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Volumn 20, Issue 1, 2013, Pages 123-133

Identification of widespread adenosine nucleotide binding in mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE;

EID: 84872908803     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2012.11.008     Document Type: Article
Times cited : (44)

References (42)
  • 2
    • 35848965006 scopus 로고    scopus 로고
    • Activity-based protein profiling for the functional annotation of enzymes
    • DOI 10.1038/nmeth1092, PII NMETH1092
    • K.T. Barglow, and B.F. Cravatt Activity-based protein profiling for the functional annotation of enzymes Nat. Methods 4 2007 822 827 (Pubitemid 350055579)
    • (2007) Nature Methods , vol.4 , Issue.10 , pp. 822-827
    • Barglow, K.T.1    Cravatt, B.F.2
  • 3
    • 0034060929 scopus 로고    scopus 로고
    • Powers and pitfalls in sequence analysis: The 70% hurdle
    • DOI 10.1101/gr.10.4.398
    • P. Bork Powers and pitfalls in sequence analysis: the 70% hurdle Genome Res. 10 2000 398 400 (Pubitemid 30259070)
    • (2000) Genome Research , vol.10 , Issue.4 , pp. 398-400
    • Bork, P.1
  • 4
    • 0031897589 scopus 로고    scopus 로고
    • Predicting functions from protein sequences - Where are the bottlenecks?
    • DOI 10.1038/ng0498-313
    • P. Bork, and E.V. Koonin Predicting functions from protein sequences - where are the bottlenecks? Nat. Genet. 18 1998 313 318 (Pubitemid 28158157)
    • (1998) Nature Genetics , vol.18 , Issue.4 , pp. 313-318
    • Bork, P.1    Koonin, E.V.2
  • 5
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry to proteomic chemistry
    • B.F. Cravatt, A.T. Wright, and J.W. Kozarich Activity-based protein profiling: from enzyme chemistry to proteomic chemistry Annu. Rev. Biochem. 77 2008 383 414
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 7
    • 33847167237 scopus 로고
    • Mechanism and catalysis of reactions of acyl phosphates. I. Nucleophilic reactions
    • G. DiSabato, and W.P. Jencks Mechanism and catalysis of reactions of acyl phosphates. I. Nucleophilic reactions J. Am. Chem. Soc. 83 1961 4393 4400
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 4393-4400
    • Disabato, G.1    Jencks, W.P.2
  • 8
    • 84859260583 scopus 로고    scopus 로고
    • Annotation of the M. tuberculosis hypothetical orfeome: Adding functional information to more than half of the uncharacterized proteins
    • T. Doerks, V. van Noort, P. Minguez, and P. Bork Annotation of the M. tuberculosis hypothetical orfeome: adding functional information to more than half of the uncharacterized proteins PLoS ONE 7 2012 e34302
    • (2012) PLoS ONE , vol.7 , pp. 34302
    • Doerks, T.1    Van Noort, V.2    Minguez, P.3    Bork, P.4
  • 10
    • 77955042462 scopus 로고    scopus 로고
    • From complete genome sequence to 'complete' understanding?
    • M.Y. Galperin, and E.V. Koonin From complete genome sequence to 'complete' understanding? Trends Biotechnol. 28 2010 398 406
    • (2010) Trends Biotechnol. , vol.28 , pp. 398-406
    • Galperin, M.Y.1    Koonin, E.V.2
  • 12
    • 78951489323 scopus 로고    scopus 로고
    • Probing bacterial pathogenesis with genetics, genomics, and chemical biology: Past, present, and future approaches
    • J.E. Gomez, A. Clatworthy, and D.T. Hung Probing bacterial pathogenesis with genetics, genomics, and chemical biology: past, present, and future approaches Crit. Rev. Biochem. Mol. Biol. 46 2011 41 66
    • (2011) Crit. Rev. Biochem. Mol. Biol. , vol.46 , pp. 41-66
    • Gomez, J.E.1    Clatworthy, A.2    Hung, D.T.3
  • 13
  • 14
    • 0037249633 scopus 로고    scopus 로고
    • The TIGRFAMs database of protein families
    • DOI 10.1093/nar/gkg128
    • D.H. Haft, J.D. Selengut, and O. White The TIGRFAMs database of protein families Nucleic Acids Res. 31 2003 371 373 (Pubitemid 36150405)
    • (2003) Nucleic Acids Research , vol.31 , Issue.1 , pp. 371-373
    • Haft, D.H.1    Selengut, J.D.2    White, O.3
  • 15
    • 0031754882 scopus 로고    scopus 로고
    • The anti-sigma factors
    • DOI 10.1146/annurev.micro.52.1.231
    • K.T. Hughes, and K. Mathee The anti-sigma factors Annu. Rev. Microbiol. 52 1998 231 286 (Pubitemid 28481193)
    • (1998) Annual Review of Microbiology , vol.52 , pp. 231-286
    • Hughes, K.T.1    Mathee, K.2
  • 16
    • 0033832615 scopus 로고    scopus 로고
    • Predicting protein function by genomic context: Quantitative evaluation and qualitative inferences
    • M. Huynen, B. Snel, W. Lathe 3rd, and P. Bork Predicting protein function by genomic context: quantitative evaluation and qualitative inferences Genome Res. 10 2000 1204 1210
    • (2000) Genome Res. , vol.10 , pp. 1204-1210
    • Huynen, M.1    Snel, B.2    Lathe III, W.3    Bork, P.4
  • 18
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • L.A. Kelley, and M.J. Sternberg Protein structure prediction on the Web: a case study using the Phyre server Nat. Protoc. 4 2009 363 371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 20
    • 0034530012 scopus 로고    scopus 로고
    • Acyl phosphate esters: Charge-directed acylation and artificial blood
    • R. Kluger Acyl phosphate esters: charge-directed acylation and artificial blood Synlett 12 2000 1708 1720 (Pubitemid 32005583)
    • (2000) Synlett , Issue.12 , pp. 1708-1720
    • Kluger, R.1
  • 23
    • 25144441735 scopus 로고    scopus 로고
    • A non-RD1 gene cluster is required for Snm secretion in Mycobacterium tuberculosis
    • DOI 10.1111/j.1365-2958.2005.04800.x
    • J.A. MacGurn, S. Raghavan, S.A. Stanley, and J.S. Cox A non-RD1 gene cluster is required for Snm secretion in Mycobacterium tuberculosis Mol. Microbiol. 57 2005 1653 1663 (Pubitemid 41337393)
    • (2005) Molecular Microbiology , vol.57 , Issue.6 , pp. 1653-1663
    • MacGurn, J.A.1    Raghavan, S.2    Stanley, S.A.3    Cox, J.S.4
  • 26
    • 82955194511 scopus 로고    scopus 로고
    • The DinB superfamily includes novel mycothiol, bacillithiol, and glutathione S-transferases
    • G.L. Newton, S.S. Leung, J.I. Wakabayashi, M. Rawat, and R.C. Fahey The DinB superfamily includes novel mycothiol, bacillithiol, and glutathione S-transferases Biochemistry 50 2011 10751 10760
    • (2011) Biochemistry , vol.50 , pp. 10751-10760
    • Newton, G.L.1    Leung, S.S.2    Wakabayashi, J.I.3    Rawat, M.4    Fahey, R.C.5
  • 28
    • 34848865681 scopus 로고    scopus 로고
    • Orthologous transcription factors in bacteria have different functions and regulate different genes
    • DOI 10.1371/journal.pcbi.0030175
    • M.N. Price, P.S. Dehal, and A.P. Arkin Orthologous transcription factors in bacteria have different functions and regulate different genes PLoS Comput. Biol. 3 2007 1739 1750 (Pubitemid 47502978)
    • (2007) PLoS Computational Biology , vol.3 , Issue.9 , pp. 1739-1750
    • Price, M.N.1    Dehal, P.S.2    Arkin, A.P.3
  • 29
    • 34547739476 scopus 로고    scopus 로고
    • Probing adenosine nucleotide-binding proteins with an affinity-labeled nucleotide probe and mass spectrometry
    • DOI 10.1021/ac0622375
    • H. Qiu, and Y. Wang Probing adenosine nucleotide-binding proteins with an affinity-labeled nucleotide probe and mass spectrometry Anal. Chem. 79 2007 5547 5556 (Pubitemid 47229799)
    • (2007) Analytical Chemistry , vol.79 , Issue.15 , pp. 5547-5556
    • Qiu, H.1    Wang, Y.2
  • 31
    • 55449113709 scopus 로고    scopus 로고
    • Comparative analyses of fundamental differences in membrane transport capabilities in prokaryotes and eukaryotes
    • Q. Ren, and I.T. Paulsen Comparative analyses of fundamental differences in membrane transport capabilities in prokaryotes and eukaryotes PLoS Comput. Biol. 1 2005 e27
    • (2005) PLoS Comput. Biol. , vol.1 , pp. 27
    • Ren, Q.1    Paulsen, I.T.2
  • 32
    • 0036308741 scopus 로고    scopus 로고
    • Enzyme function less conserved than anticipated
    • DOI 10.1016/S0022-2836(02)00016-5
    • B. Rost Enzyme function less conserved than anticipated J. Mol. Biol. 318 2002 595 608 (Pubitemid 34734850)
    • (2002) Journal of Molecular Biology , vol.318 , Issue.2 , pp. 595-608
    • Rost, B.1
  • 35
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • DOI 10.1046/j.1365-2958.2003.03425.x
    • C.M. Sassetti, D.H. Boyd, and E.J. Rubin Genes required for mycobacterial growth defined by high density mutagenesis Mol. Microbiol. 48 2003 77 84 (Pubitemid 36411469)
    • (2003) Molecular Microbiology , vol.48 , Issue.1 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 38
    • 77951216021 scopus 로고    scopus 로고
    • Activity-based proteomics of enzyme superfamilies: Serine hydrolases as a case study
    • G.M. Simon, and B.F. Cravatt Activity-based proteomics of enzyme superfamilies: serine hydrolases as a case study J. Biol. Chem. 285 2010 11051 11055
    • (2010) J. Biol. Chem. , vol.285 , pp. 11051-11055
    • Simon, G.M.1    Cravatt, B.F.2
  • 39
    • 22244445882 scopus 로고    scopus 로고
    • A tandem orthogonal proteolysis strategy for high-content chemical proteomics
    • DOI 10.1021/ja0532842
    • A.E. Speers, and B.F. Cravatt A tandem orthogonal proteolysis strategy for high-content chemical proteomics J. Am. Chem. Soc. 127 2005 10018 10019 (Pubitemid 40995443)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.28 , pp. 10018-10019
    • Speers, A.E.1    Cravatt, B.F.2
  • 40
    • 0037462106 scopus 로고    scopus 로고
    • Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3 + 2] cycloaddition
    • DOI 10.1021/ja034490h
    • A.E. Speers, G.C. Adam, and B.F. Cravatt Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition J. Am. Chem. Soc. 125 2003 4686 4687 (Pubitemid 36505343)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.16 , pp. 4686-4687
    • Speers, A.E.1    Adam, G.C.2    Cravatt, B.F.3
  • 41
    • 84860575662 scopus 로고    scopus 로고
    • Proteogenomic analysis of bacteria and archaea: A 46 organism case study
    • E. Venter, R.D. Smith, and S.H. Payne Proteogenomic analysis of bacteria and archaea: a 46 organism case study PLoS ONE 6 2011 e27587
    • (2011) PLoS ONE , vol.6 , pp. 27587
    • Venter, E.1    Smith, R.D.2    Payne, S.H.3
  • 42
    • 33646264529 scopus 로고    scopus 로고
    • Advances in proteomics data analysis and display using an accurate mass and time tag approach
    • J.S. Zimmer, M.E. Monroe, W.J. Qian, and R.D. Smith Advances in proteomics data analysis and display using an accurate mass and time tag approach Mass Spectrom. Rev. 25 2006 450 482
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 450-482
    • Zimmer, J.S.1    Monroe, M.E.2    Qian, W.J.3    Smith, R.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.