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Volumn 288, Issue 20, 2013, Pages 14114-14124

Correction: Cyclic AMP-dependent protein lysine acylation in mycobacteria regulates fatty acid and propionate metabolism (Journal of Biological Chemistry (2013) 288 (14114–14124) DOI: 10.1074/jbc.M113.463992);Cyclic AMP-dependent protein lysine acylation in mycobacteria regulates fatty acid and propionate metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION; AMINO ACIDS; BACTERIOLOGY; ENZYMES; METABOLISM; SUBSTRATES;

EID: 84877882503     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.AAC119.009859     Document Type: Erratum
Times cited : (94)

References (59)
  • 2
    • 0034005701 scopus 로고    scopus 로고
    • Functional classification of cNMP-binding proteins and nucleotide cyclases with implications for novel regulatory pathways in Mycobacterium tuberculosis
    • DOI 10.1101/gr.10.2.204
    • McCue, L. A., McDonough, K. A., and Lawrence, C. E. (2000) Functional classification of cNMP-binding proteins and nucleotide cyclases with implications for novel regulatory pathways in Mycobacterium tuberculosis. Genome Res. 10, 204-219 (Pubitemid 30119589)
    • (2000) Genome Research , vol.10 , Issue.2 , pp. 204-219
    • McCue, L.A.1    McDonough, K.A.2    Lawrence, C.E.3
  • 3
    • 1542334336 scopus 로고    scopus 로고
    • A survey of nucleotide cyclases in Actinobacteria: Unique domain organization and expansion of the class III cyclase family in Mycobacterium tuberculosis
    • DOI 10.1002/cfg.349
    • Shenoy, A. R., Sivakumar, K., Krupa, A., Srinivasan, N., and Visweswariah, S. S. (2004) A survey of nucleotide cyclases in actinobacteria. Unique domain organization and expansion of the class III cyclase family in Mycobacterium tuberculosis. Comp. Funct. Genomics 5, 17-38 (Pubitemid 38744634)
    • (2004) Comparative and Functional Genomics , vol.5 , Issue.1 , pp. 17-38
    • Shenoy, A.R.1    Sivakumar, K.2    Krupa, A.3    Srinivasan, N.4    Visweswariah, S.S.5
  • 4
    • 33750984748 scopus 로고    scopus 로고
    • New messages from old messengers: cAMP and mycobacteria
    • DOI 10.1016/j.tim.2006.10.005, PII S0966842X06002514
    • Shenoy, A. R., and Visweswariah, S. S. (2006) New messages from old messengers. cAMP and mycobacteria. Trends Microbiol. 14, 543-550 (Pubitemid 44751458)
    • (2006) Trends in Microbiology , vol.14 , Issue.12 , pp. 543-550
    • Shenoy, A.R.1    Visweswariah, S.S.2
  • 5
    • 83855165675 scopus 로고    scopus 로고
    • The myriad roles of cyclic AMP in microbial pathogens. From signal to sword
    • McDonough, K. A., and Rodriguez, A. (2012) The myriad roles of cyclic AMP in microbial pathogens. From signal to sword. Nat. Rev. Microbiol. 10, 27-38
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 27-38
    • McDonough, K.A.1    Rodriguez, A.2
  • 6
    • 67650074482 scopus 로고    scopus 로고
    • Cyclic AMP intoxication of macrophages by a Mycobacterium tuberculosis adenylate cyclase
    • Agarwal, N., Lamichhane, G., Gupta, R., Nolan, S., and Bishai, W. R. (2009) Cyclic AMP intoxication of macrophages by a Mycobacterium tuberculosis adenylate cyclase. Nature 460, 98-102
    • (2009) Nature , vol.460 , pp. 98-102
    • Agarwal, N.1    Lamichhane, G.2    Gupta, R.3    Nolan, S.4    Bishai, W.R.5
  • 7
    • 44349093807 scopus 로고    scopus 로고
    • Cyclic AMP in mycobacteria: Characterization and functional role of the Rv1647 ortholog in Mycobacterium smegmatis
    • DOI 10.1128/JB.00138-08
    • Dass, B. K., Sharma, R., Shenoy, A. R., Mattoo, R., and Visweswariah, S. S. (2008) Cyclic AMP in mycobacteria. Characterization and functional role of the Rv1647 ortholog in Mycobacterium smegmatis. J. Bacteriol. 190, 3824-3834 (Pubitemid 351732861)
    • (2008) Journal of Bacteriology , vol.190 , Issue.11 , pp. 3824-3834
    • Dass, B.K.M.1    Sharma, R.2    Shenoy, A.R.3    Mattoo, R.4    Visweswariah, S.S.5
  • 8
    • 33845800991 scopus 로고    scopus 로고
    • Capturing cyclic nucleotides in action: Snapshots from crystallographic studies
    • DOI 10.1038/nrm2082, PII NRM2082
    • Rehmann, H., Wittinghofer, A., and Bos, J. L. (2007) Capturing cyclic nucleotides in action. Snapshots from crystallographic studies. Nat. Rev. Mol. Cell Biol. 8, 63-73 (Pubitemid 46012015)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.1 , pp. 63-73
    • Rehmann, H.1    Wittinghofer, A.2    Bos, J.L.3
  • 9
    • 0035810698 scopus 로고    scopus 로고
    • Allosteric regulation of the cAMP receptor protein
    • Harman, J. G. (2001) Allosteric regulation of the cAMP receptor protein. Biochim. Biophys. Acta 1547, 1-17
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 1-17
    • Harman, J.G.1
  • 10
    • 77955285819 scopus 로고    scopus 로고
    • cAMP-regulated protein lysine acetylases in mycobacteria
    • Nambi, S., Basu, N., and Visweswariah, S. S. (2010) cAMP-regulated protein lysine acetylases in mycobacteria. J. Biol. Chem. 285, 24313-24323
    • (2010) J. Biol. Chem. , vol.285 , pp. 24313-24323
    • Nambi, S.1    Basu, N.2    Visweswariah, S.S.3
  • 11
    • 84861565305 scopus 로고    scopus 로고
    • Cyclic AMP-induced conformational changes in mycobacterial protein acetyltransferases
    • Nambi, S., Badireddy, S., Visweswariah, S. S., and Anand, G. S. (2012) Cyclic AMP-induced conformational changes in mycobacterial protein acetyltransferases. J. Biol. Chem. 287, 18115-18129
    • (2012) J. Biol. Chem. , vol.287 , pp. 18115-18129
    • Nambi, S.1    Badireddy, S.2    Visweswariah, S.S.3    Anand, G.S.4
  • 12
    • 84864658349 scopus 로고    scopus 로고
    • Cyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosis
    • Lee, H. J., Lang, P. T., Fortune, S. M., Sassetti, C. M., and Alber, T. (2012) Cyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosis. Nat. Struct. Mol. Biol. 19, 811-818
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 811-818
    • Lee, H.J.1    Lang, P.T.2    Fortune, S.M.3    Sassetti, C.M.4    Alber, T.5
  • 16
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • Tamura, K., Dudley, J., Nei, M., and Kumar, S. (2007) MEGA4. Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24, 1596-1599 (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 18
    • 23944504781 scopus 로고    scopus 로고
    • Analysis of p300 acetyltransferase substrate specificity by MALDI TOF mass spectrometry
    • DOI 10.1016/j.ymeth.2005.03.006, PII S1046202305000770, Protein Acetylation
    • Dormeyer, W., Ott, M., and Schnölzer, M. (2005) Analysis of p300 acetyltransferase substrate specificity by MALDI TOF mass spectrometry. Methods 36, 376-382 (Pubitemid 41188069)
    • (2005) Methods , vol.36 , Issue.4 , pp. 376-382
    • Dormeyer, W.1    Ott, M.2    Schnolzer, M.3
  • 19
    • 79959791094 scopus 로고    scopus 로고
    • Reversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMP
    • Xu, H., Hegde, S. S., and Blanchard, J. S. (2011) Reversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMP. Biochemistry 50, 5883-5892
    • (2011) Biochemistry , vol.50 , pp. 5883-5892
    • Xu, H.1    Hegde, S.S.2    Blanchard, J.S.3
  • 20
    • 84861993618 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis very-long-chain fatty acyl-CoA synthetase. Structural basis for housing lipid substrates longer than the enzyme
    • Andersson, C. S., Lundgren, C. A., Magnúsdóttir, A., Ge, C., Wieslander, A., Martinez Molina, D., and Högbom, M. (2012) The Mycobacterium tuberculosis very-long-chain fatty acyl-CoA synthetase. Structural basis for housing lipid substrates longer than the enzyme. Structure 20, 1062-1070
    • (2012) Structure , vol.20 , pp. 1062-1070
    • Andersson, C.S.1    Lundgren, C.A.2    Magnúsdóttir, A.3    Ge, C.4    Wieslander, A.5    Martinez Molina, D.6    Högbom, M.7
  • 21
    • 79551592420 scopus 로고    scopus 로고
    • Molecular modeling studies of Fatty acyl-CoA synthetase (FadD13) from Mycobacterium tuberculosis. A potential target for the development of antitubercular drugs
    • Jatana, N., Jangid, S., Khare, G., Tyagi, A. K., and Latha, N. (2011) Molecular modeling studies of Fatty acyl-CoA synthetase (FadD13) from Mycobacterium tuberculosis. A potential target for the development of antitubercular drugs. J. Mol. Model 17, 301-313
    • (2011) J. Mol. Model , vol.17 , pp. 301-313
    • Jatana, N.1    Jangid, S.2    Khare, G.3    Tyagi, A.K.4    Latha, N.5
  • 22
    • 77949511370 scopus 로고    scopus 로고
    • Dissecting the role of critical residues and substrate preference of a Fatty Acyl-CoA synthetase (FadD13) of Mycobacterium tuberculosis
    • Khare, G., Gupta, V., Gupta, R. K., Gupta, R., Bhat, R., and Tyagi, A. K. (2009) Dissecting the role of critical residues and substrate preference of a Fatty Acyl-CoA synthetase (FadD13) of Mycobacterium tuberculosis. PLoS One 4, e8387
    • (2009) PLoS One , vol.4
    • Khare, G.1    Gupta, V.2    Gupta, R.K.3    Gupta, R.4    Bhat, R.5    Tyagi, A.K.6
  • 23
    • 84860289203 scopus 로고    scopus 로고
    • Adenylating enzymes in Mycobacterium tuberculosis as drug targets
    • Duckworth, B. P., Nelson, K. M., and Aldrich, C. C. (2012) Adenylating enzymes in Mycobacterium tuberculosis as drug targets. Curr. Top Med. Chem. 12, 766-796
    • (2012) Curr. Top Med. Chem. , vol.12 , pp. 766-796
    • Duckworth, B.P.1    Nelson, K.M.2    Aldrich, C.C.3
  • 24
    • 65449166411 scopus 로고    scopus 로고
    • Novel structural insights into class I and II histone deacetylases
    • Ficner, R. (2009) Novel structural insights into class I and II histone deacetylases. Curr. Top Med. Chem. 9, 235-240
    • (2009) Curr. Top Med. Chem. , vol.9 , pp. 235-240
    • Ficner, R.1
  • 25
    • 84857113471 scopus 로고    scopus 로고
    • Biochemical and thermodynamic analyses of Salmonella enterica Pat, a multidomain, multimeric N(ε)-lysine acetyltransferase involved in carbon and energy metabolism
    • Thao, S., and Escalante-Semerena, J. C. (2011) Biochemical and thermodynamic analyses of Salmonella enterica Pat, a multidomain, multimeric N(ε)-lysine acetyltransferase involved in carbon and energy metabolism. mBio 2, e00216-211
    • (2011) mBio , vol.2
    • Thao, S.1    Escalante-Semerena, J.C.2
  • 26
    • 3242788065 scopus 로고    scopus 로고
    • Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica
    • DOI 10.1016/j.jmb.2004.05.010, PII S0022283604005650
    • Starai, V. J., and Escalante-Semerena, J. C. (2004) Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica. J. Mol. Biol. 340, 1005-1012 (Pubitemid 38968698)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.5 , pp. 1005-1012
    • Starai, V.J.1    Escalante-Semerena, J.C.2
  • 27
    • 0035895275 scopus 로고    scopus 로고
    • Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product
    • DOI 10.1073/pnas.031563798
    • Tanny, J. C., and Moazed, D. (2001) Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2. Evidence for acetyl transfer from substrate to an NAD breakdown product. Proc. Natl. Acad. Sci. U.S.A. 98, 415-420 (Pubitemid 32105055)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.2 , pp. 415-420
    • Tanny, J.C.1    Moazed, D.2
  • 28
    • 33746228121 scopus 로고    scopus 로고
    • Sirtuins in Aging and Age-Related Disease
    • DOI 10.1016/j.cell.2006.07.002, PII S0092867406008920
    • Longo, V. D., and Kennedy, B. K. (2006) Sirtuins in aging and age-related disease. Cell 126, 257-268 (Pubitemid 44092970)
    • (2006) Cell , vol.126 , Issue.2 , pp. 257-268
    • Longo, V.D.1    Kennedy, B.K.2
  • 29
    • 38349074340 scopus 로고    scopus 로고
    • Mycobacterial phenolic glycolipid virulence factor biosynthesis. Mechanism and small-molecule inhibition of polyketide chain initiation
    • Ferreras, J. A., Stirrett, K. L., Lu, X., Ryu, J. S., Soll, C. E., Tan, D. S., and Quadri, L. E. (2008) Mycobacterial phenolic glycolipid virulence factor biosynthesis. Mechanism and small-molecule inhibition of polyketide chain initiation. Chem. Biol. 15, 51-61
    • (2008) Chem. Biol. , vol.15 , pp. 51-61
    • Ferreras, J.A.1    Stirrett, K.L.2    Lu, X.3    Ryu, J.S.4    Soll, C.E.5    Tan, D.S.6    Quadri, L.E.7
  • 31
    • 79951471277 scopus 로고    scopus 로고
    • Cycli cAMP signalling in mycobacteria. Redirecting the conversation with a common currency
    • Bai, G., Knapp, G. S., and McDonough, K. A. (2011) Cycli cAMP signalling in mycobacteria. Redirecting the conversation with a common currency. Cell Microbiol. 13, 349-358
    • (2011) Cell Microbiol. , vol.13 , pp. 349-358
    • Bai, G.1    Knapp, G.S.2    McDonough, K.A.3
  • 32
    • 33745235266 scopus 로고    scopus 로고
    • Role of the methylcitrate cycle in Mycobacterium tuberculosis metabolism, intracellular growth, and virulence
    • Muñoz-Elías, E. J., Upton, A. M., Cherian, J., and McKinney, J. D. (2006) Role of the methylcitrate cycle in Mycobacterium tuberculosis metabolism, intracellular growth, and virulence. Mol. Microbiol. 60, 1109-1122
    • (2006) Mol. Microbiol. , vol.60 , pp. 1109-1122
    • Muñoz-Elías, E.J.1    Upton, A.M.2    Cherian, J.3    McKinney, J.D.4
  • 33
    • 44349163542 scopus 로고    scopus 로고
    • 12-dependent methylmalonyl pathway in Mycobacterium tuberculosis: Implications for propionate metabolism during growth on fatty acids
    • DOI 10.1128/JB.01767-07
    • Savvi, S., Warner, D. F., Kana, B. D., McKinney, J. D., Mizrahi, V., and Dawes, S. S. (2008) Functional characterization of a vitamin B12-dependent methylmalonyl pathway in Mycobacterium tuberculosis. Implications for propionate metabolism during growth on fatty acids. J. Bacteriol. 190, 3886-3895 (Pubitemid 351732867)
    • (2008) Journal of Bacteriology , vol.190 , Issue.11 , pp. 3886-3895
    • Savvi, S.1    Warner, D.F.2    Kana, B.D.3    McKinney, J.D.4    Mizrahi, V.5    Dawes, S.S.6
  • 34
    • 37449003688 scopus 로고    scopus 로고
    • Role of the methylcitrate cycle in propionate metabolism and detoxification in Mycobacterium smegmatis
    • Upton, A. M., and McKinney, J. D. (2007) Role of the methylcitrate cycle in propionate metabolism and detoxification in Mycobacterium smegmatis. Microbiology 153, 3973-3982
    • (2007) Microbiology , vol.153 , pp. 3973-3982
    • Upton, A.M.1    McKinney, J.D.2
  • 35
    • 80455129274 scopus 로고    scopus 로고
    • Purification and characterization of the acetyl-CoA synthetase from Mycobacterium tuberculosis
    • Li, R., Gu, J., Chen, P., Zhang, Z., Deng, J., and Zhang, X. (2011) Purification and characterization of the acetyl-CoA synthetase from Mycobacterium tuberculosis. Acta Biochim. Biophys. Sin. 43, 891-899
    • (2011) Acta Biochim. Biophys. Sin. , vol.43 , pp. 891-899
    • Li, R.1    Gu, J.2    Chen, P.3    Zhang, Z.4    Deng, J.5    Zhang, X.6
  • 36
    • 84870309723 scopus 로고    scopus 로고
    • Structural insights into the substrate specificity of the Rhodopseudomonas palustris protein acetyltransferase RpPat. Identification of a loop critical for recognition by RpPat
    • Crosby, H. A., Rank, K. C., Rayment, I., and Escalante-Semerena, J. C. (2012) Structural insights into the substrate specificity of the Rhodopseudomonas palustris protein acetyltransferase RpPat. Identification of a loop critical for recognition by RpPat. J. Biol. Chem. 287, 41392-41404
    • (2012) J. Biol. Chem. , vol.287 , pp. 41392-41404
    • Crosby, H.A.1    Rank, K.C.2    Rayment, I.3    Escalante-Semerena, J.C.4
  • 37
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation. A regulatory modification to rival phosphorylation?
    • Kouzarides, T. (2000) Acetylation. A regulatory modification to rival phosphorylation? EMBO J. 19, 1176-1179
    • (2000) EMBO J. , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 39
    • 0027102583 scopus 로고
    • Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau
    • Takemura, R., Okabe, S., Umeyama, T., Kanai, Y., Cowan, N. J., and Hirokawa, N. (1992) Increased microtubule stability and α tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau. J. Cell Sci. 103, 953-964 (Pubitemid 23042239)
    • (1992) Journal of Cell Science , vol.103 , Issue.4 , pp. 953-964
    • Takemura, R.1    Okabe, S.2    Umeyama, T.3    Kanai, Y.4    Cowan, N.J.5    Hirokawa, N.6
  • 40
    • 38649092744 scopus 로고    scopus 로고
    • Regulation of protein turnover by acetyltransferases and deacetylases
    • DOI 10.1016/j.biochi.2007.06.009, PII S030090840700168X
    • Sadoul, K., Boyault, C., Pabion, M., and Khochbin, S. (2008) Regulation of protein turnover by acetyltransferases and deacetylases. Biochimie 90, 306-312 (Pubitemid 351172566)
    • (2008) Biochimie , vol.90 , Issue.2 , pp. 306-312
    • Sadoul, K.1    Boyault, C.2    Pabion, M.3    Khochbin, S.4
  • 44
    • 1842577641 scopus 로고    scopus 로고
    • Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria
    • DOI 10.1038/nature02384
    • Trivedi, O. A., Arora, P., Sridharan, V., Tickoo, R., Mohanty, D., and Gokhale, R. S. (2004) Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria. Nature 428, 441-445 (Pubitemid 38419691)
    • (2004) Nature , vol.428 , Issue.6981 , pp. 441-445
    • Trivedi, O.A.1    Arora, P.2    Sridharan, V.3    Tickoo, R.4    Mohanty, D.5    Gokhale, R.S.6
  • 46
    • 84865421953 scopus 로고    scopus 로고
    • Mitochondrial sirtuins. Regulators of protein acylation and metabolism
    • He, W., Newman, J. C., Wang, M. Z., Ho, L., and Verdin, E. (2012) Mitochondrial sirtuins. Regulators of protein acylation and metabolism. Trends Endocrinol. Metab. 23, 467-476
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 467-476
    • He, W.1    Newman, J.C.2    Wang, M.Z.3    Ho, L.4    Verdin, E.5
  • 47
    • 0038148638 scopus 로고    scopus 로고
    • pckA-deficient Mycobacterium bovis BCG shows attenuated virulence in mice and in macrophages
    • Liu, K., Yu, J., and Russell, D. G. (2003) pckA-deficient Mycobacterium bovis BCG shows attenuated virulence in mice and in macrophages. Microbiology 149, 1829-1835 (Pubitemid 36874328)
    • (2003) Microbiology , vol.149 , Issue.7 , pp. 1829-1835
    • Liu, K.1    Yu, J.2    Russell, D.G.3
  • 48
    • 77953105101 scopus 로고    scopus 로고
    • Gluconeogenic carbon flow of tricarboxylic acid cycle intermediates is critical for Mycobacterium tuberculosis to establish and maintain infection
    • Marrero, J., Rhee, K. Y., Schnappinger, D., Pethe, K., and Ehrt, S. (2010) Gluconeogenic carbon flow of tricarboxylic acid cycle intermediates is critical for Mycobacterium tuberculosis to establish and maintain infection. Proc. Natl. Acad. Sci. U.S.A. 107, 9819-9824
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 9819-9824
    • Marrero, J.1    Rhee, K.Y.2    Schnappinger, D.3    Pethe, K.4    Ehrt, S.5
  • 50
    • 20944450448 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis isocitrate lyases 1 and 2 are jointly required for in vivo growth and virulence
    • DOI 10.1038/nm1252
    • Muñoz-Elías, E. J., and McKinney, J. D. (2005) Mycobacterium tuberculosis isocitrate lyases 1 and 2 are jointly required for in vivo growth and virulence. Nat. Med. 11, 638-644 (Pubitemid 40868304)
    • (2005) Nature Medicine , vol.11 , Issue.6 , pp. 638-644
    • Munoz-Elias, E.J.1    McKinney, J.D.2
  • 55
    • 77953200061 scopus 로고    scopus 로고
    • Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis
    • Siméone, R., Léger, M., Constant, P., Malaga, W., Marrakchi, H., Daffé, M., Guilhot, C., and Chalut, C. (2010) Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis. FEBS J. 277, 2715-2725
    • (2010) FEBS J. , vol.277 , pp. 2715-2725
    • Siméone, R.1    Léger, M.2    Constant, P.3    Malaga, W.4    Marrakchi, H.5    Daffé, M.6    Guilhot, C.7    Chalut, C.8
  • 56
    • 33645535557 scopus 로고    scopus 로고
    • The fadD2 gene is required for efficient Mycobacterium avium invasion of mucosal epithelial cells
    • Dam, T., Danelishvili, L., Wu, M., and Bermudez, L. E. (2006) The fadD2 gene is required for efficient Mycobacterium avium invasion of mucosal epithelial cells. J. Infect. Dis. 193, 1135-1142
    • (2006) J. Infect. Dis. , vol.193 , pp. 1135-1142
    • Dam, T.1    Danelishvili, L.2    Wu, M.3    Bermudez, L.E.4
  • 57
    • 77950292485 scopus 로고    scopus 로고
    • Attenuation of Mycobacterium tuberculosis functionally disrupted in a fatty acyl-coenzyme A synthetase gene fadD5
    • Dunphy, K. Y., Senaratne, R. H., Masuzawa, M., Kendall, L. V., and Riley, L. W. (2010) Attenuation of Mycobacterium tuberculosis functionally disrupted in a fatty acyl-coenzyme A synthetase gene fadD5. J. Infect. Dis. 201, 1232-1239
    • (2010) J. Infect. Dis. , vol.201 , pp. 1232-1239
    • Dunphy, K.Y.1    Senaratne, R.H.2    Masuzawa, M.3    Kendall, L.V.4    Riley, L.W.5
  • 58
    • 84872370910 scopus 로고    scopus 로고
    • FadD3 is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria
    • Casabon, I., Crowe, A. M., Liu, J., and Eltis, L. D. (2013) FadD3 is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. Mol. Microbiol. 87, 269-283
    • (2013) Mol. Microbiol. , vol.87 , pp. 269-283
    • Casabon, I.1    Crowe, A.M.2    Liu, J.3    Eltis, L.D.4
  • 59
    • 20144369733 scopus 로고    scopus 로고
    • Transposon mutagenesis of Mb0100 at the ppe1-nrp locus in Mycobacterium bovis disrupts phthiocerol dimycocerosate (PDIM) and glycosylphenol-PDIM biosynthesis, producing an avirulent strain with vaccine properties at least equal to those of M. bovis BCG
    • DOI 10.1128/JB.187.7.2267-2277.2005
    • Hotter, G. S., Wards, B. J., Mouat, P., Besra, G. S., Gomes, J., Singh, M., Bassett, S., Kawakami, P., Wheeler, P. R., de Lisle, G. W., and Collins, D. M. (2005) Transposon mutagenesis of Mb0100 at the ppe1-nrp locus in Mycobacterium bovis disrupts phthiocerol dimycocerosate (PDIM) and glycosylphenol-PDIM biosynthesis, producing an avirulent strain with vaccine properties at least equal to those of M. bovis BCG. J. Bacteriol. 187, 2267-2277 (Pubitemid 40389125)
    • (2005) Journal of Bacteriology , vol.187 , Issue.7 , pp. 2267-2277
    • Hotter, G.S.1    Wards, B.J.2    Mouat, P.3    Besra, G.S.4    Gomes, J.5    Singh, M.6    Bassett, S.7    Kawakami, P.8    Wheeler, P.R.9    De Lisle, G.W.10    Collins, D.M.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.