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Volumn 7, Issue 3, 2011, Pages 299-310

Global transcriptome analysis of the E. coli O157 response to Agrimonia pilosa extract

Author keywords

Agrimonia pilosa; Antibiotic; Cell wall inhibition; Cys sulfur metabolism; FolA

Indexed keywords


EID: 84863011514     PISSN: 1738642X     EISSN: 20928467     Source Type: Journal    
DOI: 10.1007/s13273-011-0036-7     Document Type: Article
Times cited : (7)

References (70)
  • 1
    • 57449117697 scopus 로고    scopus 로고
    • Risk of hepatotoxicity associated with the use of telithromycin: A signal detection using data mining algorithms
    • Chen, Y., Guo, J. J., Healy, D. P., Lin, X. & Patel, N. C. Risk of hepatotoxicity associated with the use of telithromycin: a signal detection using data mining algorithms. Ann Pharmacother 42:1791-1796 (2008).
    • (2008) Ann Pharmacother , vol.42 , pp. 1791-1796
    • Chen, Y.1    Guo, J.J.2    Healy, D.P.3    Lin, X.4    Patel, N.C.5
  • 2
    • 0042534744 scopus 로고
    • What is an antibiotic or an antibiotic substance
    • Waksman, S. A. What is an antibiotic or an antibiotic substance. Micologia 5:565-569 (1947).
    • (1947) Micologia , vol.5 , pp. 565-569
    • Waksman, S.A.1
  • 3
    • 84863020153 scopus 로고    scopus 로고
    • Effect of extract Agrimonia pilosa L. on biological activity in rats Korean
    • Lee, Y. H., Kim, M. B. & Chung, D. S. Effect of extract Agrimonia pilosa L. on biological activity in rats Korean. J Medicinal Crop Sci 10:167 (2002).
    • (2002) J Medicinal Crop Sci , vol.10 , pp. 167
    • Lee, Y.H.1    Kim, M.B.2    Chung, D.S.3
  • 4
    • 31344477956 scopus 로고    scopus 로고
    • Polyphenolic profile characterization of Agrimonia eupatoria L. by HPLC with different detection devices
    • DOI 10.1002/bmc.533
    • Correia, H., Gonzalez-Paramas, A., Amaral, M. T., Santos-Buelga, C. & Batista, M. T. Polyphenolic profile characterization of Agrimonia eupatoria L. by HPLC with different detection devices. Biomed Chromatogr 20:88-94 (2006). (Pubitemid 43141410)
    • (2006) Biomedical Chromatography , vol.20 , Issue.1 , pp. 88-94
    • Correia, H.1    Gonzalez-Paramas, A.2    Amaral, M.T.3    Santos-Buelga, C.4    Batista, M.T.5
  • 6
    • 79952032148 scopus 로고    scopus 로고
    • Drug hypersensitivity: Flare-up reactions, cross-reactivity and multiple drug hypersensitivity
    • Pichler, W. J., Daubner, B. & Kawabata, T. Drug hypersensitivity: Flare-up reactions, cross-reactivity and multiple drug hypersensitivity. J Dermatol 38:216-221 (2011).
    • (2011) J Dermatol , vol.38 , pp. 216-221
    • Pichler, W.J.1    Daubner, B.2    Kawabata, T.3
  • 7
    • 33745842893 scopus 로고    scopus 로고
    • The solution structure of Escherichia coli Wzb reveals a novel substrate recognition mechanism of prokaryotic low molecular weight protein-tyrosine phosphatases
    • DOI 10.1074/jbc.M601263200
    • Lescop, E. et al. The solution structure of Escherichia coli Wzb reveals a novel substrate recognition mechanism of prokaryotic low molecular weight proteintyrosine phosphatases. J Biol Chem 281:19570-19577 (2006). (Pubitemid 44035460)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.28 , pp. 19570-19577
    • Lescop, E.1    Hu, Y.2    Xu, H.3    Hu, W.4    Chen, J.5    Xia, B.6    Jin, C.7
  • 8
    • 0032549520 scopus 로고    scopus 로고
    • The Src and signal transducers and activators of transcription pathways as specific targets for low molecular weight phosphotyrosine-protein phosphatase in platelet-derived growth factor signaling
    • DOI 10.1074/jbc.273.12.6776
    • Chiarugi, P. et al. The Src and signal transducers and activators of transcription pathways as specific targets for low molecular weight phosphotyrosine-protein phosphatase in platelet-derived growth factor signaling. J Biol Chem 273:6776-6785 (1998). (Pubitemid 28160340)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.12 , pp. 6776-6785
    • Chiarugi, P.1    Cirri, P.2    Marra, F.3    Raugei, G.4    Fiaschi, T.5    Camici, G.6    Manao, G.7    Romanelli, R.G.8    Ramponi, G.9
  • 11
    • 0026589363 scopus 로고
    • D-alanine: D-alanine ligase of escherichia coli. Expression, purification and inhibitory studies on the cloned enzyme
    • al-Bar, O. A., O'Connor, C. D., Giles, I. G. & Akhtar, M. D-alanine: D-alanine ligase of Escherichia coli. Expression, purification and inhibitory studies on the cloned enzyme. Biochem J 282:747-752 (1992).
    • (1992) Biochem J , vol.282 , pp. 747-752
    • Al-Bar, O.A.1    O'Connor, C.D.2    Giles, I.G.3    Akhtar, M.4
  • 12
    • 77649268964 scopus 로고    scopus 로고
    • Bacterial translation elongation factor EF-tu interacts and colocalizes with actin-like MreB protein
    • Defeu Soufo, H. J. et al. Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein. Proc Natl Acad Sci USA 107:3163-3168 (2010).
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3163-3168
    • Defeu Soufo, H.J.1
  • 13
    • 60649104907 scopus 로고    scopus 로고
    • Regulation of cell wall morphogenesis in bacillus subtilis by recruitment of PBP1 to the MreB helix
    • Kawai, Y., Daniel, R. A. & Errington, J. Regulation of cell wall morphogenesis in Bacillus subtilis by recruitment of PBP1 to the MreB helix. Mol Microbiol 71: 1131-1144 (2009).
    • (2009) Mol Microbiol , vol.71 , pp. 1131-1144
    • Kawai, Y.1    Daniel, R.A.2    Errington, J.3
  • 14
    • 0041836122 scopus 로고    scopus 로고
    • Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli
    • DOI 10.1128/JB.185.18.5342-5348.2003
    • Meisel, U., Holtje, J. V. & Vollmer, W. Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli. J Bacteriol 185:5342-5348 (2003). (Pubitemid 37082390)
    • (2003) Journal of Bacteriology , vol.185 , Issue.18 , pp. 5342-5348
    • Meisel, U.1    Holtje, J.-V.2    Vollmer, W.3
  • 16
    • 0027432886 scopus 로고
    • Two overlapping genes encoding membrane proteins required for bacteriophage N4 adsorption
    • Kiino, D. R., Singer, M. S. & Rothman-Denes, L. B. Two overlapping genes encoding membrane proteins required for bacteriophage N4 adsorption. J Bacteriol 175:7081-7085 (1993). (Pubitemid 23322461)
    • (1993) Journal of Bacteriology , vol.175 , Issue.21 , pp. 7081-7085
    • Kiino, D.R.1    Singer, M.S.2    Rothman-Denes, L.B.3
  • 18
    • 2442605626 scopus 로고    scopus 로고
    • As(III) and Sb(III) Uptake by GlpF and Efflux by ArsB in Escherichia coli
    • DOI 10.1074/jbc.M400037200
    • Meng, Y. L., Liu, Z. & Rosen, B. P. As(III) and Sb(III) uptake by GlpF and efflux by ArsB in Escherichia coli. J Biol Chem 279:18334-18341 (2004). (Pubitemid 38623248)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18334-18341
    • Meng, Y.-L.1    Liu, Z.2    Rosen, B.P.3
  • 20
    • 0033374883 scopus 로고    scopus 로고
    • TRAP transporters: An ancient family of extracytoplasmic solute-receptor-dependent secondary active transporters
    • Rabus, R., Jack, D. L., Kelly, D. J. & Saier, M. H., Jr. TRAP transporters: an ancient family of extracytoplasmic solute-receptor-dependent secondary active transporters. Microbiology 145:3431-3445 (1999). (Pubitemid 30018787)
    • (1999) Microbiology , vol.145 , Issue.12 , pp. 3431-3445
    • Rabus, R.1    Jack, D.L.2    Kelly, D.J.3    Saier Jr., M.H.4
  • 22
    • 33845991863 scopus 로고    scopus 로고
    • On parallel and antiparallel topology of a homodimeric multidrug transporter
    • DOI 10.1074/jbc.M607186200
    • Soskine, M., Mark, S., Tayer, N., Mizrachi, R. & Schuldiner, S. On parallel and antiparallel topology of a homodimeric multidrug transporter. J Biol Chem 281: 36205-36212 (2006). (Pubitemid 46041355)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 36205-36212
    • Soskine, M.1    Mark, S.2    Tayer, N.3    Mizrachi, R.4    Schuldiner, S.5
  • 23
    • 0034680862 scopus 로고    scopus 로고
    • Identification of the putrescine recognition site on polyamine transport protein PotE
    • Kashiwagi, K. et al. Identification of the putrescine recognition site on polyamine transport protein PotE. J Biol Chem 275:36007-36012 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 36007-36012
    • Kashiwagi, K.1
  • 24
    • 33749376764 scopus 로고    scopus 로고
    • Identification of the cadaverine recognition site on the cadaverine-lysine antiporter CadB
    • DOI 10.1074/jbc.M600754200
    • Soksawatmaekhin, W., Uemura, T., Fukiwake, N., Kashiwagi, K. & Igarashi, K. Identification of the cadaverine recognition site on the cadaverine-lysine antiporter CadB. J Biol Chem 281:29213-29220 (2006). (Pubitemid 44507064)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 29213-29220
    • Soksawatmaekhin, W.1    Uemura, T.2    Fukiwake, N.3    Kashiwagi, K.4    Igarashi, K.5
  • 25
    • 0036064516 scopus 로고    scopus 로고
    • The putative response regulator BaeR stimulates multidrug resistance of Escherichia coli via a novel multidrug exporter system, MdtABC
    • DOI 10.1128/JB.184.15.4161-4167.2002
    • Nagakubo, S., Nishino, K., Hirata, T. & Yamaguchi, A. The putative response regulator BaeR stimulates multidrug resistance of Escherichia coli via a novel multidrug exporter system, MdtABC. J Bacteriol 184: 4161-4167 (2002). (Pubitemid 34774296)
    • (2002) Journal of Bacteriology , vol.184 , Issue.15 , pp. 4161-4167
    • Nagakubo, S.1    Nishino, K.2    Hirata, T.3    Yamaguchi, A.4
  • 26
    • 0036206907 scopus 로고    scopus 로고
    • EvgA of the two-component signal transduction system modulates production of the YhiUV multidrug transporter in Escherichia coli
    • DOI 10.1128/JB.184.8.2319-2323.2002
    • Nishino, K. & Yamaguchi, A. EvgA of the two-component signal transduction system modulates production of the yhiUV multidrug transporter in Escherichia coli. J Bacteriol 184:2319-2323 (2002). (Pubitemid 34259685)
    • (2002) Journal of Bacteriology , vol.184 , Issue.8 , pp. 2319-2323
    • Nishino, K.1    Yamaguchi, A.2
  • 27
    • 77955849245 scopus 로고    scopus 로고
    • Contribution of rpoS and bolA genes in biofilm formation in escherichia coli K-12 MG1655
    • Adnan, M., Morton, G., Singh, J. & Hadi, S. Contribution of rpoS and bolA genes in biofilm formation in Escherichia coli K-12 MG1655. Mol Cell Biochem 342:207-213 (2010).
    • (2010) Mol Cell Biochem , vol.342 , pp. 207-213
    • Adnan, M.1    Morton, G.2    Singh, J.3    Hadi, S.4
  • 28
    • 67650835651 scopus 로고    scopus 로고
    • Localized expression profiles of rpoS in escherichia coli biofilms
    • Ito, A., May, T., Taniuchi, A., Kawata, K. & Okabe, S. Localized expression profiles of rpoS in Escherichia coli biofilms. Biotechnol Bioeng 103:975-983 (2009).
    • (2009) Biotechnol Bioeng , vol.103 , pp. 975-983
    • Ito, A.1    May, T.2    Taniuchi, A.3    Kawata, K.4    Okabe, S.5
  • 29
    • 33745210122 scopus 로고    scopus 로고
    • Effect of rpoS gene knockout on the metabolism of escherichia coli during exponential growth phase and early stationary phase based on gene expressions, enzyme activities and intracellular metabolite concentrations
    • Rahman, M., Hasan, M. R., Oba, T. & Shimizu, K. Effect of rpoS gene knockout on the metabolism of Escherichia coli during exponential growth phase and early stationary phase based on gene expressions, enzyme activities and intracellular metabolite concentrations. Biotechnol Bioeng 94:585-595 (2006).
    • (2006) Biotechnol Bioeng , vol.94 , pp. 585-595
    • Rahman, M.1    Hasan, M.R.2    Oba, T.3    Shimizu, K.4
  • 30
    • 5144223827 scopus 로고    scopus 로고
    • Stress and survival of aging Escherichia coli rpoS colonies
    • DOI 10.1534/genetics.104.028704
    • Saint-Ruf, C., Taddei, F. & Matic, I. Stress and survival of aging Escherichia coli rpoS colonies. Genetics 168:541-546 (2004). (Pubitemid 39346615)
    • (2004) Genetics , vol.168 , Issue.1 , pp. 541-546
    • Saint-Ruf, C.1    Taddei, F.2    Matic, I.3
  • 31
    • 4744338150 scopus 로고    scopus 로고
    • Genetic evidence for pre-recruitment as the mechanism of transcription activation by SoxS of Escherichia coli: The dominance of DNA binding mutations of SoxS
    • DOI 10.1016/j.jmb.2004.09.007, PII S0022283604011349
    • Griffith, K. L. & Wolf, R. E., Jr. Genetic evidence for pre-recruitment as the mechanism of transcription activation by SoxS of Escherichia coli: the dominance of DNA binding mutations of SoxS. J Mol Biol 344: 1-10 (2004). (Pubitemid 39422371)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.1 , pp. 1-10
    • Griffith, K.L.1    Wolf Jr., R.E.2
  • 32
    • 77954760817 scopus 로고    scopus 로고
    • Proteinprotein interactions between sigma(70) region 4 of RNA polymerase and escherichia coli SoxS, a transcription activator that functions by the prerecruitment mechanism: Evidence for "off-DNA" and, "on-DNA" interactions
    • Zafar, M. A., Shah, I. M. & Wolf, R. E., Jr. Proteinprotein interactions between sigma(70) region 4 of RNA polymerase and Escherichia coli SoxS, a transcription activator that functions by the prerecruitment mechanism: evidence for "off-DNA" and "on-DNA" interactions. J Mol Biol 401:13-32 (2010).
    • (2010) J Mol Biol , vol.401 , pp. 13-32
    • Zafar, M.A.1    Shah, I.M.2    Wolf Jr., R.E.3
  • 33
    • 4744368729 scopus 로고    scopus 로고
    • Novel protein-protein interaction between Escherichia coli SoxS and the DNA binding determinant of the RNA polymerase α subunit: SoxS functions as a co-sigma factor and redeploys RNA polymerase from UP-element-containing promoters to SoxS-dependent promoters during oxidative stress
    • DOI 10.1016/j.jmb.2004.08.057, PII S0022283604010484
    • Shah, I. M. & Wolf, R. E., Jr. Novel protein - protein interaction between Escherichia coli SoxS and the DNA binding determinant of the RNA polymerase alpha subunit: SoxS functions as a co-sigma factor and redeploys RNA polymerase from UP-element-containing promoters to SoxS-dependent promoters during oxidative stress. J Mol Biol 343:513-532 (2004). (Pubitemid 39311602)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.3 , pp. 513-532
    • Shah, I.M.1    Wolf Jr., R.E.2
  • 34
    • 3142764685 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis cysD and cysNC genes form a stress-induced operon that encodes a tri-functional sulfate-activating complex
    • Pinto, R., Tang, Q. X., Britton, W. J., Leyh, T. S. & Triccas, J. A. The Mycobacterium tuberculosis cysD and cysNC genes form a stress-induced operon that encodes a tri-functional sulfate-activating complex. Microbiology 150:1681-1686 (2004). (Pubitemid 38923667)
    • (2004) Microbiology , vol.150 , Issue.6 , pp. 1681-1686
    • Pinto, R.1    Tang, Q.X.2    Britton, W.J.3    Leyh, T.S.4    Triccas, J.A.5
  • 36
    • 56449090762 scopus 로고    scopus 로고
    • Rising from the RecQ-age: The role of human RecQ helicases in genome maintenance
    • Bohr, V. A. Rising from the RecQ-age: the role of human RecQ helicases in genome maintenance. Trends Biochem Sci 33:609-620 (2008).
    • (2008) Trends Biochem Sci , vol.33 , pp. 609-620
    • Bohr, V.A.1
  • 37
    • 13244284641 scopus 로고    scopus 로고
    • The structure of the TrmE GTP-binding protein and its implications for tRNA modification
    • DOI 10.1038/sj.emboj.7600507
    • Scrima, A., Vetter, I. R., Armengod, M. E. & Wittinghofer, A. The structure of the TrmE GTP-binding protein and its implications for tRNA modification. EMBO J 24:23-33 (2005). (Pubitemid 40188460)
    • (2005) EMBO Journal , vol.24 , Issue.1 , pp. 23-33
    • Scrima, A.1    Vetter, I.R.2    Armengod, M.E.3    Wittinghofer, A.4
  • 38
    • 77952787295 scopus 로고    scopus 로고
    • Stabilization of G domain conformations in the tRNA-modifying MnmE-gida complex observed with double electron electron resonance spectroscopy
    • Bohme, S. et al. Stabilization of G domain conformations in the tRNA-modifying MnmE-GidA complex observed with double electron electron resonance spectroscopy. J Biol Chem 285:16991-17000 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 16991-17000
    • Bohme, S.1
  • 39
    • 0023645239 scopus 로고
    • Structure of escherichia coli dnaC. Identification of a cysteine residue possibly involved in association with dnaB protein
    • Nakayama, N., Bond, M. W., Miyajima, A., Kobori, J. & Arai, K. Structure of Escherichia coli dnaC. Identification of a cysteine residue possibly involved in association with dnaB protein. J Biol Chem 262:10475-10480 (1987).
    • (1987) J Biol Chem , vol.262 , pp. 10475-10480
    • Nakayama, N.1    Bond, M.W.2    Miyajima, A.3    Kobori, J.4    Arai, K.5
  • 40
    • 44949157717 scopus 로고    scopus 로고
    • Biochemical identification of base and phosphate contacts between fis and a high-affinity DNA binding site
    • Shao, Y., Feldman-Cohen, L. S. & Osuna, R. Biochemical identification of base and phosphate contacts between Fis and a high-affinity DNA binding site. J Mol Biol 380:327-339 (2008).
    • (2008) J Mol Biol , vol.380 , pp. 327-339
    • Shao, Y.1    Feldman-Cohen, L.S.2    Osuna, R.3
  • 41
    • 0031442693 scopus 로고    scopus 로고
    • Folate and antifolate pharmacology
    • Kamen, B. Folate and antifolate pharmacology. Semin Oncol 24:S18-30-S18-39 (1997).
    • (1997) Semin Oncol , vol.24
    • Kamen, B.1
  • 42
    • 0031903189 scopus 로고    scopus 로고
    • Folate, vitamin B12, homocysteine status and DNA damage in young Australian adults
    • DOI 10.1093/carcin/19.7.1163
    • Fenech, M., Aitken, C. & Rinaldi, J. Folate, vitamin B12, homocysteine status and DNA damage in young Australian adults. Carcinogenesis 19:1163-1171 (1998). (Pubitemid 28375365)
    • (1998) Carcinogenesis , vol.19 , Issue.7 , pp. 1163-1171
    • Fenech, M.1    Aitken, C.2    Rinaldi, J.3
  • 43
    • 0027615606 scopus 로고
    • Anemias due to disorder of folate, vitamin B12 and transcobalamin metabolism
    • Zittoun, J. Anemias due to disorder of folate, vitamin B12 and transcobalamin metabolism. Rev Prat 43:1358-1363 (1993).
    • (1993) Rev Prat , vol.43 , pp. 1358-1363
    • Zittoun, J.1
  • 44
    • 0023645289 scopus 로고
    • Identification and nucleotide sequence of a gene encoding 5'-phosphori-bosylglycinamide transformylase in escherichia coli K12
    • Smith, J. M. & Daum, H. A., 3rd Identification and nucleotide sequence of a gene encoding 5'-phosphori-bosylglycinamide transformylase in Escherichia coli K12. J Biol Chem 262:10565-10569 (1987).
    • (1987) J Biol Chem , vol.262 , pp. 10565-10569
    • Smith, J.M.1    Daum Iii, H.A.2
  • 45
    • 65549100581 scopus 로고    scopus 로고
    • Oxidation of cysteine 645 of cobalamin-independent methionine synthase causes a methionine limitation in escherichia coli
    • Hondorp, E. R. & Matthews, R. G. Oxidation of cysteine 645 of cobalamin-independent methionine synthase causes a methionine limitation in Escherichia coli. J Bacteriol 191:3407-3410 (2009).
    • (2009) J Bacteriol , vol.191 , pp. 3407-3410
    • Hondorp, E.R.1    Matthews, R.G.2
  • 47
    • 0032993401 scopus 로고    scopus 로고
    • TorC apocytochrome negatively autoregulates the trimethylamine N-oxide (TMAO) reductase operon in Escherichia coli
    • DOI 10.1046/j.1365-2958.1999.01468.x
    • Ansaldi, M., Bordi, C., Lepelletier, M. & Mejean, V. TorC apocytochrome negatively autoregulates the trimethylamine N-oxide (TMAO) reductase operon in Escherichia coli. Mol Microbiol 33:284-295 (1999). (Pubitemid 29322515)
    • (1999) Molecular Microbiology , vol.33 , Issue.2 , pp. 284-295
    • Ansaldi, M.1    Bordi, C.2    Lepelletier, M.3    Mejean, V.4
  • 48
    • 0035853704 scopus 로고    scopus 로고
    • Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in escherichia coli
    • Gon, S., Giudici-Orticoni, M. T., Mejean, V. & Iobbi-Nivol, C. Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli. J Biol Chem 276:11545-11551 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 11545-11551
    • Gon, S.1    Giudici-Orticoni, M.T.2    Mejean, V.3    Iobbi-Nivol, C.4
  • 49
    • 18144409383 scopus 로고    scopus 로고
    • TorD, an essential chaperone for TorA molybdoenzyme maturation at high temperature
    • DOI 10.1074/jbc.M501119200
    • Genest, O., Ilbert, M., Mejean, V. & Iobbi-Nivol, C. TorD, an essential chaperone for TorA molybdoenzyme maturation at high temperature. J Biol Chem 280: 15644-15648 (2005). (Pubitemid 40616682)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 15644-15648
    • Genest, O.1    Ilbert, M.2    Mejean, V.3    Iobbi-Nivol, C.4
  • 51
    • 74549156360 scopus 로고    scopus 로고
    • Intrinsic GTPase activity of a bacterial twin-arginine translocation proofreading chaperone induced by domain swapping
    • Guymer, D., Maillard, J., Agacan, M. F., Brearley, C. A. & Sargent, F. Intrinsic GTPase activity of a bacterial twin-arginine translocation proofreading chaperone induced by domain swapping. FEBS J 277:511-525 (2010).
    • (2010) FEBS J , vol.277 , pp. 511-525
    • Guymer, D.1    Maillard, J.2    Agacan, M.F.3    Brearley, C.A.4    Sargent, F.5
  • 52
    • 77950600645 scopus 로고    scopus 로고
    • Mechanisms of the hsp70 chaperone system
    • Young, J. C. Mechanisms of the Hsp70 chaperone system. Biochem Cell Biol 88:291-300 (2010).
    • (2010) Biochem Cell Biol , vol.88 , pp. 291-300
    • Young, J.C.1
  • 53
    • 77954377096 scopus 로고    scopus 로고
    • Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of escherichia coli heat shock protein 70 (Hsp70/DnaK)
    • Chang, L., Thompson, A. D., Ung, P., Carlson, H. A. & Gestwicki, J. E. Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK). J Biol Chem 285:21282-21291 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 21282-21291
    • Chang, L.1    Thompson, A.D.2    Ung, P.3    Carlson, H.A.4    Gestwicki, J.E.5
  • 54
    • 51149100951 scopus 로고    scopus 로고
    • The proper ratio of GrpE to DnaK is important for protein quality control by the DnaK-dnaj-grpe chaperone system and for cell division
    • Sugimoto, S., Saruwatari, K., Higashi, C. & Sonomoto, K. The proper ratio of GrpE to DnaK is important for protein quality control by the DnaK-DnaJ-GrpE chaperone system and for cell division. Microbiology 154: 1876-1885 (2008).
    • (2008) Microbiology , vol.154 , pp. 1876-1885
    • Sugimoto, S.1    Saruwatari, K.2    Higashi, C.3    Sonomoto, K.4
  • 55
    • 33745610915 scopus 로고    scopus 로고
    • Structural determinants of HscA peptide-binding specificity
    • DOI 10.1021/bi0606187
    • Tapley, T. L., Cupp-Vickery, J. R. & Vickery, L. E. Structural determinants of HscA peptide-binding specificity. Biochemistry 45:8058-8066 (2006). (Pubitemid 43993226)
    • (2006) Biochemistry , vol.45 , Issue.26 , pp. 8058-8066
    • Tapley, T.L.1    Cupp-Vickery, J.R.2    Vickery, L.E.3
  • 57
    • 22344447035 scopus 로고    scopus 로고
    • Not all J domains are created equal: Implications for the specificity of Hsp40-Hsp70 interactions
    • DOI 10.1110/ps.051406805
    • Hennessy, F., Nicoll, W. S., Zimmermann, R., Cheetham, M. E. & Blatch, G. L. Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions. Protein Sci 14:1697-1709 (2005). (Pubitemid 41001413)
    • (2005) Protein Science , vol.14 , Issue.7 , pp. 1697-1709
    • Hennessy, F.1    Nicoll, W.S.2    Zimmermann, R.3    Cheetham, M.E.4    Blatch, G.L.5
  • 58
    • 53049103895 scopus 로고    scopus 로고
    • Revisiting the GroEL-groes reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant
    • Koike-Takeshita, A., Yoshida, M. & Taguchi, H. Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant. J Biol Chem 283:23774-23781 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 23774-23781
    • Koike-Takeshita, A.1    Yoshida, M.2    Taguchi, H.3
  • 59
    • 0028785583 scopus 로고
    • Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
    • Weissman, J. S. et al. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell 83:577-587 (1995).
    • (1995) Cell , vol.83 , pp. 577-587
    • Weissman, J.S.1
  • 60
    • 61749094567 scopus 로고    scopus 로고
    • GroEL assisted folding of large polypeptide substrates in escherichia coli: Present scenario and assignments for the future
    • Chaudhuri, T. K., Verma, V. K. & Maheshwari, A. GroEL assisted folding of large polypeptide substrates in Escherichia coli: Present scenario and assignments for the future. Prog Biophys Mol Biol 99:42-50 (2009).
    • (2009) Prog Biophys Mol Biol , vol.99 , pp. 42-50
    • Chaudhuri, T.K.1    Verma, V.K.2    Maheshwari, A.3
  • 61
    • 18244398660 scopus 로고    scopus 로고
    • Localization of chaperones DnaK and GroEL in bacterial inclusion bodies
    • DOI 10.1128/JB.187.10.3599-3601.2005
    • Carrio, M. M. & Villaverde, A. Localization of chaperones DnaK and GroEL in bacterial inclusion bodies. J Bacteriol 187:3599-3601 (2005). (Pubitemid 40628721)
    • (2005) Journal of Bacteriology , vol.187 , Issue.10 , pp. 3599-3601
    • Carrio, M.M.1    Villaverde, A.2
  • 62
    • 20444480246 scopus 로고    scopus 로고
    • Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon
    • DOI 10.1128/JB.187.12.4207-4213.2005
    • Fredriksson, A., Ballesteros, M., Dukan, S. & Nystrom, T. Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon. J Bacteriol 187:4207-4213 (2005). (Pubitemid 40827802)
    • (2005) Journal of Bacteriology , vol.187 , Issue.12 , pp. 4207-4213
    • Fredriksson, A.1    Ballesteros, M.2    Dukan, S.3    Nystrom, T.4
  • 63
    • 76849111527 scopus 로고    scopus 로고
    • Escherichia coli heat-shock proteins IbpA and IbpB affect biofilm formation by influencing the level of extracellular indole
    • Kuczynska-Wisnik, D., Matuszewska, E. & Laskowska, E. Escherichia coli heat-shock proteins IbpA and IbpB affect biofilm formation by influencing the level of extracellular indole. Microbiology 156:148-157 (2009).
    • (2009) Microbiology , vol.156 , pp. 148-157
    • Kuczynska-Wisnik, D.1    Matuszewska, E.2    Laskowska, E.3
  • 64
    • 58549098512 scopus 로고    scopus 로고
    • Distinct activities of escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation
    • Ratajczak, E., Zietkiewicz, S. & Liberek, K. Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation. J Mol Biol 386:178-189 (2009).
    • (2009) J Mol Biol , vol.386 , pp. 178-189
    • Ratajczak, E.1    Zietkiewicz, S.2    Liberek, K.3
  • 65
    • 78650749888 scopus 로고    scopus 로고
    • Multiple layers of control govern expression of the escherichia coli ibpAB heat-shock operon
    • Gaubig, L. C., Waldminghaus, T. & Narberhaus, F. Multiple layers of control govern expression of the Escherichia coli ibpAB heat-shock operon. Microbiology 157:66-76 (2010).
    • (2010) Microbiology , vol.157 , pp. 66-76
    • Gaubig, L.C.1    Waldminghaus, T.2    Narberhaus, F.3
  • 66
    • 77949346874 scopus 로고    scopus 로고
    • The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ lon protease
    • Bissonnette, S. A., Rivera-Rivera, I., Sauer, R. T. & Baker, T. A. The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease. Mol Microbiol 75:1539-1549 (2010).
    • (2010) Mol Microbiol , vol.75 , pp. 1539-1549
    • Bissonnette, S.A.1    Rivera-Rivera, I.2    Sauer, R.T.3    Baker, T.A.4
  • 67
    • 0026697593 scopus 로고
    • The DNA sequence of the sulfate activation locus from escherichia coli K-12
    • Leyh, T. S., Vogt, T. F. & Suo, Y. The DNA sequence of the sulfate activation locus from Escherichia coli K-12. J Biol Chem 267:10405-10410 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 10405-10410
    • Leyh, T.S.1    Vogt, T.F.2    Suo, Y.3
  • 68
    • 0028849610 scopus 로고
    • Reaction mechanism of thioredoxin: 3'-phosphoadenylylsulfate reductase investigated by site-directed mutagenesis
    • Berendt, U., Haverkamp, T., Prior, A. & Schwenn, J. D. Reaction mechanism of thioredoxin: 3'-phosphoadenylylsulfate reductase investigated by site-directed mutagenesis. Eur J Biochem 233:347-356 (1995).
    • (1995) Eur J Biochem , vol.233 , pp. 347-356
    • Berendt, U.1    Haverkamp, T.2    Prior, A.3    Schwenn, J.D.4
  • 69
    • 0026553921 scopus 로고
    • Anaerobic induction of the alkylation-inducible escherichia coli aidB gene involves genes of the cysteine biosyn-thetic pathway
    • Matijasevic, Z., Hajec, L. I. & Volkert, M. R. Anaerobic induction of the alkylation-inducible Escherichia coli aidB gene involves genes of the cysteine biosyn-thetic pathway. J Bacteriol 174:2043-2046 (1992).
    • (1992) J Bacteriol , vol.174 , pp. 2043-2046
    • Matijasevic, Z.1    Hajec, L.I.2    Volkert, M.R.3
  • 70
    • 0024430827 scopus 로고
    • 4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase
    • Ostrowski, J. et al. Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase. J Biol Chem 264:15726-15737 (1989). (Pubitemid 19242953)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.26 , pp. 15726-15737
    • Ostrowski, J.1    Wu, J.-Y.2    Rueger, D.C.3    Miller, B.E.4    Siegel, L.M.5    Kredich, N.M.6


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