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Volumn 12, Issue 2, 2013, Pages 844-851

Comprehensive profiling of protein lysine acetylation in Escherichia coli

Author keywords

Escherichia coli (E. coli); lysine acetylation; mass spectrometry (MS); post translational modifications (PTMs)

Indexed keywords

LYSINE;

EID: 84873343462     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr300912q     Document Type: Article
Times cited : (190)

References (29)
  • 1
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. Chromatin modifications and their function Cell 2007, 128 (4) 693-705
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 2
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • Glozak, M. A.; Sengupta, N.; Zhang, X.; Seto, E. Acetylation and deacetylation of non-histone proteins Gene 2005, 363, 15-23
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 4
    • 50049125680 scopus 로고    scopus 로고
    • Strategy for determination of in vitro protein acetylation sites by using isotope-labeled acetyl coenzyme A and liquid chromatography-mass spectrometry
    • Wu, H. Y.; Huang, F. Y.; Chang, Y. C.; Hsieh, M. C.; Liao, P. C. Strategy for determination of in vitro protein acetylation sites by using isotope-labeled acetyl coenzyme A and liquid chromatography-mass spectrometry Anal. Chem. 2008, 80 (16) 6178-89
    • (2008) Anal. Chem. , vol.80 , Issue.16 , pp. 6178-6189
    • Wu, H.Y.1    Huang, F.Y.2    Chang, Y.C.3    Hsieh, M.C.4    Liao, P.C.5
  • 5
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary, C.; Kumar, C.; Gnad, F.; Nielsen, M. L.; Rehman, M.; Walther, T. C.; Olsen, J. V.; Mann, M. Lysine acetylation targets protein complexes and co-regulates major cellular functions Science 2009, 325 (5942) 834-40
    • (2009) Science , vol.325 , Issue.5942 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6    Olsen, J.V.7    Mann, M.8
  • 6
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: Codified crosstalk with other posttranslational modifications
    • Yang, X. J.; Seto, E. Lysine acetylation: codified crosstalk with other posttranslational modifications Mol. Cell 2008, 31 (4) 449-61
    • (2008) Mol. Cell , vol.31 , Issue.4 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 13
    • 77954013335 scopus 로고    scopus 로고
    • Bacterial protein acetylation: The dawning of a new age
    • Hu, L. I.; Lima, B. P.; Wolfe, A. J. Bacterial protein acetylation: the dawning of a new age Mol. Microbiol. 2010, 77 (1) 15-21
    • (2010) Mol. Microbiol. , vol.77 , Issue.1 , pp. 15-21
    • Hu, L.I.1    Lima, B.P.2    Wolfe, A.J.3
  • 14
    • 80053595149 scopus 로고    scopus 로고
    • Acetylation regulates the stability of a bacterial protein: Growth stage-dependent modification of RNase R
    • Liang, W.; Malhotra, A.; Deutscher, M. P. Acetylation regulates the stability of a bacterial protein: growth stage-dependent modification of RNase R Mol. Cell 2011, 44 (1) 160-6
    • (2011) Mol. Cell , vol.44 , Issue.1 , pp. 160-166
    • Liang, W.1    Malhotra, A.2    Deutscher, M.P.3
  • 15
    • 61649089277 scopus 로고    scopus 로고
    • Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli
    • Zhang, J.; Sprung, R.; Pei, J.; Tan, X.; Kim, S.; Zhu, H.; Liu, C. F.; Grishin, N. V.; Zhao, Y. Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli Mol. Cell. Proteomics 2009, 8 (2) 215-25
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.2 , pp. 215-225
    • Zhang, J.1    Sprung, R.2    Pei, J.3    Tan, X.4    Kim, S.5    Zhu, H.6    Liu, C.F.7    Grishin, N.V.8    Zhao, Y.9
  • 16
    • 33845461566 scopus 로고    scopus 로고
    • A clean, more efficient method for in-solution digestion of protein mixtures without detergent or urea
    • Kim, S. C.; Chen, Y.; Mirza, S.; Xu, Y.; Lee, J.; Liu, P.; Zhao, Y. A clean, more efficient method for in-solution digestion of protein mixtures without detergent or urea J. Proteome Res. 2006, 5 (12) 3446-52
    • (2006) J. Proteome Res. , vol.5 , Issue.12 , pp. 3446-3452
    • Kim, S.C.1    Chen, Y.2    Mirza, S.3    Xu, Y.4    Lee, J.5    Liu, P.6    Zhao, Y.7
  • 17
    • 78650516004 scopus 로고    scopus 로고
    • Identification of lysine succinylation as a new post-translational modification
    • Zhang, Z.; Tan, M.; Xie, Z.; Dai, L.; Chen, Y.; Zhao, Y. Identification of lysine succinylation as a new post-translational modification Nat. Chem. Biol. 2011, 7 (1) 58-63
    • (2011) Nat. Chem. Biol. , vol.7 , Issue.1 , pp. 58-63
    • Zhang, Z.1    Tan, M.2    Xie, Z.3    Dai, L.4    Chen, Y.5    Zhao, Y.6
  • 19
    • 39749166860 scopus 로고    scopus 로고
    • Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation
    • Macek, B.; Gnad, F.; Soufi, B.; Kumar, C.; Olsen, J. V.; Mijakovic, I.; Mann, M. Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation Mol. Cell. Proteomics 2008, 7 (2) 299-307
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.2 , pp. 299-307
    • MacEk, B.1    Gnad, F.2    Soufi, B.3    Kumar, C.4    Olsen, J.V.5    Mijakovic, I.6    Mann, M.7
  • 21
    • 0028854123 scopus 로고
    • Site-directed mutagenesis of cysteine-195 in isocitrate lyase from Escherichia coli ML308
    • Robertson, A. G.; Nimmo, H. G. Site-directed mutagenesis of cysteine-195 in isocitrate lyase from Escherichia coli ML308 Biochem. J. 1995, 305 (Pt 1) 239-44
    • (1995) Biochem. J. , vol.305 , Issue.PART 1 , pp. 239-244
    • Robertson, A.G.1    Nimmo, H.G.2
  • 22
    • 11844292767 scopus 로고    scopus 로고
    • MRNA helicase activity of the ribosome
    • Takyar, S.; Hickerson, R. P.; Noller, H. F. mRNA helicase activity of the ribosome Cell 2005, 120 (1) 49-58
    • (2005) Cell , vol.120 , Issue.1 , pp. 49-58
    • Takyar, S.1    Hickerson, R.P.2    Noller, H.F.3
  • 23
    • 28544436370 scopus 로고    scopus 로고
    • Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human RNA polymerase II
    • Meka, H.; Werner, F.; Cordell, S. C.; Onesti, S.; Brick, P. Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human RNA polymerase II Nucleic Acids Res. 2005, 33 (19) 6435-44
    • (2005) Nucleic Acids Res. , vol.33 , Issue.19 , pp. 6435-6444
    • Meka, H.1    Werner, F.2    Cordell, S.C.3    Onesti, S.4    Brick, P.5
  • 25
    • 0033120903 scopus 로고    scopus 로고
    • The structural basis for terminator recognition by the Rho transcription termination factor
    • Bogden, C. E.; Fass, D.; Bergman, N.; Nichols, M. D.; Berger, J. M. The structural basis for terminator recognition by the Rho transcription termination factor Mol. Cell 1999, 3 (4) 487-93
    • (1999) Mol. Cell , vol.3 , Issue.4 , pp. 487-493
    • Bogden, C.E.1    Fass, D.2    Bergman, N.3    Nichols, M.D.4    Berger, J.M.5
  • 26
    • 77955156087 scopus 로고    scopus 로고
    • Lysine acetylation: The tale of a modification from transcription regulation to metabolism
    • Arif, M.; Selvi, B. R.; Kundu, T. K. Lysine acetylation: the tale of a modification from transcription regulation to metabolism ChemBioChem 2010, 11 (11) 1501-4
    • (2010) ChemBioChem , vol.11 , Issue.11 , pp. 1501-1504
    • Arif, M.1    Selvi, B.R.2    Kundu, T.K.3
  • 27
    • 77953669993 scopus 로고    scopus 로고
    • Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease
    • Ye, H.; Rouault, T. A. Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease Biochemistry 2010, 49 (24) 4945-56
    • (2010) Biochemistry , vol.49 , Issue.24 , pp. 4945-4956
    • Ye, H.1    Rouault, T.A.2
  • 28
    • 84864835959 scopus 로고    scopus 로고
    • Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity
    • Kim, E. Y.; Kim, W. K.; Kang, H. J.; Kim, J. H.; Chung, S. J.; Seo, Y. S.; Park, S. G.; Lee, S. C.; Bae, K. H. Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity J. Lipid Res. 2012, 53 (9) 1864-76
    • (2012) J. Lipid Res. , vol.53 , Issue.9 , pp. 1864-1876
    • Kim, E.Y.1    Kim, W.K.2    Kang, H.J.3    Kim, J.H.4    Chung, S.J.5    Seo, Y.S.6    Park, S.G.7    Lee, S.C.8    Bae, K.H.9
  • 29
    • 0037795745 scopus 로고    scopus 로고
    • The oxidative pentose phosphate pathway: Structure and organisation
    • Kruger, N. J.; von Schaewen, A. The oxidative pentose phosphate pathway: structure and organisation Curr. Opin. Plant Biol. 2003, 6 (3) 236-46
    • (2003) Curr. Opin. Plant Biol. , vol.6 , Issue.3 , pp. 236-246
    • Kruger, N.J.1    Von Schaewen, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.