메뉴 건너뛰기




Volumn 97, Issue , 2014, Pages 265-286

Beyond gene expression: The impact of protein post-translational modifications in bacteria

Author keywords

Bacterial signalling; Mass spectrometry; Peptide enrichment; Post translational modifications

Indexed keywords

ARGININE; ASPARTIC ACID; BACTERIAL PROTEIN; CYSTEINE; HISTIDINE; PROTEINASE; SERINE; THREONINE; TYROSINE;

EID: 84892876508     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.08.012     Document Type: Review
Times cited : (149)

References (282)
  • 1
    • 0036127088 scopus 로고    scopus 로고
    • Campylobacter protein glycosylation affects host cell interactions
    • Szymanski C.M., Burr D.H., Guerry P. Campylobacter protein glycosylation affects host cell interactions. Infect Immun 2002, 70:2242-2244.
    • (2002) Infect Immun , vol.70 , pp. 2242-2244
    • Szymanski, C.M.1    Burr, D.H.2    Guerry, P.3
  • 2
    • 47249127304 scopus 로고    scopus 로고
    • Biochemical and mutational analyses of AcuA, the acetyltransferase enzyme that controls the activity of the acetyl coenzyme A synthetase (AcsA) in Bacillus subtilis
    • Gardner J.G., Escalante-Semerena J.C. Biochemical and mutational analyses of AcuA, the acetyltransferase enzyme that controls the activity of the acetyl coenzyme A synthetase (AcsA) in Bacillus subtilis. J Bacteriol 2008, 190:5132-5136.
    • (2008) J Bacteriol , vol.190 , pp. 5132-5136
    • Gardner, J.G.1    Escalante-Semerena, J.C.2
  • 3
    • 79953174969 scopus 로고    scopus 로고
    • Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-Linked glycoproteome of Campylobacter jejuni
    • [M000031MCP201]
    • Scott N.E., Parker B.L., Connolly A.M., Paulech J., Edwards A.V., Crossett B., et al. Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-Linked glycoproteome of Campylobacter jejuni. Mol Cell Proteomics 2011, 10. [M000031MCP201].
    • (2011) Mol Cell Proteomics , vol.10
    • Scott, N.E.1    Parker, B.L.2    Connolly, A.M.3    Paulech, J.4    Edwards, A.V.5    Crossett, B.6
  • 4
    • 84857642951 scopus 로고    scopus 로고
    • Evidence for a new post-translational modification in Staphylococcus aureus: hydroxymethylation of asparagine and glutamine
    • Waridel P., Ythier M., Gfeller A., Moreillon P., Quadroni M. Evidence for a new post-translational modification in Staphylococcus aureus: hydroxymethylation of asparagine and glutamine. J Proteomics 2012, 75:1742-1751.
    • (2012) J Proteomics , vol.75 , pp. 1742-1751
    • Waridel, P.1    Ythier, M.2    Gfeller, A.3    Moreillon, P.4    Quadroni, M.5
  • 5
    • 79954439899 scopus 로고    scopus 로고
    • Focus on phosphoaspartate and phosphoglutamate
    • Attwood P.V., Besant P.G., Piggott M.J. Focus on phosphoaspartate and phosphoglutamate. Amino Acids 2011, 40:1035-1051.
    • (2011) Amino Acids , vol.40 , pp. 1035-1051
    • Attwood, P.V.1    Besant, P.G.2    Piggott, M.J.3
  • 6
    • 79960127921 scopus 로고    scopus 로고
    • Phosphorylation of basic amino acid residues in proteins: Important but easily missed
    • Ciesla J., Fraczyk T., Rode W. Phosphorylation of basic amino acid residues in proteins: Important but easily missed. Acta Biochim Pol 2011, 58:137-147.
    • (2011) Acta Biochim Pol , vol.58 , pp. 137-147
    • Ciesla, J.1    Fraczyk, T.2    Rode, W.3
  • 7
    • 63049113651 scopus 로고    scopus 로고
    • Analytical strategies for phosphoproteomics
    • Thingholm T.E., Jensen O.N., Larsen M.R. Analytical strategies for phosphoproteomics. Proteomics 2009, 9:1451-1468.
    • (2009) Proteomics , vol.9 , pp. 1451-1468
    • Thingholm, T.E.1    Jensen, O.N.2    Larsen, M.R.3
  • 8
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen M.R., Thingholm T.E., Jensen O.N., Roepstorff P., Jorgensen T.J.D. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol Cell Proteomics 2005, 4:873-886.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.D.5
  • 9
    • 27744563093 scopus 로고    scopus 로고
    • State-of-the-art in phosphoproteomics
    • Reinders J., Sickmann A. State-of-the-art in phosphoproteomics. Proteomics 2005, 5:4052-4061.
    • (2005) Proteomics , vol.5 , pp. 4052-4061
    • Reinders, J.1    Sickmann, A.2
  • 11
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., et al. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127:635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6
  • 12
    • 34247325212 scopus 로고    scopus 로고
    • The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis
    • Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., et al. The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol Cell Proteomics 2007, 6:697-707.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 697-707
    • Macek, B.1    Mijakovic, I.2    Olsen, J.V.3    Gnad, F.4    Kumar, C.5    Jensen, P.R.6
  • 13
    • 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., et al. Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol Cell Proteomics 2008, 7:299-307.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 299-307
    • Macek, B.1    Gnad, F.2    Soufi, B.3    Kumar, C.4    Olsen, J.V.5    Mijakovic, I.6
  • 14
    • 79953712602 scopus 로고    scopus 로고
    • Phosphoproteome analysis of the pathogenic bacterium Helicobacter pylori reveals over-representation of tyrosine phosphorylation and multiply phosphorylated proteins
    • Ge R.G., Sun X.S., Xiao C.L., Yin X.F., Shan W.R., Chen Z., et al. Phosphoproteome analysis of the pathogenic bacterium Helicobacter pylori reveals over-representation of tyrosine phosphorylation and multiply phosphorylated proteins. Proteomics 2011, 11:1449-1461.
    • (2011) Proteomics , vol.11 , pp. 1449-1461
    • Ge, R.G.1    Sun, X.S.2    Xiao, C.L.3    Yin, X.F.4    Shan, W.R.5    Chen, Z.6
  • 15
    • 75149190104 scopus 로고    scopus 로고
    • Phosphoproteomics of Klebsiella pneumoniae NTUH-K2044 reveals a tight link between tyrosine phosphorylation and virulence
    • Lin M.H., Hsu T.L., Lin S.Y., Pan Y.J., Jan J.T., Wang J.T., et al. Phosphoproteomics of Klebsiella pneumoniae NTUH-K2044 reveals a tight link between tyrosine phosphorylation and virulence. Mol Cell Proteomics 2009, 8:2613-2623.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2613-2623
    • Lin, M.H.1    Hsu, T.L.2    Lin, S.Y.3    Pan, Y.J.4    Jan, J.T.5    Wang, J.T.6
  • 16
    • 52649125713 scopus 로고    scopus 로고
    • The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins
    • Soufi B., Gnad F., Jensen P.R., Petranovic D., Mann M., Mijakovic I., et al. The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins. Proteomics 2008, 8:3486-3493.
    • (2008) Proteomics , vol.8 , pp. 3486-3493
    • Soufi, B.1    Gnad, F.2    Jensen, P.R.3    Petranovic, D.4    Mann, M.5    Mijakovic, I.6
  • 17
    • 76449114765 scopus 로고    scopus 로고
    • High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans
    • Cao X.J., Dai J., Xu H., Nie S., Chang X., Hu B.Y., et al. High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans. Cell Res 2010, 20:197-210.
    • (2010) Cell Res , vol.20 , pp. 197-210
    • Cao, X.J.1    Dai, J.2    Xu, H.3    Nie, S.4    Chang, X.5    Hu, B.Y.6
  • 18
    • 77952132933 scopus 로고    scopus 로고
    • Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases
    • Prisic S., Dankwa S., Schwartz D., Chou M.F., Locasale J.W., Kang C.M., et al. Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases. Proc Natl Acad Sci U S A 2010, 107:7521-7526.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 7521-7526
    • Prisic, S.1    Dankwa, S.2    Schwartz, D.3    Chou, M.F.4    Locasale, J.W.5    Kang, C.M.6
  • 20
    • 66449094321 scopus 로고    scopus 로고
    • Ser/Thr/Tyr phosphoproteome analysis of pathogenic and non-pathogenic Pseudomonas species
    • Ravichandran A., Sugiyama N., Tomita M., Swarup S., Ishihama Y. Ser/Thr/Tyr phosphoproteome analysis of pathogenic and non-pathogenic Pseudomonas species. Proteomics 2009, 9:2764-2775.
    • (2009) Proteomics , vol.9 , pp. 2764-2775
    • Ravichandran, A.1    Sugiyama, N.2    Tomita, M.3    Swarup, S.4    Ishihama, Y.5
  • 21
    • 84868320346 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of Rhodopseudomonas palustris reveals the role of pyruvate phosphate dikinase phosphorylation in lipid production
    • Hu C.W., Lin M.H., Huang H.C., Ku W.C., Yi T.H., Tsai C.F., et al. Phosphoproteomic analysis of Rhodopseudomonas palustris reveals the role of pyruvate phosphate dikinase phosphorylation in lipid production. J Proteome Res 2012, 11:5362-5375.
    • (2012) J Proteome Res , vol.11 , pp. 5362-5375
    • Hu, C.W.1    Lin, M.H.2    Huang, H.C.3    Ku, W.C.4    Yi, T.H.5    Tsai, C.F.6
  • 22
    • 73649133664 scopus 로고    scopus 로고
    • Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae
    • Sun X.S., Ge F., Xiao C.L., Yin X.F., Ge R.G., Zhang L.H., et al. Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae. J Proteome Res 2010, 9:275-282.
    • (2010) J Proteome Res , vol.9 , pp. 275-282
    • Sun, X.S.1    Ge, F.2    Xiao, C.L.3    Yin, X.F.4    Ge, R.G.5    Zhang, L.H.6
  • 23
    • 82755198873 scopus 로고    scopus 로고
    • Phosphoproteome analysis of Streptomyces development reveals extensive protein phosphorylation accompanying bacterial differentiation
    • Manteca A., Ye J., Sanchez J., Jensen O.N. Phosphoproteome analysis of Streptomyces development reveals extensive protein phosphorylation accompanying bacterial differentiation. J Proteome Res 2011, 10:5481-5492.
    • (2011) J Proteome Res , vol.10 , pp. 5481-5492
    • Manteca, A.1    Ye, J.2    Sanchez, J.3    Jensen, O.N.4
  • 24
    • 37049007689 scopus 로고    scopus 로고
    • The cytoplasmic phosphoproteome of the Gram-negative bacterium Campylobacter jejuni: evidence for modification by unidentified protein kinases
    • Voisin S., Watson D.C., Tessier L., Ding W., Foote S., Bhatia S., et al. The cytoplasmic phosphoproteome of the Gram-negative bacterium Campylobacter jejuni: evidence for modification by unidentified protein kinases. Proteomics 2007, 7:4338-4348.
    • (2007) Proteomics , vol.7 , pp. 4338-4348
    • Voisin, S.1    Watson, D.C.2    Tessier, L.3    Ding, W.4    Foote, S.5    Bhatia, S.6
  • 26
    • 77953160473 scopus 로고    scopus 로고
    • The phosphoproteome of the minimal bacterium Mycoplasma pneumoniae: Analysis of the complete known Ser/Thr kinome suggests the existence of novel kinases
    • Schmidl S.R., Gronau K., Pietack N., Hecker M., Becher D., Stulke J. The phosphoproteome of the minimal bacterium Mycoplasma pneumoniae: Analysis of the complete known Ser/Thr kinome suggests the existence of novel kinases. Mol Cell Proteomics 2010, 9:1228-1242.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1228-1242
    • Schmidl, S.R.1    Gronau, K.2    Pietack, N.3    Hecker, M.4    Becher, D.5    Stulke, J.6
  • 28
    • 0043162014 scopus 로고    scopus 로고
    • Protein PknE, a novel transmembrane eukaryotic-like serine/threonine kinase from Mycobacterium tuberculosis
    • Molle V., Girard-Blanc C., Kremer L., Doublet P., Cozzone A.J., Prost J.F. Protein PknE, a novel transmembrane eukaryotic-like serine/threonine kinase from Mycobacterium tuberculosis. Biochem Biophys Res Commun 2003, 308:820-825.
    • (2003) Biochem Biophys Res Commun , vol.308 , pp. 820-825
    • Molle, V.1    Girard-Blanc, C.2    Kremer, L.3    Doublet, P.4    Cozzone, A.J.5    Prost, J.F.6
  • 29
    • 69249225578 scopus 로고    scopus 로고
    • Tyrosine-kinases in bacteria: from a matter of controversy to the status of key regulatory enzymes
    • Bechet E., Guiral S., Torres S., Mijakovic I., Cozzone A.J., Grangeasse C. Tyrosine-kinases in bacteria: from a matter of controversy to the status of key regulatory enzymes. Amino Acids 2009, 37:499-507.
    • (2009) Amino Acids , vol.37 , pp. 499-507
    • Bechet, E.1    Guiral, S.2    Torres, S.3    Mijakovic, I.4    Cozzone, A.J.5    Grangeasse, C.6
  • 31
    • 84864271151 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and bacterial virulence
    • Whitmore S.E., Lamont R.J. Tyrosine phosphorylation and bacterial virulence. Int J Oral Sci 2012, 4:1-6.
    • (2012) Int J Oral Sci , vol.4 , pp. 1-6
    • Whitmore, S.E.1    Lamont, R.J.2
  • 32
    • 84865095336 scopus 로고    scopus 로고
    • Bacterial tyrosine kinases: evolution, biological function and structural insights
    • Grangeasse C., Nessler S., Mijakovic I. Bacterial tyrosine kinases: evolution, biological function and structural insights. Philos Trans R Soc B 2012, 367:2640-2655.
    • (2012) Philos Trans R Soc B , vol.367 , pp. 2640-2655
    • Grangeasse, C.1    Nessler, S.2    Mijakovic, I.3
  • 33
    • 84863006375 scopus 로고    scopus 로고
    • Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis
    • Dago A.E., Schug A., Procaccini A., Hoch J.A., Weigt M., Szurmant H. Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis. Proc Natl Acad Sci U S A 2012, 109:E1733-E1742.
    • (2012) Proc Natl Acad Sci U S A , vol.109
    • Dago, A.E.1    Schug, A.2    Procaccini, A.3    Hoch, J.A.4    Weigt, M.5    Szurmant, H.6
  • 35
    • 84856158810 scopus 로고    scopus 로고
    • Chasing phosphohistidine, an elusive sibling in the phosphoamino acid family
    • Kee J.M., Muir T.W. Chasing phosphohistidine, an elusive sibling in the phosphoamino acid family. ACS Chem Biol 2012, 7:44-51.
    • (2012) ACS Chem Biol , vol.7 , pp. 44-51
    • Kee, J.M.1    Muir, T.W.2
  • 36
    • 84861864686 scopus 로고    scopus 로고
    • Activity-based probe for histidine kinase signaling
    • Wilke K.E., Francis S., Carlson E.E. Activity-based probe for histidine kinase signaling. J Am Chem Soc 2012, 134:9150-9153.
    • (2012) J Am Chem Soc , vol.134 , pp. 9150-9153
    • Wilke, K.E.1    Francis, S.2    Carlson, E.E.3
  • 39
    • 66749180668 scopus 로고    scopus 로고
    • McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR
    • Fuhrmann J., Schmidt A., Spiess S., Lehner A., Turgay K., Mechtler K., et al. McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR. Science 2009, 324:1323-1327.
    • (2009) Science , vol.324 , pp. 1323-1327
    • Fuhrmann, J.1    Schmidt, A.2    Spiess, S.3    Lehner, A.4    Turgay, K.5    Mechtler, K.6
  • 40
  • 41
    • 84866550022 scopus 로고    scopus 로고
    • Protein cysteine phosphorylation of SarA/MgrA family transcriptional regulators mediates bacterial virulence and antibiotic resistance
    • Sun F., Ding Y., Ji Q.J., Liang Z.J., Deng X., Wong C.C.L., et al. Protein cysteine phosphorylation of SarA/MgrA family transcriptional regulators mediates bacterial virulence and antibiotic resistance. Proc Natl Acad Sci U S A 2012, 109:15461-15466.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 15461-15466
    • Sun, F.1    Ding, Y.2    Ji, Q.J.3    Liang, Z.J.4    Deng, X.5    Wong, C.C.L.6
  • 42
    • 33750230997 scopus 로고    scopus 로고
    • An oxidation-sensing mechanism is used by the global regulator MgrA in Staphylococcus aureus
    • Chen P.R., Bae T., Williams W.A., Duguid E.M., Rice P.A., Schneewind O., et al. An oxidation-sensing mechanism is used by the global regulator MgrA in Staphylococcus aureus. Nat Chem Biol 2006, 2:591-595.
    • (2006) Nat Chem Biol , vol.2 , pp. 591-595
    • Chen, P.R.1    Bae, T.2    Williams, W.A.3    Duguid, E.M.4    Rice, P.A.5    Schneewind, O.6
  • 43
    • 58149105545 scopus 로고    scopus 로고
    • A new oxidative sensing and regulation pathway mediated by the MgrA homologue SarZ in Staphylococcus aureus
    • Chen P.R., Nishida S., Poor C.B., Cheng A., Bae T., Kuechenmeister L., et al. A new oxidative sensing and regulation pathway mediated by the MgrA homologue SarZ in Staphylococcus aureus. Mol Microbiol 2009, 71:198-211.
    • (2009) Mol Microbiol , vol.71 , pp. 198-211
    • Chen, P.R.1    Nishida, S.2    Poor, C.B.3    Cheng, A.4    Bae, T.5    Kuechenmeister, L.6
  • 44
    • 72049090645 scopus 로고    scopus 로고
    • Staphylococcus aureus SarA is a regulatory protein responsive to redox and pH that can support bacteriophage lambda integrase-mediated excision/recombination
    • Fujimoto D.F., Higginbotham R.H., Sterba K.M., Maleki S.J., Segall A.M., Smeltzer M.S., et al. Staphylococcus aureus SarA is a regulatory protein responsive to redox and pH that can support bacteriophage lambda integrase-mediated excision/recombination. Mol Microbiol 2009, 74:1445-1458.
    • (2009) Mol Microbiol , vol.74 , pp. 1445-1458
    • Fujimoto, D.F.1    Higginbotham, R.H.2    Sterba, K.M.3    Maleki, S.J.4    Segall, A.M.5    Smeltzer, M.S.6
  • 45
    • 0007852927 scopus 로고
    • Presence of acetyl groups in histones
    • Phillips D.M. Presence of acetyl groups in histones. Biochem J 1963, 87:258-263.
    • (1963) Biochem J , vol.87 , pp. 258-263
    • Phillips, D.M.1
  • 48
    • 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., et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009, 325:834-840.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6
  • 49
    • 32344453899 scopus 로고    scopus 로고
    • Mass spectrometric characterization of human histone H3: a bird's eye view
    • Thomas C.E., Kelleher N.L., Mizzen C.A. Mass spectrometric characterization of human histone H3: a bird's eye view. J Proteome Res 2006, 5:240-247.
    • (2006) J Proteome Res , vol.5 , pp. 240-247
    • Thomas, C.E.1    Kelleher, N.L.2    Mizzen, C.A.3
  • 50
    • 61649089277 scopus 로고    scopus 로고
    • Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli
    • Zhang J.M., Sprung R., Pei J.M., Tan X.H., Kim S., Zhu H., et al. Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics 2009, 8:215-225.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 215-225
    • Zhang, J.M.1    Sprung, R.2    Pei, J.M.3    Tan, X.H.4    Kim, S.5    Zhu, H.6
  • 51
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang Q., Zhang Y., Yang C., Xiong H., Lin Y., Yao J., et al. Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 2010, 327:1004-1007.
    • (2010) Science , vol.327 , pp. 1004-1007
    • Wang, Q.1    Zhang, Y.2    Yang, C.3    Xiong, H.4    Lin, Y.5    Yao, J.6
  • 52
    • 0034996629 scopus 로고    scopus 로고
    • Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis
    • Barak R., Eisenbach M. Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis. Mol Microbiol 2001, 40:731-743.
    • (2001) Mol Microbiol , vol.40 , pp. 731-743
    • Barak, R.1    Eisenbach, M.2
  • 54
    • 84860868848 scopus 로고    scopus 로고
    • System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases
    • Crosby H.A., Pelletier D.A., Hurst G.B., Escalante-Semerena J.C. System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. J Biol Chem 2012, 287:15590-15601.
    • (2012) J Biol Chem , vol.287 , pp. 15590-15601
    • Crosby, H.A.1    Pelletier, D.A.2    Hurst, G.B.3    Escalante-Semerena, J.C.4
  • 55
    • 79960318555 scopus 로고    scopus 로고
    • Protein acetylation in prokaryotes increases stress resistance
    • Ma Q., Wood T.K. Protein acetylation in prokaryotes increases stress resistance. Biochem Biophys Res Commun 2011, 410:846-851.
    • (2011) Biochem Biophys Res Commun , vol.410 , pp. 846-851
    • Ma, Q.1    Wood, T.K.2
  • 56
    • 3242788065 scopus 로고    scopus 로고
    • Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica
    • Starai V.J., Escalante-Semerena J.C. Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica. J Mol Biol 2004, 340:1005-1012.
    • (2004) J Mol Biol , vol.340 , pp. 1005-1012
    • Starai, V.J.1    Escalante-Semerena, J.C.2
  • 57
    • 79953058855 scopus 로고    scopus 로고
    • In Salmonella enterica, the sirtuin-dependent protein acylation/deacylation system (SDPADS) maintains energy homeostasis during growth on low concentrations of acetate
    • Chan C.H., Garrity J., Crosby H.A., Escalante-Semerena J.C. In Salmonella enterica, the sirtuin-dependent protein acylation/deacylation system (SDPADS) maintains energy homeostasis during growth on low concentrations of acetate. Mol Microbiol 2011, 80:168-183.
    • (2011) Mol Microbiol , vol.80 , pp. 168-183
    • Chan, C.H.1    Garrity, J.2    Crosby, H.A.3    Escalante-Semerena, J.C.4
  • 59
    • 63049137277 scopus 로고    scopus 로고
    • In Bacillus subtilis, the sirtuin protein deacetylase, encoded by the srtN gene (formerly yhdZ), and functions encoded by the acuABC genes control the activity of acetyl coenzyme A synthetase
    • Gardner J.G., Escalante-Semerena J.C. In Bacillus subtilis, the sirtuin protein deacetylase, encoded by the srtN gene (formerly yhdZ), and functions encoded by the acuABC genes control the activity of acetyl coenzyme A synthetase. J Bacteriol 2009, 191:1749-1755.
    • (2009) J Bacteriol , vol.191 , pp. 1749-1755
    • Gardner, J.G.1    Escalante-Semerena, J.C.2
  • 60
    • 77952222270 scopus 로고    scopus 로고
    • ε-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris
    • ε-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris. Mol Microbiol 2010, 76:874-888.
    • (2010) Mol Microbiol , vol.76 , pp. 874-888
    • Crosby, H.A.1    Heiniger, E.K.2    Harwood, C.S.3    Escalante-Semerena, J.C.4
  • 61
    • 80455129274 scopus 로고    scopus 로고
    • Purification and characterization of the acetyl-CoA synthetase from Mycobacterium tuberculosis
    • Li R., Gu J., Chen P., Zhang Z.P., Deng J.Y., Zhang X.E. Purification and characterization of the acetyl-CoA synthetase from Mycobacterium tuberculosis. Acta Biochim Biophys Sin (Shanghai) 2011, 43:891-899.
    • (2011) Acta Biochim Biophys Sin (Shanghai) , vol.43 , pp. 891-899
    • Li, R.1    Gu, J.2    Chen, P.3    Zhang, Z.P.4    Deng, J.Y.5    Zhang, X.E.6
  • 63
    • 34247644455 scopus 로고    scopus 로고
    • Analysis of temporal gene expression during Bacillus subtilis spore germination and outgrowth
    • Keijser B.J.F., Ter Beek A., Rauwerda H., Schuren F., Montijn R., van der Spek H., et al. Analysis of temporal gene expression during Bacillus subtilis spore germination and outgrowth. J Bacteriol 2007, 189:3624-3634.
    • (2007) J Bacteriol , vol.189 , pp. 3624-3634
    • Keijser, B.J.F.1    Ter Beek, A.2    Rauwerda, H.3    Schuren, F.4    Montijn, R.5    van der Spek, H.6
  • 64
    • 80051937249 scopus 로고    scopus 로고
    • Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter
    • Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D., Brinsmade S.R., et al. Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter. Mol Microbiol 2011, 81:1190-1204.
    • (2011) Mol Microbiol , vol.81 , pp. 1190-1204
    • Lima, B.P.1    Antelmann, H.2    Gronau, K.3    Chi, B.K.4    Becher, D.5    Brinsmade, S.R.6
  • 65
    • 55949133763 scopus 로고    scopus 로고
    • Rv0802c from Mycobacterium tuberculosis: the first structure of a succinyltransferase with the GNAT fold
    • Vetting M.W., Errey J.C., Blanchard J.S. Rv0802c from Mycobacterium tuberculosis: the first structure of a succinyltransferase with the GNAT fold. Acta Crystallogr Sect F 2008, 64:978-985.
    • (2008) Acta Crystallogr Sect F , vol.64 , pp. 978-985
    • Vetting, M.W.1    Errey, J.C.2    Blanchard, J.S.3
  • 66
    • 1942490112 scopus 로고    scopus 로고
    • A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones
    • Vetting M.W., Magnet S., Nieves E., Roderick S.L., Blanchard J.S. A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones. Chem Biol 2004, 11:565-573.
    • (2004) Chem Biol , vol.11 , pp. 565-573
    • Vetting, M.W.1    Magnet, S.2    Nieves, E.3    Roderick, S.L.4    Blanchard, J.S.5
  • 67
    • 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, 7:58-63.
    • (2011) Nat Chem Biol , vol.7 , pp. 58-63
    • Zhang, Z.1    Tan, M.2    Xie, Z.3    Dai, L.4    Chen, Y.5    Zhao, Y.6
  • 68
    • 83055173304 scopus 로고    scopus 로고
    • The first identification of lysine malonylation substrates and its regulatory enzyme
    • Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., et al. The first identification of lysine malonylation substrates and its regulatory enzyme. Mol Cell Proteomics 2011, 10.
    • (2011) Mol Cell Proteomics , vol.10
    • Peng, C.1    Lu, Z.2    Xie, Z.3    Cheng, Z.4    Chen, Y.5    Tan, M.6
  • 70
    • 0018870981 scopus 로고
    • Ribosomal protein modification in Escherichia coli II. Studies of a mutant lacking the N-terminal acetylation of protein S18
    • Isono K., Isono S. Ribosomal protein modification in Escherichia coli II. Studies of a mutant lacking the N-terminal acetylation of protein S18. Mol Gen Genet 1980, 177:645-651.
    • (1980) Mol Gen Genet , vol.177 , pp. 645-651
    • Isono, K.1    Isono, S.2
  • 71
    • 0018405372 scopus 로고
    • Ribosomal protein modification in Escherichia coli I. Mutant lacking the N-terminal acetylation of protein S5 exhibits thermosensitivity
    • Cumberlidge A.G., Isono K. Ribosomal protein modification in Escherichia coli I. Mutant lacking the N-terminal acetylation of protein S5 exhibits thermosensitivity. J Mol Biol 1979, 131:169-189.
    • (1979) J Mol Biol , vol.131 , pp. 169-189
    • Cumberlidge, A.G.1    Isono, K.2
  • 72
    • 0019793141 scopus 로고
    • Ribosomal protein modification in Escherichia coli III. Studies of mutants lacking an acetylase activity specific for protein L12
    • Isono S., Isono K. Ribosomal protein modification in Escherichia coli III. Studies of mutants lacking an acetylase activity specific for protein L12. Mol Gen Genet 1981, 183:473-477.
    • (1981) Mol Gen Genet , vol.183 , pp. 473-477
    • Isono, S.1    Isono, K.2
  • 73
    • 0024381096 scopus 로고
    • Cloning and molecular characterization of the gene rimL which encodes an enzyme acetylating ribosomal protein L12 of Escherichia coli K12
    • Tanaka S., Matsushita Y., Yoshikawa A., Isono K. Cloning and molecular characterization of the gene rimL which encodes an enzyme acetylating ribosomal protein L12 of Escherichia coli K12. Mol Gen Genet 1989, 217:289-293.
    • (1989) Mol Gen Genet , vol.217 , pp. 289-293
    • Tanaka, S.1    Matsushita, Y.2    Yoshikawa, A.3    Isono, K.4
  • 75
    • 5644237689 scopus 로고    scopus 로고
    • CFP10 discriminates between nonacetylated and acetylated ESAT-6 of Mycobacterium tuberculosis by differential interaction
    • Okkels L.M., Muller E.C., Schmid M., Rosenkrands I., Kaufmann S.H.E., Andersen P., et al. CFP10 discriminates between nonacetylated and acetylated ESAT-6 of Mycobacterium tuberculosis by differential interaction. Proteomics 2004, 4:2954-2960.
    • (2004) Proteomics , vol.4 , pp. 2954-2960
    • Okkels, L.M.1    Muller, E.C.2    Schmid, M.3    Rosenkrands, I.4    Kaufmann, S.H.E.5    Andersen, P.6
  • 76
    • 84859739265 scopus 로고    scopus 로고
    • Novel bacterial lipoprotein structures conserved in low-GC content Gram-positive bacteria are recognized by toll-like receptor 2
    • Kurokawa K., Ryu K.H., Ichikawa R., Masuda A., Kim M.S., Lee H., et al. Novel bacterial lipoprotein structures conserved in low-GC content Gram-positive bacteria are recognized by toll-like receptor 2. J Biol Chem 2012, 287:13170-13181.
    • (2012) J Biol Chem , vol.287 , pp. 13170-13181
    • Kurokawa, K.1    Ryu, K.H.2    Ichikawa, R.3    Masuda, A.4    Kim, M.S.5    Lee, H.6
  • 77
    • 0037462954 scopus 로고    scopus 로고
    • N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins
    • Polevoda B., Sherman F. N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins. J Mol Biol 2003, 325:595-622.
    • (2003) J Mol Biol , vol.325 , pp. 595-622
    • Polevoda, B.1    Sherman, F.2
  • 78
    • 0034711184 scopus 로고    scopus 로고
    • α-terminal acetylation of eukaryotic proteins
    • α-terminal acetylation of eukaryotic proteins. J Biol Chem 2000, 275:36479-36482.
    • (2000) J Biol Chem , vol.275 , pp. 36479-36482
    • Polevoda, B.1    Sherman, F.2
  • 81
    • 84859490749 scopus 로고    scopus 로고
    • Protein N-terminal acetyltransferases: when the start matters
    • Starheim K.K., Gevaert K., Arnesen T. Protein N-terminal acetyltransferases: when the start matters. Trends Biochem Sci 2012, 37:152-161.
    • (2012) Trends Biochem Sci , vol.37 , pp. 152-161
    • Starheim, K.K.1    Gevaert, K.2    Arnesen, T.3
  • 82
    • 0023427972 scopus 로고
    • Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal-proteINS S18 and S5 of Escherichia coli K12
    • Yoshikawa A., Isono S., Sheback A., Isono K. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal-proteINS S18 and S5 of Escherichia coli K12. Mol Gen Genet 1987, 209:481-488.
    • (1987) Mol Gen Genet , vol.209 , pp. 481-488
    • Yoshikawa, A.1    Isono, S.2    Sheback, A.3    Isono, K.4
  • 83
    • 52949119208 scopus 로고    scopus 로고
    • Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for Nα-acetylation of ribosomal protein S18
    • Vetting M.W., Bareich D.C., Yu M., Blanchard J.S. Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for Nα-acetylation of ribosomal protein S18. Protein Sci 2008, 17:1781-1790.
    • (2008) Protein Sci , vol.17 , pp. 1781-1790
    • Vetting, M.W.1    Bareich, D.C.2    Yu, M.3    Blanchard, J.S.4
  • 86
    • 0033578923 scopus 로고    scopus 로고
    • Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector
    • Orth K., Palmer L.E., Bao Z.Q., Stewart S., Rudolph A.E., Bliska J.B., et al. Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector. Science 1999, 285:1920-1923.
    • (1999) Science , vol.285 , pp. 1920-1923
    • Orth, K.1    Palmer, L.E.2    Bao, Z.Q.3    Stewart, S.4    Rudolph, A.E.5    Bliska, J.B.6
  • 87
    • 33744457909 scopus 로고    scopus 로고
    • Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation
    • Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J., et al. Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. Science 2006, 312:1211-1214.
    • (2006) Science , vol.312 , pp. 1211-1214
    • Mukherjee, S.1    Keitany, G.2    Li, Y.3    Wang, Y.4    Ball, H.L.5    Goldsmith, E.J.6
  • 88
    • 0034711403 scopus 로고    scopus 로고
    • Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease
    • Orth K., Xu Z.H., Mudgett M.B., Bao Z.Q., Palmer L.E., Bliska J.B., et al. Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease. Science 2000, 290:1594-1597.
    • (2000) Science , vol.290 , pp. 1594-1597
    • Orth, K.1    Xu, Z.H.2    Mudgett, M.B.3    Bao, Z.Q.4    Palmer, L.E.5    Bliska, J.B.6
  • 89
    • 56449118262 scopus 로고    scopus 로고
    • Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis
    • Pearce M.J., Mintseris J., Ferreyra J., Gygi S.P., Darwin K.H. Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science 2008, 322:1104-1107.
    • (2008) Science , vol.322 , pp. 1104-1107
    • Pearce, M.J.1    Mintseris, J.2    Ferreyra, J.3    Gygi, S.P.4    Darwin, K.H.5
  • 90
    • 77956162428 scopus 로고    scopus 로고
    • Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis
    • Cerda-Maira F.A., Pearce M.J., Fuortes M., Bishai W.R., Hubbard S.R., Darwin K.H. Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis. Mol Microbiol 2010, 77:1123-1135.
    • (2010) Mol Microbiol , vol.77 , pp. 1123-1135
    • Cerda-Maira, F.A.1    Pearce, M.J.2    Fuortes, M.3    Bishai, W.R.4    Hubbard, S.R.5    Darwin, K.H.6
  • 91
    • 77952559910 scopus 로고    scopus 로고
    • Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the side chain of its C-terminal glutamate
    • Sutter M., Damberger F.F., Imkamp F., Allain F.H.T., Weber-Ban E. Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the side chain of its C-terminal glutamate. J Am Chem Soc 2010, 132:5610-5612.
    • (2010) J Am Chem Soc , vol.132 , pp. 5610-5612
    • Sutter, M.1    Damberger, F.F.2    Imkamp, F.3    Allain, F.H.T.4    Weber-Ban, E.5
  • 92
    • 79953005868 scopus 로고    scopus 로고
    • Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated Pup intermediate
    • Guth E., Thommen M., Weber-Ban E. Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated Pup intermediate. J Biol Chem 2011, 286:4412-4419.
    • (2011) J Biol Chem , vol.286 , pp. 4412-4419
    • Guth, E.1    Thommen, M.2    Weber-Ban, E.3
  • 93
    • 78549285675 scopus 로고    scopus 로고
    • "Depupylation" of prokaryotic ubiquitin-like protein from Mycobacterial proteasome substrates
    • Burns K.E., Cerda-Maira F.A., Wang T., Li H.L., Bishai W.R., Darwin K.H. "Depupylation" of prokaryotic ubiquitin-like protein from Mycobacterial proteasome substrates. Mol Cell 2010, 39:821-827.
    • (2010) Mol Cell , vol.39 , pp. 821-827
    • Burns, K.E.1    Cerda-Maira, F.A.2    Wang, T.3    Li, H.L.4    Bishai, W.R.5    Darwin, K.H.6
  • 94
    • 77957231199 scopus 로고    scopus 로고
    • Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway
    • Imkamp F., Striebel F., Sutter M., Ozcelik D., Zimmermann N., Sander P., et al. Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway. EMBO Rep 2010, 11:791-797.
    • (2010) EMBO Rep , vol.11 , pp. 791-797
    • Imkamp, F.1    Striebel, F.2    Sutter, M.3    Ozcelik, D.4    Zimmermann, N.5    Sander, P.6
  • 95
    • 75149113560 scopus 로고    scopus 로고
    • Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo
    • Imkamp F., Rosenberger T., Striebel F., Keller P.M., Amstutz B., Sander P., et al. Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo. Mol Microbiol 2010, 75:744-754.
    • (2010) Mol Microbiol , vol.75 , pp. 744-754
    • Imkamp, F.1    Rosenberger, T.2    Striebel, F.3    Keller, P.M.4    Amstutz, B.5    Sander, P.6
  • 96
    • 77952575956 scopus 로고    scopus 로고
    • Prokaryotic ubiquitin-like protein provides a two-part degron to Mycobacterium proteasome substrates
    • Burns K.E., Pearce M.J., Darwin K.H. Prokaryotic ubiquitin-like protein provides a two-part degron to Mycobacterium proteasome substrates. J Bacteriol 2010, 192:2933-2935.
    • (2010) J Bacteriol , vol.192 , pp. 2933-2935
    • Burns, K.E.1    Pearce, M.J.2    Darwin, K.H.3
  • 97
    • 84858212561 scopus 로고    scopus 로고
    • PupDB: a database of pupylated proteins
    • Tung C.W. PupDB: a database of pupylated proteins. BMC Bioinformatics 2012, 13.
    • (2012) BMC Bioinformatics , pp. 13
    • Tung, C.W.1
  • 98
    • 84858039698 scopus 로고    scopus 로고
    • Activity of the Mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation
    • Delley C.L., Striebel F., Heydenreich F.M., Ozcelik D., Weber-Ban E. Activity of the Mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation. J Biol Chem 2012, 287:7907-7914.
    • (2012) J Biol Chem , vol.287 , pp. 7907-7914
    • Delley, C.L.1    Striebel, F.2    Heydenreich, F.M.3    Ozcelik, D.4    Weber-Ban, E.5
  • 99
    • 79961022536 scopus 로고    scopus 로고
    • Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli
    • Cerda-Maira F.A., McAllister F., Bode N.J., Burns K.E., Gygi S.P., Darwin K.H. Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli. EMBO Rep 2011, 12:863-870.
    • (2011) EMBO Rep , vol.12 , pp. 863-870
    • Cerda-Maira, F.A.1    McAllister, F.2    Bode, N.J.3    Burns, K.E.4    Gygi, S.P.5    Darwin, K.H.6
  • 100
    • 84871050281 scopus 로고    scopus 로고
    • Two protein lysine methyltransferases methylate outer membrane protein B from Rickettsia
    • Abeykoon A.H., Chao C.C., Wang G.H., Gucek M., Yang D.C.H., Ching W.M. Two protein lysine methyltransferases methylate outer membrane protein B from Rickettsia. J Bacteriol 2012, 194:6410-6418.
    • (2012) J Bacteriol , vol.194 , pp. 6410-6418
    • Abeykoon, A.H.1    Chao, C.C.2    Wang, G.H.3    Gucek, M.4    Yang, D.C.H.5    Ching, W.M.6
  • 101
    • 0026249693 scopus 로고
    • Isolation and partial characterization of the M(r) 100kDa protein from Rickettsia prowazekii strains of different virulence
    • Rodionov A.V., Eremeeva M.E., Balayeva N.M. Isolation and partial characterization of the M(r) 100kDa protein from Rickettsia prowazekii strains of different virulence. Acta Virol 1991, 35:557-565.
    • (1991) Acta Virol , vol.35 , pp. 557-565
    • Rodionov, A.V.1    Eremeeva, M.E.2    Balayeva, N.M.3
  • 102
    • 47049130021 scopus 로고    scopus 로고
    • Serological reactivity and biochemical characterization of methylated and unmethylated forms of a recombinant protein fragment derived from outer membrane protein B of Rickettsia typhi
    • Chao C.C., Zhang Z., Wang H., Alkhalil A., Ching W.M. Serological reactivity and biochemical characterization of methylated and unmethylated forms of a recombinant protein fragment derived from outer membrane protein B of Rickettsia typhi. Clin Vaccine Immunol 2008, 15:684-690.
    • (2008) Clin Vaccine Immunol , vol.15 , pp. 684-690
    • Chao, C.C.1    Zhang, Z.2    Wang, H.3    Alkhalil, A.4    Ching, W.M.5
  • 103
    • 82555179173 scopus 로고    scopus 로고
    • Protein dynamics and mechanisms controlling the rotational behaviour of the bacterial flagellar motor
    • Brown M.T., Delalez N.J., Armitage J.P. Protein dynamics and mechanisms controlling the rotational behaviour of the bacterial flagellar motor. Curr Opin Microbiol 2011, 14:734-740.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 734-740
    • Brown, M.T.1    Delalez, N.J.2    Armitage, J.P.3
  • 104
    • 10044252242 scopus 로고    scopus 로고
    • Making sense of it all: bacterial chemotaxis
    • Wadhams G.H., Armitage J.P. Making sense of it all: bacterial chemotaxis. Nat Rev Mol Cell Biol 2004, 5:1024-1037.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 1024-1037
    • Wadhams, G.H.1    Armitage, J.P.2
  • 105
    • 70349797209 scopus 로고    scopus 로고
    • Chemotaxis: how bacteria use memory
    • Vladimirov N., Sourjik V. Chemotaxis: how bacteria use memory. Biol Chem 2009, 390:1097-1104.
    • (2009) Biol Chem , vol.390 , pp. 1097-1104
    • Vladimirov, N.1    Sourjik, V.2
  • 106
    • 0032884359 scopus 로고    scopus 로고
    • Clustering of the chemoreceptor complex in Escherichia coli is independent of the methyltransferase CheR and the methylesterase CheB
    • Lybarger S.R., Maddock J.R. Clustering of the chemoreceptor complex in Escherichia coli is independent of the methyltransferase CheR and the methylesterase CheB. J Bacteriol 1999, 181:5527-5529.
    • (1999) J Bacteriol , vol.181 , pp. 5527-5529
    • Lybarger, S.R.1    Maddock, J.R.2
  • 107
    • 0021755612 scopus 로고
    • In vitro methylation and demethylation of methyl-accepting chemotaxis proteins in Bacillus subtilis
    • Goldman D.J., Ordal G.W. In vitro methylation and demethylation of methyl-accepting chemotaxis proteins in Bacillus subtilis. Biochemistry 1984, 23:2600-2606.
    • (1984) Biochemistry , vol.23 , pp. 2600-2606
    • Goldman, D.J.1    Ordal, G.W.2
  • 108
    • 0020162182 scopus 로고
    • Adaption in bacterial chemotaxis: CheB-dependent modification permits additional methylations of sensory transducer proteins
    • Kehry M.R., Dahlquist F.W. Adaption in bacterial chemotaxis: CheB-dependent modification permits additional methylations of sensory transducer proteins. Cell 1982, 29:761-772.
    • (1982) Cell , vol.29 , pp. 761-772
    • Kehry, M.R.1    Dahlquist, F.W.2
  • 109
    • 0020770030 scopus 로고
    • Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product
    • Kehry M.R., Bond M.W., Hunkapiller M.W., Dahlquist F.W. Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product. P Natl Acad Sci-Biol 1983, 80:3599-3603.
    • (1983) P Natl Acad Sci-Biol , vol.80 , pp. 3599-3603
    • Kehry, M.R.1    Bond, M.W.2    Hunkapiller, M.W.3    Dahlquist, F.W.4
  • 110
    • 0020625453 scopus 로고
    • Multiple covalent modifications of Trg, a sensory transducer of Escherichia coli
    • Kehry M.R., Engstrom P., Dahlquist F.W., Hazelbauer G.L. Multiple covalent modifications of Trg, a sensory transducer of Escherichia coli. J Biol Chem 1983, 258:5050-5055.
    • (1983) J Biol Chem , vol.258 , pp. 5050-5055
    • Kehry, M.R.1    Engstrom, P.2    Dahlquist, F.W.3    Hazelbauer, G.L.4
  • 111
    • 0021112484 scopus 로고
    • Sites of methyl esterification on the aspartate receptor involved in bacterial chemotaxis
    • Terwilliger T.C., Bogonez E., Wang E.A., Koshland D.E. Sites of methyl esterification on the aspartate receptor involved in bacterial chemotaxis. J Biol Chem 1983, 258:9608-9611.
    • (1983) J Biol Chem , vol.258 , pp. 9608-9611
    • Terwilliger, T.C.1    Bogonez, E.2    Wang, E.A.3    Koshland, D.E.4
  • 112
    • 0021279624 scopus 로고
    • Site of methyl esterification and deamination on the aspartate receptor involved in chemotaxis
    • Terwilliger T.C., Koshland D.E. Site of methyl esterification and deamination on the aspartate receptor involved in chemotaxis. J Biol Chem 1984, 259:7719-7725.
    • (1984) J Biol Chem , vol.259 , pp. 7719-7725
    • Terwilliger, T.C.1    Koshland, D.E.2
  • 113
    • 0025883204 scopus 로고
    • Sites of deamidation and methylation in Tsr, a bacterial chemotaxis sensory transducer
    • Rice M.S., Dahlquist F.W. Sites of deamidation and methylation in Tsr, a bacterial chemotaxis sensory transducer. J Biol Chem 1991, 266:9746-9753.
    • (1991) J Biol Chem , vol.266 , pp. 9746-9753
    • Rice, M.S.1    Dahlquist, F.W.2
  • 114
    • 33744745630 scopus 로고    scopus 로고
    • Identification of methylation sites in Thermotoga maritima chemotaxis receptors
    • Perez E., Zheng H., Stock A.M. Identification of methylation sites in Thermotoga maritima chemotaxis receptors. J Bacteriol 2006, 188:4093-4100.
    • (2006) J Bacteriol , vol.188 , pp. 4093-4100
    • Perez, E.1    Zheng, H.2    Stock, A.M.3
  • 115
    • 0032491213 scopus 로고    scopus 로고
    • Activation of methylesterase CheB: evidence of a dual role for the regulatory domain
    • Anand G.S., Goudreau P.N., Stock A.M. Activation of methylesterase CheB: evidence of a dual role for the regulatory domain. Biochemistry 1998, 37:14038-14047.
    • (1998) Biochemistry , vol.37 , pp. 14038-14047
    • Anand, G.S.1    Goudreau, P.N.2    Stock, A.M.3
  • 116
    • 0037188414 scopus 로고    scopus 로고
    • Kinetic basis for the stimulatory effect of phosphorylation on the methylesterase activity of CheB
    • Anand G.S., Stock A.M. Kinetic basis for the stimulatory effect of phosphorylation on the methylesterase activity of CheB. Biochemistry 2002, 41:6752-6760.
    • (2002) Biochemistry , vol.41 , pp. 6752-6760
    • Anand, G.S.1    Stock, A.M.2
  • 117
    • 4344633161 scopus 로고    scopus 로고
    • Targeting of the chemotaxis methylesterase/deamidase CheB to the polar receptor-kinase cluster in an Escherichia coli cell
    • Banno S., Shiomi D., Homma M., Kawagishi I. Targeting of the chemotaxis methylesterase/deamidase CheB to the polar receptor-kinase cluster in an Escherichia coli cell. Mol Microbiol 2004, 53:1051-1063.
    • (2004) Mol Microbiol , vol.53 , pp. 1051-1063
    • Banno, S.1    Shiomi, D.2    Homma, M.3    Kawagishi, I.4
  • 118
    • 0037067781 scopus 로고    scopus 로고
    • Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis
    • Kristich C.J., Ordal G.W. Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis. J Biol Chem 2002, 277:25356-25362.
    • (2002) J Biol Chem , vol.277 , pp. 25356-25362
    • Kristich, C.J.1    Ordal, G.W.2
  • 119
    • 84857757077 scopus 로고    scopus 로고
    • Methylation and in vivo expression of the surface-exposed Leptospira interrogans outer-membrane protein OmpL32
    • Eshghi A., Pinne M., Haake D.A., Zuerner R.L., Frank A., Cameron C.E. Methylation and in vivo expression of the surface-exposed Leptospira interrogans outer-membrane protein OmpL32. Microbiol-SGM 2012, 158:622-635.
    • (2012) Microbiol-SGM , vol.158 , pp. 622-635
    • Eshghi, A.1    Pinne, M.2    Haake, D.A.3    Zuerner, R.L.4    Frank, A.5    Cameron, C.E.6
  • 120
    • 0035807996 scopus 로고    scopus 로고
    • Critical involvement of a carbamylated lysine in catalytic function of class D β-lactamases
    • Golemi D., Maveyraud L., Vakulenko S., Samama J.P., Mobashery S. Critical involvement of a carbamylated lysine in catalytic function of class D β-lactamases. Proc Natl Acad Sci U S A 2001, 98:14280-14285.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14280-14285
    • Golemi, D.1    Maveyraud, L.2    Vakulenko, S.3    Samama, J.P.4    Mobashery, S.5
  • 122
    • 84863837183 scopus 로고    scopus 로고
    • Carboxylation and decarboxylation of active site Lys 84 controls the activity of OXA-24 β-lactamase of Acinetobacter baumannii: Raman crystallographic and solution evidence
    • Che T., Bonomo R.A., Shanmugam S., Bethel C.R., Pusztai-Carey M., Buynak J.D., et al. Carboxylation and decarboxylation of active site Lys 84 controls the activity of OXA-24 β-lactamase of Acinetobacter baumannii: Raman crystallographic and solution evidence. J Am Chem Soc 2012, 134:11206-11215.
    • (2012) J Am Chem Soc , vol.134 , pp. 11206-11215
    • Che, T.1    Bonomo, R.A.2    Shanmugam, S.3    Bethel, C.R.4    Pusztai-Carey, M.5    Buynak, J.D.6
  • 123
    • 0034476988 scopus 로고    scopus 로고
    • Insights into class D β-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa
    • Maveyraud L., Golemi D., Kotra L.P., Tranier S., Vakulenko S., Mobashery S., et al. Insights into class D β-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa. Structure 2000, 8:1289-1298.
    • (2000) Structure , vol.8 , pp. 1289-1298
    • Maveyraud, L.1    Golemi, D.2    Kotra, L.P.3    Tranier, S.4    Vakulenko, S.5    Mobashery, S.6
  • 124
    • 0037216363 scopus 로고    scopus 로고
    • Comparison of β-lactamases of classes A and D: 1.5-Å crystallographic structure of the class D OXA-1 oxacillinase
    • Sun T., Nukaga M., Mayama K., Braswell E.H., Knox J.R. Comparison of β-lactamases of classes A and D: 1.5-Å crystallographic structure of the class D OXA-1 oxacillinase. Protein Sci 2003, 12:82-91.
    • (2003) Protein Sci , vol.12 , pp. 82-91
    • Sun, T.1    Nukaga, M.2    Mayama, K.3    Braswell, E.H.4    Knox, J.R.5
  • 125
    • 0038381513 scopus 로고    scopus 로고
    • Resistance to β-lactam antibiotics and its mediation by the sensor domain of the transmembrane BlaR signaling pathway in Staphylococcus aureus
    • Golemi-Kotra D., Cha J.Y., Meroueh S.O., Vakulenko S.B., Mobashery S. Resistance to β-lactam antibiotics and its mediation by the sensor domain of the transmembrane BlaR signaling pathway in Staphylococcus aureus. J Biol Chem 2003, 278:18419-18425.
    • (2003) J Biol Chem , vol.278 , pp. 18419-18425
    • Golemi-Kotra, D.1    Cha, J.Y.2    Meroueh, S.O.3    Vakulenko, S.B.4    Mobashery, S.5
  • 126
    • 84859588905 scopus 로고    scopus 로고
    • Site-saturation mutagenesis of position V117 in OXA-1 β-lactamase: effect of side chain polarity on enzyme carboxylation and substrate turnover
    • Buchman J.S., Schneider K.D., Lloyd A.R., Pavlish S.L., Leonard D.A. Site-saturation mutagenesis of position V117 in OXA-1 β-lactamase: effect of side chain polarity on enzyme carboxylation and substrate turnover. Biochemistry 2012, 51:3143-3150.
    • (2012) Biochemistry , vol.51 , pp. 3143-3150
    • Buchman, J.S.1    Schneider, K.D.2    Lloyd, A.R.3    Pavlish, S.L.4    Leonard, D.A.5
  • 127
    • 80054821662 scopus 로고    scopus 로고
    • Hydrolytic mechanism of OXA-58 enzyme, a carbapenem-hydrolyzing class D β-lactamase from Acinetobacter baumannii
    • Verma V., Testero S.A., Amini K., Wei W., Liu J., Balachandran N., et al. Hydrolytic mechanism of OXA-58 enzyme, a carbapenem-hydrolyzing class D β-lactamase from Acinetobacter baumannii. J Biol Chem 2011, 286:37292-37303.
    • (2011) J Biol Chem , vol.286 , pp. 37292-37303
    • Verma, V.1    Testero, S.A.2    Amini, K.3    Wei, W.4    Liu, J.5    Balachandran, N.6
  • 128
    • 80052404275 scopus 로고    scopus 로고
    • ζ-decarboxylation switch and activation of the β-Lactam sensor domain of BlaR1 protein of methicillin-resistant Staphylococcus aureus
    • ζ-decarboxylation switch and activation of the β-Lactam sensor domain of BlaR1 protein of methicillin-resistant Staphylococcus aureus. J Biol Chem 2011, 286:31466-31472.
    • (2011) J Biol Chem , vol.286 , pp. 31466-31472
    • Borbulevych, O.1    Kumarasiri, M.2    Wilson, B.3    Llarrull, L.I.4    Lee, M.5    Hesek, D.6
  • 129
    • 34247104129 scopus 로고    scopus 로고
    • ζ-decarboxylation in the BlaR1 protein from Staphylococcus aureus at the root of its function as an antibiotic sensor
    • ζ-decarboxylation in the BlaR1 protein from Staphylococcus aureus at the root of its function as an antibiotic sensor. J Am Chem Soc 2007, 129:3834-3835.
    • (2007) J Am Chem Soc , vol.129 , pp. 3834-3835
    • Cha, J.1    Mobashery, S.2
  • 131
    • 77955571741 scopus 로고    scopus 로고
    • Reversible post-translational carboxylation modulates the enzymatic activity of N-Acetyl-L-ornithine transcarbamylase
    • Li Y.D., Yu X.L., Ho J., Fushman D., Allewell N.M., Tuchman M., et al. Reversible post-translational carboxylation modulates the enzymatic activity of N-Acetyl-L-ornithine transcarbamylase. Biochemistry 2010, 49:6887-6895.
    • (2010) Biochemistry , vol.49 , pp. 6887-6895
    • Li, Y.D.1    Yu, X.L.2    Ho, J.3    Fushman, D.4    Allewell, N.M.5    Tuchman, M.6
  • 132
    • 0029032588 scopus 로고
    • 3-Dimensional structure of the binuclear center of phosphotriesterase
    • Benning M.M., Kuo J.M., Raushel F.M., Holden H.M. 3-Dimensional structure of the binuclear center of phosphotriesterase. Biochemistry 1995, 34:7973-7978.
    • (1995) Biochemistry , vol.34 , pp. 7973-7978
    • Benning, M.M.1    Kuo, J.M.2    Raushel, F.M.3    Holden, H.M.4
  • 133
    • 0037046968 scopus 로고    scopus 로고
    • The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity
    • Abendroth J., Niefind K., May O., Siemann M., Syldatk C., Schomburg D. The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity. Biochemistry 2002, 41:8589-8597.
    • (2002) Biochemistry , vol.41 , pp. 8589-8597
    • Abendroth, J.1    Niefind, K.2    May, O.3    Siemann, M.4    Syldatk, C.5    Schomburg, D.6
  • 134
    • 0037199453 scopus 로고    scopus 로고
    • Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity
    • Cheon Y.H., Kim H.S., Han K.H., Abendroth J., Niefind K., Schomburg D., et al. Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity. Biochemistry 2002, 41:9410-9417.
    • (2002) Biochemistry , vol.41 , pp. 9410-9417
    • Cheon, Y.H.1    Kim, H.S.2    Han, K.H.3    Abendroth, J.4    Niefind, K.5    Schomburg, D.6
  • 135
    • 0038492663 scopus 로고    scopus 로고
    • Crystal structure of D-hydantoinase from Burkholderia pickettii at a resolution of 2.7Å: insights into the molecular basis of enzyme thermostability
    • Xu Z., Liu Y.Q., Yang Y.L., Jiang W.H., Arnold E., Ding J.P. Crystal structure of D-hydantoinase from Burkholderia pickettii at a resolution of 2.7Å: insights into the molecular basis of enzyme thermostability. J Bacteriol 2003, 185:4038-4049.
    • (2003) J Bacteriol , vol.185 , pp. 4038-4049
    • Xu, Z.1    Liu, Y.Q.2    Yang, Y.L.3    Jiang, W.H.4    Arnold, E.5    Ding, J.P.6
  • 136
    • 57149125703 scopus 로고    scopus 로고
    • Effect of metal binding and posttranslational lysine carboxylation on the activity of recombinant hydantoinase
    • Huang C.Y., Hsu C.C., Chen M.C., Yang Y.S. Effect of metal binding and posttranslational lysine carboxylation on the activity of recombinant hydantoinase. J Biol Inorg Chem 2009, 14:111-121.
    • (2009) J Biol Inorg Chem , vol.14 , pp. 111-121
    • Huang, C.Y.1    Hsu, C.C.2    Chen, M.C.3    Yang, Y.S.4
  • 137
    • 79955758350 scopus 로고    scopus 로고
    • Carboxylated lysine is required for higher activities in hydantoinases
    • Kumar V., Saxena N., Sarma M., Kishan K.V.R. Carboxylated lysine is required for higher activities in hydantoinases. Protein Pept Lett 2011, 18:663-669.
    • (2011) Protein Pept Lett , vol.18 , pp. 663-669
    • Kumar, V.1    Saxena, N.2    Sarma, M.3    Kishan, K.V.R.4
  • 138
    • 0029647957 scopus 로고
    • The crystal structure of urease from Klebsiella aerogenes
    • Jabri E., Carr M.B., Hausinger R.P., Karplus P.A. The crystal structure of urease from Klebsiella aerogenes. Science 1995, 268:998-1004.
    • (1995) Science , vol.268 , pp. 998-1004
    • Jabri, E.1    Carr, M.B.2    Hausinger, R.P.3    Karplus, P.A.4
  • 139
    • 0035912842 scopus 로고    scopus 로고
    • Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center
    • Thoden J.B., Phillips G.N., Neal T.M., Raushel F.M., Holden H.M. Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Biochemistry 2001, 40:6989-6997.
    • (2001) Biochemistry , vol.40 , pp. 6989-6997
    • Thoden, J.B.1    Phillips, G.N.2    Neal, T.M.3    Raushel, F.M.4    Holden, H.M.5
  • 142
    • 14144251463 scopus 로고    scopus 로고
    • Molecular structure of D-hydantoinase from Bacillus sp AR9: evidence for mercury inhibition
    • Kishan K.V.R., Vohra R.M., Ganesan K., Sharma V., Sharma R. Molecular structure of D-hydantoinase from Bacillus sp AR9: evidence for mercury inhibition. J Mol Biol 2005, 347:95-105.
    • (2005) J Mol Biol , vol.347 , pp. 95-105
    • Kishan, K.V.R.1    Vohra, R.M.2    Ganesan, K.3    Sharma, V.4    Sharma, R.5
  • 143
    • 0038394520 scopus 로고    scopus 로고
    • Proteases: a primer
    • Hooper N.M. Proteases: a primer. Essays Biochem 2002, 38:1-8.
    • (2002) Essays Biochem , vol.38 , pp. 1-8
    • Hooper, N.M.1
  • 145
    • 84857817395 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics strategies for protease cleavage site identification
    • van den Berg B.H.J., Tholey A. Mass spectrometry-based proteomics strategies for protease cleavage site identification. Proteomics 2012, 12:516-529.
    • (2012) Proteomics , vol.12 , pp. 516-529
    • van den Berg, B.H.J.1    Tholey, A.2
  • 147
    • 52649141086 scopus 로고    scopus 로고
    • Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N-termini
    • Mahrus S., Trinidad J.C., Barkan D.T., Sali A., Burlingame A.L., Wells J.A. Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N-termini. Cell 2008, 134:866-876.
    • (2008) Cell , vol.134 , pp. 866-876
    • Mahrus, S.1    Trinidad, J.C.2    Barkan, D.T.3    Sali, A.4    Burlingame, A.L.5    Wells, J.A.6
  • 148
    • 77749320923 scopus 로고    scopus 로고
    • Isotopic labeling of terminal amines in complex samples identifies protein N-termini and protease cleavage products
    • Kleifeld O., Doucet A., Keller U.A.D., Prudova A., Schilling O., Kainthan R.K., et al. Isotopic labeling of terminal amines in complex samples identifies protein N-termini and protease cleavage products. Nat Biotechnol 2010, 28:281-288.
    • (2010) Nat Biotechnol , vol.28 , pp. 281-288
    • Kleifeld, O.1    Doucet, A.2    Keller, U.A.D.3    Prudova, A.4    Schilling, O.5    Kainthan, R.K.6
  • 149
    • 77954693076 scopus 로고    scopus 로고
    • Proteome-wide analysis of protein carboxy termini: C-terminomics
    • Schilling O., Barre O., Huesgen P.F., Overall C.M. Proteome-wide analysis of protein carboxy termini: C-terminomics. Nat Methods 2010, 7:508-511.
    • (2010) Nat Methods , vol.7 , pp. 508-511
    • Schilling, O.1    Barre, O.2    Huesgen, P.F.3    Overall, C.M.4
  • 150
    • 79551520250 scopus 로고    scopus 로고
    • Selective isolation of N-blocked peptide by combining AspN digestion, transamination, and tosylhydrazine glass treatment
    • Sonomura K., Kuyama H., Matsuo E., Tsunasawa S., Futaki S., Nishimura O. Selective isolation of N-blocked peptide by combining AspN digestion, transamination, and tosylhydrazine glass treatment. Anal Biochem 2011, 410:214-223.
    • (2011) Anal Biochem , vol.410 , pp. 214-223
    • Sonomura, K.1    Kuyama, H.2    Matsuo, E.3    Tsunasawa, S.4    Futaki, S.5    Nishimura, O.6
  • 152
    • 78651069641 scopus 로고    scopus 로고
    • Characterization of the prime and non-prime active site specificities of proteases by proteome-derived peptide libraries and tandem mass spectrometry
    • Schilling O., Huesgen P.F., Barre O., Keller U.A.D., Overall C.M. Characterization of the prime and non-prime active site specificities of proteases by proteome-derived peptide libraries and tandem mass spectrometry. Nat Protoc 2011, 6:111-120.
    • (2011) Nat Protoc , vol.6 , pp. 111-120
    • Schilling, O.1    Huesgen, P.F.2    Barre, O.3    Keller, U.A.D.4    Overall, C.M.5
  • 155
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of Gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • Navarre W.W., Schneewind O. Surface proteins of Gram-positive bacteria and mechanisms of their targeting to the cell wall envelope. Microbiol Mol Biol Rev 1999, 63:174-229.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 156
    • 84862104148 scopus 로고    scopus 로고
    • Bacillus licheniformis BlaR1 L3 loop is a zinc metalloprotease activated by self-proteolysis
    • Berzigotti S., Benlafya K., Sepulchre J., Amoroso A., Joris B. Bacillus licheniformis BlaR1 L3 loop is a zinc metalloprotease activated by self-proteolysis. PLoS One 2012, 7.
    • (2012) PLoS One , vol.7
    • Berzigotti, S.1    Benlafya, K.2    Sepulchre, J.3    Amoroso, A.4    Joris, B.5
  • 157
    • 84862167966 scopus 로고    scopus 로고
    • Dissection of events in the resistance to β-lactam antibiotics mediated by the protein BlaR1 from Staphylococcus aureus
    • Llarrull L.I., Mobashery S. Dissection of events in the resistance to β-lactam antibiotics mediated by the protein BlaR1 from Staphylococcus aureus. Biochemistry 2012, 51:4642-4649.
    • (2012) Biochemistry , vol.51 , pp. 4642-4649
    • Llarrull, L.I.1    Mobashery, S.2
  • 158
    • 80055092265 scopus 로고    scopus 로고
    • Activation of BlaR1 protein of methicillin-resistant Staphylococcus aureus, its proteolytic processing, and recovery from induction of resistance
    • Llarrull L.I., Toth M., Champion M.M., Mobashery S. Activation of BlaR1 protein of methicillin-resistant Staphylococcus aureus, its proteolytic processing, and recovery from induction of resistance. J Biol Chem 2011, 286:38148-38158.
    • (2011) J Biol Chem , vol.286 , pp. 38148-38158
    • Llarrull, L.I.1    Toth, M.2    Champion, M.M.3    Mobashery, S.4
  • 159
    • 77956509713 scopus 로고    scopus 로고
    • Comprehensive characterization of methicillin-resistant Staphylococcus aureus subsp. aureus COL secretome by two-dimensional liquid chromatography and mass spectrometry
    • Ravipaty S., Reilly J.P. Comprehensive characterization of methicillin-resistant Staphylococcus aureus subsp. aureus COL secretome by two-dimensional liquid chromatography and mass spectrometry. Mol Cell Proteomics 2010, 9:1898-1919.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1898-1919
    • Ravipaty, S.1    Reilly, J.P.2
  • 160
    • 76749149598 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the Campylobacter jejuni adherence factor CadF reveals post-translational processing that removes immunogenicity while retaining fibronectin binding
    • Scott N.E., Marzook N.B., Deutscher A., Falconer L., Crossett B., Djordjevic S.P., et al. Mass spectrometric characterization of the Campylobacter jejuni adherence factor CadF reveals post-translational processing that removes immunogenicity while retaining fibronectin binding. Proteomics 2010, 10:277-288.
    • (2010) Proteomics , vol.10 , pp. 277-288
    • Scott, N.E.1    Marzook, N.B.2    Deutscher, A.3    Falconer, L.4    Crossett, B.5    Djordjevic, S.P.6
  • 161
    • 77958599627 scopus 로고    scopus 로고
    • A processed multidomain Mycoplasma hyopneumoniae adhesin binds fibronectin, plasminogen, and swine respiratory cilia
    • Seymour L.M., Deutscher A.T., Jenkins C., Kuit T.A., Falconer L., Minion F.C., et al. A processed multidomain Mycoplasma hyopneumoniae adhesin binds fibronectin, plasminogen, and swine respiratory cilia. J Biol Chem 2010, 285:33971-33978.
    • (2010) J Biol Chem , vol.285 , pp. 33971-33978
    • Seymour, L.M.1    Deutscher, A.T.2    Jenkins, C.3    Kuit, T.A.4    Falconer, L.5    Minion, F.C.6
  • 162
    • 82355164186 scopus 로고    scopus 로고
    • Sequence TTKF↓QE defines the site of proteolytic cleavage in Mhp683 protein, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniae
    • Bogema D.R., Scott N.E., Padula M.P., Tacchi J.L., Raymond B.B.A., Jenkins C., et al. Sequence TTKF↓QE defines the site of proteolytic cleavage in Mhp683 protein, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniae. J Biol Chem 2011, 286:41217-41229.
    • (2011) J Biol Chem , vol.286 , pp. 41217-41229
    • Bogema, D.R.1    Scott, N.E.2    Padula, M.P.3    Tacchi, J.L.4    Raymond, B.B.A.5    Jenkins, C.6
  • 163
    • 84860528192 scopus 로고    scopus 로고
    • Characterization of cleavage events in the multifunctional cilium adhesin Mhp684 (P146) reveals a mechanism by which Mycoplasma hyopneumoniae regulates surface topography
    • Bogema D.R., Deutscher A.T., Woolley L.K., Seymour L.M., Raymond B.B.A., Tacchi J.L., et al. Characterization of cleavage events in the multifunctional cilium adhesin Mhp684 (P146) reveals a mechanism by which Mycoplasma hyopneumoniae regulates surface topography. mBio 2012, 3.
    • (2012) mBio , vol.3
    • Bogema, D.R.1    Deutscher, A.T.2    Woolley, L.K.3    Seymour, L.M.4    Raymond, B.B.A.5    Tacchi, J.L.6
  • 164
    • 84857880464 scopus 로고    scopus 로고
    • Mycoplasma hyopneumoniae surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifs
    • Deutscher A.T., Tacchi J.L., Minion F.C., Padula M.P., Crossett B., Bogema D.R., et al. Mycoplasma hyopneumoniae surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifs. J Proteome Res 2012, 11:1924-1936.
    • (2012) J Proteome Res , vol.11 , pp. 1924-1936
    • Deutscher, A.T.1    Tacchi, J.L.2    Minion, F.C.3    Padula, M.P.4    Crossett, B.5    Bogema, D.R.6
  • 165
    • 84862666467 scopus 로고    scopus 로고
    • Roles and underlying mechanisms of ESAT-6 in the context of Mycobacterium tuberculosis-host interaction from a systems biology perspective
    • Yu X.W., Xie J.P. Roles and underlying mechanisms of ESAT-6 in the context of Mycobacterium tuberculosis-host interaction from a systems biology perspective. Cell Signal 2012, 24:1841-1846.
    • (2012) Cell Signal , vol.24 , pp. 1841-1846
    • Yu, X.W.1    Xie, J.P.2
  • 166
    • 0037044765 scopus 로고    scopus 로고
    • Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni
    • Young N.M., Brisson J.R., Kelly J., Watson D.C., Tessier L., Lanthier P.H., et al. Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni. J Biol Chem 2002, 277:42530-42539.
    • (2002) J Biol Chem , vol.277 , pp. 42530-42539
    • Young, N.M.1    Brisson, J.R.2    Kelly, J.3    Watson, D.C.4    Tessier, L.5    Lanthier, P.H.6
  • 167
    • 33646564396 scopus 로고    scopus 로고
    • Definition of the bacterial N-glycosylation site consensus sequence
    • Kowarik M., Young N.M., Numao S., Schulz B.L., Hug I., Callewaert N., et al. Definition of the bacterial N-glycosylation site consensus sequence. EMBO J 2006, 25:1957-1966.
    • (2006) EMBO J , vol.25 , pp. 1957-1966
    • Kowarik, M.1    Young, N.M.2    Numao, S.3    Schulz, B.L.4    Hug, I.5    Callewaert, N.6
  • 168
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • Szymanski C.M., Yao R.J., Ewing C.P., Trust T.J., Guerry P. Evidence for a system of general protein glycosylation in Campylobacter jejuni. Mol Microbiol 1999, 32:1022-1030.
    • (1999) Mol Microbiol , vol.32 , pp. 1022-1030
    • Szymanski, C.M.1    Yao, R.J.2    Ewing, C.P.3    Trust, T.J.4    Guerry, P.5
  • 169
    • 28844508716 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycopeptides with PgIB, a bacterial oligosaccharyl transferase from Campylobacter jejuni
    • Glover K.J., Weerapana E., Numao S., Imperiali B. Chemoenzymatic synthesis of glycopeptides with PgIB, a bacterial oligosaccharyl transferase from Campylobacter jejuni. Chem Biol 2005, 12:1311-1316.
    • (2005) Chem Biol , vol.12 , pp. 1311-1316
    • Glover, K.J.1    Weerapana, E.2    Numao, S.3    Imperiali, B.4
  • 170
    • 33645228374 scopus 로고    scopus 로고
    • Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer
    • Kelly J., Jarrell H., Millar L., Tessier L., Fiori L.M., Lau P.C., et al. Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer. J Bacteriol 2006, 188:2427-2434.
    • (2006) J Bacteriol , vol.188 , pp. 2427-2434
    • Kelly, J.1    Jarrell, H.2    Millar, L.3    Tessier, L.4    Fiori, L.M.5    Lau, P.C.6
  • 171
    • 84869211725 scopus 로고    scopus 로고
    • Diversity in the protein N-glycosylation pathways within the Campylobacter genus
    • Nothaft H., Scott N.E., Vinogradov E., Liu X., Hu R., Beadle B., et al. Diversity in the protein N-glycosylation pathways within the Campylobacter genus. Mol Cell Proteomics 2012, 11:1203-1219.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1203-1219
    • Nothaft, H.1    Scott, N.E.2    Vinogradov, E.3    Liu, X.4    Hu, R.5    Beadle, B.6
  • 172
    • 70350029185 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the surface-associated 42kDa lipoprotein JlpA as a glycosylated antigen in strains of Campylobacter jejuni
    • Scott N.E., Bogema D.R., Connolly A.M., Falconer L., Djordjevic S.P., Cordwell S.J. Mass spectrometric characterization of the surface-associated 42kDa lipoprotein JlpA as a glycosylated antigen in strains of Campylobacter jejuni. J Proteome Res 2009, 8:4654-4664.
    • (2009) J Proteome Res , vol.8 , pp. 4654-4664
    • Scott, N.E.1    Bogema, D.R.2    Connolly, A.M.3    Falconer, L.4    Djordjevic, S.P.5    Cordwell, S.J.6
  • 173
    • 84865479016 scopus 로고    scopus 로고
    • Modification of the Campylobacter jejuni N-Linked glycan by EptC protein-mediated addition of phosphoethanolamine
    • Scott N.E., Nothaft H., Edwards A.V., Labbate M., Djordjevic S.P., Larsen M.R., et al. Modification of the Campylobacter jejuni N-Linked glycan by EptC protein-mediated addition of phosphoethanolamine. J Biol Chem 2012, 287:29384-29396.
    • (2012) J Biol Chem , vol.287 , pp. 29384-29396
    • Scott, N.E.1    Nothaft, H.2    Edwards, A.V.3    Labbate, M.4    Djordjevic, S.P.5    Larsen, M.R.6
  • 174
    • 33748505442 scopus 로고    scopus 로고
    • Mass spectrometry-based glycomics strategy for exploring N-linked glycosylation in eukaryotes and bacteria
    • Liu X., McNally D.J., Nothaft H., Szymanski C.M., Brisson J.R., Li J.J. Mass spectrometry-based glycomics strategy for exploring N-linked glycosylation in eukaryotes and bacteria. Anal Chem 2006, 78:6081-6087.
    • (2006) Anal Chem , vol.78 , pp. 6081-6087
    • Liu, X.1    McNally, D.J.2    Nothaft, H.3    Szymanski, C.M.4    Brisson, J.R.5    Li, J.J.6
  • 175
    • 70349279995 scopus 로고    scopus 로고
    • Study of free oligosaccharides derived from the bacterial N-glycosylation pathway
    • Nothaft H., Liu X., McNally D.J., Li J.J., Szymanski C.M. Study of free oligosaccharides derived from the bacterial N-glycosylation pathway. Proc Natl Acad Sci U S A 2009, 106:15019-15024.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 15019-15024
    • Nothaft, H.1    Liu, X.2    McNally, D.J.3    Li, J.J.4    Szymanski, C.M.5
  • 176
    • 3142673556 scopus 로고    scopus 로고
    • The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks
    • Karlyshev A.V., Everest P., Linton D., Cawthraw S., Newell D.G., Wren B.W. The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks. Microbiology 2004, 150:1957-1964.
    • (2004) Microbiology , vol.150 , pp. 1957-1964
    • Karlyshev, A.V.1    Everest, P.2    Linton, D.3    Cawthraw, S.4    Newell, D.G.5    Wren, B.W.6
  • 177
    • 0035860764 scopus 로고    scopus 로고
    • Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin
    • Thibault P., Logan S.M., Kelly J.F., Brisson J.R., Ewing C.P., Trust T.J., et al. Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin. J Biol Chem 2001, 276:34862-34870.
    • (2001) J Biol Chem , vol.276 , pp. 34862-34870
    • Thibault, P.1    Logan, S.M.2    Kelly, J.F.3    Brisson, J.R.4    Ewing, C.P.5    Trust, T.J.6
  • 178
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria: sweeter than ever
    • Nothaft H., Szymanski C.M. Protein glycosylation in bacteria: sweeter than ever. Nat Rev Microbiol 2010, 8:765-778.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 179
    • 80053280679 scopus 로고    scopus 로고
    • Lipoprotein sorting in bacteria
    • S. Gottesman, C.S. Harwood (Eds.)
    • Okuda S., Tokuda H., Okuda S., Tokuda H. Lipoprotein sorting in bacteria. Annu Rev Microbiol 2011, 239-259. S. Gottesman, C.S. Harwood (Eds.).
    • (2011) Annu Rev Microbiol , pp. 239-259
    • Okuda, S.1    Tokuda, H.2    Okuda, S.3    Tokuda, H.4
  • 180
    • 34447505050 scopus 로고    scopus 로고
    • Identification of two Mycobacterium smegmatis lipoproteins exported by a SecA2-dependent pathway
    • Gibbons H.S., Wolschendorf F., Abshire M., Niederweis M., Braunstein M. Identification of two Mycobacterium smegmatis lipoproteins exported by a SecA2-dependent pathway. J Bacteriol 2007, 189:5090-5100.
    • (2007) J Bacteriol , vol.189 , pp. 5090-5100
    • Gibbons, H.S.1    Wolschendorf, F.2    Abshire, M.3    Niederweis, M.4    Braunstein, M.5
  • 181
    • 51549088570 scopus 로고    scopus 로고
    • Characterization of the accessory Sec system of Staphylococcus aureus
    • Siboo I.R., Chaffin D.O., Rubens C.E., Sullam P.M. Characterization of the accessory Sec system of Staphylococcus aureus. J Bacteriol 2008, 190:6188-6196.
    • (2008) J Bacteriol , vol.190 , pp. 6188-6196
    • Siboo, I.R.1    Chaffin, D.O.2    Rubens, C.E.3    Sullam, P.M.4
  • 182
    • 77952528533 scopus 로고    scopus 로고
    • Twin arginine translocase pathway and fast-folding lipoprotein biosynthesis in E. coli: interesting implications and applications
    • Shruthi H., Anand P., Murugan V., Sankaran K. Twin arginine translocase pathway and fast-folding lipoprotein biosynthesis in E. coli: interesting implications and applications. Mol Biosyst 2010, 6:999-1007.
    • (2010) Mol Biosyst , vol.6 , pp. 999-1007
    • Shruthi, H.1    Anand, P.2    Murugan, V.3    Sankaran, K.4
  • 184
    • 61549096272 scopus 로고    scopus 로고
    • Prediction of lipoprotein signal peptides in Gram-positive bacteria with a Hidden Markov Model
    • Bagos P.G., Tslrigos K.D., Liakopoulos T.D., Hamodrakas S.J. Prediction of lipoprotein signal peptides in Gram-positive bacteria with a Hidden Markov Model. J Proteome Res 2008, 7:5082-5093.
    • (2008) J Proteome Res , vol.7 , pp. 5082-5093
    • Bagos, P.G.1    Tslrigos, K.D.2    Liakopoulos, T.D.3    Hamodrakas, S.J.4
  • 185
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein: transfer of diacylglycery moiety from phosphatidyl glycerol
    • Sankaran K., Wu H.C. Lipid modification of bacterial prolipoprotein: transfer of diacylglycery moiety from phosphatidyl glycerol. J Biol Chem 1994, 269:19701-19706.
    • (1994) J Biol Chem , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 186
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome
    • Tjalsma H., Bolhuis A., Jongbloed J.D.H., Bron S., van Dijl J.M. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol Mol Biol Rev 2000, 64:515-+.
    • (2000) Microbiol Mol Biol Rev , vol.64
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.H.3    Bron, S.4    van Dijl, J.M.5
  • 188
    • 84864009033 scopus 로고    scopus 로고
    • Environment-mediated accumulation of diacyl lipoproteins over their triacyl counterparts in Staphylococcus aureus
    • Kurokawa K., Kim M.S., Ichikawa R., Ryu K.H., Dohmae N., Nakayama H., et al. Environment-mediated accumulation of diacyl lipoproteins over their triacyl counterparts in Staphylococcus aureus. J Bacteriol 2012, 194:3299-3306.
    • (2012) J Bacteriol , vol.194 , pp. 3299-3306
    • Kurokawa, K.1    Kim, M.S.2    Ichikawa, R.3    Ryu, K.H.4    Dohmae, N.5    Nakayama, H.6
  • 189
    • 65249085615 scopus 로고    scopus 로고
    • Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB
    • Okuda S., Tokuda H. Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB. Proc Natl Acad Sci U S A 2009, 106:5877-5882.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 5877-5882
    • Okuda, S.1    Tokuda, H.2
  • 190
    • 80052551712 scopus 로고    scopus 로고
    • Overexpression of LolCDE allows deletion of the Escherichia coli gene encoding apolipoprotein N-acyltransferase
    • Narita S., Tokuda H. Overexpression of LolCDE allows deletion of the Escherichia coli gene encoding apolipoprotein N-acyltransferase. J Bacteriol 2011, 193:4832-4840.
    • (2011) J Bacteriol , vol.193 , pp. 4832-4840
    • Narita, S.1    Tokuda, H.2
  • 191
    • 0037044719 scopus 로고    scopus 로고
    • Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals
    • Fukuda A., Matsuyama S., Hara T., Nakayama J., Nagasawa H., Tokuda H. Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals. J Biol Chem 2002, 277:43512-43518.
    • (2002) J Biol Chem , vol.277 , pp. 43512-43518
    • Fukuda, A.1    Matsuyama, S.2    Hara, T.3    Nakayama, J.4    Nagasawa, H.5    Tokuda, H.6
  • 192
    • 34250351484 scopus 로고    scopus 로고
    • Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins
    • Narita S.I., Tokuda H. Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins. J Biol Chem 2007, 282:13372-13378.
    • (2007) J Biol Chem , vol.282 , pp. 13372-13378
    • Narita, S.I.1    Tokuda, H.2
  • 193
    • 0035861554 scopus 로고    scopus 로고
    • Lipoprotein sorting signals evaluated as the Lo1A-dependent release of lipoproteins from the cytoplasmic membrane of Escherichia coli
    • Terada M., Kuroda T., Matsuyama S., Tokuda H. Lipoprotein sorting signals evaluated as the Lo1A-dependent release of lipoproteins from the cytoplasmic membrane of Escherichia coli. J Biol Chem 2001, 276:47690-47694.
    • (2001) J Biol Chem , vol.276 , pp. 47690-47694
    • Terada, M.1    Kuroda, T.2    Matsuyama, S.3    Tokuda, H.4
  • 194
    • 0035997276 scopus 로고    scopus 로고
    • Profiling the alkaline membrane proteome of Caulobacter crescentus with two-dimensional electrophoresis and mass spectrometry
    • Molloy M.P., Phadke N.D., Chen H., Tyldesley R., Garfin D.E., Maddock J.R., et al. Profiling the alkaline membrane proteome of Caulobacter crescentus with two-dimensional electrophoresis and mass spectrometry. Proteomics 2002, 2:899-910.
    • (2002) Proteomics , vol.2 , pp. 899-910
    • Molloy, M.P.1    Phadke, N.D.2    Chen, H.3    Tyldesley, R.4    Garfin, D.E.5    Maddock, J.R.6
  • 195
    • 33846247863 scopus 로고    scopus 로고
    • Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes
    • Baumgartner M., Karst U., Gerstel B., Loessner M., Wehland J., Jansch L. Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes. J Bacteriol 2007, 189:313-324.
    • (2007) J Bacteriol , vol.189 , pp. 313-324
    • Baumgartner, M.1    Karst, U.2    Gerstel, B.3    Loessner, M.4    Wehland, J.5    Jansch, L.6
  • 196
    • 49649123115 scopus 로고    scopus 로고
    • Lipoproteins of Listeria monocytogenes are critical for virulence and TLR2-mediated immune activation
    • Machata S., Tchatalbachev S., Mohamed W., Jansch L., Hain T., Chakraborty T. Lipoproteins of Listeria monocytogenes are critical for virulence and TLR2-mediated immune activation. J Immunol 2008, 181:2028-2035.
    • (2008) J Immunol , vol.181 , pp. 2028-2035
    • Machata, S.1    Tchatalbachev, S.2    Mohamed, W.3    Jansch, L.4    Hain, T.5    Chakraborty, T.6
  • 197
    • 66849132084 scopus 로고    scopus 로고
    • Impact of Lgt mutation on lipoprotein biosynthesis and in vitro phenotypes of Streptococcus agalactiae
    • Bray B.A., Sutcliffe I.C., Harrington D.J. Impact of Lgt mutation on lipoprotein biosynthesis and in vitro phenotypes of Streptococcus agalactiae. Microbiology 2009, 155:1451-1458.
    • (2009) Microbiology , vol.155 , pp. 1451-1458
    • Bray, B.A.1    Sutcliffe, I.C.2    Harrington, D.J.3
  • 198
    • 67649392525 scopus 로고    scopus 로고
    • Contribution of lipoproteins and lipoprotein processing to endocarditis virulence in Streptococcus sanguinis
    • Das S., Kanamoto T., Ge X.C., Xu P., Unoki T., Munro C.L., et al. Contribution of lipoproteins and lipoprotein processing to endocarditis virulence in Streptococcus sanguinis. J Bacteriol 2009, 191:4166-4179.
    • (2009) J Bacteriol , vol.191 , pp. 4166-4179
    • Das, S.1    Kanamoto, T.2    Ge, X.C.3    Xu, P.4    Unoki, T.5    Munro, C.L.6
  • 199
    • 84155164753 scopus 로고    scopus 로고
    • Lipoprotein biosynthesis by prolipoprotein diacylglyceryl transferase is required for efficient spore germination and full virulence of Bacillus anthracis
    • Okugawa S., Moayeri M., Pomerantsev A.P., Sastalla I., Crown D., Gupta P.K., et al. Lipoprotein biosynthesis by prolipoprotein diacylglyceryl transferase is required for efficient spore germination and full virulence of Bacillus anthracis. Mol Microbiol 2012, 83:96-109.
    • (2012) Mol Microbiol , vol.83 , pp. 96-109
    • Okugawa, S.1    Moayeri, M.2    Pomerantsev, A.P.3    Sastalla, I.4    Crown, D.5    Gupta, P.K.6
  • 200
    • 84857711626 scopus 로고    scopus 로고
    • The prolipoprotein diacylglyceryl transferase (Lgt) of Enterococcus faecalis contributes to virulence
    • Reffuveille F., Serror P., Chevalier S., Budin-Verneuil A., Ladjouzi R., Bernay B., et al. The prolipoprotein diacylglyceryl transferase (Lgt) of Enterococcus faecalis contributes to virulence. Microbiology 2012, 158:816-825.
    • (2012) Microbiology , vol.158 , pp. 816-825
    • Reffuveille, F.1    Serror, P.2    Chevalier, S.3    Budin-Verneuil, A.4    Ladjouzi, R.5    Bernay, B.6
  • 201
    • 79951905038 scopus 로고    scopus 로고
    • Structural evidence of α-aminoacylated lipoproteins of Staphylococcus aureus
    • Asanuma M., Kurokawa K., Ichikawa R., Ryu K.H., Chae J.H., Dohmae N., et al. Structural evidence of α-aminoacylated lipoproteins of Staphylococcus aureus. FEBS J 2011, 278:716-728.
    • (2011) FEBS J , vol.278 , pp. 716-728
    • Asanuma, M.1    Kurokawa, K.2    Ichikawa, R.3    Ryu, K.H.4    Chae, J.H.5    Dohmae, N.6
  • 202
    • 70350437568 scopus 로고    scopus 로고
    • Identification of apolipoprotein N-acyltransferase (Lnt) in Mycobacteria
    • Tschumi A., Nai C., Auchli Y., Hunziker P., Gehrig P., Keller P., et al. Identification of apolipoprotein N-acyltransferase (Lnt) in Mycobacteria. J Biol Chem 2009, 284:27146-27156.
    • (2009) J Biol Chem , vol.284 , pp. 27146-27156
    • Tschumi, A.1    Nai, C.2    Auchli, Y.3    Hunziker, P.4    Gehrig, P.5    Keller, P.6
  • 204
    • 84867033119 scopus 로고    scopus 로고
    • The ppm operon is essential for acylation and glycosylation of lipoproteins in Corynebacterium glutamicum
    • Mohiman N., Argentini M., Batt S.M., Cornu D., Masi M., Eggeling L., et al. The ppm operon is essential for acylation and glycosylation of lipoproteins in Corynebacterium glutamicum. PLoS One 2012, 7.
    • (2012) PLoS One , vol.7
    • Mohiman, N.1    Argentini, M.2    Batt, S.M.3    Cornu, D.4    Masi, M.5    Eggeling, L.6
  • 205
    • 33645972887 scopus 로고    scopus 로고
    • A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins
    • Babu M.M., Priya M.L., Selvan A.T., Madera M., Gough J., Aravind L., et al. A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins. J Bacteriol 2006, 188:2761-2773.
    • (2006) J Bacteriol , vol.188 , pp. 2761-2773
    • Babu, M.M.1    Priya, M.L.2    Selvan, A.T.3    Madera, M.4    Gough, J.5    Aravind, L.6
  • 206
    • 0028987131 scopus 로고
    • Lipoproteins of Gram-positive bacteria
    • Sutcliffe I.C., Russell R.R.B. Lipoproteins of Gram-positive bacteria. J Bacteriol 1995, 177:1123-1128.
    • (1995) J Bacteriol , vol.177 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.B.2
  • 207
    • 63649086089 scopus 로고    scopus 로고
    • Evf, a virulence factor produced by the Drosophila pathogen Erwinia carotovora, is an S-palmitoylated protein with a new fold that binds to lipid vesicles
    • Quevillon-Cheruel S., Leulliot N., Muniz C.A., Vincent M., Gallay J., Argentini M., et al. Evf, a virulence factor produced by the Drosophila pathogen Erwinia carotovora, is an S-palmitoylated protein with a new fold that binds to lipid vesicles. J Biol Chem 2009, 284:3552-3562.
    • (2009) J Biol Chem , vol.284 , pp. 3552-3562
    • Quevillon-Cheruel, S.1    Leulliot, N.2    Muniz, C.A.3    Vincent, M.4    Gallay, J.5    Argentini, M.6
  • 208
    • 77954593444 scopus 로고    scopus 로고
    • O-Mycoloylated proteins from Corynebacterium: an unprecedented post-translational modification in bacteria
    • Huc E., Meniche X., Benz R., Bayan N., Ghazi A., Tropis M., et al. O-Mycoloylated proteins from Corynebacterium: an unprecedented post-translational modification in bacteria. J Biol Chem 2010, 285:21908-21912.
    • (2010) J Biol Chem , vol.285 , pp. 21908-21912
    • Huc, E.1    Meniche, X.2    Benz, R.3    Bayan, N.4    Ghazi, A.5    Tropis, M.6
  • 209
    • 80052726194 scopus 로고    scopus 로고
    • Functional expression of the PorAH channel from Corynebacterium glutamicum in cell-free expression systems: implications for the role of the naturally occurring mycolic acid modification
    • Rath P., Demange P., Saurel O., Tropis M., Daffe M., Dotsch V., et al. Functional expression of the PorAH channel from Corynebacterium glutamicum in cell-free expression systems: implications for the role of the naturally occurring mycolic acid modification. J Biol Chem 2011, 286:32525-32532.
    • (2011) J Biol Chem , vol.286 , pp. 32525-32532
    • Rath, P.1    Demange, P.2    Saurel, O.3    Tropis, M.4    Daffe, M.5    Dotsch, V.6
  • 210
    • 17644396395 scopus 로고    scopus 로고
    • A Salmonella typhimurium effector protein SifA is modified by host cell prenylation and S-acylation machinery
    • Reinicke A.T., Hutchinson J.L., Magee A.I., Mastroeni P., Trowsdale J., Kelly A.P. A Salmonella typhimurium effector protein SifA is modified by host cell prenylation and S-acylation machinery. J Biol Chem 2005, 280:14620-14627.
    • (2005) J Biol Chem , vol.280 , pp. 14620-14627
    • Reinicke, A.T.1    Hutchinson, J.L.2    Magee, A.I.3    Mastroeni, P.4    Trowsdale, J.5    Kelly, A.P.6
  • 211
    • 34548671163 scopus 로고    scopus 로고
    • New type III effectors from Xanthomonas campestris pv. vesicatoria trigger plant reactions dependent on a conserved N-myristoylation motif
    • Thieme F., Szczesny R., Urban A., Kirchner O., Hause G., Bonas U. New type III effectors from Xanthomonas campestris pv. vesicatoria trigger plant reactions dependent on a conserved N-myristoylation motif. Mol Plant Microbe Interact 2007, 20:1250-1261.
    • (2007) Mol Plant Microbe Interact , vol.20 , pp. 1250-1261
    • Thieme, F.1    Szczesny, R.2    Urban, A.3    Kirchner, O.4    Hause, G.5    Bonas, U.6
  • 212
    • 41949130227 scopus 로고    scopus 로고
    • The HopZ family of Pseudomonas syringae type III effectors require myristoylation for virulence and avirulence functions in Arabidopsis thaliana
    • Lewis J.D., Abada W., Ma W.B., Guttman D.S., Desveaux D. The HopZ family of Pseudomonas syringae type III effectors require myristoylation for virulence and avirulence functions in Arabidopsis thaliana. J Bacteriol 2008, 190:2880-2891.
    • (2008) J Bacteriol , vol.190 , pp. 2880-2891
    • Lewis, J.D.1    Abada, W.2    Ma, W.B.3    Guttman, D.S.4    Desveaux, D.5
  • 213
    • 67650115862 scopus 로고    scopus 로고
    • A family of bacterial cysteine protease type III effectors utilizes acylation-dependent and -independent strategies to localize to plasma membranes
    • Dowen R.H., Engel J.L., Shao F., Ecker J.R., Dixon J.E. A family of bacterial cysteine protease type III effectors utilizes acylation-dependent and -independent strategies to localize to plasma membranes. J Biol Chem 2009, 284:15867-15879.
    • (2009) J Biol Chem , vol.284 , pp. 15867-15879
    • Dowen, R.H.1    Engel, J.L.2    Shao, F.3    Ecker, J.R.4    Dixon, J.E.5
  • 214
    • 78049354410 scopus 로고    scopus 로고
    • Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins
    • Ivanov S.S., Charron G., Hang H.C., Roy C.R. Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins. J Biol Chem 2010, 285:34686-34698.
    • (2010) J Biol Chem , vol.285 , pp. 34686-34698
    • Ivanov, S.S.1    Charron, G.2    Hang, H.C.3    Roy, C.R.4
  • 215
    • 80052929972 scopus 로고    scopus 로고
    • S-Bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics
    • Chi B.K., Gronau K., Mader U., Hessling B., Becher D., Antelmann H. S-Bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics. Mol Cell Proteomics 2011, 10.
    • (2011) Mol Cell Proteomics , vol.10
    • Chi, B.K.1    Gronau, K.2    Mader, U.3    Hessling, B.4    Becher, D.5    Antelmann, H.6
  • 216
    • 84860176878 scopus 로고    scopus 로고
    • Endogenous protein S-nitrosylation in E. coli: regulation by OxyR
    • Seth D., Hausladen A., Wang Y.J., Stamler J.S. Endogenous protein S-nitrosylation in E. coli: regulation by OxyR. Science 2012, 336:470-473.
    • (2012) Science , vol.336 , pp. 470-473
    • Seth, D.1    Hausladen, A.2    Wang, Y.J.3    Stamler, J.S.4
  • 217
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M., Aslund F., Storz G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 1998, 279:1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 218
    • 84860507742 scopus 로고    scopus 로고
    • Global regulation of gene expression by OxyR in an important human opportunistic pathogen
    • Wei Q., Phu N.L.M., Dotsch A., Hildebrand F., Panmanee W., Elfarash A., et al. Global regulation of gene expression by OxyR in an important human opportunistic pathogen. Nucleic Acids Res 2012, 40:4320-4333.
    • (2012) Nucleic Acids Res , vol.40 , pp. 4320-4333
    • Wei, Q.1    Phu, N.L.M.2    Dotsch, A.3    Hildebrand, F.4    Panmanee, W.5    Elfarash, A.6
  • 219
    • 66149098151 scopus 로고    scopus 로고
    • Bacterial FIC proteins AMP up infection
    • Roy C.R., Mukherjee S. Bacterial FIC proteins AMP up infection. Sci Signal 2009, 2.
    • (2009) Sci Signal , vol.2
    • Roy, C.R.1    Mukherjee, S.2
  • 220
    • 79954423286 scopus 로고    scopus 로고
    • Adenylylation: renaissance of a forgotten post-translational modification
    • Itzen A., Blankenfeldt W., Goody R.S. Adenylylation: renaissance of a forgotten post-translational modification. Trends Biochem Sci 2011, 36:219-226.
    • (2011) Trends Biochem Sci , vol.36 , pp. 219-226
    • Itzen, A.1    Blankenfeldt, W.2    Goody, R.S.3
  • 221
    • 84855890898 scopus 로고    scopus 로고
    • A new chemical handle for protein AMPylation at the host-pathogen interface
    • Broncel M., Serwa R.A., Tate E.W. A new chemical handle for protein AMPylation at the host-pathogen interface. Chembiochem 2012, 13:183-185.
    • (2012) Chembiochem , vol.13 , pp. 183-185
    • Broncel, M.1    Serwa, R.A.2    Tate, E.W.3
  • 222
    • 80055015456 scopus 로고    scopus 로고
    • A chemical reporter for protein AMPylation
    • Grammel M., Luong P., Orth K., Hang H.C. A chemical reporter for protein AMPylation. J Am Chem Soc 2011, 133:17103-17105.
    • (2011) J Am Chem Soc , vol.133 , pp. 17103-17105
    • Grammel, M.1    Luong, P.2    Orth, K.3    Hang, H.C.4
  • 223
    • 84861121301 scopus 로고    scopus 로고
    • Probing adenylation: using a fluorescently labelled ATP probe to directly label and immunoprecipitate VopS substrates
    • Lewallen D.M., Steckler C.J., Knuckley B., Chalmers M.J., Thompson P.R. Probing adenylation: using a fluorescently labelled ATP probe to directly label and immunoprecipitate VopS substrates. Mol Biosyst 2012, 8:1701-1706.
    • (2012) Mol Biosyst , vol.8 , pp. 1701-1706
    • Lewallen, D.M.1    Steckler, C.J.2    Knuckley, B.3    Chalmers, M.J.4    Thompson, P.R.5
  • 224
    • 0343766370 scopus 로고
    • Fatty-acid composition and components of the hydrophilic part of lipid A in the lipopolysaccharide from Pseudomonas syringae
    • Zdorovenko G.M., Veremeichenko S.N., Solyanik L.P. Fatty-acid composition and components of the hydrophilic part of lipid A in the lipopolysaccharide from Pseudomonas syringae. Biochemistry 1995, 60:787-793.
    • (1995) Biochemistry , vol.60 , pp. 787-793
    • Zdorovenko, G.M.1    Veremeichenko, S.N.2    Solyanik, L.P.3
  • 225
    • 11244304238 scopus 로고    scopus 로고
    • Periplasmic cleavage and modification of the 1-phosphate group of Helicobacter pylori lipid A
    • Tran A.X., Karbarz M.J., Wang X.Y., Raetz C.R.H., McGrath S.C., Cotter R.J., et al. Periplasmic cleavage and modification of the 1-phosphate group of Helicobacter pylori lipid A. J Biol Chem 2004, 279:55780-55791.
    • (2004) J Biol Chem , vol.279 , pp. 55780-55791
    • Tran, A.X.1    Karbarz, M.J.2    Wang, X.Y.3    Raetz, C.R.H.4    McGrath, S.C.5    Cotter, R.J.6
  • 226
    • 44049093956 scopus 로고    scopus 로고
    • The acylation and phosphorylation pattern of lipid A from Xanthomonas campestris strongly influence its ability to trigger the innate immune response in Arabidopsis
    • Silipo A., Sturiale L., Garozzo D., Erbs G., Jensen T.T., Lanzetta R., et al. The acylation and phosphorylation pattern of lipid A from Xanthomonas campestris strongly influence its ability to trigger the innate immune response in Arabidopsis. Chembiochem 2008, 9:896-904.
    • (2008) Chembiochem , vol.9 , pp. 896-904
    • Silipo, A.1    Sturiale, L.2    Garozzo, D.3    Erbs, G.4    Jensen, T.T.5    Lanzetta, R.6
  • 227
    • 69249088084 scopus 로고    scopus 로고
    • Natural phosphoryl and acyl variants of lipid A from Neisseria meningitidis strain 89I differentially induce tumor necrosis factor-α in human monocytes
    • John C.M., Liu M.F., Jarvis G.A. Natural phosphoryl and acyl variants of lipid A from Neisseria meningitidis strain 89I differentially induce tumor necrosis factor-α in human monocytes. J Biol Chem 2009, 284:21515-21525.
    • (2009) J Biol Chem , vol.284 , pp. 21515-21525
    • John, C.M.1    Liu, M.F.2    Jarvis, G.A.3
  • 228
    • 77953523940 scopus 로고    scopus 로고
    • Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides
    • Herrera C.M., Hankins J.V., Trent M.S. Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides. Mol Microbiol 2010, 76:1444-1460.
    • (2010) Mol Microbiol , vol.76 , pp. 1444-1460
    • Herrera, C.M.1    Hankins, J.V.2    Trent, M.S.3
  • 229
    • 79960309927 scopus 로고    scopus 로고
    • The pmrCAB operon mediates polymyxin resistance in Acinetobacter baumannii ATCC 17978 and clinical isolates through phosphoethanolamine modification of lipid A
    • Arroyo L.A., Herrera C.M., Fernandez L., Hankins J.V., Trent M.S., Hancock R.E.W. The pmrCAB operon mediates polymyxin resistance in Acinetobacter baumannii ATCC 17978 and clinical isolates through phosphoethanolamine modification of lipid A. Antimicrob Agents Chemother 2011, 55:3743-3751.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 3743-3751
    • Arroyo, L.A.1    Herrera, C.M.2    Fernandez, L.3    Hankins, J.V.4    Trent, M.S.5    Hancock, R.E.W.6
  • 230
    • 79955533843 scopus 로고    scopus 로고
    • Absence of PmrAB-mediated phosphoethanolamine modifications of Citrobacter rodentium lipopolysaccharide affects outer membrane integrity
    • Viau C., Le Sage V., Ting D.K., Gross J., Le Moual H. Absence of PmrAB-mediated phosphoethanolamine modifications of Citrobacter rodentium lipopolysaccharide affects outer membrane integrity. J Bacteriol 2011, 193:2168-2176.
    • (2011) J Bacteriol , vol.193 , pp. 2168-2176
    • Viau, C.1    Le Sage, V.2    Ting, D.K.3    Gross, J.4    Le Moual, H.5
  • 231
    • 84869022848 scopus 로고    scopus 로고
    • The PmrAB system-inducing conditions control both lipid A remodeling and O-antigen length distribution, influencing the Salmonella typhimurium-host interactions
    • Farizano J.V., Pescaretti M.D., Lopez F.E., Hsu F.F., Delgado M.A. The PmrAB system-inducing conditions control both lipid A remodeling and O-antigen length distribution, influencing the Salmonella typhimurium-host interactions. J Biol Chem 2012, 287:38778-38789.
    • (2012) J Biol Chem , vol.287 , pp. 38778-38789
    • Farizano, J.V.1    Pescaretti, M.D.2    Lopez, F.E.3    Hsu, F.F.4    Delgado, M.A.5
  • 232
    • 84866844194 scopus 로고    scopus 로고
    • A novel plasmid-encoded serotype conversion mechanism through addition of phosphoethanolamine to the O-antigen of Shigella flexneri
    • Sun Q.Z., Knirel Y.A., Lan R.T., Wang J.P., Senchenkova S.N., Jin D., et al. A novel plasmid-encoded serotype conversion mechanism through addition of phosphoethanolamine to the O-antigen of Shigella flexneri. PLoS One 2012, 7.
    • (2012) PLoS One , vol.7
    • Sun, Q.Z.1    Knirel, Y.A.2    Lan, R.T.3    Wang, J.P.4    Senchenkova, S.N.5    Jin, D.6
  • 233
    • 84861215746 scopus 로고    scopus 로고
    • Phosphorylcholine allows for evasion of bactericidal antibody by Haemophilus influenzae
    • Clark S.E., Snow J., Li J.J., Zola T.A., Weiser J.N. Phosphorylcholine allows for evasion of bactericidal antibody by Haemophilus influenzae. PLoS Pathog 2012, 8.
    • (2012) PLoS Pathog , vol.8
    • Clark, S.E.1    Snow, J.2    Li, J.J.3    Zola, T.A.4    Weiser, J.N.5
  • 234
    • 77950451125 scopus 로고    scopus 로고
    • A link between the assembly of flagella and lipooligosaccharide of the Gram-negative bacterium Campylobacter jejuni
    • Cullen T.W., Trent M.S. A link between the assembly of flagella and lipooligosaccharide of the Gram-negative bacterium Campylobacter jejuni. Proc Natl Acad Sci U S A 2010, 107:5160-5165.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5160-5165
    • Cullen, T.W.1    Trent, M.S.2
  • 235
    • 84856258886 scopus 로고    scopus 로고
    • Characterization of unique modification of flagellar rod protein FlgG by Campylobacter jejuni lipid A phosphoethanolamine transferase, linking bacterial locomotion and antimicrobial peptide resistance
    • Cullen T.W., Madsen J.A., Ivanov P.L., Brodbelt J.S., Trent M.S. Characterization of unique modification of flagellar rod protein FlgG by Campylobacter jejuni lipid A phosphoethanolamine transferase, linking bacterial locomotion and antimicrobial peptide resistance. J Biol Chem 2012, 287:3326-3336.
    • (2012) J Biol Chem , vol.287 , pp. 3326-3336
    • Cullen, T.W.1    Madsen, J.A.2    Ivanov, P.L.3    Brodbelt, J.S.4    Trent, M.S.5
  • 236
    • 3242663192 scopus 로고    scopus 로고
    • Unique modifications with phosphocholine and phosphoethanolamine define alternate antigenic forms of Neisseria gonorrhoeae type IV pili
    • Hegge F.T., Hitchen P.G., Aas F.E., Kristiansen H., Lovold C., Egge-Jacobsen W., et al. Unique modifications with phosphocholine and phosphoethanolamine define alternate antigenic forms of Neisseria gonorrhoeae type IV pili. Proc Natl Acad Sci U S A 2004, 101:10798-10803.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10798-10803
    • Hegge, F.T.1    Hitchen, P.G.2    Aas, F.E.3    Kristiansen, H.4    Lovold, C.5    Egge-Jacobsen, W.6
  • 237
    • 33748792256 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae type IV pili undergo multisite, hierarchical modifications with phosphoethanolamine and phosphocholine requiring an enzyme structurally related to lipopolysaccharide phosphoethanolamine transferases
    • Aas F.E., Egge-Jacobsen W., Winther-Larsen H.C., Lovold C., Hitchen P.G., Dell A., et al. Neisseria gonorrhoeae type IV pili undergo multisite, hierarchical modifications with phosphoethanolamine and phosphocholine requiring an enzyme structurally related to lipopolysaccharide phosphoethanolamine transferases. J Biol Chem 2006, 281:27712-27723.
    • (2006) J Biol Chem , vol.281 , pp. 27712-27723
    • Aas, F.E.1    Egge-Jacobsen, W.2    Winther-Larsen, H.C.3    Lovold, C.4    Hitchen, P.G.5    Dell, A.6
  • 238
    • 37549047175 scopus 로고    scopus 로고
    • Genetic and functional analyses of PptA, a phospho-form transferase targeting type IV pili in Neisseria gonorrhoeae
    • Naessan C.L., Egge-Jacobsen W., Heiniger R.W., Wolfgang M.C., Aas F.E., Rohr A., et al. Genetic and functional analyses of PptA, a phospho-form transferase targeting type IV pili in Neisseria gonorrhoeae. J Bacteriol 2008, 190:387-400.
    • (2008) J Bacteriol , vol.190 , pp. 387-400
    • Naessan, C.L.1    Egge-Jacobsen, W.2    Heiniger, R.W.3    Wolfgang, M.C.4    Aas, F.E.5    Rohr, A.6
  • 239
    • 84857092026 scopus 로고    scopus 로고
    • Novel protein substrates of the phospho-form modification system in Neisseria gonorrhoeae and their connection to O-Linked protein glycosylation
    • Anonsen J.H., Egge-Jacobsen W., Aas F.E., Borud B., Koomey M., Vik A. Novel protein substrates of the phospho-form modification system in Neisseria gonorrhoeae and their connection to O-Linked protein glycosylation. Infect Immun 2012, 80:22-30.
    • (2012) Infect Immun , vol.80 , pp. 22-30
    • Anonsen, J.H.1    Egge-Jacobsen, W.2    Aas, F.E.3    Borud, B.4    Koomey, M.5    Vik, A.6
  • 240
    • 0345714747 scopus 로고    scopus 로고
    • Identification and characterization of pptA: a gene involved in the phase-variable expression of phosphorylcholine on pili of Neisseria meningitidis
    • Warren M.J., Jennings M.P. Identification and characterization of pptA: a gene involved in the phase-variable expression of phosphorylcholine on pili of Neisseria meningitidis. Infect Immun 2003, 71:6892-6898.
    • (2003) Infect Immun , vol.71 , pp. 6892-6898
    • Warren, M.J.1    Jennings, M.P.2
  • 241
    • 80052399642 scopus 로고    scopus 로고
    • Modulation of Rab GTPase function by a protein phosphocholine transferase
    • Mukherjee S., Liu X.Y., Arasaki K., McDonough J., Galan J.E., Roy C.R. Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature 2011, 477:103-106.
    • (2011) Nature , vol.477 , pp. 103-106
    • Mukherjee, S.1    Liu, X.Y.2    Arasaki, K.3    McDonough, J.4    Galan, J.E.5    Roy, C.R.6
  • 242
    • 84855504174 scopus 로고    scopus 로고
    • Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination
    • Tan Y.H., Arnold R.J., Luo Z.Q. Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination. Proc Natl Acad Sci U S A 2011, 108:21212-21217.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 21212-21217
    • Tan, Y.H.1    Arnold, R.J.2    Luo, Z.Q.3
  • 243
    • 84863399784 scopus 로고    scopus 로고
    • Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins
    • Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A., Goody R.S. Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins. EMBO J 2012, 31:1774-1784.
    • (2012) EMBO J , vol.31 , pp. 1774-1784
    • Goody, P.R.1    Heller, K.2    Oesterlin, L.K.3    Muller, M.P.4    Itzen, A.5    Goody, R.S.6
  • 244
    • 84859564863 scopus 로고    scopus 로고
    • Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor
    • Oesterlin L.K., Goody R.S., Itzen A. Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor. Proc Natl Acad Sci U S A 2012, 109:5621-5626.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 5621-5626
    • Oesterlin, L.K.1    Goody, R.S.2    Itzen, A.3
  • 245
    • 0029951972 scopus 로고    scopus 로고
    • Discovery of a novel protein modification: α-Glycerophosphate is a substituent of meningococcal pilin
    • Stimson E., Virji M., Barker S., Panico M., Blench I., Saunders J., et al. Discovery of a novel protein modification: α-Glycerophosphate is a substituent of meningococcal pilin. Biochem J 1996, 316:29-33.
    • (1996) Biochem J , vol.316 , pp. 29-33
    • Stimson, E.1    Virji, M.2    Barker, S.3    Panico, M.4    Blench, I.5    Saunders, J.6
  • 246
    • 79951506883 scopus 로고    scopus 로고
    • Posttranslational modification of pili upon cell contact triggers N. meningitidis dissemination
    • Chamot-Rooke J., Mikaty G., Malosse C., Soyer M., Dumont A., Gault J., et al. Posttranslational modification of pili upon cell contact triggers N. meningitidis dissemination. Science 2011, 331:778-782.
    • (2011) Science , vol.331 , pp. 778-782
    • Chamot-Rooke, J.1    Mikaty, G.2    Malosse, C.3    Soyer, M.4    Dumont, A.5    Gault, J.6
  • 247
  • 248
    • 58149400542 scopus 로고    scopus 로고
    • AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling
    • Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K. AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 2009, 323:269-272.
    • (2009) Science , vol.323 , pp. 269-272
    • Yarbrough, M.L.1    Li, Y.2    Kinch, L.N.3    Grishin, N.V.4    Ball, H.L.5    Orth, K.6
  • 249
    • 84856417389 scopus 로고    scopus 로고
    • Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins
    • [107-U38.cbe]
    • Engel P., Goepfert A., Stanger F.V., Harms A., Schmidt A., Schirmer T., et al. Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins. Nature 2012, 482. [107-U38.cbe].
    • (2012) Nature , vol.482
    • Engel, P.1    Goepfert, A.2    Stanger, F.V.3    Harms, A.4    Schmidt, A.5    Schirmer, T.6
  • 251
    • 77955872117 scopus 로고    scopus 로고
    • The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
    • Muller M.P., Peters H., Blumer J., Blankenfeldt W., Goody R.S., Itzen A. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 2010, 329:946-949.
    • (2010) Science , vol.329 , pp. 946-949
    • Muller, M.P.1    Peters, H.2    Blumer, J.3    Blankenfeldt, W.4    Goody, R.S.5    Itzen, A.6
  • 252
    • 84860541901 scopus 로고    scopus 로고
    • A Xanthomonas uridine 5 '-monophosphate transferase inhibits plant immune kinases
    • Feng F., Yang F., Rong W., Wu X.G., Zhang J., Chen S., et al. A Xanthomonas uridine 5 '-monophosphate transferase inhibits plant immune kinases. Nature 2012, 485:114-118.
    • (2012) Nature , vol.485 , pp. 114-118
    • Feng, F.1    Yang, F.2    Rong, W.3    Wu, X.G.4    Zhang, J.5    Chen, S.6
  • 253
    • 84867421460 scopus 로고    scopus 로고
    • Characterization of enzymes from Legionella pneumophila involved in reversible adenylylation of Rab1 protein
    • Muller M.P., Shkumatov A.V., Oesterlin L.K., Schoebel S., Goody P.R., Goody R.S., et al. Characterization of enzymes from Legionella pneumophila involved in reversible adenylylation of Rab1 protein. J Biol Chem 2012, 287:35036-35046.
    • (2012) J Biol Chem , vol.287 , pp. 35036-35046
    • Muller, M.P.1    Shkumatov, A.V.2    Oesterlin, L.K.3    Schoebel, S.4    Goody, P.R.5    Goody, R.S.6
  • 254
    • 79960929331 scopus 로고    scopus 로고
    • Legionella pneumophila SidD is a deAMPylase that modifies Rab1
    • Tan Y.H., Luo Z.Q. Legionella pneumophila SidD is a deAMPylase that modifies Rab1. Nature 2011, 475:506-509.
    • (2011) Nature , vol.475 , pp. 506-509
    • Tan, Y.H.1    Luo, Z.Q.2
  • 256
    • 0032571385 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa exoenzyme S ADP-ribosylates Ras at multiple sites
    • Ganesan A.K., Frank D.W., Misra R.P., Schmidt G., Barbieri J.T. Pseudomonas aeruginosa exoenzyme S ADP-ribosylates Ras at multiple sites. J Biol Chem 1998, 273:7332-7337.
    • (1998) J Biol Chem , vol.273 , pp. 7332-7337
    • Ganesan, A.K.1    Frank, D.W.2    Misra, R.P.3    Schmidt, G.4    Barbieri, J.T.5
  • 257
    • 0033515484 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa exoenzyme S, a double ADP-ribosyltransferase, resembles vertebrate mono-ADP-ribosyltransferases
    • Ganesan A.K., Mende-Mueller L., Selzer J., Barbieri J.T. Pseudomonas aeruginosa exoenzyme S, a double ADP-ribosyltransferase, resembles vertebrate mono-ADP-ribosyltransferases. J Biol Chem 1999, 274:9503-9508.
    • (1999) J Biol Chem , vol.274 , pp. 9503-9508
    • Ganesan, A.K.1    Mende-Mueller, L.2    Selzer, J.3    Barbieri, J.T.4
  • 258
    • 0037199493 scopus 로고    scopus 로고
    • ADP-ribosylation and functional effects of Pseudomonas exoenzyme S on cellular RalA
    • Fraylick J.E., Riese M.J., Vincent T.S., Barbieri J.T., Olson J.C. ADP-ribosylation and functional effects of Pseudomonas exoenzyme S on cellular RalA. Biochemistry 2002, 41:9680-9687.
    • (2002) Biochemistry , vol.41 , pp. 9680-9687
    • Fraylick, J.E.1    Riese, M.J.2    Vincent, T.S.3    Barbieri, J.T.4    Olson, J.C.5
  • 260
    • 0029767410 scopus 로고    scopus 로고
    • ADP-ribosylation of proteins in Bacillus subtilis and its possible importance in sporulation
    • Huh J.W., Shima J., Ochi K. ADP-ribosylation of proteins in Bacillus subtilis and its possible importance in sporulation. J Bacteriol 1996, 178:4935-4941.
    • (1996) J Bacteriol , vol.178 , pp. 4935-4941
    • Huh, J.W.1    Shima, J.2    Ochi, K.3
  • 261
    • 0025290963 scopus 로고
    • ADP-ribosylation of membrane proteins of Streptomyces griseus strain 52-1
    • Penyige A., Barabas G., Szabo I., Ensign J.C. ADP-ribosylation of membrane proteins of Streptomyces griseus strain 52-1. FEMS Microbiol Lett 1990, 69:293-297.
    • (1990) FEMS Microbiol Lett , vol.69 , pp. 293-297
    • Penyige, A.1    Barabas, G.2    Szabo, I.3    Ensign, J.C.4
  • 262
  • 263
    • 0030137024 scopus 로고    scopus 로고
    • ADP-ribosylation of an 70-kilodalton protein of Klebsiella pneumoniae
    • Geipel U., Just I., Aktories K. ADP-ribosylation of an 70-kilodalton protein of Klebsiella pneumoniae. Infect Immun 1996, 64:1720-1723.
    • (1996) Infect Immun , vol.64 , pp. 1720-1723
    • Geipel, U.1    Just, I.2    Aktories, K.3
  • 264
    • 0024311314 scopus 로고
    • Demonstration and partial characterization of ADP-ribosylation in Pseudomonas maltophilia
    • Edmonds C., Griffin G.E., Johnstone A.P. Demonstration and partial characterization of ADP-ribosylation in Pseudomonas maltophilia. Biochem J 1989, 261:113-118.
    • (1989) Biochem J , vol.261 , pp. 113-118
    • Edmonds, C.1    Griffin, G.E.2    Johnstone, A.P.3
  • 265
    • 0035400143 scopus 로고    scopus 로고
    • An abundance of bacterial ADP-ribosyltransferases - implications for the origin of exotoxins and their human homologues
    • Pallen M.J., Lam A.C., Loman N.J., McBride A. An abundance of bacterial ADP-ribosyltransferases - implications for the origin of exotoxins and their human homologues. Trends Microbiol 2001, 9:302-307.
    • (2001) Trends Microbiol , vol.9 , pp. 302-307
    • Pallen, M.J.1    Lam, A.C.2    Loman, N.J.3    McBride, A.4
  • 266
    • 77956296853 scopus 로고    scopus 로고
    • Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family
    • Cui J.X., Yao Q., Li S., Ding X.J., Lu Q.H., Mao H.B., et al. Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family. Science 2010, 329:1215-1218.
    • (2010) Science , vol.329 , pp. 1215-1218
    • Cui, J.X.1    Yao, Q.2    Li, S.3    Ding, X.J.4    Lu, Q.H.5    Mao, H.B.6
  • 269
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides: succinimide-linked reactions that contribute to protein degradation
    • Geiger T., Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides: succinimide-linked reactions that contribute to protein degradation. J Biol Chem 1987, 262:785-794.
    • (1987) J Biol Chem , vol.262 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 270
    • 0015938729 scopus 로고
    • Rates of nonenyzmatic deamidation of glutaminyl and asparaginyl residues in pentapeptides
    • Robinson A.B., Scotchle Jw, McKerrow J.H. Rates of nonenyzmatic deamidation of glutaminyl and asparaginyl residues in pentapeptides. J Am Chem Soc 1973, 95:8156-8160.
    • (1973) J Am Chem Soc , vol.95 , pp. 8156-8160
    • Robinson, A.B.1    Scotchle, J.2    McKerrow, J.H.3
  • 271
    • 0034989185 scopus 로고    scopus 로고
    • Mass spectrometric evaluation of synthetic peptides as primary structure models for peptide and protein deamidation
    • Robinson N.E., Robinson A.B., Merrifield R.B. Mass spectrometric evaluation of synthetic peptides as primary structure models for peptide and protein deamidation. J Pept Res 2001, 57:483-493.
    • (2001) J Pept Res , vol.57 , pp. 483-493
    • Robinson, N.E.1    Robinson, A.B.2    Merrifield, R.B.3
  • 273
    • 0035836730 scopus 로고    scopus 로고
    • Prediction of protein deamidation rates from primary and three-dimensional structure
    • Robinson N.E., Robinson A.B. Prediction of protein deamidation rates from primary and three-dimensional structure. Proc Natl Acad Sci U S A 2001, 98:4367-4372.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4367-4372
    • Robinson, N.E.1    Robinson, A.B.2
  • 275
    • 0015102730 scopus 로고
    • Deamidation of asparaginyl residues as a hazard in experimental protein and peptide procedures
    • McKerrow J.H., Robinson A.B. Deamidation of asparaginyl residues as a hazard in experimental protein and peptide procedures. Anal Biochem 1971, 42:565-568.
    • (1971) Anal Biochem , vol.42 , pp. 565-568
    • McKerrow, J.H.1    Robinson, A.B.2
  • 276
    • 0016188201 scopus 로고
    • Deamidation of glutaminyl residues: dependence on pH, temperature and ionic-strength
    • Scotchle J.W., Robinson A.B. Deamidation of glutaminyl residues: dependence on pH, temperature and ionic-strength. Anal Biochem 1974, 59:319-322.
    • (1974) Anal Biochem , vol.59 , pp. 319-322
    • Scotchle, J.W.1    Robinson, A.B.2
  • 277
    • 0026008859 scopus 로고
    • Distribution of glutamine and asparagine residues and their near neighbors in peptides and proteins
    • Robinson A.B., Robinson L.R. Distribution of glutamine and asparagine residues and their near neighbors in peptides and proteins. Proc Natl Acad Sci U S A 1991, 88:8880-8884.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 8880-8884
    • Robinson, A.B.1    Robinson, L.R.2
  • 278
    • 38449123879 scopus 로고    scopus 로고
    • Chronoregulation by asparagine deamidation
    • Weintraub S.J., Deverman B.E. Chronoregulation by asparagine deamidation. Sci Signal 2007, 2007:re7.
    • (2007) Sci Signal , vol.2007
    • Weintraub, S.J.1    Deverman, B.E.2
  • 279
    • 77949425431 scopus 로고    scopus 로고
    • Widespread occurrence of non-enzymatic deamidations of asparagine residues in Yersinia pestis proteins resulting from alkaline pH membrane extraction conditions
    • Suh M.J., Alami H., Clark D.J., Parmar P.P., Robinson J.M., Huang S.T., et al. Widespread occurrence of non-enzymatic deamidations of asparagine residues in Yersinia pestis proteins resulting from alkaline pH membrane extraction conditions. Open Proteomics J 2008, 1:106-115.
    • (2008) Open Proteomics J , vol.1 , pp. 106-115
    • Suh, M.J.1    Alami, H.2    Clark, D.J.3    Parmar, P.P.4    Robinson, J.M.5    Huang, S.T.6
  • 281
    • 77952812537 scopus 로고    scopus 로고
    • Mass spectrometric analysis of asparagine deamidation and aspartate isomerization in polypeptides
    • Yang H.Q., Zubarev R.A. Mass spectrometric analysis of asparagine deamidation and aspartate isomerization in polypeptides. Electrophoresis 2010, 31:1764-1772.
    • (2010) Electrophoresis , vol.31 , pp. 1764-1772
    • Yang, H.Q.1    Zubarev, R.A.2
  • 282
    • 84864072032 scopus 로고    scopus 로고
    • Proteomics reveals evidence of cross-talk between protein modifications in bacteria: focus on acetylation and phosphorylation
    • Soufi B., Soares N.C., Ravikumar V., Macek B. Proteomics reveals evidence of cross-talk between protein modifications in bacteria: focus on acetylation and phosphorylation. Curr Opin Microbiol 2012, 15:357-363.
    • (2012) Curr Opin Microbiol , vol.15 , pp. 357-363
    • Soufi, B.1    Soares, N.C.2    Ravikumar, V.3    Macek, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.