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Volumn 4, Issue 12, 2008, Pages

Resistance to mucosal lysozyme compensates for the fitness deficit of peptidoglycan modifications by Streptococcus pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ENZYME; LYSOZYME; N ACETYLGLUCOSAMINE; PEPTIDOGLYCAN; AMIDASE; BACTERIAL PROTEIN; LYSOZYME M, MOUSE; PGDA PROTEIN, STREPTOCOCCUS PNEUMONIAE;

EID: 58149240262     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1000241     Document Type: Article
Times cited : (87)

References (47)
  • 1
    • 0037114149 scopus 로고    scopus 로고
    • Cationic polypeptides are required for antibacterial activity of human airway fluid
    • Cole A, Liao H, Stuchlik O, Tilan J, Pohl J, et al. (2002) Cationic polypeptides are required for antibacterial activity of human airway fluid. J Immunol 169: 6985-6991.
    • (2002) J Immunol , vol.169 , pp. 6985-6991
    • Cole, A.1    Liao, H.2    Stuchlik, O.3    Tilan, J.4    Pohl, J.5
  • 2
    • 0015104633 scopus 로고
    • Distribution of lysosomal enzymes, cationic proteins, and bactericidal substances in subcellular fractions of human polymorphonuclear leukocytes
    • Welsh I, Spitznagel J (1971) Distribution of lysosomal enzymes, cationic proteins, and bactericidal substances in subcellular fractions of human polymorphonuclear leukocytes. Infect Immun 4: 97-102.
    • (1971) Infect Immun , vol.4 , pp. 97-102
    • Welsh, I.1    Spitznagel, J.2
  • 3
    • 0442297898 scopus 로고    scopus 로고
    • Mouse lysozyme M is important in pulmonary host defense against Klebsiella pneumoniae infection
    • Markart P, Korfhagen T, Weaver T, Akinbi H (2004) Mouse lysozyme M is important in pulmonary host defense against Klebsiella pneumoniae infection. Am J Respir Crit Care Med 169: 454-458.
    • (2004) Am J Respir Crit Care Med , vol.169 , pp. 454-458
    • Markart, P.1    Korfhagen, T.2    Weaver, T.3    Akinbi, H.4
  • 4
    • 0023260229 scopus 로고
    • Ultrastructural localization of lysozyme in human neutrophils by immunogold
    • Cramer E, Breton-Gorius J (1987) Ultrastructural localization of lysozyme in human neutrophils by immunogold. J Leukoc Biol 41: 242-247.
    • (1987) J Leukoc Biol , vol.41 , pp. 242-247
    • Cramer, E.1    Breton-Gorius, J.2
  • 5
    • 0035964823 scopus 로고    scopus 로고
    • Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function
    • Ibrahim H, Matsuzaki T, Aoki T (2001) Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function. FEBS Lett 506: 27-32.
    • (2001) FEBS Lett , vol.506 , pp. 27-32
    • Ibrahim, H.1    Matsuzaki, T.2    Aoki, T.3
  • 6
    • 33745303470 scopus 로고    scopus 로고
    • The peptidoglycan-degrading property of lysozyme is not required for bactercidal activity in vivo
    • Nash J, Ballard T, Weaver T, Akinbi H (2006) The peptidoglycan-degrading property of lysozyme is not required for bactercidal activity in vivo. J Immunol 177: 519-526.
    • (2006) J Immunol , vol.177 , pp. 519-526
    • Nash, J.1    Ballard, T.2    Weaver, T.3    Akinbi, H.4
  • 7
    • 0035941271 scopus 로고    scopus 로고
    • A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action
    • Ibrahim H, Thomas U, Pellegrini A (2001) A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. J Biol Chem 276: 43767-43774.
    • (2001) J Biol Chem , vol.276 , pp. 43767-43774
    • Ibrahim, H.1    Thomas, U.2    Pellegrini, A.3
  • 8
    • 0034669924 scopus 로고    scopus 로고
    • Bacterial killing is enhanced by expression of lysozyme in the lungs of transgenic mice
    • Akinbi H, Epaud R, Bhatt H, Weaver T (2000) Bacterial killing is enhanced by expression of lysozyme in the lungs of transgenic mice. J Immunol 165: 5760-5766.
    • (2000) J Immunol , vol.165 , pp. 5760-5766
    • Akinbi, H.1    Epaud, R.2    Bhatt, H.3    Weaver, T.4
  • 9
    • 27644434474 scopus 로고    scopus 로고
    • Decreased clearance of Pseudomonas aeruginosa from airways of mice deficient in lysozyme M
    • Cole A, Thapa D, Gabayan V, Liao H, Liu L, et al. (2005) Decreased clearance of Pseudomonas aeruginosa from airways of mice deficient in lysozyme M. J Leukoc Biol 78: 1081-1085.
    • (2005) J Leukoc Biol , vol.78 , pp. 1081-1085
    • Cole, A.1    Thapa, D.2    Gabayan, V.3    Liao, H.4    Liu, L.5
  • 10
    • 0034617218 scopus 로고    scopus 로고
    • The pgdA gene encodes for a peptidoglycan N-acetylglucosamine deacetylase in Streptococcus pneumoniae
    • Vollmer W, Tomasz A (2000) The pgdA gene encodes for a peptidoglycan N-acetylglucosamine deacetylase in Streptococcus pneumoniae. J Biol Chem 275: 20496-20501.
    • (2000) J Biol Chem , vol.275 , pp. 20496-20501
    • Vollmer, W.1    Tomasz, A.2
  • 11
    • 12844275936 scopus 로고    scopus 로고
    • Identification of the namH gene, encoding the hydroxylase responsible for the N-glycolylation of the mycobacterial peptidoglycan
    • Raymond J, Mahapatra S, Crick D, Pavelka M Jr (2005) Identification of the namH gene, encoding the hydroxylase responsible for the N-glycolylation of the mycobacterial peptidoglycan. J Biol Chem 280: 326-333.
    • (2005) J Biol Chem , vol.280 , pp. 326-333
    • Raymond, J.1    Mahapatra, S.2    Crick, D.3    Pavelka Jr, M.4
  • 12
    • 24744461366 scopus 로고    scopus 로고
    • Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis
    • Psylinakis E, Boneca I, Mavromatis K, Deli A, Hayhurst E, et al. (2005) Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis. J Biol Chem 280: 30856-30863.
    • (2005) J Biol Chem , vol.280 , pp. 30856-30863
    • Psylinakis, E.1    Boneca, I.2    Mavromatis, K.3    Deli, A.4    Hayhurst, E.5
  • 13
    • 34547629994 scopus 로고    scopus 로고
    • Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci
    • doi:10.1371/journal.ppat. 0030102
    • Herbert S, Bera A, Nerz C, Kraus D, Peschel A, et al. (2007) Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci. PLoS Pathog 3: e102. doi:10.1371/journal.ppat. 0030102.
    • (2007) PLoS Pathog , vol.3
    • Herbert, S.1    Bera, A.2    Nerz, C.3    Kraus, D.4    Peschel, A.5
  • 14
    • 35648939765 scopus 로고    scopus 로고
    • Enterococcus faecalis constitutes an unusual bacterial model in lysozyme resistance
    • Hébert L, Courtin P, Torelli R, Sanguinetti M, Chapot-Chartier M, et al. (2007) Enterococcus faecalis constitutes an unusual bacterial model in lysozyme resistance. Infect Immun 75: 5390-5398.
    • (2007) Infect Immun , vol.75 , pp. 5390-5398
    • Hébert, L.1    Courtin, P.2    Torelli, R.3    Sanguinetti, M.4    Chapot-Chartier, M.5
  • 15
    • 14544285468 scopus 로고    scopus 로고
    • A polysacchride deacetylase homologue, PdaA in Bacillus subtilis acts as an N-acetylmuramic acid deacetylase in vitro
    • Fukushima T, Kitajima T, Sekiguchi J (2005) A polysacchride deacetylase homologue, PdaA in Bacillus subtilis acts as an N-acetylmuramic acid deacetylase in vitro. J Bacteriol 187: 1287-1292.
    • (2005) J Bacteriol , vol.187 , pp. 1287-1292
    • Fukushima, T.1    Kitajima, T.2    Sekiguchi, J.3
  • 16
    • 33846526208 scopus 로고    scopus 로고
    • A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune system
    • Boneca I, Dussurget O, Cabanes D, Nahori M, Sousa S, et al. (2007) A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune system. Proc Natl Acad Sci 104: 997-1002.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 997-1002
    • Boneca, I.1    Dussurget, O.2    Cabanes, D.3    Nahori, M.4    Sousa, S.5
  • 17
    • 0019127047 scopus 로고
    • The peptidoglycan of Neisseria gonorrhoeae: O-acetyl groups and lysozyme sensitivity
    • Blundell J, Smith G, Perkins H (1980) The peptidoglycan of Neisseria gonorrhoeae: O-acetyl groups and lysozyme sensitivity. FEMS Microbiol Lett 9: 259-261.
    • (1980) FEMS Microbiol Lett , vol.9 , pp. 259-261
    • Blundell, J.1    Smith, G.2    Perkins, H.3
  • 18
    • 13444282403 scopus 로고    scopus 로고
    • Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus
    • Bera A, Herbert S, Jakob A, Vollmer W, Götz F (2005) Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Mol Microbiol 55: 778-787.
    • (2005) Mol Microbiol , vol.55 , pp. 778-787
    • Bera, A.1    Herbert, S.2    Jakob, A.3    Vollmer, W.4    Götz, F.5
  • 19
    • 33845941753 scopus 로고    scopus 로고
    • Influence of wall teichoic acid on lysozyme resistance in Staphylococcus aureus
    • Bera A, Biswas R, Herbert S, Kulauzovic E, Weidenmaier C, et al. (2007) Influence of wall teichoic acid on lysozyme resistance in Staphylococcus aureus. J Bacteriol 189: 280-283.
    • (2007) J Bacteriol , vol.189 , pp. 280-283
    • Bera, A.1    Biswas, R.2    Herbert, S.3    Kulauzovic, E.4    Weidenmaier, C.5
  • 20
    • 0025083176 scopus 로고
    • Covalent linkage between the capsular polysaccharide and the cell wall peptidoglycan of Streptococcus pneumoniae revealed by immunochemical methods
    • Sørensen U, Henrichsen J, Chen H, Szu S (1990) Covalent linkage between the capsular polysaccharide and the cell wall peptidoglycan of Streptococcus pneumoniae revealed by immunochemical methods. Microb Pathog 8: 325-334.
    • (1990) Microb Pathog , vol.8 , pp. 325-334
    • Sørensen, U.1    Henrichsen, J.2    Chen, H.3    Szu, S.4
  • 21
    • 33748494268 scopus 로고    scopus 로고
    • Attenuation of penicillin resistance in a peptidoglycan O-acetyl transferase mutant of Streptococcus pneumoniae
    • Crisóstomo M, Vollmer W, Kharat A, Inhülsen S, Gehre F, et al. (2006) Attenuation of penicillin resistance in a peptidoglycan O-acetyl transferase mutant of Streptococcus pneumoniae. Mol Microbiol 61: 1497-1509.
    • (2006) Mol Microbiol , vol.61 , pp. 1497-1509
    • Crisóstomo, M.1    Vollmer, W.2    Kharat, A.3    Inhülsen, S.4    Gehre, F.5
  • 22
    • 0036892246 scopus 로고    scopus 로고
    • Peptidoglycan N-acetylglucosamine deacetylase, a putative virulence factor in Streptococcus pneumoniae
    • Vollmer W, Tomasz A (2002) Peptidoglycan N-acetylglucosamine deacetylase, a putative virulence factor in Streptococcus pneumoniae. Infect Immun 70: 7176-7178.
    • (2002) Infect Immun , vol.70 , pp. 7176-7178
    • Vollmer, W.1    Tomasz, A.2
  • 23
    • 0009785235 scopus 로고
    • Mouse lysozyme M gene: Isolation, characterization, and expression studies
    • Cross M, Mangelsdorf I, Wedel A, Renkawitz R (1988) Mouse lysozyme M gene: Isolation, characterization, and expression studies. Proc Natl Acad Sci 85: 6232-6236.
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 6232-6236
    • Cross, M.1    Mangelsdorf, I.2    Wedel, A.3    Renkawitz, R.4
  • 24
    • 0031906480 scopus 로고    scopus 로고
    • Association of intrastrain phase variation in quantity of capsular polysaccharide and teichoic acid with the virulence of Streptococcus pneumoniae
    • Kim J, Weiser J (1998) Association of intrastrain phase variation in quantity of capsular polysaccharide and teichoic acid with the virulence of Streptococcus pneumoniae. J Infect Dis 177: 368-377.
    • (1998) J Infect Dis , vol.177 , pp. 368-377
    • Kim, J.1    Weiser, J.2
  • 25
    • 0035016182 scopus 로고    scopus 로고
    • Requirement for capsule in colonization by Streptococcus pneumoniae
    • Magee A, Yother J (2001) Requirement for capsule in colonization by Streptococcus pneumoniae. Infect Immun 69: 3755-3761.
    • (2001) Infect Immun , vol.69 , pp. 3755-3761
    • Magee, A.1    Yother, J.2
  • 26
    • 33846015873 scopus 로고    scopus 로고
    • Capsule enhances pneumococcal colonization by limiting mucus-mediated clearance
    • Nelson A, Roche A, Gould J, Chim K, Ratner A, et al. (2007) Capsule enhances pneumococcal colonization by limiting mucus-mediated clearance. Infect Immun 75: 83-90.
    • (2007) Infect Immun , vol.75 , pp. 83-90
    • Nelson, A.1    Roche, A.2    Gould, J.3    Chim, K.4    Ratner, A.5
  • 27
    • 33748670479 scopus 로고    scopus 로고
    • A function dlt operon, encoding proteins required for incorporation of D-alanine in teichoic acids in Gram-positive bacteria, confers resistance to cationic antimicrobial peptides in Streptococcus pneumoniae
    • Kovács M, Halfmann A, Fedtke I, Heintz M, Peschel A, et al. (2006) A function dlt operon, encoding proteins required for incorporation of D-alanine in teichoic acids in Gram-positive bacteria, confers resistance to cationic antimicrobial peptides in Streptococcus pneumoniae. J Bacteriol 188: 5797-5805.
    • (2006) J Bacteriol , vol.188 , pp. 5797-5805
    • Kovács, M.1    Halfmann, A.2    Fedtke, I.3    Heintz, M.4    Peschel, A.5
  • 28
    • 0025194489 scopus 로고
    • 1H NMR studies of human lysozyme: Spectral assignment and comparison with hen lysozyme
    • Redfield C, Dobson C (1990) 1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme. Biochemistry 29: 7201-7214.
    • (1990) Biochemistry , vol.29 , pp. 7201-7214
    • Redfield, C.1    Dobson, C.2
  • 29
    • 0024403169 scopus 로고
    • The human lysozyme gene. Sequence organization and chromosomal localization
    • Peters C, Kruse U, Pollwein R, Grzeschik K, Sippel A (1989) The human lysozyme gene. Sequence organization and chromosomal localization. Eur J Biochem 182: 507-516.
    • (1989) Eur J Biochem , vol.182 , pp. 507-516
    • Peters, C.1    Kruse, U.2    Pollwein, R.3    Grzeschik, K.4    Sippel, A.5
  • 30
    • 0019143031 scopus 로고
    • Exons encode functional and structural units of chicken lysozyme
    • Jung A, Sippel A, Grez M, Schütz G (1980) Exons encode functional and structural units of chicken lysozyme. Proc Natl Acad Sci 77: 5759-5763.
    • (1980) Proc Natl Acad Sci , vol.77 , pp. 5759-5763
    • Jung, A.1    Sippel, A.2    Grez, M.3    Schütz, G.4
  • 31
    • 39149102149 scopus 로고    scopus 로고
    • Structural variation in the glycan strands of bacterial peptidoglycan
    • Vollmer W (2008) Structural variation in the glycan strands of bacterial peptidoglycan. FEMS Microbiol Rev 32: 287-306.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 287-306
    • Vollmer, W.1
  • 32
    • 0021256398 scopus 로고
    • Glucosamine substitution and muramidase susceptibility in Bacillus anthracis
    • Zipperle G Jr, Ezzell J Jr, Doyle R (1984) Glucosamine substitution and muramidase susceptibility in Bacillus anthracis. Can J Microbiol 30: 553-559.
    • (1984) Can J Microbiol , vol.30 , pp. 553-559
    • Zipperle Jr, G.1    Ezzell Jr, J.2    Doyle, R.3
  • 33
    • 31044439427 scopus 로고    scopus 로고
    • Identification and characterization of O-acetylpeptidoglycan esterase: A novel enzyme discovered in Neisseria gonorrhoeae
    • Weadge J, Clarke A (2006) Identification and characterization of O-acetylpeptidoglycan esterase: a novel enzyme discovered in Neisseria gonorrhoeae. Biochemistry 45: 839-851.
    • (2006) Biochemistry , vol.45 , pp. 839-851
    • Weadge, J.1    Clarke, A.2
  • 34
    • 0016730533 scopus 로고
    • Lysis of modified walls from Lactobacillus fermentum
    • Logardt I, Neujahr H (1975) Lysis of modified walls from Lactobacillus fermentum. J Bacteriol 124: 73-77.
    • (1975) J Bacteriol , vol.124 , pp. 73-77
    • Logardt, I.1    Neujahr, H.2
  • 35
    • 0015212189 scopus 로고
    • Enzymatic deacetylation of N-acetylglucosamine residues in peptidoglycan from Bacillus cereus cell walls
    • Araki Y, Fukuoka S, Oba S, Ito E (1971) Enzymatic deacetylation of N-acetylglucosamine residues in peptidoglycan from Bacillus cereus cell walls. Biochem Biophys Res Commun 45: 751-758.
    • (1971) Biochem Biophys Res Commun , vol.45 , pp. 751-758
    • Araki, Y.1    Fukuoka, S.2    Oba, S.3    Ito, E.4
  • 36
    • 0037458665 scopus 로고    scopus 로고
    • Host recognition of bacterial muramyl dipeptide mediated through Nod2: Implications for crohn's disease
    • Inohara N, Ogura Y, Fontalba A, Gutierrez O, Pons F, et al. (2003) Host recognition of bacterial muramyl dipeptide mediated through Nod2: Implications for crohn's disease. J Biol Chem 278: 5509-5512.
    • (2003) J Biol Chem , vol.278 , pp. 5509-5512
    • Inohara, N.1    Ogura, Y.2    Fontalba, A.3    Gutierrez, O.4    Pons, F.5
  • 37
    • 0012722659 scopus 로고    scopus 로고
    • Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection
    • Girardin S, Boneca I, Viala J, Chamaillard M, Labigne A, et al. (2003) Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J Biol Chem 278: 8869-8872.
    • (2003) J Biol Chem , vol.278 , pp. 8869-8872
    • Girardin, S.1    Boneca, I.2    Viala, J.3    Chamaillard, M.4    Labigne, A.5
  • 38
    • 0038615855 scopus 로고    scopus 로고
    • Nod1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan
    • Girardin S, Boneca I, Carneiro L, Antignac A, Jéhanno M, et al. (2003) Nod1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan. Science 300: 1584-1587.
    • (2003) Science , vol.300 , pp. 1584-1587
    • Girardin, S.1    Boneca, I.2    Carneiro, L.3    Antignac, A.4    Jéhanno, M.5
  • 39
    • 0038824980 scopus 로고    scopus 로고
    • An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid
    • Chamaillard M, Hashimoto M, Horie Y, Masumoto J, Qiu S, et al. (2003) An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid. Nat Immunol 4: 702-707.
    • (2003) Nat Immunol , vol.4 , pp. 702-707
    • Chamaillard, M.1    Hashimoto, M.2    Horie, Y.3    Masumoto, J.4    Qiu, S.5
  • 40
    • 0035919670 scopus 로고    scopus 로고
    • Complete genome sequence of a virulent isolate of Streptococcus pneumoniae
    • Tettelin H, Nelson K, Paulsen I, Eisen J, Read T, et al. (2001) Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science 293: 498-506.
    • (2001) Science , vol.293 , pp. 498-506
    • Tettelin, H.1    Nelson, K.2    Paulsen, I.3    Eisen, J.4    Read, T.5
  • 41
    • 0035512266 scopus 로고    scopus 로고
    • An rpsL cassette, janus, for gene replacement through negative selection in Streptococcus pneumoniae
    • Sung C, Li H, Claverys J, Morrison D (2001) An rpsL cassette, janus, for gene replacement through negative selection in Streptococcus pneumoniae. Appl Environ Microbiol 67: 5190-5196.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 5190-5196
    • Sung, C.1    Li, H.2    Claverys, J.3    Morrison, D.4
  • 42
    • 0028800518 scopus 로고
    • Isolation and characterization of kinC, a gene that encodes a sensor kinase homologous to the sporulation sensor kinase KinA and KinB in Bacillus subtilis
    • LeDeaux J, Grossman A (1995) Isolation and characterization of kinC, a gene that encodes a sensor kinase homologous to the sporulation sensor kinase KinA and KinB in Bacillus subtilis. J Bacteriol 177: 166-175.
    • (1995) J Bacteriol , vol.177 , pp. 166-175
    • LeDeaux, J.1    Grossman, A.2
  • 43
    • 0036334551 scopus 로고    scopus 로고
    • Short-sequence tandem and nontandem DNA repeats and endogenous hydrogen peroxide production contribute to genetic instability of Streptococcus pneumoniae
    • Pericone C, Bae D, Shchepetov M, McCool T, Weiser J (2002) Short-sequence tandem and nontandem DNA repeats and endogenous hydrogen peroxide production contribute to genetic instability of Streptococcus pneumoniae. J Bacteriol 184: 4392-4399.
    • (2002) J Bacteriol , vol.184 , pp. 4392-4399
    • Pericone, C.1    Bae, D.2    Shchepetov, M.3    McCool, T.4    Weiser, J.5
  • 44
    • 0034662159 scopus 로고    scopus 로고
    • Insertion of enhanced green fluorescent protein into the lysozyme gene creates mice with green fluorescent granulocytes and macrophages
    • Faust N, Varas F, Kelly L, Heck S, Graf T (2000) Insertion of enhanced green fluorescent protein into the lysozyme gene creates mice with green fluorescent granulocytes and macrophages. Blood 96: 719-726.
    • (2000) Blood , vol.96 , pp. 719-726
    • Faust, N.1    Varas, F.2    Kelly, L.3    Heck, S.4    Graf, T.5
  • 45
    • 0026072892 scopus 로고
    • Characterization and regulation of RB6-8C5 antigen expression on murine bone marrow cells
    • Hestdal K, Ruscetti F, Ihle J, Jacobsen S, Dubois C, et al. (1991) Characterization and regulation of RB6-8C5 antigen expression on murine bone marrow cells. J Immunol 147: 22-28.
    • (1991) J Immunol , vol.147 , pp. 22-28
    • Hestdal, K.1    Ruscetti, F.2    Ihle, J.3    Jacobsen, S.4    Dubois, C.5
  • 46
    • 1642525905 scopus 로고    scopus 로고
    • Deceptive multilineage reconstitution analysis of mice transplanted with hemopoietic stem cells, and implications for assessment of stem cell numbers and lineage potentials
    • Bryder D, Sasaki Y, Borge O, Jacobsen S (2004) Deceptive multilineage reconstitution analysis of mice transplanted with hemopoietic stem cells, and implications for assessment of stem cell numbers and lineage potentials. J Immunol 172: 1548-1552.
    • (2004) J Immunol , vol.172 , pp. 1548-1552
    • Bryder, D.1    Sasaki, Y.2    Borge, O.3    Jacobsen, S.4
  • 47
    • 77951051419 scopus 로고    scopus 로고
    • The role of innate immune responses in the outcome of interspecies competition for colonization of mucosal surfaces
    • doi:10.1371/journal.ppat.0010001
    • Lysenko E, Ratner A, Nelson A, Weiser J (2005) The role of innate immune responses in the outcome of interspecies competition for colonization of mucosal surfaces. PLoS Pathog 1: e1. doi:10.1371/journal.ppat.0010001.
    • (2005) PLoS Pathog , vol.1
    • Lysenko, E.1    Ratner, A.2    Nelson, A.3    Weiser, J.4


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