메뉴 건너뛰기




Volumn 12, Issue 3, 2013, Pages 599-610

The escherichia coli peripheral inner membrane proteome

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYTOPLASM PROTEIN; CYTOPLASMIC PERIPHERAL INNER MEMBRANE PROTEOME; MULTIPROTEIN COMPLEX; PROTEOME; UNCLASSIFIED DRUG;

EID: 84874592097     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.024711     Document Type: Article
Times cited : (69)

References (89)
  • 5
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the universal protein resource (UniProt
    • Consortium, T. U. (2012) Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Res. 40, D71-D75
    • (2012) Nucleic Acids Res , vol.40
    • Consortium, T.U.1
  • 6
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer, S. J., and Nicolson, G. L. (1972) The fluid mosaic model of the structure of cell membranes. Science 175, 720-731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 7
    • 84882524309 scopus 로고    scopus 로고
    • Chapter 1: Functional roles of lipids in membranes
    • (E. V. Dennis and E. V. Jean, eds) 5th Ed., 1-I, Elsevier, San Diego
    • Dowhan, W., Bogdanov, M., and Mileykovskaya, E. (2008) Chapter 1: Functional roles of lipids in membranes. In Biochemistry of Lipids, Lipoproteins and Membranes (E. V. Dennis and E. V. Jean, eds) 5th Ed., pp. 1-I, Elsevier, San Diego
    • (2008) Biochemistry of Lipids, Lipoproteins and Membranes
    • Dowhan, W.1    Bogdanov, M.2    Mileykovskaya, E.3
  • 9
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • DOI 10.1083/jcb.93.1.97
    • Fujiki, Y., Hubbard, A. L., Fowler, S., and Lazarow, P. B. (1982) Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum. J. Cell Biol. 93, 97-102 (Pubitemid 12117045)
    • (1982) Journal of Cell Biology , vol.93 , Issue.1 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 10
    • 84874599474 scopus 로고    scopus 로고
    • Extraction of membrane proteins
    • (P. Cutler, ed) 2nd Ed., Humana Press, Totowa, NJ
    • Ohlendieck, K. (2003) Extraction of membrane proteins. In Protein Purification Protocols (P. Cutler, ed) 2nd Ed., pp. 283-290, Humana Press, Totowa, NJ
    • (2003) Protein Purification Protocols , pp. 283-290
    • Ohlendieck, K.1
  • 11
    • 0016221429 scopus 로고
    • Selective release of content from microsomal vesicles without membrane disassembly
    • Kreibich, G., and Sabatini, D. D. (1974) Selective release of content from microsomal vesicles without membrane disassembly. J. Cell Biol. 61, 789-807
    • (1974) J. Cell Biol. , vol.61 , pp. 789-807
    • Kreibich, G.1    Sabatini, D.D.2
  • 12
    • 34548202704 scopus 로고    scopus 로고
    • Proteomics of integral membrane proteins - Theory and application
    • DOI 10.1021/cr068286z
    • Speers, A. E., and Wu, C. C. (2007) Proteomics of integral membrane proteins: Theory and application. Chem. Rev. 107, 3687-3714 (Pubitemid 47322748)
    • (2007) Chemical Reviews , vol.107 , Issue.8 , pp. 3687-3714
    • Speers, A.E.1    Wu, C.C.2
  • 13
    • 33745127048 scopus 로고    scopus 로고
    • The Escherichia coli proteome: Past, present, and future prospects
    • DOI 10.1128/MMBR.00036-05
    • Han, M. J., and Lee, S. Y. (2006) The Escherichia coli proteome: Past, present, and future prospects. Microbiol. Mol. Biol. R. 70, 362-439 (Pubitemid 43895032)
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.2 , pp. 362-439
    • Han, M.-J.1    Lee, S.Y.2
  • 14
    • 70349327690 scopus 로고    scopus 로고
    • Exploring the inner membrane proteome of Escherichia coli: Which proteins are eluding detection and why?
    • Bernsel, A., and Daley, D. (2009) Exploring the inner membrane proteome of Escherichia coli: Which proteins are eluding detection and why? Trends Microbiol. 17, 444-449
    • (2009) Trends Microbiol. , vol.17 , pp. 444-449
    • Bernsel, A.1    Daley, D.2
  • 15
    • 23344450195 scopus 로고    scopus 로고
    • Detection and identification of stable oligomeric protein complexes in Escherichi coli inner membranes: A proteomics approach
    • DOI 10.1074/jbc.M501617200
    • Spelbrink, R. E. J., Kolkman, A., Slijper, M., Killian, J. A., and de Kruijff, B. (2005) Detection and identification of stable oligomeric protein complexes in Escherichia coli inner membranes. J. Biol. Chem. 280, 28742-28748 (Pubitemid 41105775)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.31 , pp. 28742-28748
    • Spelbrink, R.E.J.1    Kolkman, A.2    Slijper, M.3    Killian, J.A.4    De Kruijff, B.5
  • 17
    • 33845382343 scopus 로고    scopus 로고
    • Systematic identification of the subproteome of Escherichia coli cell envelope reveals the interaction network of membrane proteins and membrane-associated peripheral proteins
    • DOI 10.1021/pr060257h
    • Huang, C. Z., Lin, X. M., Wu, L. N., Zhang, D. F., Liu, D., Wang, S. Y., and Peng, X. X. (2006) Systematic identification of the subproteome of Escherichia coli cell envelope reveals the interaction network of membrane proteins and membrane-associated peripheral proteins. J. Proteome Res. 5, 3268-3276 (Pubitemid 44904318)
    • (2006) Journal of Proteome Research , vol.5 , Issue.12 , pp. 3268-3276
    • Huang, C.-Z.1    Lin, X.-M.2    Wu, L.-N.3    Zhang, D.-F.4    Liu, D.5    Wang, S.-Y.6    Peng, X.-X.7
  • 18
    • 33748346853 scopus 로고    scopus 로고
    • A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis
    • DOI 10.1002/elps.200500912
    • Lasserre, J. P., Beyne, E., Pyndiah, S., Lapaillerie, D., Claverol, S., and Bonneu, M. (2006) A complexomic study of Escherichia coli using twodimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27, 3306-3321 (Pubitemid 44336018)
    • (2006) Electrophoresis , vol.27 , Issue.16 , pp. 3306-3321
    • Lasserre, J.-P.1    Beyne, E.2    Pyndiah, S.3    Lapaillerie, D.4    Claverol, S.5    Bonneu, M.6
  • 19
    • 77954381798 scopus 로고    scopus 로고
    • Complexome of Escherichia coli envelope proteins under normal physiological conditions
    • Pan, J. Y., Li, H., Ma, Y., Chen, P., Zhao, P., Wang, S. Y., and Peng, X. X. (2010) Complexome of Escherichia coli envelope proteins under normal physiological conditions. J. Proteome Res. 9, 3730-3740
    • (2010) J. Proteome Res. , vol.9 , pp. 3730-3740
    • Pan, J.Y.1    Li, H.2    Ma, Y.3    Chen, P.4    Zhao, P.5    Wang, S.Y.6    Peng, X.X.7
  • 20
    • 84864661530 scopus 로고    scopus 로고
    • Alterations of protein complexes and pathways in genetic information flow and response to stimulus contribute to Escherichia coli resistance to balofloxacin
    • Li, H., Pan, J. Y., Liu, X. J., Gao, J. X., Wu, H. K., Wang, C., and Peng, X. X. (2012) Alterations of protein complexes and pathways in genetic information flow and response to stimulus contribute to Escherichia coli resistance to balofloxacin. Mol. Biosyst. 8, 2303-2311
    • (2012) Mol. Biosyst. , vol.8 , pp. 2303-2311
    • Li, H.1    Pan, J.Y.2    Liu, X.J.3    Gao, J.X.4    Wu, H.K.5    Wang, C.6    Peng, X.X.7
  • 23
    • 58349122286 scopus 로고    scopus 로고
    • EchoLOCATION: An in silico analysis of the subcellular locations of Escherichia coli proteins and comparison with experimentally derived locations
    • Horler, R. S. P., Butcher, A., Papangelopoulos, N., Ashton, P. D., and Thomas, G. H. (2009) EchoLOCATION: An in silico analysis of the subcellular locations of Escherichia coli proteins and comparison with experimentally derived locations. Bioinformatics 25, 163-166
    • (2009) Bioinformatics , vol.25 , pp. 163-166
    • Horler, R.S.P.1    Butcher, A.2    Papangelopoulos, N.3    Ashton, P.D.4    Thomas, G.H.5
  • 24
    • 0015993851 scopus 로고
    • Orientation of membrane vesicles from Escherichia coli prepared by different procedures
    • Futai, M. (1974) Orientation of membrane vesicles from Escherichia coli prepared by different procedures. J. Membrane Biol. 15, 15-28
    • (1974) J. Membrane Biol. , vol.15 , pp. 15-28
    • Futai, M.1
  • 25
    • 0016226796 scopus 로고
    • The organization of proteins in the human red blood cell membrane
    • Steck, T. L. (1974) The organization of proteins in the human red blood cell membrane. J. Cell Biol. 62, 1-19
    • (1974) J. Cell Biol. , vol.62 , pp. 1-19
    • Steck, T.L.1
  • 30
    • 27944504787 scopus 로고    scopus 로고
    • Analysis of the Escherichia coli RNA degradosome composition by a proteomic approach
    • DOI 10.1016/j.biochi.2005.07.012, PII S0300908405001902
    • Regonesi, M. E., Del Favero, M., Basilico, F., Briani, F., Benazzi, L., Tortora, P., Mauri, P., and Deho, G. (2006) Analysis of the Escherichia coli RNA degradosome composition by a proteomic approach. Biochimie (Paris) 88, 151-161 (Pubitemid 41668606)
    • (2006) Biochimie , vol.88 , Issue.2 , pp. 151-161
    • Regonesi, M.E.1    Del Favero, M.2    Basilico, F.3    Briani, F.4    Benazzi, L.5    Tortora, P.6    Mauri, P.7    Deho, G.8
  • 33
    • 75149180460 scopus 로고    scopus 로고
    • Unbiased quantitation of Escherichia coli membrane proteome using phase transfer surfactants
    • Masuda, T., Saito, N., Tomita, M., and Ishihama, Y. (2009) Unbiased quantitation of Escherichia coli membrane proteome using phase transfer surfactants. Mol. Cell. Proteomics 8, 2770-2777
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2770-2777
    • Masuda, T.1    Saito, N.2    Tomita, M.3    Ishihama, Y.4
  • 35
    • 77955102352 scopus 로고    scopus 로고
    • Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells
    • Taniguchi, Y., Choi, P. J., Li, G. W., Chen, H., Babu, M., Hearn, J., Emili, A., and Xie, X. S. (2010) Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells. Science 329, 533-538
    • (2010) Science , vol.329 , pp. 533-538
    • Taniguchi, Y.1    Choi, P.J.2    Li, G.W.3    Chen, H.4    Babu, M.5    Hearn, J.6    Emili, A.7    Xie, X.S.8
  • 37
    • 0037699937 scopus 로고    scopus 로고
    • Division site selection in Escherichia coli involves dynamic redistribution of min proteins within coiled structures that extend between the two cell poles
    • DOI 10.1073/pnas.1232225100
    • Shih, Y. L., Le, T., and Rothfield, L. (2003) Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles. Proc. Natl. Acad. Sci. U.S.A. 100, 7865-7870 (Pubitemid 36760061)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.13 , pp. 7865-7870
    • Shih, Y.-L.1    Le, T.2    Rothfield, L.3
  • 38
    • 0038444526 scopus 로고    scopus 로고
    • Membrane binding by MinD involves insertion of hydrophobic residues within the C-terminal amphipathic helix into the bilayer
    • DOI 10.1128/JB.185.15.4326-4335.2003
    • Zhou, H., and Lutkenhaus, J. (2003) Membrane binding by MinD involves insertion of hydrophobic residues within the C-Terminal amphipathic helix into the bilayer. J. Bacteriol. 185, 4326-4335 (Pubitemid 36890478)
    • (2003) Journal of Bacteriology , vol.185 , Issue.15 , pp. 4326-4335
    • Zhou, H.1    Lutkenhaus, J.2
  • 39
    • 0037101782 scopus 로고    scopus 로고
    • Aerobic sn-Glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic α-helix
    • DOI 10.1042/BJ20011853
    • Walz, A. C., Demel, R. A., de Kruijff, B., and Mutzel, R. (2002) Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic alpha-helix. Biochem. J. 365, 471-479 (Pubitemid 36135318)
    • (2002) Biochemical Journal , vol.365 , Issue.2 , pp. 471-479
    • Walz, A.-C.1    Demel, R.A.2    De Kruijff, B.3    Mutzel, R.4
  • 40
    • 0037406076 scopus 로고    scopus 로고
    • Solution structure of the N-terminal amphitropic domain of Escherichia coli glucose-specific enzyme IIA in membrane-mimetic micelles
    • DOI 10.1110/ps.0301503
    • Wang, G., Keifer, P. A., and Peterkofsky, A. (2003) Solution structure of the N-terminal amphitropic domain of Escherichia coli glucose-specific enzyme IIA in membrane-mimetic micelles. Protein Sci. 12, 1087-1096 (Pubitemid 36505442)
    • (2003) Protein Science , vol.12 , Issue.5 , pp. 1087-1096
    • Wang, G.1    Keifer, P.A.2    Peterkofsky, A.3
  • 41
    • 0034704122 scopus 로고    scopus 로고
    • Glucose of the Escherichia coli phosphotransferase system
    • DOI 10.1074/jbc.C000709200
    • Wang, G., Peterkofsky, A., and Clore, G. M. (2000) A novel membrane anchor function for the N-terminal amphipathic sequence of the signaltransducing protein IIAglucose of the Escherichia coli phosphotransferase system. J. Biol. Chem. 275, 39811-39814 (Pubitemid 32064597)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 39811-39814
    • Wang, G.1    Peterkofsky, A.2    Clore, G.M.3
  • 42
    • 34547584314 scopus 로고    scopus 로고
    • Advantages of combined transmembrane topology and signal peptide prediction - The Phobius web server
    • Kall, L., Krogh, A., and Sonnhammer, E. L. (2007) Advantages of combined transmembrane topology and signal peptide prediction-the Phobius web server. Nucleic Acids Res. 35, W429-W432
    • (2007) Nucleic Acids Res , vol.35
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 43
    • 0346494858 scopus 로고    scopus 로고
    • DEG: A database of essential genes
    • Zhang, R., Ou, H. Y., and Zhang, C. T. (2004) DEG: A database of essential genes. Nucleic Acids Res. 32, D271-D272 (Pubitemid 38081654)
    • (2004) Nucleic Acids Research , vol.32 , Issue.DATABASE ISS.
    • Zhang, R.1    Ou, H.-Y.2    Zhang, C.-T.3
  • 46
    • 0030956145 scopus 로고    scopus 로고
    • Bacterial cell division and the Z ring
    • DOI 10.1146/annurev.biochem.66.1.93
    • Lutkenhaus, J., and Addinall, S. G. (1997) Bacterial cell division and the Z ring. Annu. Rev. Biochem. 66, 93-116 (Pubitemid 27274653)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 93-116
    • Lutkenhaus, J.1    Addinall, S.G.2
  • 47
    • 33645699946 scopus 로고    scopus 로고
    • Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: Identification of new proteins at the DNA replication factory
    • Meile, J., Wu, L., Ehrlich, S., Errington, J., and Noirot, P. (2006) Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: Identification of new proteins at the DNA replication factory. Proteomics 6, 2135-2146
    • (2006) Proteomics , vol.6 , pp. 2135-2146
    • Meile, J.1    Wu, L.2    Ehrlich, S.3    Errington, J.4    Noirot, P.5
  • 48
    • 0042232285 scopus 로고    scopus 로고
    • The biotin carboxylase-biotin carboxyl carrier protein complex of Escherichia coli acetyl-CoA carboxylase
    • DOI 10.1074/jbc.M302507200
    • Choi-Rhee, E., and Cronan, J. E. (2003) The biotin carboxylase-biotin carboxyl carrier protein complex of Escherichia coli acetyl-CoA carboxylase. J. Biol. Chem. 278, 30806-30812 (Pubitemid 36994588)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 30806-30812
    • Choi-Rhee, E.1    Cronan, J.E.2
  • 49
    • 80054012758 scopus 로고    scopus 로고
    • Patterns of indirect protein interactions suggest a spatial organization to metabolism
    • Perez-Bercoff, A., McLysaght, A., and Conant, G. C. (2011) Patterns of indirect protein interactions suggest a spatial organization to metabolism. Mol. Biosyst. 7, 3056-3064
    • (2011) Mol. Biosyst. , vol.7 , pp. 3056-3064
    • Perez-Bercoff, A.1    McLysaght, A.2    Conant, G.C.3
  • 50
    • 43449119501 scopus 로고    scopus 로고
    • A computational analysis of protein interactions in metabolic networks reveals novel enzyme pairs potentially involved in metabolic channeling
    • DOI 10.1016/j.jtbi.2007.09.042, PII S0022519307004742
    • Huthmacher, C., Gille, C., and Holzhutter, H.-G. (2008) A computational analysis of protein interactions in metabolic networks reveals novel enzyme pairs potentially involved in metabolic channeling. J. Theor. Biol. 252, 456-464 (Pubitemid 351671801)
    • (2008) Journal of Theoretical Biology , vol.252 , Issue.3 , pp. 456-464
    • Huthmacher, C.1    Gille, C.2    Holzhutter, H.-G.3
  • 52
    • 11144273935 scopus 로고    scopus 로고
    • Arabidopsis plasma membrane proteomics identifies components of transport, signal transduction and membrane trafficking
    • Alexandersson, E., Saalbach, G., Larsson, C., and Kjellbom, P. (2004) Arabidopsis plasma membrane proteomics identifies components of transport, signal transduction and membrane trafficking. Plant Cell Physiol. 45, 1543-1556 (Pubitemid 40033462)
    • (2004) Plant and Cell Physiology , vol.45 , Issue.11 , pp. 1543-1556
    • Alexandersson, E.1    Saalbach, G.2    Larsson, C.3    Kjellbom, P.4
  • 53
    • 31344458312 scopus 로고    scopus 로고
    • Proteomic analysis of chlorosome-depleted membranes of the green sulfur bacterium Chlorobium tepidum
    • DOI 10.1002/pmic.200402030
    • Aivaliotis, M., Haase, W., Karas, M., and Tsiotis, G. (2006) Proteomic analysis of chlorosome-depleted membranes of the green sulfur bacterium Chlorobium tepidum. Proteomics 6, 217-232 (Pubitemid 43142947)
    • (2006) Proteomics , vol.6 , Issue.1 , pp. 217-232
    • Aivaliotis, M.1    Haase, W.2    Karas, M.3    Tsiotis, G.4
  • 54
    • 33947577006 scopus 로고    scopus 로고
    • An alternative strategy for the membrane proteome analysis of the green sulfur bacterium Chlorobium tepidum using blue native PAGE and 2-D PAGE on purified membranes
    • DOI 10.1021/pr060553u
    • Aivaliotis, M., Karas, M., and Tsiotis, G. (2007) An alternative strategy for the membrane proteome analysis of the green sulfur bacterium Chlorobium tepidum using blue native PAGE and 2-D PAGE on purified membranes. J. Proteome Res. 6, 1048-1058 (Pubitemid 46480469)
    • (2007) Journal of Proteome Research , vol.6 , Issue.3 , pp. 1048-1058
    • Aivaliotis, M.1    Karas, M.2    Tsiotis, G.3
  • 55
    • 77956058146 scopus 로고    scopus 로고
    • Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry
    • Sinz, A. (2010) Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry. Anal. Bioanal. Chem. 397, 3433-3440
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 3433-3440
    • Sinz, A.1
  • 56
    • 84862687131 scopus 로고    scopus 로고
    • In vivo protein complex topologies: Sights through a cross-linking lens
    • Bruce, J. E. (2012) In vivo protein complex topologies: Sights through a cross-linking lens. Proteomics 12, 1565-1575
    • (2012) Proteomics , vol.12 , pp. 1565-1575
    • Bruce, J.E.1
  • 57
    • 79851513173 scopus 로고    scopus 로고
    • The beginning of a beautiful friendship: Cross-linking/ mass spectrometry and modelling of proteins and multi-protein complexes
    • Rappsilber, J. (2011) The beginning of a beautiful friendship: Cross-linking/ mass spectrometry and modelling of proteins and multi-protein complexes. J. Struct. Biol. 173, 530-540
    • (2011) J. Struct. Biol. , vol.173 , pp. 530-540
    • Rappsilber, J.1
  • 58
    • 0032857728 scopus 로고    scopus 로고
    • The Escherichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltransferase activity
    • Raffaelli, N., Lorenzi, T., Mariani, P. L., Emanuelli, M., Amici, A., Ruggieri, S., and Magni, G. (1999) The Escherichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltransferase activity. J. Bacteriol. 181, 5509-5511 (Pubitemid 29416377)
    • (1999) Journal of Bacteriology , vol.181 , Issue.17 , pp. 5509-5511
    • Raffaelli, N.1    Lorenzi, T.2    Mariani, P.L.3    Emanuelli, M.4    Amici, A.5    Ruggieri, S.6    Magni, G.7
  • 62
    • 54249138245 scopus 로고    scopus 로고
    • The RNase E of Escherichia coli is a membrane-binding protein
    • Khemici, V., Poljak, L., Luisi, B. F., and Carpousis, A. J. (2008) The RNase E of Escherichia coli is a membrane-binding protein. Mol. Microbiol. 70, 799-813
    • (2008) Mol. Microbiol. , vol.70 , pp. 799-813
    • Khemici, V.1    Poljak, L.2    Luisi, B.F.3    Carpousis, A.J.4
  • 63
    • 34548704307 scopus 로고    scopus 로고
    • Escherichia coli phage-shock protein A (PspA) binds to membrane phospholipids and repairs proton leakage of the damaged membranes
    • DOI 10.1111/j.1365-2958.2007.05893.x
    • Kobayashi, R., Suzuki, T., and Yoshida, M. (2007) Escherichia coli phageshock protein A (PspA) binds to membrane phospholipids and repairs proton leakage of the damaged membranes. Mol. Microbiol. 66, 100-109 (Pubitemid 47414790)
    • (2007) Molecular Microbiology , vol.66 , Issue.1 , pp. 100-109
    • Kobayashi, R.1    Suzuki, T.2    Yoshida, M.3
  • 64
    • 0037315127 scopus 로고    scopus 로고
    • Interactions between phage-shock proteins in Escherichia coli
    • DOI 10.1128/JB.185.4.1174-1180.2003
    • Adams, H., Teertstra, W., Demmers, J., Boesten, R., and Tommassen, J. (2003) Interactions between phage-shock proteins in Escherichia coli. J. Bacteriol. 185, 1174-1180 (Pubitemid 36176849)
    • (2003) Journal of Bacteriology , vol.185 , Issue.4 , pp. 1174-1180
    • Adams, H.1    Teertstra, W.2    Demmers, J.3    Boesten, R.4    Tommassen, J.5
  • 65
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • DOI 10.1016/S0968-0004(98)01335-8, PII S0968000498013358
    • Jeffery, C. J. (1999) Moonlighting proteins. Trends Biochem. Sci. 24, 8-11 (Pubitemid 29074455)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.1 , pp. 8-11
    • Jeffery, C.J.1
  • 67
    • 33845933677 scopus 로고    scopus 로고
    • Antagonistic interactions of kleisins and DNA with bacterial condensin MukB
    • DOI 10.1074/jbc.M606723200
    • Petrushenko, Z. M., Lai, C. H., and Rybenkov, V. V. (2006) Antagonistic interactions of kleisins and DNA with bacterial Condensin MukB. J. Biol. Chem. 281, 34208-34217 (Pubitemid 46036629)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 34208-34217
    • Petrushenko, Z.M.1    Lai, C.-H.2    Rybenkov, V.V.3
  • 68
    • 78649646536 scopus 로고    scopus 로고
    • Advances in understanding E. coli cell fission
    • de Boer, P. A. (2010) Advances in understanding E. coli cell fission. Curr. Opin. Microbiol. 13, 730-737
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 730-737
    • De Boer, P.A.1
  • 69
    • 45249100907 scopus 로고    scopus 로고
    • The extracytoplasmic stress factor, sigma(E), is required to maintain cell envelope integrity in Escherichia coli
    • Hayden, J. D., and Ades, S. E. (2008) The extracytoplasmic stress factor, sigma(E), is required to maintain cell envelope integrity in Escherichia coli. PLoS One 3, e1573
    • (2008) PLoS One , vol.3
    • Hayden, J.D.1    Ades, S.E.2
  • 71
    • 77949567575 scopus 로고    scopus 로고
    • Bacterial actin MreB assembles in complex with cell shape protein RodZ
    • van den Ent, F., Johnson, C. M., Persons, L., de Boer, P., and Lowe, J. (2010) Bacterial actin MreB assembles in complex with cell shape protein RodZ. EMBO J. 29, 1081-1090
    • (2010) EMBO J. , vol.29 , pp. 1081-1090
    • Van Den Ent, F.1    Johnson, C.M.2    Persons, L.3    De Boer, P.4    Lowe, J.5
  • 72
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli
    • Bendezu, F. O., Hale, C. A., Bernhardt, T. G., and de Boer, P. A. (2009) RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli. EMBO J. 28, 193-204
    • (2009) EMBO J. , vol.28 , pp. 193-204
    • Bendezu, F.O.1    Hale, C.A.2    Bernhardt, T.G.3    De Boer, P.A.4
  • 73
    • 79960913936 scopus 로고    scopus 로고
    • Direct membrane binding by bacterial actin MreB
    • Salje, J., van den Ent, F., de Boer, P., and Lowe, J. (2011) Direct membrane binding by bacterial actin MreB. Mol. Cell 43, 478-487
    • (2011) Mol. Cell , vol.43 , pp. 478-487
    • Salje, J.1    Van Den Ent, F.2    De Boer, P.3    Lowe, J.4
  • 74
    • 29944438325 scopus 로고    scopus 로고
    • Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli
    • DOI 10.1101/gad.366606
    • Kruse, T., Blagoev, B., Lobner-Olesen, A., Wachi, M., Sasaki, K., Iwai, N., Mann, M., and Gerdes, K. (2006) Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli. Gene Dev. 20, 113-124 (Pubitemid 43042672)
    • (2006) Genes and Development , vol.20 , Issue.1 , pp. 113-124
    • Kruse, T.1    Blagoev, B.2    Lobner-Olesen, A.3    Wachi, M.4    Sasaki, K.5    Iwai, N.6    Mann, M.7    Gerdes, K.8
  • 76
    • 0017878274 scopus 로고
    • Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli
    • Schryvers, A., Lohmeier, E., and Weiner, J. H. (1978) Chemical and functional properties of the native and reconstituted forms of the membranebound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli. J. Biol. Chem. 253, 783-788 (Pubitemid 8271455)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.3 , pp. 783-788
    • Schryvers, A.1    Lohmeier, E.2    Weiner, J.H.3
  • 77
    • 0013818652 scopus 로고
    • Growth stasis by accumulated L-alpha-glycerophosphate in Escherichia coli
    • Cozzarelli, N. R., Koch, J. P., Hayashi, S., and Lin, E. C. (1965) Growth stasis by accumulated L-alpha-glycerophosphate in Escherichia coli. J. Bacteriol. 90, 1325-1329
    • (1965) J. Bacteriol. , vol.90 , pp. 1325-1329
    • Cozzarelli, N.R.1    Koch, J.P.2    Hayashi, S.3    Lin, E.C.4
  • 79
    • 77649268964 scopus 로고    scopus 로고
    • Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein
    • Soufo, H., Reimold, C., Linne, U., Knust, T., Gescher, J., and Graumann, P. L. (2010) Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein. Proc. Natl. Acad. Sci. U.S.A. 107, 3163-3168
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 3163-3168
    • Soufo, H.1    Reimold, C.2    Linne, U.3    Knust, T.4    Gescher, J.5    Graumann, P.L.6
  • 81
    • 77955237447 scopus 로고    scopus 로고
    • UniProt, The Universal Protein Resource (UniProt) in 2010
    • UniProt (2010) The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res. 38, D142-D148
    • (2010) Nucleic Acids Res. , vol.38
  • 82
    • 0036674269 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • DOI 10.1101/gr.473902
    • Rappsilber, J., Ryder, U., Lamond, A. I., and Mann, M. (2002) Large-scale proteomic analysis of the human spliceosome. Genome Res. 12, 1231-1245 (Pubitemid 41264425)
    • (2002) Genome Research , vol.12 , Issue.8 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 83
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • DOI 10.1038/nmeth785
    • Elias, J. E., Haas, W., Faherty, B. K., and Gygi, S. P. (2005) Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations. Nat. Meth. 2, 667-675 (Pubitemid 41223093)
    • (2005) Nature Methods , vol.2 , Issue.9 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 85
    • 0033971754 scopus 로고    scopus 로고
    • EcoGene: A genome sequence database for Escherichia coli K-12
    • Rudd, K. E. (2000) EcoGene: A genome sequence database for Escherichia coli K-12. Nucleic Acids Res. 28, 60-64 (Pubitemid 30047714)
    • (2000) Nucleic Acids Research , vol.28 , Issue.1 , pp. 60-64
    • Rudd, K.E.1
  • 86
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotech. 26, 1367-1372
    • (2008) Nat. Biotech. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 89
    • 84870859321 scopus 로고    scopus 로고
    • Breaking on through to the other side: Protein export through the bacterial Sec system
    • Chatzi, K., Sardis, M. F., Karamanou, S., and Economou, A. (2013) Breaking on through to the other side: Protein export through the bacterial Sec system. Biochem. J. 449, 25-37
    • (2013) Biochem. J. , vol.449 , pp. 25-37
    • Chatzi, K.1    Sardis, M.F.2    Karamanou, S.3    Economou, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.