메뉴 건너뛰기




Volumn 14, Issue 4, 2015, Pages 989-1008

A metaproteomics approach to elucidate host and pathogen protein expression during catheter-associated urinary tract infections (CAUTIs)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; PROTEOME; SIDEROPHORE; UREA; BACTERIAL PROTEIN;

EID: 84926475403     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.043463     Document Type: Article
Times cited : (47)

References (138)
  • 1
    • 0025948047 scopus 로고
    • Catheter-associated urinary tract infections: Epidemiology, pathogenesis, and prevention
    • Stamm, W. E. (1991) Catheter-associated urinary tract infections: zpidzemiology, pathogenesis, and prevention. Am. J. Med. 91, 65S-71S
    • (1991) Am. J. Med. , vol.91 , pp. 65S-71S
    • Stamm, W.E.1
  • 2
    • 0026011826 scopus 로고
    • The catheter and urinary tract infection
    • Warren, J. W. (1991) The catheter and urinary tract infection. Med. Clin. North. Am. 75, 481-493
    • (1991) Med. Clin. North. Am. , vol.75 , pp. 481-493
    • Warren, J.W.1
  • 3
    • 0034643067 scopus 로고    scopus 로고
    • Catheter-associated urinary tract infection is rarely symptomatic: A prospective study of 1497 catheterized patients
    • Tambyah, P. A., and Maki, D. G. (2000) Catheter-associated urinary tract infection is rarely symptomatic: a prospective study of 1497 catheterized patients. Arch. Intern. Med. 160, 678-682
    • (2000) Arch. Intern. Med. , vol.160 , pp. 678-682
    • Tambyah, P.A.1    Maki, D.G.2
  • 4
    • 0020465781 scopus 로고
    • A prospective microbiologic study of bacteriuria in patients with chronic indwelling urethral catheters
    • Warren, J. W., Tenney, J. H., Hoopes, J. M., Muncie, H. L., and Anthony, W. C. (1982) A prospective microbiologic study of bacteriuria in patients with chronic indwelling urethral catheters. J. Infect. Dis. 146, 719-723
    • (1982) J. Infect. Dis. , vol.146 , pp. 719-723
    • Warren, J.W.1    Tenney, J.H.2    Hoopes, J.M.3    Muncie, H.L.4    Anthony, W.C.5
  • 5
    • 0035070214 scopus 로고    scopus 로고
    • Catheter-associated urinary tract infections
    • Warren, J. W. (2001) Catheter-associated urinary tract infections. Int. J. Antimicrob. Agents 17, 299-303
    • (2001) Int. J. Antimicrob. Agents , vol.17 , pp. 299-303
    • Warren, J.W.1
  • 6
    • 0023182435 scopus 로고
    • Fever, bacteremia, and death as complications of bacteriuria in women with long-term urethral catheters
    • Warren, J. W., Damron, D., Tenney, J. H., Hoopes, J. M., Deforge, B., and Muncie, H. L., Jr. (1987) Fever, bacteremia, and death as complications of bacteriuria in women with long-term urethral catheters. J. Infect. Dis. 155, 1151-1158
    • (1987) J. Infect. Dis. , vol.155 , pp. 1151-1158
    • Warren, J.W.1    Damron, D.2    Tenney, J.H.3    Hoopes, J.M.4    Deforge, B.5    Muncie, H.L.6
  • 7
    • 56349166986 scopus 로고    scopus 로고
    • Bacterial biofilms in patients with indwelling urinary catheters
    • Stickler, D. J. (2008) Bacterial biofilms in patients with indwelling urinary catheters. Nat. Clin. Pract. Urol. 5, 598-608
    • (2008) Nat. Clin. Pract. Urol. , vol.5 , pp. 598-608
    • Stickler, D.J.1
  • 8
    • 0035029378 scopus 로고    scopus 로고
    • Biofilms and device-associated infections
    • Donlan, R. M. (2001) Biofilms and device-associated infections. Emerg. Infect. Dis. 7, 277-281
    • (2001) Emerg. Infect. Dis. , vol.7 , pp. 277-281
    • Donlan, R.M.1
  • 9
    • 1842612577 scopus 로고    scopus 로고
    • Bacterial biofilms: From the natural environment to infectious diseases
    • Hall-Stoodley, L., Costerton, J. W., and Stoodley, P. (2004) Bacterial biofilms: from the natural environment to infectious diseases. Nat. Rev. Microbiol. 2, 95-108
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 95-108
    • Hall-Stoodley, L.1    Costerton, J.W.2    Stoodley, P.3
  • 10
    • 0036711963 scopus 로고    scopus 로고
    • Biofilms: Microbial life on surfaces
    • Donlan, R. M. (2002) Biofilms: microbial life on surfaces. Emerg. Infect. Dis. 8, 881-890
    • (2002) Emerg. Infect. Dis. , vol.8 , pp. 881-890
    • Donlan, R.M.1
  • 11
    • 0035859467 scopus 로고    scopus 로고
    • Antibiotic resistance of bacteria in biofilms
    • Stewart, P. S., and Costerton, J. W. (2001) Antibiotic resistance of bacteria in biofilms. Lancet 358, 135-138
    • (2001) Lancet , vol.358 , pp. 135-138
    • Stewart, P.S.1    Costerton, J.W.2
  • 12
    • 0035077009 scopus 로고    scopus 로고
    • Riddle of biofilm resistance
    • Lewis, K. (2001) Riddle of biofilm resistance. Antimicrob. Agents Chemother. 45, 999-1007
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 999-1007
    • Lewis, K.1
  • 14
    • 36448977895 scopus 로고    scopus 로고
    • Species interactions in mixed-community crystalline biofilms on urinary catheters
    • Macleod, S. M., and Stickler, D. J. (2007) Species interactions in mixed-community crystalline biofilms on urinary catheters. J. Med. Microbiol. 56, 1549-1557
    • (2007) J. Med. Microbiol. , vol.56 , pp. 1549-1557
    • Macleod, S.M.1    Stickler, D.J.2
  • 15
    • 77957940304 scopus 로고    scopus 로고
    • Comparative genomic analysis of pathogenic and probiotic Enterococcus faecalis isolates, and their transcriptional responses to growth in human urine
    • Vebø, H. C., Solheim, M., Snipen, L., Nes, I. F., and Brede, D. A. (2010) Comparative genomic analysis of pathogenic and probiotic Enterococcus faecalis isolates, and their transcriptional responses to growth in human urine. PloS One 5, e12489
    • (2010) PloS One , vol.5 , pp. e12489
    • Vebø, H.C.1    Solheim, M.2    Snipen, L.3    Nes, I.F.4    Brede, D.A.5
  • 16
    • 34249881603 scopus 로고    scopus 로고
    • Quantitative profile of the uropathogenic Escherichia coli outer membrane proteome during growth in human urine
    • Alteri, C. J., and Mobley, H. L. (2007) Quantitative profile of the uropathogenic Escherichia coli outer membrane proteome during growth in human urine. Infect. Immun. 75, 2679-2688
    • (2007) Infect. Immun. , vol.75 , pp. 2679-2688
    • Alteri, C.J.1    Mobley, H.L.2
  • 17
    • 33646915688 scopus 로고    scopus 로고
    • Global gene expression profiling of the asymptomatic bacteriuria Escherichia coli strain 83972 in the human urinary tract
    • Roos, V., and Klemm, P. (2006) Global gene expression profiling of the asymptomatic bacteriuria Escherichia coli strain 83972 in the human urinary tract. Infect. Immun. 74, 3565-3575
    • (2006) Infect. Immun. , vol.74 , pp. 3565-3575
    • Roos, V.1    Klemm, P.2
  • 18
    • 79959473042 scopus 로고    scopus 로고
    • Transcriptome of Proteus mirabilis in the murine urinary tract: Virulence and nitrogen assimilation gene expression
    • Pearson, M. M., Yep, A., Smith, S. N., and Mobley, H. L. (2011) Transcriptome of Proteus mirabilis in the murine urinary tract: virulence and nitrogen assimilation gene expression. Infect. Immun. 79, 2619-2631
    • (2011) Infect. Immun. , vol.79 , pp. 2619-2631
    • Pearson, M.M.1    Yep, A.2    Smith, S.N.3    Mobley, H.L.4
  • 20
    • 79251526849 scopus 로고    scopus 로고
    • Escherichia coli global gene expression in urine from women with urinary tract infection
    • Hagan, E. C., Lloyd, A. L., Rasko, D. A., Faerber, G. J., and Mobley, H. L. (2010) Escherichia coli global gene expression in urine from women with urinary tract infection. PLoS Pathog. 6, e1001187
    • (2010) PLoS Pathog. , vol.6 , pp. e1001187
    • Hagan, E.C.1    Lloyd, A.L.2    Rasko, D.A.3    Faerber, G.J.4    Mobley, H.L.5
  • 22
    • 0033786377 scopus 로고    scopus 로고
    • Classification, identification, and clinical significance of Proteus, Providencia, and Morganella
    • O'Hara, C. M., Brenner, F. W., and Miller, J. M. (2000) Classification, identification, and clinical significance of Proteus, Providencia, and Morganella. Clin. Microbiol. Rev. 13, 534-546
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 534-546
    • O'Hara, C.M.1    Brenner, F.W.2    Miller, J.M.3
  • 23
    • 0020520748 scopus 로고
    • Serious nosocomial infection caused by Morganella morganii and Proteus mirabilis in a cardiac surgery unit
    • Williams, E. W., Hawkey, P. M., Penner, J. L., Senior, B. W., and Barton, L. J. (1983) Serious nosocomial infection caused by Morganella morganii and Proteus mirabilis in a cardiac surgery unit. J. Clin. Microbiol. 18, 5-9
    • (1983) J. Clin. Microbiol. , vol.18 , pp. 5-9
    • Williams, E.W.1    Hawkey, P.M.2    Penner, J.L.3    Senior, B.W.4    Barton, L.J.5
  • 25
    • 84926511815 scopus 로고    scopus 로고
    • Draft genome sequence of the opportunistic human pathogen Morganella morganii SC01
    • Khatri, I., Dureja, C., Raychaudhuri, S., and Subramanian, S. (2013) Draft genome sequence of the opportunistic human pathogen Morganella morganii SC01. Genome Announc. 1, e00051-12
    • (2013) Genome Announc. , vol.1 , pp. e00051-e00112
    • Khatri, I.1    Dureja, C.2    Raychaudhuri, S.3    Subramanian, S.4
  • 26
    • 0019852773 scopus 로고
    • Hospital cluster epidemic with Morganella morganii
    • Tucci, V., and Isenberg, H. D. (1981) Hospital cluster epidemic with Morganella morganii. J. Clin. Microbiol. 14, 563-566
    • (1981) J. Clin. Microbiol. , vol.14 , pp. 563-566
    • Tucci, V.1    Isenberg, H.D.2
  • 27
    • 0029952117 scopus 로고    scopus 로고
    • A bifunctional urease enhances survival of pathogenic Yersinia enterocolitica and Morganella morganii at low pH
    • Young, G. M., Amid, D., and Miller, V. L. (1996) A bifunctional urease enhances survival of pathogenic Yersinia enterocolitica and Morganella morganii at low pH. J. Bacteriol. 178, 6487-6495
    • (1996) J. Bacteriol. , vol.178 , pp. 6487-6495
    • Young, G.M.1    Amid, D.2    Miller, V.L.3
  • 28
    • 0032921096 scopus 로고    scopus 로고
    • Cloning, sequence analyses, expression, and distribution of ampC-ampR from Morganella morganii clinical isolates
    • Poirel, L., Guibert, M., Girlich, D., Naas, T., and Nordmann, P. (1999) Cloning, sequence analyses, expression, and distribution of ampC-ampR from Morganella morganii clinical isolates. Antimicrob. Agents Chemother. 43, 769-776
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 769-776
    • Poirel, L.1    Guibert, M.2    Girlich, D.3    Naas, T.4    Nordmann, P.5
  • 29
    • 52649134285 scopus 로고    scopus 로고
    • Current concepts of molecular defence mechanisms operative during urinary tract infection
    • Weichhart, T., Haidinger, M., Hörl, W. H., and Säemann, M. D. (2008) Current concepts of molecular defence mechanisms operative during urinary tract infection. Eur. J. Clin. Invest. 38, 29-38
    • (2008) Eur. J. Clin. Invest. , vol.38 , pp. 29-38
    • Weichhart, T.1    Haidinger, M.2    Hörl, W.H.3    Säemann, M.D.4
  • 30
    • 35848948624 scopus 로고    scopus 로고
    • Antimicrobial peptides, innate immunity, and the normally sterile urinary tract
    • Zasloff, M. (2007) Antimicrobial peptides, innate immunity, and the normally sterile urinary tract. J. Am. Soc. Nephrol. 18, 2810-2816
    • (2007) J. Am. Soc. Nephrol. , vol.18 , pp. 2810-2816
    • Zasloff, M.1
  • 31
    • 0027180019 scopus 로고
    • Interleukin-8 and the neutrophil response to mucosal gram-negative infection
    • Agace, W. W., Hedges, S. R., Ceska, M., and Svanborg, C. (1993) Interleukin-8 and the neutrophil response to mucosal gram-negative infection. J. Clin. Invest. 92, 780-785
    • (1993) J. Clin. Invest. , vol.92 , pp. 780-785
    • Agace, W.W.1    Hedges, S.R.2    Ceska, M.3    Svanborg, C.4
  • 33
    • 0026059712 scopus 로고
    • Interleukin-6 response to deliberate colonization of the human urinary tract with gram-negative bacteria
    • Hedges, S., Anderson, P., Lidin-Janson, G., de Man, P., and Svanborg, C. (1991) Interleukin-6 response to deliberate colonization of the human urinary tract with gram-negative bacteria. Infect. Immun. 59, 421-427
    • (1991) Infect. Immun. , vol.59 , pp. 421-427
    • Hedges, S.1    Anderson, P.2    Lidin-Janson, G.3    De Man, P.4    Svanborg, C.5
  • 34
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • Selsted, M. E., and Ouellette, A. J. (2005) Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 6, 551-557
    • (2005) Nat. Immunol. , vol.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 36
    • 0033801238 scopus 로고    scopus 로고
    • Human lactoferrin and peptides derived from a surface-exposed helical region reduce experimental Escherichia coli urinary tract infection in mice
    • Håversen, L. A., Engberg, I., Baltzer, L., Dolphin, G., Hanson, L. A., and Mattsby-Baltzer, I. (2000) Human lactoferrin and peptides derived from a surface-exposed helical region reduce experimental Escherichia coli urinary tract infection in mice. Infect. Immun. 68, 5816-5823
    • (2000) Infect. Immun. , vol.68 , pp. 5816-5823
    • Håversen, L.A.1    Engberg, I.2    Baltzer, L.3    Dolphin, G.4    Hanson, L.A.5    Mattsby-Baltzer, I.6
  • 38
    • 4644298916 scopus 로고    scopus 로고
    • Minireview: Functions of the renal tract epithelium in coordinating the innate immune response to infection
    • Chowdhury, P., Sacks, S. H., and Sheerin, N. S. (2004) Minireview: functions of the renal tract epithelium in coordinating the innate immune response to infection. Kidney Int. 66, 1334-1344
    • (2004) Kidney Int. , vol.66 , pp. 1334-1344
    • Chowdhury, P.1    Sacks, S.H.2    Sheerin, N.S.3
  • 39
    • 0035810399 scopus 로고    scopus 로고
    • Complement. First of two parts
    • Walport, M. J. (2001) Complement. First of two parts. N. Engl. J. Med. 344, 1058-1066
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1058-1066
    • Walport, M.J.1
  • 40
    • 0023280596 scopus 로고
    • Local and systemic antibody responses accompany spontaneous resolution of experimental cystitis in cynomolgus monkeys
    • Hopkins, W. J., Uehling, D. T., and Balish, E. (1987) Local and systemic antibody responses accompany spontaneous resolution of experimental cystitis in cynomolgus monkeys. Infect. Immun. 55, 1951-1956
    • (1987) Infect. Immun. , vol.55 , pp. 1951-1956
    • Hopkins, W.J.1    Uehling, D.T.2    Balish, E.3
  • 41
    • 0032862854 scopus 로고    scopus 로고
    • Susceptibility of immunodeficient gene-knockout mice to urinary tract infection
    • Jones-Carson, J., Balish, E., and Uehling, D. T. (1999) Susceptibility of immunodeficient gene-knockout mice to urinary tract infection. J. Urol. 161, 338-341
    • (1999) J. Urol. , vol.161 , pp. 338-341
    • Jones-Carson, J.1    Balish, E.2    Uehling, D.T.3
  • 42
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 43
    • 0030894262 scopus 로고    scopus 로고
    • A simple artificial urine for the growth of urinary pathogens
    • Brooks, T., and Keevil, C. W. (1997) A simple artificial urine for the growth of urinary pathogens. Lett. Appl. Microbiol. 24, 203-206
    • (1997) Lett. Appl. Microbiol. , vol.24 , pp. 203-206
    • Brooks, T.1    Keevil, C.W.2
  • 44
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 45
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, V., Arold, N., Taube, D., and Ehrhardt, W. (1988) Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9, 255-262
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 47
    • 84870817972 scopus 로고    scopus 로고
    • Virtual metagenome reconstruction from 16S rRNA gene sequences
    • Okuda, S., Tsuchiya, Y., Kiriyama, C., Itoh, M., and Morisaki, H. (2012) Virtual metagenome reconstruction from 16S rRNA gene sequences. Nat. Commun. 3, 1203
    • (2012) Nat. Commun. , vol.3 , pp. 1203
    • Okuda, S.1    Tsuchiya, Y.2    Kiriyama, C.3    Itoh, M.4    Morisaki, H.5
  • 50
    • 79959744012 scopus 로고    scopus 로고
    • Structure and function of the symbiosis partners of the lung lichen (Lobaria pulmonaria L. Hoffm.) analyzed by metaproteomics
    • Schneider, T., Schmid, E., de Castro, J. V., Jr., Cardinale, M., Eberl, L., Grube, M., Berg, G., and Riedel, K. (2011) Structure and function of the symbiosis partners of the lung lichen (Lobaria pulmonaria L. Hoffm.) analyzed by metaproteomics. Proteomics 11, 2752-2756
    • (2011) Proteomics , vol.11 , pp. 2752-2756
    • Schneider, T.1    Schmid, E.2    De Castro, J.V.3    Cardinale, M.4    Eberl, L.5    Grube, M.6    Berg, G.7    Riedel, K.8
  • 51
    • 0038438514 scopus 로고    scopus 로고
    • IMPALA: Matching a protein sequence against a collection of PSI-BLAST-constructed position-specific score matrices
    • Schäffer, A. A., Wolf, Y. I., Ponting, C. P., Koonin, E. V., Aravind, L., and Altschul, S. F. (1999) IMPALA: matching a protein sequence against a collection of PSI-BLAST-constructed position-specific score matrices. Bioinformatics 15, 1000-1011
    • (1999) Bioinformatics , vol.15 , pp. 1000-1011
    • SchäFfer, A.A.1    Wolf, Y.I.2    Ponting, C.P.3    Koonin, E.V.4    Aravind, L.5    Altschul, S.F.6
  • 52
    • 80055082271 scopus 로고    scopus 로고
    • Accelerated Profile HMM Searches
    • Eddy, S. R. (2011) Accelerated Profile HMM Searches. PLoS Comput. Biol. 7, e1002195
    • (2011) PLoS Comput. Biol. , vol.7 , pp. e1002195
    • Eddy, S.R.1
  • 56
    • 84872268114 scopus 로고    scopus 로고
    • Proteomics approaches for the analysis of enriched microbial subpopulations and visualization of complex functional information
    • Bernhardt, J., Michalik, S., Wollscheid, B., Völker, U., and Schmidt, F. (2013) Proteomics approaches for the analysis of enriched microbial subpopulations and visualization of complex functional information. Curr. Opin. Biotechnol. 24, 112-119
    • (2013) Curr. Opin. Biotechnol. , vol.24 , pp. 112-119
    • Bernhardt, J.1    Michalik, S.2    Wollscheid, B.3    Völker, U.4    Schmidt, F.5
  • 57
    • 83455197438 scopus 로고    scopus 로고
    • Validating T-RFLP as a sensitive and high-throughput approach to assess bacterial diversity patterns in human anterior nares
    • Camarinha-Silva, A., Wos-Oxley, M. L., Jáuregui, R., Becker, K., and Pieper, D. H. (2012) Validating T-RFLP as a sensitive and high-throughput approach to assess bacterial diversity patterns in human anterior nares. FEMS Microbiol. Ecol. 79, 98-108
    • (2012) FEMS Microbiol. Ecol. , vol.79 , pp. 98-108
    • Camarinha-Silva, A.1    Wos-Oxley, M.L.2    Jáuregui, R.3    Becker, K.4    Pieper, D.H.5
  • 59
    • 0001857117 scopus 로고
    • 16S/23S rRNA sequencing
    • Stackebrandt E., Good-fellow M. Chichester, United Kingdom: John Wiley and Sons 1991
    • Lane, D. J. (1991) 16S/23S rRNA sequencing. In: Stackebrandt E., Good-fellow M., eds. Nucleic acid techniques in bacterial systematics. Chichester, United Kingdom: John Wiley and Sons; 1991. pp. 115-175
    • (1991) Nucleic Acid Techniques in Bacterial Systematics. , pp. 115-175
    • Lane, D.J.1
  • 61
    • 0031970701 scopus 로고    scopus 로고
    • Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signaling pathways: A genetic analysis
    • O'Toole, G. A., and Kolter, R. (1998) Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signaling pathways: a genetic analysis. Mol. Microbiol. 28, 449-461
    • (1998) Mol. Microbiol. , vol.28 , pp. 449-461
    • O'Toole, G.A.1    Kolter, R.2
  • 62
    • 34249100313 scopus 로고    scopus 로고
    • Clinical and environmental Burkholderia strains: Biofilm production and intracellular survival
    • Savoia, D., and Zucca, M. (2007) Clinical and environmental Burkholderia strains: biofilm production and intracellular survival. Curr. Microbiol. 54, 440-444
    • (2007) Curr. Microbiol. , vol.54 , pp. 440-444
    • Savoia, D.1    Zucca, M.2
  • 63
    • 0013902668 scopus 로고
    • Antibiotic susceptibility testing by a standardized single disk method
    • Bauer, A. W., Kirby, W. M., Sherris, J. C., and Turck, M. (1966) Antibiotic susceptibility testing by a standardized single disk method. Am. J Clin. Pathol. 45, 493-496
    • (1966) Am. J Clin. Pathol. , vol.45 , pp. 493-496
    • Bauer, A.W.1    Kirby, W.M.2    Sherris, J.C.3    Turck, M.4
  • 64
    • 0023636563 scopus 로고
    • Urease-positive bacteriuria and obstruction of long-term urinary catheters
    • Mobley, H. L., and Warren, J. W. (1987) Urease-positive bacteriuria and obstruction of long-term urinary catheters. J. Clin. Microbiol. 25, 2216-2217
    • (1987) J. Clin. Microbiol. , vol.25 , pp. 2216-2217
    • Mobley, H.L.1    Warren, J.W.2
  • 65
    • 0019852248 scopus 로고
    • Bacitracin and protease production in relation to sporulation during exponential growth of Bacillus licheniformis on poorly utilized carbon and nitrogen sources
    • Hanlon, G. W., and Hodges, N. A. (1981) Bacitracin and protease production in relation to sporulation during exponential growth of Bacillus licheniformis on poorly utilized carbon and nitrogen sources. J. Bacteriol. 147, 427-431
    • (1981) J. Bacteriol. , vol.147 , pp. 427-431
    • Hanlon, G.W.1    Hodges, N.A.2
  • 66
    • 0000271704 scopus 로고
    • Genetic recombination in Pseudomonas aeruginosa
    • Holloway, B. W. (1955) Genetic recombination in Pseudomonas aeruginosa. J. Gen. Microbiol. 13, 572-581
    • (1955) J. Gen. Microbiol. , vol.13 , pp. 572-581
    • Holloway, B.W.1
  • 68
    • 77149152780 scopus 로고    scopus 로고
    • Environmental proteomics: Analysis of structure and function of microbial communities
    • Schneider, T., and Riedel, K. (2010) Environmental proteomics: analysis of structure and function of microbial communities. Proteomics 10, 785-798
    • (2010) Proteomics , vol.10 , pp. 785-798
    • Schneider, T.1    Riedel, K.2
  • 69
    • 84887096280 scopus 로고    scopus 로고
    • Host-centric proteomics of stool: A novel strategy focused on intestinal responses to the gut microbiota
    • Lichtman, J. S., Marcobal, A., Sonnenburg, J. L., and Elias, J. E. (2013) Host-centric proteomics of stool: a novel strategy focused on intestinal responses to the gut microbiota. Mol. Cell. Proteomics 12, 3310-3318
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3310-3318
    • Lichtman, J.S.1    Marcobal, A.2    Sonnenburg, J.L.3    Elias, J.E.4
  • 71
    • 0028789238 scopus 로고
    • Role of the ferric uptake regulator of Pseudomonas aeruginosa in the regulation of siderophores and exotoxin A expression: Purification and activity on iron-regulated promoters
    • Ochsner, U. A., Vasil, A. I., and Vasil, M. L. (1995) Role of the ferric uptake regulator of Pseudomonas aeruginosa in the regulation of siderophores and exotoxin A expression: purification and activity on iron-regulated promoters. J. Bacteriol. 177, 7194-7201
    • (1995) J. Bacteriol. , vol.177 , pp. 7194-7201
    • Ochsner, U.A.1    Vasil, A.I.2    Vasil, M.L.3
  • 72
    • 0032786580 scopus 로고    scopus 로고
    • Characterization and purification of an outer membrane metalloproteinase from Pseudomonas aeruginosa with fibrinogenolytic activity
    • Fricke, B., Parchmann, O., Kruse, K., Rücknagel, P., Schierhorn, A., and Menge, S. (1999) Characterization and purification of an outer membrane metalloproteinase from Pseudomonas aeruginosa with fibrinogenolytic activity. Biochim. Biophys. Acta 1454, 236-250
    • (1999) Biochim. Biophys. Acta , vol.1454 , pp. 236-250
    • Fricke, B.1    Parchmann, O.2    Kruse, K.3    Rücknagel, P.4    Schierhorn, A.5    Menge, S.6
  • 73
    • 38549128203 scopus 로고    scopus 로고
    • Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilis
    • Jacobsen, S. M., Stickler, D. J., Mobley, H. L., and Shirtliff, M. E. (2008) Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilis. Clin. Microbiol. Rev. 21, 26-59
    • (2008) Clin. Microbiol. Rev. , vol.21 , pp. 26-59
    • Jacobsen, S.M.1    Stickler, D.J.2    Mobley, H.L.3    Shirtliff, M.E.4
  • 74
    • 0017238988 scopus 로고
    • Urease. The primary cause of infection-induced urinary stones
    • Griffith, D. P., Musher, D. M., and Itin, C. (1976) Urease. The primary cause of infection-induced urinary stones. Invest. Urol. 13, 346-350
    • (1976) Invest. Urol. , vol.13 , pp. 346-350
    • Griffith, D.P.1    Musher, D.M.2    Itin, C.3
  • 78
    • 78649738763 scopus 로고    scopus 로고
    • Portrait of a pathogen: The Mycobacterium tuberculosis proteome in vivo
    • Kruh, N. A., Troudt, J., Izzo, A., Prenni, J., and Dobos, K. M. (2010) Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo. PloS One 5, e13938
    • (2010) PloS One , vol.5 , pp. e13938
    • Kruh, N.A.1    Troudt, J.2    Izzo, A.3    Prenni, J.4    Dobos, K.M.5
  • 79
    • 1342303482 scopus 로고    scopus 로고
    • Of mice and not men: Differences between mouse and human immunology
    • Mestas, J., and Hughes, C. C. (2004) Of mice and not men: differences between mouse and human immunology. J. Immunol. 172, 2731-2738
    • (2004) J. Immunol. , vol.172 , pp. 2731-2738
    • Mestas, J.1    Hughes, C.C.2
  • 80
    • 12944297142 scopus 로고    scopus 로고
    • Can laboratory reference strains mirror "real-world" pathogenesis?
    • Fux, C. A., Shirtliff, M., Stoodley, P., and Costerton, J. W. (2005) Can laboratory reference strains mirror "real-world" pathogenesis? Trends Microbiol. 13, 58-63
    • (2005) Trends Microbiol. , vol.13 , pp. 58-63
    • Fux, C.A.1    Shirtliff, M.2    Stoodley, P.3    Costerton, J.W.4
  • 81
    • 0015139958 scopus 로고
    • The development of neutrophilic polymorphonuclear leukocytes in human bone marrow
    • Bainton, D. F., Ullyot, J. L., and Farquhar, M. G. (1971) The development of neutrophilic polymorphonuclear leukocytes in human bone marrow. J. Exp. Med. 134, 907-934
    • (1971) J. Exp. Med. , vol.134 , pp. 907-934
    • Bainton, D.F.1    Ullyot, J.L.2    Farquhar, M.G.3
  • 82
    • 0038819118 scopus 로고    scopus 로고
    • The in vivo profile of transcription factors during neutrophil differentiation in human bone marrow
    • Bjerregaard, M. D., Jurlander, J., Klausen, P., Borregaard, N., and Cowland, J. B. (2003) The in vivo profile of transcription factors during neutrophil differentiation in human bone marrow. Blood 101, 4322-4332
    • (2003) Blood , vol.101 , pp. 4322-4332
    • Bjerregaard, M.D.1    Jurlander, J.2    Klausen, P.3    Borregaard, N.4    Cowland, J.B.5
  • 83
    • 84891938742 scopus 로고    scopus 로고
    • Evaluating the impact of different sequence databases on metaproteome analysis: Insights from a lab-assembled microbial mixture
    • Tanca, A., Palomba, A., Deligios, M., Cubeddu, T., Fraumene, C., Biosa, G., Pagnozzi, D., Addis, M. F., and Uzzau, S. (2013) Evaluating the impact of different sequence databases on metaproteome analysis: insights from a lab-assembled microbial mixture. PloS One 8, e82981
    • (2013) PloS One , vol.8 , pp. e82981
    • Tanca, A.1    Palomba, A.2    Deligios, M.3    Cubeddu, T.4    Fraumene, C.5    Biosa, G.6    Pagnozzi, D.7    Addis, M.F.8    Uzzau, S.9
  • 84
    • 84870673207 scopus 로고    scopus 로고
    • Flexible survival strategies of Pseudomonas aeruginosa in biofilms result in increased fitness compared with Candida albicans
    • Purschke, F. G., Hiller, E., Trick, I., and Rupp, S. (2012) Flexible survival strategies of Pseudomonas aeruginosa in biofilms result in increased fitness compared with Candida albicans. Mol. Cell. Proteomics 11, 1652-1669
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 1652-1669
    • Purschke, F.G.1    Hiller, E.2    Trick, I.3    Rupp, S.4
  • 86
    • 19444368356 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa pirA gene encodes a second receptor for ferrienterobactin and synthetic catecholate analogs
    • Ghysels, B., Ochsner, U., Möllman, U., Heinisch, L., Vasil, M., Cornelis, P., and Matthijs, S. (2005) The Pseudomonas aeruginosa pirA gene encodes a second receptor for ferrienterobactin and synthetic catecholate analogs. FEMS Microbiol. Lett. 246, 167-174
    • (2005) FEMS Microbiol. Lett. , vol.246 , pp. 167-174
    • Ghysels, B.1    Ochsner, U.2    Möllman, U.3    Heinisch, L.4    Vasil, M.5    Cornelis, P.6    Matthijs, S.7
  • 87
    • 0027398117 scopus 로고
    • Cloning and characterization of the ferric enterobactin receptor gene (pfeA) of Pseudomonas aeruginosa
    • Dean, C. R., and Poole, K. (1993) Cloning and characterization of the ferric enterobactin receptor gene (pfeA) of Pseudomonas aeruginosa. J. Bacteriol. 175, 317-324
    • (1993) J. Bacteriol. , vol.175 , pp. 317-324
    • Dean, C.R.1    Poole, K.2
  • 88
    • 79955603039 scopus 로고    scopus 로고
    • The role of iron in the immune response to bacterial infection
    • Cherayil, B. J. (2011) The role of iron in the immune response to bacterial infection. Immunol. Res. 50, 1-9
    • (2011) Immunol. Res. , vol.50 , pp. 1-9
    • Cherayil, B.J.1
  • 89
    • 0037198693 scopus 로고    scopus 로고
    • A component of innate immunity prevents bacterial biofilm development
    • Singh, P. K., Parsek, M. R., Greenberg, E. P., and Welsh, M. J. (2002) A component of innate immunity prevents bacterial biofilm development. Nature 417, 552-555
    • (2002) Nature , vol.417 , pp. 552-555
    • Singh, P.K.1    Parsek, M.R.2    Greenberg, E.P.3    Welsh, M.J.4
  • 90
    • 0034873465 scopus 로고    scopus 로고
    • Characterization of an endoprotease (PrpL) encoded by a PvdS-regulated gene in Pseudomonas aeruginosa
    • Wilderman, P. J., Vasil, A. I., Johnson, Z., Wilson, M. J., Cunliffe, H. E., Lamont, I. L., and Vasil, M. L. (2001) Characterization of an endoprotease (PrpL) encoded by a PvdS-regulated gene in Pseudomonas aeruginosa. Infect Immun. 69, 5385-5394
    • (2001) Infect Immun. , vol.69 , pp. 5385-5394
    • Wilderman, P.J.1    Vasil, A.I.2    Johnson, Z.3    Wilson, M.J.4    Cunliffe, H.E.5    Lamont, I.L.6    Vasil, M.L.7
  • 91
    • 33646947821 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin, a siderophore-binding eukaryotic protein
    • Borregaard, N., and Cowland, J. B. (2006) Neutrophil gelatinase-associated lipocalin, a siderophore-binding eukaryotic protein. Biometals 19, 211-215
    • (2006) Biometals , vol.19 , pp. 211-215
    • Borregaard, N.1    Cowland, J.B.2
  • 95
    • 84857982248 scopus 로고    scopus 로고
    • Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp
    • Grinter, R., Milner, J., and Walker, D. (2012) Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp. PloS One 7, e33033
    • (2012) PloS One , vol.7 , pp. e33033
    • Grinter, R.1    Milner, J.2    Walker, D.3
  • 96
    • 0842264185 scopus 로고    scopus 로고
    • The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen
    • Baughn, A. D., and Malamy, M. H. (2004) The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen. Nature 427, 441-444
    • (2004) Nature , vol.427 , pp. 441-444
    • Baughn, A.D.1    Malamy, M.H.2
  • 97
    • 78549290620 scopus 로고    scopus 로고
    • Anaerobic physiology of Pseudomonas aeruginosa in the cystic fibrosis lung
    • Schobert, M., and Jahn, D. (2010) Anaerobic physiology of Pseudomonas aeruginosa in the cystic fibrosis lung. Int. J. Med. Microbiol. 300, 549-556
    • (2010) Int. J. Med. Microbiol. , vol.300 , pp. 549-556
    • Schobert, M.1    Jahn, D.2
  • 99
    • 0033396672 scopus 로고    scopus 로고
    • Respiratory burst in human neutrophils
    • Dahlgren, C., and Karlsson, A. (1999) Respiratory burst in human neutrophils. J. Immunol. Methods. 232, 3-14
    • (1999) J. Immunol. Methods. , vol.232 , pp. 3-14
    • Dahlgren, C.1    Karlsson, A.2
  • 101
    • 0026601820 scopus 로고
    • Effect of Pseudomonas aeruginosa elastase and alkaline protease on serum complement and isolated components C1q and C3
    • Hong, Y. Q., and Ghebrehiwet, B. (1992) Effect of Pseudomonas aeruginosa elastase and alkaline protease on serum complement and isolated components C1q and C3. Clin. Immunol. Immunopathol. 62, 133-138
    • (1992) Clin. Immunol. Immunopathol. , vol.62 , pp. 133-138
    • Hong, Y.Q.1    Ghebrehiwet, B.2
  • 102
    • 84855396914 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa alkaline protease blocks complement activation via the classical and lectin pathways
    • Laarman, A. J., Bardoel, B. W., Ruyken, M., Fernie, J., Milder, F. J., van Strijp, J. A., and Rooijakkers, S. H. (2012) Pseudomonas aeruginosa alkaline protease blocks complement activation via the classical and lectin pathways. J. Immunol. 188, 386-393
    • (2012) J. Immunol. , vol.188 , pp. 386-393
    • Laarman, A.J.1    Bardoel, B.W.2    Ruyken, M.3    Fernie, J.4    Milder, F.J.5    Van Strijp, J.A.6    Rooijakkers, S.H.7
  • 103
    • 0025170582 scopus 로고
    • Proteolytic inactivation of cytokines by Pseudomonas aeruginosa
    • Parmely, M., Gale, A., Clabaugh, M., Horvat, R., and Zhou, W. W. (1990) Proteolytic inactivation of cytokines by Pseudomonas aeruginosa. Infect. Immun. 58, 3009-3014
    • (1990) Infect. Immun. , vol.58 , pp. 3009-3014
    • Parmely, M.1    Gale, A.2    Clabaugh, M.3    Horvat, R.4    Zhou, W.W.5
  • 104
    • 84855848528 scopus 로고    scopus 로고
    • Inhibition of Pseudomonas aeruginosa virulence: Characterization of the AprA-AprI interface and species selectivity
    • Bardoel, B. W., van Kessel, K. P., van Strijp, J. A., and Milder, F. J. (2012) Inhibition of Pseudomonas aeruginosa virulence: characterization of the AprA-AprI interface and species selectivity. J. Mol. Biol. 415, 573-583
    • (2012) J. Mol. Biol. , vol.415 , pp. 573-583
    • Bardoel, B.W.1    Van Kessel, K.P.2    Van Strijp, J.A.3    Milder, F.J.4
  • 105
    • 3142777764 scopus 로고    scopus 로고
    • Degradation of pulmonary surfactant protein D by Pseudomonas aeruginosa elastase abrogates innate immune function
    • Alcorn, J. F., and Wright, J. R. (2004) Degradation of pulmonary surfactant protein D by Pseudomonas aeruginosa elastase abrogates innate immune function. J. Biol. Chem. 279, 30871-30879
    • (2004) J. Biol. Chem. , vol.279 , pp. 30871-30879
    • Alcorn, J.F.1    Wright, J.R.2
  • 106
    • 34547622484 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa LasB metalloproteinase regulates the human urokinase-type plasminogen activator receptor through domain- specific endoproteolysis
    • Leduc, D., Beaufort, N., de Bentzmann, S., Rousselle, J. C., Namane, A., Chignard, M., and Pidard, D. (2007) The Pseudomonas aeruginosa LasB metalloproteinase regulates the human urokinase-type plasminogen activator receptor through domain- specific endoproteolysis. Infect. Immun. 75, 3848-3858
    • (2007) Infect. Immun. , vol.75 , pp. 3848-3858
    • Leduc, D.1    Beaufort, N.2    De Bentzmann, S.3    Rousselle, J.C.4    Namane, A.5    Chignard, M.6    Pidard, D.7
  • 107
    • 70349437186 scopus 로고    scopus 로고
    • Complement regulators and inhibitory proteins
    • Zipfel, P. F., and Skerka, C. (2009) Complement regulators and inhibitory proteins. Nat. Rev. Immunol. 9, 729-740
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 729-740
    • Zipfel, P.F.1    Skerka, C.2
  • 110
    • 0033953969 scopus 로고    scopus 로고
    • Identification of a chitin-binding protein secreted by Pseudomonas aeruginosa
    • Folders, J., Tommassen, J., van Loon, L. C., and Bitter, W. (2000) Identification of a chitin-binding protein secreted by Pseudomonas aeruginosa. J. Bacteriol. 182, 1257-1263
    • (2000) J. Bacteriol. , vol.182 , pp. 1257-1263
    • Folders, J.1    Tommassen, J.2    Van Loon, L.C.3    Bitter, W.4
  • 112
    • 0015428055 scopus 로고
    • The role of ferric enterochelin esterase in enterochelin-mediated iron transport and ferrochelatase activity in Escherichia coli
    • Porra, R. J., Langman, L., Young, I. G., and Gibson, F. (1972) The role of ferric enterochelin esterase in enterochelin-mediated iron transport and ferrochelatase activity in Escherichia coli. Arch. Biochem. Biophys. 153, 74-78
    • (1972) Arch. Biochem. Biophys. , vol.153 , pp. 74-78
    • Porra, R.J.1    Langman, L.2    Young, I.G.3    Gibson, F.4
  • 113
    • 0026700544 scopus 로고
    • Molecular genetics of the extracellular lipase of Pseudomonas aeruginosa PAO1
    • Wohlfarth, S., Hoesche, C., Strunk, C., and Winkler, U. K. (1992) Molecular genetics of the extracellular lipase of Pseudomonas aeruginosa PAO1. J. Gen. Microbiol. 138, 1325-1335
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1325-1335
    • Wohlfarth, S.1    Hoesche, C.2    Strunk, C.3    Winkler, U.K.4
  • 114
    • 0019538672 scopus 로고
    • Extracellular toxins of Pseudomonas aeruginosa. I. Purification and characterization of two exoproteases
    • Obernesser, H. J., Doring, G., and Botzenhart, K. (1981) Extracellular toxins of Pseudomonas aeruginosa. I. Purification and characterization of two exoproteases. Zentralbl. Bakteriol. A 249, 76-88
    • (1981) Zentralbl. Bakteriol. A , vol.249 , pp. 76-88
    • Obernesser, H.J.1    Doring, G.2    Botzenhart, K.3
  • 116
    • 33745559712 scopus 로고    scopus 로고
    • Neutrophil serine proteases: Specific regulators of inflammation
    • Pham, C. T. (2006) Neutrophil serine proteases: specific regulators of inflammation. Nat. Rev. Immunol. 6, 541-550
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 541-550
    • Pham, C.T.1
  • 117
    • 0014465369 scopus 로고
    • Resolution of granules from rabbit heterophil leukocytes into distinct populations by zonal sedimentation
    • Baggiolini, M., Hirsch, J. G., and De Duve, C. (1969) Resolution of granules from rabbit heterophil leukocytes into distinct populations by zonal sedimentation. J. Cell Biol. 40, 529-541
    • (1969) J. Cell Biol. , vol.40 , pp. 529-541
    • Baggiolini, M.1    Hirsch, J.G.2    De Duve, C.3
  • 118
    • 0017090666 scopus 로고
    • Microbicidal mechanisms of human granulocytes: Synergistic effects of granulocyte elastase and myeloperoxidase or chymotrypsin-like cationic protein
    • Odeberg, H., and Olsson, I. (1976) Microbicidal mechanisms of human granulocytes: synergistic effects of granulocyte elastase and myeloperoxidase or chymotrypsin-like cationic protein. Infect. Immun. 14, 1276-1283
    • (1976) Infect. Immun. , vol.14 , pp. 1276-1283
    • Odeberg, H.1    Olsson, I.2
  • 119
    • 0017399797 scopus 로고
    • Neutral proteases of human granulocytes. IV. Interaction between human granulocyte collagenase and plasma protease inhibitors
    • Ohlsson, K., and Olsson, I. (1977) Neutral proteases of human granulocytes. IV. Interaction between human granulocyte collagenase and plasma protease inhibitors. J. Lab. Clin. Med. 89, 269-277
    • (1977) J. Lab. Clin. Med. , vol.89 , pp. 269-277
    • Ohlsson, K.1    Olsson, I.2
  • 120
    • 0016169960 scopus 로고
    • Cationic proteins of human granulocytes. II. Separation of the cationic proteins of the granules of leukemic myeloid cells
    • Olsson, I., and Venge, P. (1974) Cationic proteins of human granulocytes. II. Separation of the cationic proteins of the granules of leukemic myeloid cells. Blood 44, 235-246
    • (1974) Blood , vol.44 , pp. 235-246
    • Olsson, I.1    Venge, P.2
  • 122
    • 0025694843 scopus 로고
    • Cloning of cDNA for proteinase 3: A serine protease, antibiotic, and autoantigen from human neutrophils
    • Campanelli, D., Melchior, M., Fu, Y., Nakata, M., Shuman, H., Nathan, C., and Gabay, J. E. (1990) Cloning of cDNA for proteinase 3: a serine protease, antibiotic, and autoantigen from human neutrophils. J. Exp. Med. 172, 1709-1715
    • (1990) J. Exp. Med. , vol.172 , pp. 1709-1715
    • Campanelli, D.1    Melchior, M.2    Fu, Y.3    Nakata, M.4    Shuman, H.5    Nathan, C.6    Gabay, J.E.7
  • 124
    • 0025239075 scopus 로고
    • Azurocidin and a homologous serine protease from neutrophils. Differential antimicrobial and proteolytic properties
    • Campanelli, D., Detmers, P. A., Nathan, C. F., and Gabay, J. E. (1990) Azurocidin and a homologous serine protease from neutrophils. Differential antimicrobial and proteolytic properties. J. Clin. Invest. 85, 904-915
    • (1990) J. Clin. Invest. , vol.85 , pp. 904-915
    • Campanelli, D.1    Detmers, P.A.2    Nathan, C.F.3    Gabay, J.E.4
  • 125
    • 0017350418 scopus 로고
    • The use of a phospholipase A-less Escherichia coli mutant to establish the action of granulocyte phospholipase A on bacterial phospholipids during killing by a highly purified granulocyte fraction
    • Weiss, J., and Elsbach, P. (1977) The use of a phospholipase A-less Escherichia coli mutant to establish the action of granulocyte phospholipase A on bacterial phospholipids during killing by a highly purified granulocyte fraction. Biochim. Biophys. Acta 466, 23-33
    • (1977) Biochim. Biophys. Acta , vol.466 , pp. 23-33
    • Weiss, J.1    Elsbach, P.2
  • 126
    • 0000255408 scopus 로고
    • Antibacterial and enzymic basic proteins from leukocyte lysosomes: Separation and identification
    • Zeya, H. I., and Spitznagel, J. K. (1963) Antibacterial and enzymic basic proteins from leukocyte lysosomes: separation and identification. Science 142, 1085-1087
    • (1963) Science , vol.142 , pp. 1085-1087
    • Zeya, H.I.1    Spitznagel, J.K.2
  • 127
    • 0014028183 scopus 로고
    • Antimicrobial specificity of leukocyte lysosomal cationic proteins
    • Zeya, H. I., and Spitznagel, J. K. (1966) Antimicrobial specificity of leukocyte lysosomal cationic proteins. Science 154, 1049-1051
    • (1966) Science , vol.154 , pp. 1049-1051
    • Zeya, H.I.1    Spitznagel, J.K.2
  • 128
    • 0013870308 scopus 로고
    • Antibacterial action of PMN lysosomal cationic proteins resolved by density gradient electrophoresis
    • Zeya, H. I., Spitznagel, J. K., and Schwab, J. H. (1966) Antibacterial action of PMN lysosomal cationic proteins resolved by density gradient electrophoresis. Proc. Soc. Exp. Biol. Med. 121, 250-253
    • (1966) Proc. Soc. Exp. Biol. Med. , vol.121 , pp. 250-253
    • Zeya, H.I.1    Spitznagel, J.K.2    Schwab, J.H.3
  • 129
    • 0018374630 scopus 로고
    • Identification of a previously undescribed cytochrome b in human neutrophils and its relationship to phagocytosis-induced oxidase activity
    • Segal, A. W., and Jones, O. T. (1979) Identification of a previously undescribed cytochrome b in human neutrophils and its relationship to phagocytosis-induced oxidase activity. Biochem. Soc. Trans. 7, 187-188
    • (1979) Biochem. Soc. Trans. , vol.7 , pp. 187-188
    • Segal, A.W.1    Jones, O.T.2
  • 130
    • 0014574791 scopus 로고
    • Lactoferrin, an iron-binding protein in neutrophilic leukocytes
    • Masson, P. L., Heremans, J. F., and Schonne, E. (1969) Lactoferrin, an iron-binding protein in neutrophilic leukocytes. J. Exp. Med. 130, 643-658
    • (1969) J. Exp. Med. , vol.130 , pp. 643-658
    • Masson, P.L.1    Heremans, J.F.2    Schonne, E.3
  • 131
    • 0034062292 scopus 로고    scopus 로고
    • Expression of lactoferrin in the kidney: Implications for innate immunity and iron metabolism
    • Abrink, M., Larsson, E., Gobl, A., and Hellman, L. (2000) Expression of lactoferrin in the kidney: implications for innate immunity and iron metabolism. Kidney Int. 57, 2004-2010
    • (2000) Kidney Int. , vol.57 , pp. 2004-2010
    • Abrink, M.1    Larsson, E.2    Gobl, A.3    Hellman, L.4
  • 132
    • 0034332193 scopus 로고    scopus 로고
    • The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations
    • Agerberth, B., Charo, J., Werr, J., Olsson, B., Idali, F., Lindbom, L., Kiessling, R., Jörnvall, H., Wigzell, H., and Gudmundsson, G. H. (2000) The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations. Blood 96, 3086-3093
    • (2000) Blood , vol.96 , pp. 3086-3093
    • Agerberth, B.1    Charo, J.2    Werr, J.3    Olsson, B.4    Idali, F.5    Lindbom, L.6    Kiessling, R.7    Jörnvall, H.8    Wigzell, H.9    Gudmundsson, G.H.10
  • 133
    • 0031913244 scopus 로고    scopus 로고
    • Mouse beta-defensin 1 is a salt-sensitive antimicrobial peptide present in epithelia of the lung and urogenital tract
    • Bals, R., Goldman, M. J., and Wilson, J. M. (1998) Mouse beta-defensin 1 is a salt-sensitive antimicrobial peptide present in epithelia of the lung and urogenital tract. Infect. Immun. 66, 1225-1232
    • (1998) Infect. Immun. , vol.66 , pp. 1225-1232
    • Bals, R.1    Goldman, M.J.2    Wilson, J.M.3
  • 135
    • 0028065442 scopus 로고
    • Molecular cloning and expression of a cDNA encoding NGAL: A lipocalin expressed in human neutrophils
    • Bundgaard, J. R., Sengelov, H., Borregaard, N., and Kjeldsen, L. (1994) Molecular cloning and expression of a cDNA encoding NGAL: a lipocalin expressed in human neutrophils. Biochem. Biophys. Res. Commun. 202, 1468-1475
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 1468-1475
    • Bundgaard, J.R.1    Sengelov, H.2    Borregaard, N.3    Kjeldsen, L.4
  • 136
    • 0346996867 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin is up-regulated in human epithelial cells by IL-1 beta, but not by TNF-alpha
    • Cowland, J. B., Sorensen, O. E., Sehested, M., and Borregaard, N. (2003) Neutrophil gelatinase-associated lipocalin is up-regulated in human epithelial cells by IL-1 beta, but not by TNF-alpha. J. Immunol. 171, 6630-6639
    • (2003) J. Immunol. , vol.171 , pp. 6630-6639
    • Cowland, J.B.1    Sorensen, O.E.2    Sehested, M.3    Borregaard, N.4
  • 137
    • 0022466359 scopus 로고
    • Localization of eosinophil cationic protein, major basic protein, and eosinophil peroxidase in human eosinophils by immunoelectron microscopic technique
    • Egesten, A., Alumets, J., von Mecklenburg, C., Palmegren, M., and Olsson, I. (1986) Localization of eosinophil cationic protein, major basic protein, and eosinophil peroxidase in human eosinophils by immunoelectron microscopic technique. J. Histochem. Cytochem. 34, 1399-1403
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 1399-1403
    • Egesten, A.1    Alumets, J.2    Von Mecklenburg, C.3    Palmegren, M.4    Olsson, I.5
  • 138
    • 0022481129 scopus 로고
    • Localization of human eosinophil granule major basic protein, eosinophil cationic protein, and eosinophil-derived neurotoxin by immunoelectron microscopy
    • Peters, M. S., Rodriguez, M., and Gleich, G. J. (1986) Localization of human eosinophil granule major basic protein, eosinophil cationic protein, and eosinophil-derived neurotoxin by immunoelectron microscopy. Lab. Invest. 54, 656-662
    • (1986) Lab. Invest. , vol.54 , pp. 656-662
    • Peters, M.S.1    Rodriguez, M.2    Gleich, G.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.