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Volumn 187, Issue 9, 2005, Pages 2974-2982

Why does Escherichia coli grow more slowly on glucosamine than on N-acetylglucosamine? Effects of enzyme levels and allosteric activation of GlcN6P deaminase (NagB) on growth rates

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSAMINE; N ACETYLGLUCOSAMINE; N ACETYLGLUCOSAMINE 6 PHOSPHATE DEAMINASE; UNCLASSIFIED DRUG;

EID: 17644396319     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.9.2974-2982.2005     Document Type: Article
Times cited : (59)

References (44)
  • 1
    • 0029046064 scopus 로고
    • Asymmetric allosteric activation of Escherichia coli glucosamine-6- phosphate deaminase produced by replacements of Tyr121
    • Altamirano, A. A., J. A. Plumbridge, E. Horjales, and M. L. Calcagno. 1995. Asymmetric allosteric activation of Escherichia coli glucosamine-6- phosphate deaminase produced by replacements of Tyr121. Biochemistry 34: 6074-6082.
    • (1995) Biochemistry , vol.34 , pp. 6074-6082
    • Altamirano, A.A.1    Plumbridge, J.A.2    Horjales, E.3    Calcagno, M.L.4
  • 2
    • 0028295442 scopus 로고
    • Spectrochemical evidence for the presence of a tyrosine residue in the allosteric site of glucosamine-6-phosphate deaminase from Escherichia coli
    • Altamirano, M. M., A. Hernandez-Arana, S. Tello-Solis, and M. L. Calcagno. 1994. Spectrochemical evidence for the presence of a tyrosine residue in the allosteric site of glucosamine-6-phosphate deaminase from Escherichia coli. Eur. J. Biochem. 220:409-413.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 409-413
    • Altamirano, M.M.1    Hernandez-Arana, A.2    Tello-Solis, S.3    Calcagno, M.L.4
  • 3
    • 0035026055 scopus 로고    scopus 로고
    • Twofold reduction of phosphofructokinase activity in Lactococcus lactis results in strong decreases in growth rate and in glycolytic flux
    • Andersen, H., C. Solem, K. Hammer, and P. Jensen. 2001. Twofold reduction of phosphofructokinase activity in Lactococcus lactis results in strong decreases in growth rate and in glycolytic flux. J. Bacteriol. 183:3458-3467.
    • (2001) J. Bacteriol. , vol.183 , pp. 3458-3467
    • Andersen, H.1    Solem, C.2    Hammer, K.3    Jensen, P.4
  • 4
    • 0014734279 scopus 로고
    • Amino sugar sensitivity in Escherichia coli mutants unable to grow on N-acetylglucosamine
    • Bernheim, N. J., and W. J. Dobrogosz. 1970. Amino sugar sensitivity in Escherichia coli mutants unable to grow on N-acetylglucosamine. J. Bacteriol. 101:384-391.
    • (1970) J. Bacteriol. , vol.101 , pp. 384-391
    • Bernheim, N.J.1    Dobrogosz, W.J.2
  • 5
    • 13444267354 scopus 로고    scopus 로고
    • Evidence for two different mechanisms triggering the change in quaternary structure of the allosteric enzyme, glucosamine-6-phosphate deaminase
    • Bustos-Jaimes, I., M. Ramirez-Costa, L. D. Anda-Aguilar, P. Hinjosa-Ocan̄a, and M. Calcagno. 2005. Evidence for two different mechanisms triggering the change in quaternary structure of the allosteric enzyme, glucosamine-6-phosphate deaminase. Biochemistry 44:1127-1135.
    • (2005) Biochemistry , vol.44 , pp. 1127-1135
    • Bustos-Jaimes, I.1    Ramirez-Costa, M.2    Anda-Aguilar, L.D.3    Hinjosa-Ocana, P.4    Calcagno, M.5
  • 6
    • 0036301014 scopus 로고    scopus 로고
    • On the role of the conformational flexibility of the active site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase
    • Bustos-Jaimes, I., A. Sosa-Peinado, E. Rudiño-Pin̄era, E. Horjales, and M. L. Calcagno. 2002. On the role of the conformational flexibility of the active site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase. J. Mol. Biol. 319:183-189.
    • (2002) J. Mol. Biol. , vol.319 , pp. 183-189
    • Bustos-Jaimes, I.1    Sosa-Peinado, A.2    Rudiño-Pinera, E.3    Horjales, E.4    Calcagno, M.L.5
  • 7
    • 0021762288 scopus 로고
    • Purification, molecular and kinetic properties of glucosamine-6-phosphate isomerase (deaminase) from E. coli
    • Calcagno, M., P. J. Campos, G. Mulliert, and J. Suastegui. 1984. Purification, molecular and kinetic properties of glucosamine-6-phosphate isomerase (deaminase) from E. coli. Biochim. Biophys. Acta 787:165-173.
    • (1984) Biochim. Biophys. Acta , vol.787 , pp. 165-173
    • Calcagno, M.1    Campos, P.J.2    Mulliert, G.3    Suastegui, J.4
  • 8
    • 0347479369 scopus 로고    scopus 로고
    • Inversion of the allosteric response of Escherichia coli glucosamine-6-P deaminase to N-acetyglucosamine 6P by single amino acid replacements
    • Cisneros, D., G. M. Montero-Morán, S. Lara-González, and M. L. Calcagno. 2003. Inversion of the allosteric response of Escherichia coli glucosamine-6-P deaminase to N-acetyglucosamine 6P by single amino acid replacements. Arch. Biochem. Biophys. 421:77-84.
    • (2003) Arch. Biochem. Biophys. , vol.421 , pp. 77-84
    • Cisneros, D.1    Montero-Morán, G.M.2    Lara-González, S.3    Calcagno, M.L.4
  • 9
    • 0016761881 scopus 로고
    • Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase, and glucokinase
    • Curtis, S. J., and W. Epstein. 1975. Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase, and glucokinase. J. Bacteriol. 122:1189-1199.
    • (1975) J. Bacteriol. , vol.122 , pp. 1189-1199
    • Curtis, S.J.1    Epstein, W.2
  • 10
    • 0034612342 scopus 로고    scopus 로고
    • One step inactivation of chromosomal genes in Escherichia coli K12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One step inactivation of chromosomal genes in Escherichia coli K12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 11
    • 0031983641 scopus 로고    scopus 로고
    • Negative transcriptional regulation of a positive regulator: The expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc
    • Decker, K., J. Plumbridge, and W. Boos. 1998. Negative transcriptional regulation of a positive regulator: the expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc. Mol. Microbiol. 27:381-390.
    • (1998) Mol. Microbiol. , vol.27 , pp. 381-390
    • Decker, K.1    Plumbridge, J.2    Boos, W.3
  • 12
    • 0014247957 scopus 로고
    • Effect of amino sugars on catabolite repression in Escherichia coli
    • Dobrogosz, W. J. 1968. Effect of amino sugars on catabolite repression in Escherichia coli. J. Bacteriol. 95:578-584.
    • (1968) J. Bacteriol. , vol.95 , pp. 578-584
    • Dobrogosz, W.J.1
  • 13
    • 0022351923 scopus 로고
    • Positive selection procedure for entrapment of insertion sequence elements in gram-negative bacteria
    • Gay, P., D. Le Coq, M. Steinmetz, T. Berkelman, and C. Kado. 1985. Positive selection procedure for entrapment of insertion sequence elements in gram-negative bacteria. J. Bacteriol. 164:918-921.
    • (1985) J. Bacteriol. , vol.164 , pp. 918-921
    • Gay, P.1    Le Coq, D.2    Steinmetz, M.3    Berkelman, T.4    Kado, C.5
  • 14
    • 0035026474 scopus 로고    scopus 로고
    • Reverse genetics of Escherichia coli glycerol kinase allosteric regulation and glucose control of glycerol utilization in vivo
    • Holtman, C., A. Pawlyk, N. Meadow, and D. Pettigrew. 2001. Reverse genetics of Escherichia coli glycerol kinase allosteric regulation and glucose control of glycerol utilization in vivo. J. Bacteriol. 183:3336-3344.
    • (2001) J. Bacteriol. , vol.183 , pp. 3336-3344
    • Holtman, C.1    Pawlyk, A.2    Meadow, N.3    Pettigrew, D.4
  • 15
    • 0033135157 scopus 로고    scopus 로고
    • The allosteric transition of glucosamine-6-phosphate deaminase: The structure of the T state at 2.3A resolution
    • Horjales, E., M. M. Altamirano, M. L. Calcagno, R. Garratt, and G. Oliva. 1999. The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3A resolution. Structure 7:527-537.
    • (1999) Structure , vol.7 , pp. 527-537
    • Horjales, E.1    Altamirano, M.M.2    Calcagno, M.L.3    Garratt, R.4    Oliva, G.5
  • 16
    • 0018842354 scopus 로고
    • Amino-sugar transport systems in Escherichia coli K12
    • Jones-Mortimer, M. C., and H. L. Kornberg. 1980. Amino-sugar transport systems in Escherichia coli K12. J. Gen. Microbiol. 117:369-376.
    • (1980) J. Gen. Microbiol. , vol.117 , pp. 369-376
    • Jones-Mortimer, M.C.1    Kornberg, H.L.2
  • 17
    • 0027301842 scopus 로고
    • A universal method for achieving increases in metabolite production
    • Kacser, H., and L. Acerenza. 1993. A universal method for achieving increases in metabolite production. Eur. J. Biochem. 270:361-367.
    • (1993) Eur. J. Biochem. , vol.270 , pp. 361-367
    • Kacser, H.1    Acerenza, L.2
  • 18
    • 0031697458 scopus 로고    scopus 로고
    • A global repressor (Mlc) is involved in glucose induction of the ptsG gene encoding major glucose transporter in Escherichia coli
    • Kimata, K., T. Inada, H. Tagami, and H. Aiba. 1998. A global repressor (Mlc) is involved in glucose induction of the ptsG gene encoding major glucose transporter in Escherichia coli. Mol. Microbiol. 29:1509-1519.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1509-1519
    • Kimata, K.1    Inada, T.2    Tagami, H.3    Aiba, H.4
  • 19
    • 0034604365 scopus 로고    scopus 로고
    • On the role of the N-terminal group in the allosteric function of glucosamine-6-phosphate deaminase from Escherichia coli
    • Lara-González, S., H. B. F. Dixon, G. Mendoza-Hernandez, M. M. Altamirano, and M. L. Calcagno. 2000. On the role of the N-terminal group in the allosteric function of glucosamine-6-phosphate deaminase from Escherichia coli. J. Mol. Biol. 301:219-227.
    • (2000) J. Mol. Biol. , vol.301 , pp. 219-227
    • Lara-González, S.1    Dixon, H.B.F.2    Mendoza-Hernandez, G.3    Altamirano, M.M.4    Calcagno, M.L.5
  • 20
    • 0017620002 scopus 로고
    • Studies on the mechanism of E. coli glucosamine-6-phosphate isomerase
    • Midelfort, C. F., and I. A. Rose. 1977. Studies on the mechanism of E. coli glucosamine-6-phosphate isomerase. Biochemistry 16:1590-1596.
    • (1977) Biochemistry , vol.16 , pp. 1590-1596
    • Midelfort, C.F.1    Rose, I.A.2
  • 21
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • Monod, J., J. Changeux, and F. Jacob. 1963. Allosteric proteins and cellular control systems. J. Mol. Biol. 6:306-329.
    • (1963) J. Mol. Biol. , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.2    Jacob, F.3
  • 22
    • 78651189765 scopus 로고
    • On the nature of the allosteric transitions: A plausible model
    • Monod, J., J. Wyman, and J. Changeux. 1965. On the nature of the allosteric transitions: a plausible model. J. Mol. Biol. 12:88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.3
  • 23
    • 0032568581 scopus 로고    scopus 로고
    • Tyr254 hydroxyl group acts as a two-way switch mechanism in the coupling of heterotropic and homotropic effects in Escherichia coli glucosamine-6- phosphate deaminase
    • Montero-Morán, G. M., E. Horjales, M. L. Calcagno, and M. M. Altamirano. 1998. Tyr254 hydroxyl group acts as a two-way switch mechanism in the coupling of heterotropic and homotropic effects in Escherichia coli glucosamine-6-phosphate deaminase. Biochemistry 37:7844-7849.
    • (1998) Biochemistry , vol.37 , pp. 7844-7849
    • Montero-Morán, G.M.1    Horjales, E.2    Calcagno, M.L.3    Altamirano, M.M.4
  • 24
    • 0035964293 scopus 로고    scopus 로고
    • On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase
    • Montero-Morán, G. M., S. Lara-González, L. I. Álvarez-Añorve, J. A. Plumbridge, and M. L. Calcagno. 2001. On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase. Biochemistry 40:10187-10196.
    • (2001) Biochemistry , vol.40 , pp. 10187-10196
    • Montero-Morán, G.M.1    Lara-González, S.2    Álvarez- Añorve, L.I.3    Plumbridge, J.A.4    Calcagno, M.L.5
  • 26
    • 0029646095 scopus 로고
    • Structure and catalytic mechanism of glucosamine-6-phosphate deaminase from Escherichia coli at 2.1A resolution
    • Oliva, G., M. Fontes, R. Garratt, M. M. Altamirano, M. L. Calcagno, and E. Horjales. 1995. Structure and catalytic mechanism of glucosamine-6-phosphate deaminase from Escherichia coli at 2.1A resolution. Structure 3:1323-1332.
    • (1995) Structure , vol.3 , pp. 1323-1332
    • Oliva, G.1    Fontes, M.2    Garratt, R.3    Altamirano, M.M.4    Calcagno, M.L.5    Horjales, E.6
  • 27
    • 0034967799 scopus 로고    scopus 로고
    • Identification of a dedicated recycling pathway for anhydroN- acetylmuramic acid and N-acetylglucosamine derived from Escherichia coli cell wall murein
    • Park, J. T. 2001. Identification of a dedicated recycling pathway for anhydroN-acetylmuramic acid and N-acetylglucosamine derived from Escherichia coli cell wall murein. J. Bacteriol. 183:3842-3847.
    • (2001) J. Bacteriol. , vol.183 , pp. 3842-3847
    • Park, J.T.1
  • 28
    • 0031973888 scopus 로고    scopus 로고
    • Control of the expression of the manXYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS
    • Plumbridge, J. 1998. Control of the expression of the manXYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS. Mol. Microbiol. 27:369-381.
    • (1998) Mol. Microbiol. , vol.27 , pp. 369-381
    • Plumbridge, J.1
  • 29
    • 0026563016 scopus 로고
    • A dominant mutation in the gene for the Nag repressor of Escherichia coli that renders the nag regulon uninducible
    • Plumbridge, J. 1992. A dominant mutation in the gene for the Nag repressor of Escherichia coli that renders the nag regulon uninducible. J. Gen. Microbiol. 138:1011-1017.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1011-1017
    • Plumbridge, J.1
  • 30
    • 0031866040 scopus 로고    scopus 로고
    • Expression of ptsG, the gene for the major glucose PTS transporter in Escherichia coli, is repressed by Mlc and induced by growth on glucose
    • Plumbridge, J. 1998. Expression of ptsG, the gene for the major glucose PTS transporter in Escherichia coli, is repressed by Mlc and induced by growth on glucose. Mol. Microbiol. 29:1053-1063.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1053-1063
    • Plumbridge, J.1
  • 31
    • 0033062699 scopus 로고    scopus 로고
    • Expression of the phosphotransferase system (PTS) both mediates and is mediated by Mlc regulation in Escherichia coli
    • Plumbridge, J. 1999. Expression of the phosphotransferase system (PTS) both mediates and is mediated by Mlc regulation in Escherichia coli. Mol. Microbiol. 33:260-273.
    • (1999) Mol. Microbiol. , vol.33 , pp. 260-273
    • Plumbridge, J.1
  • 32
    • 0025278370 scopus 로고
    • Induction of the nag regulon of Escherichia coli by N-acetylglucosamine and glucosamine: Role of the cAMP-catabolite activator protein complex in expression of the regulon
    • Plumbridge, J. 1990. Induction of the nag regulon of Escherichia coli by N-acetylglucosamine and glucosamine: role of the cAMP-catabolite activator protein complex in expression of the regulon. J. Bacteriol. 172:2728-2735.
    • (1990) J. Bacteriol. , vol.172 , pp. 2728-2735
    • Plumbridge, J.1
  • 33
    • 0033760388 scopus 로고    scopus 로고
    • A mutation which affects both the specificity of PtsG sugar transport and the regulation of ptsG expression by Mlc in Escherichia coli
    • Plumbridge, J. 2000. A mutation which affects both the specificity of PtsG sugar transport and the regulation of ptsG expression by Mlc in Escherichia coli. Microbiology 146:2655-2663.
    • (2000) Microbiology , vol.146 , pp. 2655-2663
    • Plumbridge, J.1
  • 34
    • 0025816596 scopus 로고
    • Repression and induction of the nag regulon of Escherichia coli K12: The roles of nagC and nagA in maintenance of the uninduced state
    • Plumbridge, J. 1991. Repression and induction of the nag regulon of Escherichia coli K12: the roles of nagC and nagA in maintenance of the uninduced state. Mol. Microbiol. 5:2053-2062.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2053-2062
    • Plumbridge, J.1
  • 35
    • 0027275893 scopus 로고
    • Coordinated regulation of amino sugar-synthesizing and degrading enzymes in Escherichia coli K-12
    • Plumbridge, J., O. Cochet, J. M. Souza, M. M. Altamirano, M. L. Calcagno, and B. Badet. 1993. Coordinated regulation of amino sugar-synthesizing and degrading enzymes in Escherichia coli K-12. J. Bacteriol. 175:4951-4956.
    • (1993) J. Bacteriol. , vol.175 , pp. 4951-4956
    • Plumbridge, J.1    Cochet, O.2    Souza, J.M.3    Altamirano, M.M.4    Calcagno, M.L.5    Badet, B.6
  • 36
    • 0027742098 scopus 로고
    • DNA loop formation between Nag repressor molecules bound to its two operator sites is necessary for repression of the nag regulon of Escherichia coli in vivo
    • Plumbridge, J., and A. Kolb. 1993. DNA loop formation between Nag repressor molecules bound to its two operator sites is necessary for repression of the nag regulon of Escherichia coli in vivo. Mol. Microbiol. 10:973-981.
    • (1993) Mol. Microbiol. , vol.10 , pp. 973-981
    • Plumbridge, J.1    Kolb, A.2
  • 37
    • 0032929297 scopus 로고    scopus 로고
    • Convergent pathways for utilization of the amino sugars N-acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by Escherichia coli
    • Plumbridge, J., and E. Vimr. 1999. Convergent pathways for utilization of the amino sugars N-acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by Escherichia coli. J. Bacteriol. 181:47-54.
    • (1999) J. Bacteriol. , vol.181 , pp. 47-54
    • Plumbridge, J.1    Vimr, E.2
  • 38
    • 0001014412 scopus 로고    scopus 로고
    • Phosphoenolpyruvate:carbohydrate phosphotransferase systems
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM, Washington, D.C.
    • Postma, P. W., J. W. Lengeler, and G. R. Jacobson. 1996. Phosphoenolpyruvate:carbohydrate phosphotransferase systems, p. 1149-1174. in F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 1149-1174
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 39
    • 0036006749 scopus 로고    scopus 로고
    • Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase
    • Rudin̄o-Piñera, E., S. Morales-Arrieta, S. Rojas-Trejo, and E. Horjales. 2002. Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase. Acta Crystallogr. Sect. D 58:10-20.
    • (2002) Acta Crystallogr. Sect. D , vol.58 , pp. 10-20
    • Rudino-Piñera, E.1    Morales-Arrieta, S.2    Rojas-Trejo, S.3    Horjales, E.4
  • 40
    • 0031569854 scopus 로고    scopus 로고
    • N-Acetyl-D-glucosamine-6-phosphate deacetylase from Escherichia coli: Purification and molecular and kinetic characterization
    • Souza, J.-M., J. A. Plumbridge, and M. L. Calcagno. 1997. N-Acetyl-D-glucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization. Arch. Biochem. Biophys. 340:338-346.
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 338-346
    • Souza, J.-M.1    Plumbridge, J.A.2    Calcagno, M.L.3
  • 41
    • 6044239435 scopus 로고    scopus 로고
    • The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recycling
    • Uehara, T., and J. T. Park. 2004. The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recycling. J. Bacteriol. 186:7273-7279.
    • (2004) J. Bacteriol. , vol.186 , pp. 7273-7279
    • Uehara, T.1    Park, J.T.2
  • 42
    • 0014251825 scopus 로고
    • Control of amino sugar metabolism in Escherichia coli and isolation of mutants unable to degrade amino sugars
    • White, R. J. 1968. Control of amino sugar metabolism in Escherichia coli and isolation of mutants unable to degrade amino sugars. Biochem. J. 106:847-858.
    • (1968) Biochem. J. , vol.106 , pp. 847-858
    • White, R.J.1
  • 43
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding and degrading proteins
    • Wickner, S., M. Maurizi, and S. Gottesman. 1999. Posttranslational quality control: folding, refolding and degrading proteins. Science 286:1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.2    Gottesman, S.3


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