • (2006) Anal. Chem , vol.78 , pp. 5102-5108
    • Luque-Garcia, J.L.1    Zhou, G.2    Sun, T.T.3    Neubert, T.A.4
  • 39
    • 0025283269 scopus 로고
    • A strong antibody response to the periplasmic C-terminal domain of the OmpA protein of Escherichia coli is produced by immunization with purified OmpA or with whole E. coli or Salmonella typhimurium bacteria
    • Puohiniemi, R., Karvonen, M., Vuopio-Varkila, J., Muotiala, A. et al., A strong antibody response to the periplasmic C-terminal domain of the OmpA protein of Escherichia coli is produced by immunization with purified OmpA or with whole E. coli or Salmonella typhimurium bacteria. Infect. Immun. 1990, 58, 1691-1696.
    • (1990) Infect. Immun , vol.58 , pp. 1691-1696
    • Puohiniemi, R.1    Karvonen, M.2    Vuopio-Varkila, J.3    Muotiala, A.4
  • 40
    • 0037972514 scopus 로고    scopus 로고
    • The C-terminal domain of Salmonella enterica serovar typhimurium OmpA is an immunodominant antigen in mice but appears to be only partially exposed on the bacterial cell surface
    • Singh, S. P., Williams, Y. U., Miller, S., Nikaido, H., The C-terminal domain of Salmonella enterica serovar typhimurium OmpA is an immunodominant antigen in mice but appears to be only partially exposed on the bacterial cell surface. Infect. Immun. 2003, 71, 3937-3946.
    • (2003) Infect. Immun , vol.71 , pp. 3937-3946
    • Singh, S.P.1    Williams, Y.U.2    Miller, S.3    Nikaido, H.4
  • 41
    • 0029553570 scopus 로고
    • Use of synthetic peptides to identify surface-exposed, linear B-cell epitopes within outer membrane protein F of Pseudomonas aeruginosa
    • Gilleland, H. E., Jr., Hughes, E. E., Gilleland, L. B.,Matthews-Greer, J. M., Staczek, J., Use of synthetic peptides to identify surface-exposed, linear B-cell epitopes within outer membrane protein F of Pseudomonas aeruginosa. Curr. Microbiol. 1995, 31, 279-286.
    • (1995) Curr. Microbiol , vol.31 , pp. 279-286
    • Gilleland Jr., H.E.1    Hughes, E.E.2    Gilleland, L.B.3    Matthews-Greer, J.M.4    Staczek, J.5
  • 42
    • 0029036572 scopus 로고
    • Synthetic peptides representing two protective, linear B-cell epitopes of outer membrane protein F of Pseudomonas aeruginosa elicit whole-cell-reactive antibodies that are functionally pseudomonad specific
    • Gilleland, L. B., Gilleland, H. E., Jr., Synthetic peptides representing two protective, linear B-cell epitopes of outer membrane protein F of Pseudomonas aeruginosa elicit whole-cell-reactive antibodies that are functionally pseudomonad specific. Infect. Immun. 1995, 63, 2347-2351.
    • (1995) Infect. Immun , vol.63 , pp. 2347-2351
    • Gilleland, L.B.1    Gilleland Jr., H.E.2
  • 43
    • 2442584516 scopus 로고    scopus 로고
    • Genome-wide expression analyses of Campylobacter jejuni NCTC11168 reveals coordinate regulation of motility and virulence by flhA
    • Carrillo, C. D., Taboada, E., Nash, J. H., Lanthier, P. et al., Genome-wide expression analyses of Campylobacter jejuni NCTC11168 reveals coordinate regulation of motility and virulence by flhA. J. Biol. Chem. 2004, 279, 20327-20338.
    • (2004) J. Biol. Chem , vol.279 , pp. 20327-20338
    • Carrillo, C.D.1    Taboada, E.2    Nash, J.H.3    Lanthier, P.4
  • 44
    • 0346655232 scopus 로고    scopus 로고
    • The genome-sequenced variant of Campylobacter jejuni NCTC 11168 and the original clonal clinical isolate differ markedly in colonization, gene expression, and virulence-associated phenotypes
    • Gaynor, E. C., Cawthraw, S., Manning, G., MacKichan, J. K. et al., The genome-sequenced variant of Campylobacter jejuni NCTC 11168 and the original clonal clinical isolate differ markedly in colonization, gene expression, and virulence-associated phenotypes. J. Bacteriol. 2004, 186, 503-517.
    • (2004) J. Bacteriol , vol.186 , pp. 503-517
    • Gaynor, E.C.1    Cawthraw, S.2    Manning, G.3    MacKichan, J.K.4
  • 45
    • 33845452751 scopus 로고    scopus 로고
    • Proteolytic processing is not essential for multiple functions of the Escherichia coli autotransporter adhesin involved in diffuse adherence (AIDA-I)
    • Charbonneau, M. E., Berthiaume, F., Mourez, M., Proteolytic processing is not essential for multiple functions of the Escherichia coli autotransporter adhesin involved in diffuse adherence (AIDA-I). J. Bacteriol. 2006, 188, 8504-8512.
    • (2006) J. Bacteriol , vol.188 , pp. 8504-8512
    • Charbonneau, M.E.1    Berthiaume, F.2    Mourez, M.3
  • 46
    • 38049087432 scopus 로고    scopus 로고
    • Proteomic analyses of a robust versus a poor chicken gastrointestinal colonizing isolate of Campylobacter jejuni
    • Seal, B. S., Hiett, K. L., Kuntz, R. L., Woolsey, R. et al., Proteomic analyses of a robust versus a poor chicken gastrointestinal colonizing isolate of Campylobacter jejuni. J. Proteome Res. 2007, 6, 4582-4591.
    • (2007) J. Proteome Res , vol.6 , pp. 4582-4591
    • Seal, B.S.1    Hiett, K.L.2    Kuntz, R.L.3    Woolsey, R.4
  • 47
    • 0029092472 scopus 로고
    • Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins
    • Koebnik, R., Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins. Mol. Microbiol. 1995, 16, 1269-1270.
    • (1995) Mol. Microbiol , vol.16 , pp. 1269-1270
    • Koebnik, R.1
  • 48
    • 0026065533 scopus 로고
    • Sequence and structure determinants of the nonenzymatic deamidation of asparagine and glutamine residues in proteins
    • Wright, H. T., Sequence and structure determinants of the nonenzymatic deamidation of asparagine and glutamine residues in proteins. Protein Eng. 1991, 4, 283-294.
    • (1991) Protein Eng , vol.4 , pp. 283-294
    • Wright, H.T.1


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