메뉴 건너뛰기




Volumn 96, Issue 4, 1998, Pages 257-265

Does ammonia production by Klebsiella contribute to pathogenesis?

(3)  Kleiner, D a   Traglauer, A a   Domm, S a  

a NONE

Author keywords

Ammonia; Ammonification; Klebsiella; Permeability; Protease; Review; Toxicity; Ureolysis; Virulence factors

Indexed keywords

AMMONIA;

EID: 0032192863     PISSN: 00202452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0020-2452(99)80006-2     Document Type: Review
Times cited : (15)

References (71)
  • 1
    • 0028865193 scopus 로고
    • Nitrogen control in bacteria
    • [1] Merrick, M.J.& Edwards, R.A. (1995), Nitrogen control in bacteria. Microbiol. Rev., 59, 604-622.
    • (1995) Microbiol. Rev. , vol.59 , pp. 604-622
    • Merrick, M.J.1    Edwards, R.A.2
  • 2
    • 0015197327 scopus 로고
    • Ion transport by energy-conserving biological membranes
    • [2] Henderson, P.J.F. (1971), Ion transport by energy-conserving biological membranes. Annu. Rev. Microbiol., 25, 393-428.
    • (1971) Annu. Rev. Microbiol. , vol.25 , pp. 393-428
    • Henderson, P.J.F.1
  • 5
    • 0002538616 scopus 로고
    • Some aspects of cell permeability to weak electrolytes
    • [5] Jacobs, M.H. (1940), Some aspects of cell permeability to weak electrolytes. Cold Spring Harbor Symp. Quant. Biol., 8, 30-39.
    • (1940) Cold Spring Harbor Symp. Quant. Biol. , vol.8 , pp. 30-39
    • Jacobs, M.H.1
  • 6
  • 7
    • 0013532546 scopus 로고
    • Intracellular pH regulation
    • [7] Boron, W.F. (1980), Intracellular pH regulation. Curr. Top. Membr. Transp., 13, 3-22.
    • (1980) Curr. Top. Membr. Transp. , vol.13 , pp. 3-22
    • Boron, W.F.1
  • 8
    • 0031214455 scopus 로고    scopus 로고
    • Mitochondrial ammonia metabolism and the proton-neutral theory of hepatic ammonia detoxication
    • [8] Campbell, J.W. (1997), Mitochondrial ammonia metabolism and the proton-neutral theory of hepatic ammonia detoxication. J. Exp. Zool., 278, 308-321.
    • (1997) J. Exp. Zool. , vol.278 , pp. 308-321
    • Campbell, J.W.1
  • 9
    • 0020573713 scopus 로고
    • Myeloperoxidase-dependent effect of amines on functions of isolated neutrophils
    • [9] Thomas, E.L., Grisham, M.B. & Jefferson, M.M. (1983), Myeloperoxidase-dependent effect of amines on functions of isolated neutrophils. J. Clin. Invest., 72, 441-454.
    • (1983) J. Clin. Invest. , vol.72 , pp. 441-454
    • Thomas, E.L.1    Grisham, M.B.2    Jefferson, M.M.3
  • 10
    • 0021152612 scopus 로고
    • Role of monochloramine in the oxidation of erythrocyte hemoglobin by stimulated neutrophils
    • [10] Grisham, M.B., Jefferson, M.M. & Thomas, E.L. (1984), Role of monochloramine in the oxidation of erythrocyte hemoglobin by stimulated neutrophils. J. Biol. Chem., 259, 6766-6772.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6766-6772
    • Grisham, M.B.1    Jefferson, M.M.2    Thomas, E.L.3
  • 11
    • 0001133417 scopus 로고
    • Excretory nitrogen metabolism and gluconeogenesis during development of higher vertebrates
    • [11] Campbell, J.W. (1994), Excretory nitrogen metabolism and gluconeogenesis during development of higher vertebrates. Isr. J. Zool., 40, 363-381.
    • (1994) Isr. J. Zool. , vol.40 , pp. 363-381
    • Campbell, J.W.1
  • 12
    • 0013471052 scopus 로고
    • The enzymatic steps in urea biosynthesis
    • [12] Cohen, P.P. & Hayano, M. (1948), The enzymatic steps in urea biosynthesis. J. Biol. Chem. 172, 405-15.
    • (1948) J. Biol. Chem. , vol.172 , pp. 405-415
    • Cohen, P.P.1    Hayano, M.2
  • 13
    • 0013503809 scopus 로고
    • Biosynthesis of the purines. IX. Precursors of the nitrogen atoms of the purine ring
    • [13] Sonne, J.C., Lin, I. & Buchanan, J.M. (1956), Biosynthesis of the purines. IX. precursors of the nitrogen atoms of the purine ring. J. Biol. Chem., 220, 369-378.
    • (1956) J. Biol. Chem. , vol.220 , pp. 369-378
    • Sonne, J.C.1    Lin, I.2    Buchanan, J.M.3
  • 14
    • 0001568328 scopus 로고
    • The cerebral and peripheral uptake of ammonia in liver disease with an hypothesis for the mechanism of hepatic coma
    • [14] Bessman, S.P.& Bessman, A.N. (1954), The cerebral and peripheral uptake of ammonia in liver disease with an hypothesis for the mechanism of hepatic coma. J. Clin. Invest., 34, 622-628.
    • (1954) J. Clin. Invest. , vol.34 , pp. 622-628
    • Bessman, S.P.1    Bessman, A.N.2
  • 15
    • 0021236759 scopus 로고
    • Ammonia: Its effects on biological systems, metabolic hormones, and reproduction
    • [15] Visek, W.J. (1984), Ammonia: Its effects on biological systems, metabolic hormones, and reproduction. J. Dairy Sci., 67, 481-498.
    • (1984) J. Dairy Sci. , vol.67 , pp. 481-498
    • Visek, W.J.1
  • 16
    • 0019315920 scopus 로고
    • Ammonia inhibits phagosome-lysosome fusion in macrophages
    • [16] Gordon, A.H., D'Arcy Hart, P. & Young, M.R. (1980), Ammonia inhibits phagosome-lysosome fusion in macrophages. Nature, 286, 79-80.
    • (1980) Nature , vol.286 , pp. 79-80
    • Gordon, A.H.1    D'Arcy Hart, P.2    Young, M.R.3
  • 17
    • 0013538952 scopus 로고
    • The anticomplementary effect of kidney tissue
    • [17] Beeson, P.B. & Rowley, D.R. (1959), The anticomplementary effect of kidney tissue. J. Exp. Med., 110, 685-697.
    • (1959) J. Exp. Med. , vol.110 , pp. 685-697
    • Beeson, P.B.1    Rowley, D.R.2
  • 19
    • 0015787774 scopus 로고
    • The acute action of ammonia on rat brain metabolism in vivo
    • [19] Hawkins, R.A., Miller, A.L., Nielsen, R.C. & Veech, R.L. (1973), The acute action of ammonia on rat brain metabolism in vivo. Biochem. J., 134, 1001-1008.
    • (1973) Biochem. J. , vol.134 , pp. 1001-1008
    • Hawkins, R.A.1    Miller, A.L.2    Nielsen, R.C.3    Veech, R.L.4
  • 20
    • 0028577668 scopus 로고
    • Molecular mechanism of acute ammonia toxicity and of its prevention by L-carnithine
    • [20] Felipo, V., Kosenko, E., Minana, M.-D., Marcaida, G. & Grisolia, S. (1994), Molecular mechanism of acute ammonia toxicity and of its prevention by L-carnithine. Adv. Exp. Med. Biol., 368, 65-77.
    • (1994) Adv. Exp. Med. Biol. , vol.368 , pp. 65-77
    • Felipo, V.1    Kosenko, E.2    Minana, M.-D.3    Marcaida, G.4    Grisolia, S.5
  • 21
    • 0029023214 scopus 로고
    • Nitroarginine, an inhibitor of nitric oxide synthetase, attenuates ammonia toxicity and ammonia-induced alterations in brain metabolism
    • [21] Kosenko, E., Kaminsky, Y., Grau, E., Minana, M.-D., Grisolia, S. & Felipo, V. (1995), Nitroarginine, an inhibitor of nitric oxide synthetase, attenuates ammonia toxicity and ammonia-induced alterations in brain metabolism. Neurochem. Res., 20, 451-456.
    • (1995) Neurochem. Res. , vol.20 , pp. 451-456
    • Kosenko, E.1    Kaminsky, Y.2    Grau, E.3    Minana, M.-D.4    Grisolia, S.5    Felipo, V.6
  • 22
    • 0021267002 scopus 로고
    • Effects of L-carnithine on urea synthesis following acute ammonia intoxication in mice
    • [22] Costell, M., O'Connor, J.-E., Niguez, M.-P. & Grisolia, S. (1984), Effects of L-carnithine on urea synthesis following acute ammonia intoxication in mice. Biochem. Biophys. Res. Commun., 120, 726-733.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 726-733
    • Costell, M.1    O'Connor, J.-E.2    Niguez, M.-P.3    Grisolia, S.4
  • 24
    • 0021856540 scopus 로고
    • Pathologic concentrations of ammonium ions block L-glutamate uptake
    • [24] Mena, E.E. & Cotman, C.W. (1985), Pathologic concentrations of ammonium ions block L-glutamate uptake. Exp. Neurol. 89, 259-263.
    • (1985) Exp. Neurol. , vol.89 , pp. 259-263
    • Mena, E.E.1    Cotman, C.W.2
  • 25
    • 0032518360 scopus 로고    scopus 로고
    • Roles of neuroactive amino acids in ammonia neurotoxicity
    • [25] Albrecht, J. (1998), Roles of neuroactive amino acids in ammonia neurotoxicity. J. Neurosci. Res., 51, 133-138.
    • (1998) J. Neurosci. Res. , vol.51 , pp. 133-138
    • Albrecht, J.1
  • 26
    • 0021490096 scopus 로고
    • Experimental displacement of intracellular pH and the mechanism of its subsequent recovery
    • [26] Thomas, R.C. (1984), Experimental displacement of intracellular pH and the mechanism of its subsequent recovery. J. Physiol., 354, 3P-22P.
    • (1984) J. Physiol. , vol.354
    • Thomas, R.C.1
  • 27
    • 0025354592 scopus 로고
    • Ionic control of intracellular pH in rat cerebellar Purkinje cells maintained in culture
    • [27] Gaillard, S. & Dupont, J.-L. (1990), Ionic control of intracellular pH in rat cerebellar Purkinje cells maintained in culture. J. Physiol., 425, 71-83.
    • (1990) J. Physiol. , vol.425 , pp. 71-83
    • Gaillard, S.1    Dupont, J.-L.2
  • 29
    • 0002137823 scopus 로고
    • Ecology of denitrification and dissimilatory nitrate reduction to ammonium
    • (A.J.B. Zehnder) Wiley, New York
    • [29] Tiedje, J.M. (1988), Ecology of denitrification and dissimilatory nitrate reduction to ammonium, in "Biology of Anaerobic Microorganisms" (A.J.B. Zehnder) (pp. 179-244). Wiley, New York.
    • (1988) Biology of Anaerobic Microorganisms , pp. 179-244
    • Tiedje, J.M.1
  • 30
    • 0022752857 scopus 로고
    • Uptake and transport of nonprotein nitrogen by the ruminant gut
    • [30] Huntington, G.B. (1986), Uptake and transport of nonprotein nitrogen by the ruminant gut. Fed. Proc., 45, 2272-2276.
    • (1986) Fed. Proc. , vol.45 , pp. 2272-2276
    • Huntington, G.B.1
  • 31
    • 0024514293 scopus 로고
    • Microbial ureases: Significance, regulation, and molecular characterization
    • [31] Mobley, H.L.T.& Hausinger, R.P. (1989), Microbial ureases: significance, regulation, and molecular characterization. Microbiol Rev., 53, 85-108.
    • (1989) Microbiol Rev. , vol.53 , pp. 85-108
    • Mobley, H.L.T.1    Hausinger, R.P.2
  • 32
    • 0026332997 scopus 로고    scopus 로고
    • A multiplicity of potential carbon catabolite repression mechanisms in prokaryotic and eukaryotic microorganisms
    • [32] Saier, M.H. (1998), A multiplicity of potential carbon catabolite repression mechanisms in prokaryotic and eukaryotic microorganisms. New Biol., 3, 1137-1147.
    • (1998) New Biol. , vol.3 , pp. 1137-1147
    • Saier, M.H.1
  • 35
  • 37
    • 8544249125 scopus 로고    scopus 로고
    • Effects of Helicobacter pylori eradication therapy on hyperammonaemia in patients with liver cirrhosis
    • [37] Miyaji, H., Ito, S., Azuma, T., Ito, Y., Yamazaki, Y., Ohtaki, Y., Sato, F., Hirai, M., Kuriyama, M. & Kohli, Y. (1997), Effects of Helicobacter pylori eradication therapy on hyperammonaemia in patients with liver cirrhosis. Gut, 40, 726-730.
    • (1997) Gut , vol.40 , pp. 726-730
    • Miyaji, H.1    Ito, S.2    Azuma, T.3    Ito, Y.4    Yamazaki, Y.5    Ohtaki, Y.6    Sato, F.7    Hirai, M.8    Kuriyama, M.9    Kohli, Y.10
  • 38
    • 0028893301 scopus 로고
    • Proteases and bacterial virulence: A view from the trenches
    • [38] Goguen, J.D., Hoe, N.P. & Subramanyan, Y.V. (1995), Proteases and bacterial virulence: a view from the trenches. Infect Agents Dis., 4, 47-54
    • (1995) Infect Agents Dis. , vol.4 , pp. 47-54
    • Goguen, J.D.1    Hoe, N.P.2    Subramanyan, Y.V.3
  • 39
    • 0028783299 scopus 로고
    • Are bacterial proteinases pathogenic factors?
    • [39] Travis, J., Potempa, J. & Maeda, H. (1995), Are bacterial proteinases pathogenic factors? Trends Microbiol., 3, 405-407.
    • (1995) Trends Microbiol. , vol.3 , pp. 405-407
    • Travis, J.1    Potempa, J.2    Maeda, H.3
  • 40
    • 0029879578 scopus 로고    scopus 로고
    • Pathogenic mechanisms induced by bacterial proteases in microbial infections
    • [40] Maeda, H. & Yamamoto, T. (1996), Pathogenic mechanisms induced by bacterial proteases in microbial infections. Biol. Chem. Hoppe-Seyler, 377, 217-226.
    • (1996) Biol. Chem. Hoppe-Seyler , vol.377 , pp. 217-226
    • Maeda, H.1    Yamamoto, T.2
  • 41
    • 0024828408 scopus 로고
    • Secretion, processing and activation of bacterial extracellular proteases
    • [41] Wandersman, C. (1989), Secretion, processing and activation of bacterial extracellular proteases. Mol. Microbiol., 3, 1825-1831.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1825-1831
    • Wandersman, C.1
  • 42
    • 0030624649 scopus 로고    scopus 로고
    • Are bacterial proteases important virulence factors?
    • [42] Lantz, M.S. (1997), Are bacterial proteases important virulence factors? J. Periodontal Res., 32, 126-132.
    • (1997) J. Periodontal Res. , vol.32 , pp. 126-132
    • Lantz, M.S.1
  • 43
    • 0018772853 scopus 로고
    • Experimental studies of the pathogenesis of infections due to Pseudomonas aeruginosa: Extracellular protease and elastase as in vivo virulence factors
    • [43] Holder, I.A. & Haidaris, C.G. (1979), Experimental studies of the pathogenesis of infections due to Pseudomonas aeruginosa: extracellular protease and elastase as in vivo virulence factors. Can. J. Microbiol., 25, 593-599.
    • (1979) Can. J. Microbiol. , vol.25 , pp. 593-599
    • Holder, I.A.1    Haidaris, C.G.2
  • 45
    • 0027179622 scopus 로고
    • Effect of Pseudomonas aeruginosa elastase, alkaline protease, and exotoxin A on corneal proteinases and proteins
    • [45] Twining, S.S., Kirschner, S.E., Mahnke, L.A. & Frank, D.W. (1993), Effect of Pseudomonas aeruginosa elastase, alkaline protease, and exotoxin A on corneal proteinases and proteins. Invest. Ophthalmol. Visual Sci., 34, 2699-2712.
    • (1993) Invest. Ophthalmol. Visual Sci. , vol.34 , pp. 2699-2712
    • Twining, S.S.1    Kirschner, S.E.2    Mahnke, L.A.3    Frank, D.W.4
  • 46
    • 0021335808 scopus 로고
    • Purifcation and characterization of four proteases from a clinical isolate of Serratia marcescens kums 3958
    • [46] Matsumoto, K., Maeda, H., Takota, K., Kamata, R. & Okamura, R. (1979), Purifcation and characterization of four proteases from a clinical isolate of Serratia marcescens kums 3958. J. Bacteriol., 157, 225-232.
    • (1979) J. Bacteriol. , vol.157 , pp. 225-232
    • Matsumoto, K.1    Maeda, H.2    Takota, K.3    Kamata, R.4    Okamura, R.5
  • 47
    • 0020051553 scopus 로고
    • Contribution of toxin A and elastase to virulence of Pseudomonas aeruginosa in chronic lung infecctions of rats
    • [47] Woods, D.E., Cryz, S.J., Friedman, R.L. & Iglewski, B.H. (1982), Contribution of toxin A and elastase to virulence of Pseudomonas aeruginosa in chronic lung infecctions of rats. Infect Immun., 36, 1223-1228.
    • (1982) Infect Immun. , vol.36 , pp. 1223-1228
    • Woods, D.E.1    Cryz, S.J.2    Friedman, R.L.3    Iglewski, B.H.4
  • 48
    • 0022619947 scopus 로고
    • Role of Pseudomonas aeruginosa extracellular enzymes in lung disease
    • [48] Woods, D.E. & Sokol, P.A. (1986), Role of Pseudomonas aeruginosa extracellular enzymes in lung disease. Clin Invest Med., 9, 108-112.
    • (1986) Clin Invest Med. , vol.9 , pp. 108-112
    • Woods, D.E.1    Sokol, P.A.2
  • 49
    • 0028832828 scopus 로고
    • Aminoacid utilization by Helicobacter pylori
    • [49] Mendz, G.L. & Hazell, S.L. (1995), Aminoacid utilization by Helicobacter pylori. Int. J. Biochem. Cell Biol., 27, 1085-1093.
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 1085-1093
    • Mendz, G.L.1    Hazell, S.L.2
  • 50
    • 0030928060 scopus 로고    scopus 로고
    • Amino acid utilization and deamination of glutamine and asparagine by Helicobacter pylori
    • [50] Stark, R.M., Suleiman, M.-S., Hassan, I.J., Greenman, J. & Millar, M.R. (1997), Amino acid utilization and deamination of glutamine and asparagine by Helicobacter pylori. J. Med. Microbiol., 46, 793-800.
    • (1997) J. Med. Microbiol. , vol.46 , pp. 793-800
    • Stark, R.M.1    Suleiman, M.-S.2    Hassan, I.J.3    Greenman, J.4    Millar, M.R.5
  • 52
    • 0015083679 scopus 로고
    • The amino acid-fermenting clostridia
    • [52] Mead, G.C. (1971), The amino acid-fermenting clostridia. J. Gen. Microbiol., 67, 47-56.
    • (1971) J. Gen. Microbiol. , vol.67 , pp. 47-56
    • Mead, G.C.1
  • 53
    • 0019363132 scopus 로고
    • Amno acid degradation by anaerobic bacteria
    • [53] Barker, H.A. (1981), Amno acid degradation by anaerobic bacteria. Annu. Rev. Biochem., 50, 23-40.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 23-40
    • Barker, H.A.1
  • 54
    • 0001502558 scopus 로고
    • The chemical reactions by which C. sporogenes obtains its energy
    • [54] Stickland, L.H. (1934), The chemical reactions by which C. sporogenes obtains its energy. Biochem. J., 28, 1746-1759.
    • (1934) Biochem. J. , vol.28 , pp. 1746-1759
    • Stickland, L.H.1
  • 55
    • 0000430962 scopus 로고
    • The Genus Klebsiella
    • (A. Balows, H.G. Trüper, M. Dworkin, W. Harder, and K.-H. Schleifer) Springer-Verlag, Berlin
    • [55] Grimont, F., Grimont, P.A.D. & Richard, C. (1992), The Genus Klebsiella, in "The Prokaryotes". (A. Balows, H.G. Trüper, M. Dworkin, W. Harder, and K.-H. Schleifer) (pp. 2775-2796). Springer-Verlag, Berlin.
    • (1992) The Prokaryotes , pp. 2775-2796
    • Grimont, F.1    Grimont, P.A.D.2    Richard, C.3
  • 56
    • 0001103158 scopus 로고
    • Genus V. Klebsiella Trevisan 1885
    • (N.R. Krieg and J.G. Holt) William and Wilkins, Baltimore
    • [56] Oerskov, I. (1984), Genus V. Klebsiella Trevisan 1885, in "Bergey's Manual of Systematic Bacteriology" (N.R. Krieg and J.G. Holt) (pp. 461-465). William and Wilkins, Baltimore.
    • (1984) Bergey's Manual of Systematic Bacteriology , pp. 461-465
    • Oerskov, I.1
  • 57
    • 0025615326 scopus 로고
    • The pathogenicity of Klebsiella pneumoniae
    • [57] Williams, P. & Tomas, J.M. (1990), The pathogenicity of Klebsiella pneumoniae. Rev. Med. Microbiol., 1, 196-204.
    • (1990) Rev. Med. Microbiol. , vol.1 , pp. 196-204
    • Williams, P.1    Tomas, J.M.2
  • 58
    • 0030762116 scopus 로고    scopus 로고
    • Clinical, bacteriological, and serological aspects of klebsiella infections and their spondylarthropathic sequelae
    • [58] Sahly, H. & Podschun, R. (1997), Clinical, bacteriological, and serological aspects of Klebsiella infections and their spondylarthropathic sequelae. Clin. Diagn. Lab. Immunol., 4, 393-399.
    • (1997) Clin. Diagn. Lab. Immunol. , vol.4 , pp. 393-399
    • Sahly, H.1    Podschun, R.2
  • 60
    • 0000453937 scopus 로고
    • Nitrogen fixation by members of the tribe Klebsiellae
    • [60] Mahl, M.C., Wilson, P.W., Fife, M.A. & Ewing, W.H. (1965), Nitrogen fixation by members of the tribe Klebsiellae. J. Bacteriol., 89, 1482-1487
    • (1965) J. Bacteriol. , vol.89 , pp. 1482-1487
    • Mahl, M.C.1    Wilson, P.W.2    Fife, M.A.3    Ewing, W.H.4
  • 61
    • 0021796811 scopus 로고
    • Bacterial ammonium transport
    • [61] Kleiner, D. (1985), Bacterial ammonium transport. FEMS Microbiol Rev., 32, 87-100
    • (1985) FEMS Microbiol Rev. , vol.32 , pp. 87-100
    • Kleiner, D.1
  • 62
    • 0017519549 scopus 로고
    • Urease of Klebsiella aerogenes: Control of its synthesis by glutamine synthetase
    • [62] Friedrich, B. & Magasanik, B. (1978), Urease of Klebsiella aerogenes: control of its synthesis by glutamine synthetase. J. Bacteriol., 131, 446-452.
    • (1978) J. Bacteriol. , vol.131 , pp. 446-452
    • Friedrich, B.1    Magasanik, B.2
  • 63
    • 0024308526 scopus 로고
    • Regulation of gene expression and cellular localization of cloned Klebsiella aerogenes (K. Pneumoniae) Urease
    • [63] Mulrooney, S.B., Pankratz, H.S. & Hausinger, R.P. (1989), Regulation of Gene Expression and Cellular Localization of Cloned Klebsiella aerogenes (K. pneumoniae) Urease. J. Gen. Microbiol., 135, 1769-1776
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 1769-1776
    • Mulrooney, S.B.1    Pankratz, H.S.2    Hausinger, R.P.3
  • 64
    • 0016708534 scopus 로고
    • Klebsiella pneumoniae and staphylococcus aureus infection in mice: Difference in uremia and ammoniagenesis
    • [64] Walker, R.I. & Chesbro, W. (1975), Klebsiella pneumoniae and Staphylococcus aureus infection in mice: difference in uremia and ammoniagenesis. Infect. Immun., 12, 571-575.
    • (1975) Infect. Immun. , vol.12 , pp. 571-575
    • Walker, R.I.1    Chesbro, W.2
  • 65
    • 0017238988 scopus 로고
    • Urease: The primary cause of infection-induced urinary stones
    • [65] Griffith, D.P., Musher, D.M. & 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
  • 67
    • 0018630445 scopus 로고
    • Zur Differenzierung von Klebsiella pneumoniae variatio "oxytoca"
    • [67] Lütticken, R., Korth, H. & Pulverer, G. (1979), Zur Differenzierung von Klebsiella pneumoniae variatio "oxytoca". Zbl. Bakt. Hyg., 244, 470-473.
    • (1979) Zbl. Bakt. Hyg. , vol.244 , pp. 470-473
    • Lütticken, R.1    Korth, H.2    Pulverer, G.3
  • 68
    • 0020601633 scopus 로고
    • A plasmid-linked caseinolytic activity in enterobacteriaceae
    • [68] Mignatti, P., Pagani, L. & Romero, E. (1983), A plasmid-linked caseinolytic activity in Enterobacteriaceae. Microbiologica, 6, 229-237.
    • (1983) Microbiologica , vol.6 , pp. 229-237
    • Mignatti, P.1    Pagani, L.2    Romero, E.3
  • 69
    • 0023885535 scopus 로고
    • Bacterial lysis of fibrin seal in vitro
    • [69] Hoffmann, S. & Moesgaard, F. (1988), Bacterial lysis of fibrin seal in vitro. Eur. Surg. Res., 20, 75-81.
    • (1988) Eur. Surg. Res. , vol.20 , pp. 75-81
    • Hoffmann, S.1    Moesgaard, F.2
  • 70
    • 0019973342 scopus 로고
    • Lobar pneumonia in rats produced by clinical isolates of klebsiella pneumoniae
    • [70] Domenico, P., Johanson, W.G. & Straus, D.C. (1982), Lobar pneumonia in rats produced by clinical isolates of Klebsiella pneumoniae. Infect Immun., 37, 327-335.
    • (1982) Infect Immun. , vol.37 , pp. 327-335
    • Domenico, P.1    Johanson, W.G.2    Straus, D.C.3
  • 71
    • 0026750046 scopus 로고
    • A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene
    • [71] Sugino, H., Sasaki, M., Azakami, H., Yamashita, M. & Murooka, Y. (1992), A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene. J. Bacteriol., 174, 2485-2492.
    • (1992) J. Bacteriol. , vol.174 , pp. 2485-2492
    • Sugino, H.1    Sasaki, M.2    Azakami, H.3    Yamashita, M.4    Murooka, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.