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Volumn 5, Issue 3, 2009, Pages 166-173

Mechanistic and functional insights into fatty acid activation in Mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

COENZYME A; FATTY ACID SYNTHASE; POLYKETIDE SYNTHASE; PROTEIN FAAL; UNCLASSIFIED DRUG;

EID: 60249099423     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.143     Document Type: Article
Times cited : (114)

References (50)
  • 1
    • 1842577641 scopus 로고    scopus 로고
    • Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria
    • Trivedi, O.A. et al. Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria. Nature 428, 441-445 (2004).
    • (2004) Nature , vol.428 , pp. 441-445
    • Trivedi, O.A.1
  • 2
    • 0035156443 scopus 로고    scopus 로고
    • Exploring the domain structure of modular nonribosomal peptide synthetases
    • Weber, T. & Marahiel, M.A. Exploring the domain structure of modular nonribosomal peptide synthetases. Structure 9, R3-R9 (2001).
    • (2001) Structure , vol.9
    • Weber, T.1    Marahiel, M.A.2
  • 3
    • 33748631825 scopus 로고    scopus 로고
    • Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: Logic, machinery, and mechanisms
    • Fischbach, M.A. & Walsh, C.T. Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: logic, machinery, and mechanisms. Chem. Rev. 106, 3468-3496 (2006).
    • (2006) Chem. Rev , vol.106 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 4
    • 0033179468 scopus 로고    scopus 로고
    • The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases
    • Stachelhaus, T., Mootz, H.D. & Marahiel, M.A. The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases. Chem. Biol. 6, 493-505 (1999).
    • (1999) Chem. Biol , vol.6 , pp. 493-505
    • Stachelhaus, T.1    Mootz, H.D.2    Marahiel, M.A.3
  • 5
    • 0347091999 scopus 로고    scopus 로고
    • tuberculosis persistence, latency, and drug tolerance
    • Gomez, J.E. & McKinney, J.D.M. tuberculosis persistence, latency, and drug tolerance. Tuberculosis (Edinb.) 84, 29-44 (2004).
    • (2004) Tuberculosis (Edinb.) , vol.84 , pp. 29-44
    • Gomez, J.E.1    McKinney, J.D.M.2
  • 6
    • 40549096921 scopus 로고    scopus 로고
    • World Health Organization, WHO/HTM/TB/2008.393, World Health Organization Geneva
    • World Health Organization. Global tuberculosis control: surveillance, planning, financing (WHO/HTM/TB/2008.393) (World Health Organization Geneva, 2008).
    • (2008) Global tuberculosis control: Surveillance, planning, financing
  • 7
    • 34547110777 scopus 로고    scopus 로고
    • Targeting the formation of the cell wall core of M. tuberculosis
    • Barry, C.E., Crick, D.C. & McNeil, M.R. Targeting the formation of the cell wall core of M. tuberculosis. Infect. Disord. Drug Targets 7, 182-202 (2007).
    • (2007) Infect. Disord. Drug Targets , vol.7 , pp. 182-202
    • Barry, C.E.1    Crick, D.C.2    McNeil, M.R.3
  • 8
    • 33947682112 scopus 로고    scopus 로고
    • The cell-wall core of Mycobacterium tuberculosis in the context of drug discovery
    • Brennan, P.J. & Crick, D.C. The cell-wall core of Mycobacterium tuberculosis in the context of drug discovery. Curr. Top. Med. Chem. 7, 475-488 (2007).
    • (2007) Curr. Top. Med. Chem , vol.7 , pp. 475-488
    • Brennan, P.J.1    Crick, D.C.2
  • 9
    • 36549060587 scopus 로고    scopus 로고
    • Versatility of polyketide synthases in generating metabolic diversity
    • Gokhale, R.S., Sankaranarayanan, R. & Mohanty, D. Versatility of polyketide synthases in generating metabolic diversity. Curr. Opin. Struct. Biol. 17, 736-743 (2007).
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 736-743
    • Gokhale, R.S.1    Sankaranarayanan, R.2    Mohanty, D.3
  • 10
    • 33947662068 scopus 로고    scopus 로고
    • Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids
    • Gokhale, R.S., Saxena, P., Chopra, T. & Mohanty, D. Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids. Nat. Prod. Rep. 24, 267-277 (2007).
    • (2007) Nat. Prod. Rep , vol.24 , pp. 267-277
    • Gokhale, R.S.1    Saxena, P.2    Chopra, T.3    Mohanty, D.4
  • 11
    • 33846807242 scopus 로고    scopus 로고
    • Long-chain multiple methyl-branched fatty acid-containing lipids of Mycobacterium tuberculosis: Biosynthesis, transport, regulation and biological activities
    • Jackson, M., Stadthagen, G. & Gicquel, B. Long-chain multiple methyl-branched fatty acid-containing lipids of Mycobacterium tuberculosis: biosynthesis, transport, regulation and biological activities. Tuberculosis (Edinb.) 87, 78-86 (2007).
    • (2007) Tuberculosis (Edinb.) , vol.87 , pp. 78-86
    • Jackson, M.1    Stadthagen, G.2    Gicquel, B.3
  • 13
    • 33144458001 scopus 로고    scopus 로고
    • A genetic locus required for iron acquisition in Mycobacterium tuberculosis
    • Krithika, R. et al. A genetic locus required for iron acquisition in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 103, 2069-2074 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2069-2074
    • Krithika, R.1
  • 14
    • 14644408803 scopus 로고    scopus 로고
    • Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid
    • Trivedi, O.A. et al. Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid. Mol. Cell 17, 631-643 (2005).
    • (2005) Mol. Cell , vol.17 , pp. 631-643
    • Trivedi, O.A.1
  • 15
    • 15744389881 scopus 로고    scopus 로고
    • The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: Identification of the carboxylation product and determination of the acyl-CoA carboxylase components
    • Portevin, D. et al. The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase components. J. Biol. Chem. 280, 8862-8874 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 8862-8874
    • Portevin, D.1
  • 16
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole, S.T. et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393, 537-544 (1998).
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1
  • 17
    • 39149131054 scopus 로고    scopus 로고
    • Global transcriptional profile of Mycobacterium tuberculosis during THP-1 human macrophage infection
    • Fontan, P., Aris, V., Ghanny, S., Soteropoulos, P. & Smith, I. Global transcriptional profile of Mycobacterium tuberculosis during THP-1 human macrophage infection. Infect. Immun. 76, 717-725 (2008).
    • (2008) Infect. Immun , vol.76 , pp. 717-725
    • Fontan, P.1    Aris, V.2    Ghanny, S.3    Soteropoulos, P.4    Smith, I.5
  • 18
    • 33846904705 scopus 로고    scopus 로고
    • A gene cluster encoding cholesterol catabolism in a soil actinomycete provides insight into Mycobacterium tuberculosis survival in macrophages
    • Van der Geize, R. et al. A gene cluster encoding cholesterol catabolism in a soil actinomycete provides insight into Mycobacterium tuberculosis survival in macrophages. Proc. Natl. Acad. Sci. USA 104, 1947-1952 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1947-1952
    • Van der Geize, R.1
  • 19
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti, E., Franks, N.P. & Brick, P. Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4, 287-298 (1996).
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 20
    • 0037452897 scopus 로고    scopus 로고
    • The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A
    • Gulick, A.M., Starai, V.J., Horswill, A.R., Homick, K.M. & Escalante-Semerena, J.C. The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A. Biochemistry 42, 2866-2873 (2003).
    • (2003) Biochemistry , vol.42 , pp. 2866-2873
    • Gulick, A.M.1    Starai, V.J.2    Horswill, A.R.3    Homick, K.M.4    Escalante-Semerena, J.C.5
  • 21
    • 0037126024 scopus 로고    scopus 로고
    • Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases
    • May, J.J., Kessler, N., Marahiel, M.A. & Stubbs, M.T. Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases. Proc. Natl. Acad. Sci. USA 99, 12120-12125 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12120-12125
    • May, J.J.1    Kessler, N.2    Marahiel, M.A.3    Stubbs, M.T.4
  • 22
    • 3843068822 scopus 로고    scopus 로고
    • Structural basis of the substrate-specific two-step catalysis of long chain fatty acyl-CoA synthetase dimer
    • Hisanaga, Y. et al. Structural basis of the substrate-specific two-step catalysis of long chain fatty acyl-CoA synthetase dimer. J. Biol. Chem. 279, 31717-31726 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 31717-31726
    • Hisanaga, Y.1
  • 23
    • 33645762737 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from Mycobacterium tuberculosis
    • Goyal, A. et al. Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from Mycobacterium tuberculosis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62, 350-352 (2006).
    • (2006) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.62 , pp. 350-352
    • Goyal, A.1
  • 24
    • 0030756031 scopus 로고    scopus 로고
    • Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S
    • Conti, E., Stachelhaus, T., Marahiel, M.A. & Brick, P. Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S. EMBO J. 16, 4174-4183 (1997).
    • (1997) EMBO J , vol.16 , pp. 4174-4183
    • Conti, E.1    Stachelhaus, T.2    Marahiel, M.A.3    Brick, P.4
  • 25
    • 33847112437 scopus 로고    scopus 로고
    • Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
    • Linne, U., Schafer, A., Stubbs, M.T. & Marahiel, M.A. Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains. FEBS Lett. 581, 905-910 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 905-910
    • Linne, U.1    Schafer, A.2    Stubbs, M.T.3    Marahiel, M.A.4
  • 26
    • 0035861676 scopus 로고    scopus 로고
    • Structural basis for the recognition of isoleucyladenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase
    • Nakama, T., Nureki, O. & Yokoyama, S. Structural basis for the recognition of isoleucyladenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase. J. Biol. Chem. 276, 47387-47393 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 47387-47393
    • Nakama, T.1    Nureki, O.2    Yokoyama, S.3
  • 27
    • 33344469904 scopus 로고    scopus 로고
    • Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis
    • Ferreras, J.A., Ryu, J.S., Di Lello, F., Tan, D.S. & Quadri, L.E. Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis. Nat. Chem. Biol. 1, 29-32 (2005).
    • (2005) Nat. Chem. Biol , vol.1 , pp. 29-32
    • Ferreras, J.A.1    Ryu, J.S.2    Di Lello, F.3    Tan, D.S.4    Quadri, L.E.5
  • 28
    • 30444445995 scopus 로고    scopus 로고
    • Rationally designed nucleoside antibiotics that inhibit siderophore biosynthesis of Mycobacterium tuberculosis
    • Somu, R.V. et al. Rationally designed nucleoside antibiotics that inhibit siderophore biosynthesis of Mycobacterium tuberculosis. J. Med. Chem. 49, 31-34 (2006).
    • (2006) J. Med. Chem , vol.49 , pp. 31-34
    • Somu, R.V.1
  • 29
    • 85029154891 scopus 로고    scopus 로고
    • Copeland, R.A. Tight binding inhibitors. in Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis##305-317 (Wiley-VCH, New York, 2000).
    • Copeland, R.A. Tight binding inhibitors. in Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis##305-317 (Wiley-VCH, New York, 2000).
  • 30
    • 34249002570 scopus 로고    scopus 로고
    • The loading module of mycosubtilin: An adenylation domain with fatty acid selectivity
    • Hansen, D.B., Bumpus, S.B., Aron, Z.D., Kelleher, N.L. & Walsh, C.T. The loading module of mycosubtilin: an adenylation domain with fatty acid selectivity. J. Am. Chem. Soc. 129, 6366-6367 (2007).
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 6366-6367
    • Hansen, D.B.1    Bumpus, S.B.2    Aron, Z.D.3    Kelleher, N.L.4    Walsh, C.T.5
  • 31
    • 33947316606 scopus 로고    scopus 로고
    • Yeast acyl-CoA synthetases at the crossroads of fatty acid metabolism and regulation
    • Black, P.N. & DiRusso, C.C. Yeast acyl-CoA synthetases at the crossroads of fatty acid metabolism and regulation. Biochim. Biophys. Acta 1771, 286-298 (2007).
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 286-298
    • Black, P.N.1    DiRusso, C.C.2
  • 32
    • 34248590375 scopus 로고    scopus 로고
    • Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence
    • Wang, F., Langley, R., Gulten, G., Wang, L. & Sacchettini, J.C. Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence. Chem. Biol. 14, 543-551 (2007).
    • (2007) Chem. Biol , vol.14 , pp. 543-551
    • Wang, F.1    Langley, R.2    Gulten, G.3    Wang, L.4    Sacchettini, J.C.5
  • 33
    • 21644469444 scopus 로고    scopus 로고
    • Promiscuous fatty acyl CoA ligases produce acyl-CoA and acyl-SNAC precursors for polyketide biosynthesis
    • Arora, P., Vats, A., Saxena, P., Mohanty, D. & Gokhale, R.S. Promiscuous fatty acyl CoA ligases produce acyl-CoA and acyl-SNAC precursors for polyketide biosynthesis. J. Am. Chem. Soc. 127, 9388-9389 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 9388-9389
    • Arora, P.1    Vats, A.2    Saxena, P.3    Mohanty, D.4    Gokhale, R.S.5
  • 34
    • 33747887074 scopus 로고    scopus 로고
    • Acyl-phosphates initiate membrane phospholipid synthesis in Grampositive pathogens
    • Lu, Y.J. et al. Acyl-phosphates initiate membrane phospholipid synthesis in Grampositive pathogens. Mol. Cell 23, 765-772 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 765-772
    • Lu, Y.J.1
  • 35
    • 33747484925 scopus 로고    scopus 로고
    • The soluble acyl-acyl carrier protein synthetase of Vibrio harveyi B392 is a member of the medium chain acyl-CoA synthetase family
    • Jiang, Y., Chan, C.H. & Cronan, J.E. The soluble acyl-acyl carrier protein synthetase of Vibrio harveyi B392 is a member of the medium chain acyl-CoA synthetase family. Biochemistry 45, 10008-10019 (2006).
    • (2006) Biochemistry , vol.45 , pp. 10008-10019
    • Jiang, Y.1    Chan, C.H.2    Cronan, J.E.3
  • 36
    • 33644524741 scopus 로고    scopus 로고
    • Cell-signalling dynamics in time and space
    • Kholodenko, B.N. Cell-signalling dynamics in time and space. Nat. Rev. Mol. Cell Biol. 7, 165-176 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 165-176
    • Kholodenko, B.N.1
  • 37
    • 0035826155 scopus 로고    scopus 로고
    • Exploring complex networks
    • Strogatz, S.H. Exploring complex networks. Nature 410, 268-276 (2001).
    • (2001) Nature , vol.410 , pp. 268-276
    • Strogatz, S.H.1
  • 38
    • 27144449695 scopus 로고    scopus 로고
    • Designed multiple ligands. An emerging drug discovery paradigm
    • Morphy, R. & Rankovic, Z. Designed multiple ligands. An emerging drug discovery paradigm. J. Med. Chem. 48, 6523-6543 (2005).
    • (2005) J. Med. Chem , vol.48 , pp. 6523-6543
    • Morphy, R.1    Rankovic, Z.2
  • 39
    • 77049286017 scopus 로고
    • Biochemical differentiation of Mycobacterium tuberculosis grown in vivo and in vitro
    • Bloch, H. & Segal, W. Biochemical differentiation of Mycobacterium tuberculosis grown in vivo and in vitro. J. Bacteriol. 72, 132-141 (1956).
    • (1956) J. Bacteriol , vol.72 , pp. 132-141
    • Bloch, H.1    Segal, W.2
  • 40
    • 34247617733 scopus 로고    scopus 로고
    • Lipidomics reveals control of Mycobacterium tuberculosis virulence lipids via metabolic coupling
    • Jain, M. et al. Lipidomics reveals control of Mycobacterium tuberculosis virulence lipids via metabolic coupling. Proc. Natl. Acad. Sci. USA 104, 5133-5138 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5133-5138
    • Jain, M.1
  • 41
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 42
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 43
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 44
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11, 134-138 (1993).
    • (1993) J. Mol. Graph , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 45
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40 (1993).
    • (1993) Protein Eng , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 46
    • 0024562340 scopus 로고
    • Synthesis and antiviral activity of 5′-O-(substituted) sulfamoyl pyrimidine nucleosides
    • Castro-Pichel, J. et al. Synthesis and antiviral activity of 5′-O-(substituted) sulfamoyl pyrimidine nucleosides. Arch. Pharm. (Weinheim) 322, 11-15 (1989).
    • (1989) Arch. Pharm. (Weinheim) , vol.322 , pp. 11-15
    • Castro-Pichel, J.1
  • 47
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison, J.F. & Walsh, C.T. The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. 61, 201-301 (1988).
    • (1988) Adv. Enzymol , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 48
    • 0032930265 scopus 로고    scopus 로고
    • Antimycobacterial activities of isoxyl and new derivatives through the inhibition of mycolic acid synthesis
    • Phetsuksiri, B. et al. Antimycobacterial activities of isoxyl and new derivatives through the inhibition of mycolic acid synthesis. Antimicrob. Agents Chemother. 43, 1042-1051 (1999).
    • (1999) Antimicrob. Agents Chemother , vol.43 , pp. 1042-1051
    • Phetsuksiri, B.1
  • 49
    • 0035827613 scopus 로고    scopus 로고
    • Analysis of the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Evidence that this lipid is involved in the cell wall permeability barrier
    • Camacho, L.R. et al. Analysis of the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Evidence that this lipid is involved in the cell wall permeability barrier. J. Biol. Chem. 276, 19845-19854 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 19845-19854
    • Camacho, L.R.1
  • 50
    • 0033523971 scopus 로고    scopus 로고
    • Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice
    • Cox, J.S., Chen, B., McNeil, M. & Jacobs, W.R. Jr. Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice. Nature 402, 79-83 (1999).
    • (1999) Nature , vol.402 , pp. 79-83
    • Cox, J.S.1    Chen, B.2    McNeil, M.3    Jacobs Jr., W.R.4


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