메뉴 건너뛰기




Volumn 45, Issue 1, 2012, Pages 57-103

Nuclease colicins and their immunity proteins

Author keywords

[No Author keywords available]

Indexed keywords

COLICIN; ENDONUCLEASE;

EID: 84857552907     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583511000114     Document Type: Review
Times cited : (62)

References (181)
  • 1
    • 0037484227 scopus 로고    scopus 로고
    • Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA
    • DOI 10.1074/jbc.M300411200
    • ANDERLUH, G., HONG, Q., BOETZEL, R., MACDONALD, C., MOORE, G. R., VIRDEN, R. & LAKEY, J. H. (2003). Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA. Journal of Biological Chemistry 278, 21860-21868. (Pubitemid 36792592)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 21860-21868
    • Anderluh, G.1    Hong, Q.2    Boetzel, R.3    MacDonald, C.4    Moore, G.R.5    Virden, R.6    Lakey, J.H.7
  • 2
    • 52949087550 scopus 로고    scopus 로고
    • Disparate proteins use similar architectures to damage membranes
    • ANDERLUH, G. & LAKEY, J. H. (2008). Disparate proteins use similar architectures to damage membranes. Trends in Biochemical Sciences 33, 482-490.
    • (2008) Trends in Biochemical Sciences , vol.33 , pp. 482-490
    • Anderluh, G.1    Lakey, J.H.2
  • 3
    • 65249096720 scopus 로고    scopus 로고
    • Structure and function of colicin S4, a colicin with a duplicated receptor-binding domain
    • ARNOLD, T., ZETH, K. & LINKE, D. (2009). Structure and function of colicin S4, a colicin with a duplicated receptor-binding domain. Journal of Biological Chemistry 284, 6403-6413.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 6403-6413
    • Arnold, T.1    Zeth, K.2    Linke, D.3
  • 4
    • 40049110400 scopus 로고    scopus 로고
    • Colicin N Binds to the Periphery of Its Receptor andTranslocator, Outer Membrane Protein F
    • DOI 10.1016/j.str.2007.12.023, PII S0969212608000555
    • BABOOLAL, T. G., CONROY, M. J., GILL, K., RIDLEY, H., VISUDTIPHOLE, V., BULLOUGH, P.A. & LAKEY, J.H. (2008). Colicin N binds to the periphery of its receptor and translocator, outer membrane protein F. Structure 16, 371-379. (Pubitemid 351324119)
    • (2008) Structure , vol.16 , Issue.3 , pp. 371-379
    • Baboolal, T.G.1    Conroy, M.J.2    Gill, K.3    Ridley, H.4    Visudtiphole, V.5    Bullough, P.A.6    Lakey, JeremyH.7
  • 5
    • 77957970492 scopus 로고    scopus 로고
    • Dry molten globule intermediates and the mechanism of protein unfolding
    • BALDWIN, R. L., FRIEDEN, C. & ROSE, G. D. (2010). Dry molten globule intermediates and the mechanism of protein unfolding. Proteins 78, 2725-2737.
    • (2010) Proteins , vol.78 , pp. 2725-2737
    • Baldwin, R.L.1    Frieden, C.2    Rose, G.D.3
  • 7
    • 78049435307 scopus 로고    scopus 로고
    • Interaction of the colicin K bactericidal toxin with components of its import machinery in the periplasm of Escherichia coli
    • BARNEOUD-ARNOULET, A., GAVIOLI, M., LLOUBES, R. & CASCALES, E. (2010b). Interaction of the colicin K bactericidal toxin with components of its import machinery in the periplasm of Escherichia coli. Journal of Bacteriology 192, 5934-5942.
    • (2010) Journal of Bacteriology , vol.192 , pp. 5934-5942
    • Barneoud-Arnoulet, A.1    Gavioli, M.2    Lloubes, R.3    Cascales, E.4
  • 8
    • 58149149594 scopus 로고    scopus 로고
    • E9-Im9 colicin DNaseimmunity protein biomolecular association in water: A multiple-copy and accelerated molecular dynamics simulation study
    • BARON, R., WONG, S. E., DE OLIVEIRA, C.A. & MCCAMMON, J. A. (2008). E9-Im9 colicin DNaseimmunity protein biomolecular association in water: a multiple-copy and accelerated molecular dynamics simulation study. Journal of Physical Chemistry B 112, 16802-16814.
    • (2008) Journal of Physical Chemistry B , vol.112 , pp. 16802-16814
    • Baron, R.1    Wong, S.E.2    De Oliveira, C.A.3    McCammon, J.A.4
  • 10
    • 0026089656 scopus 로고
    • Individual domains of colicins confer specificity in colicin uptake, in pore-properties and in immunity requirement
    • BENEDETTI, H., FRENETTE, M., BATY, D., KNIBIEHLER, M., PATTUS, F. & LAZDUNSKI, C. (1991). Individual domains of colicins confer specificity in colicin uptake, in poreproperties and in immunity requirement. Journal of Molecular Biology 217, 429-439. (Pubitemid 121003291)
    • (1991) Journal of Molecular Biology , vol.217 , Issue.3 , pp. 429-439
    • Benedetti, H.1    Frenette, M.2    Baty, D.3    Knibiehler, M.4    Pattus, F.5    Lazdunski, C.6
  • 11
    • 0026541379 scopus 로고
    • Colicin A unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed
    • BENEDETTI, H., LLOUBES, R., LAZDUNSKI, C. & LETELLIER, L. (1992). Colicin A unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed. EMBO Journal 11, 441-447.
    • (1992) EMBO Journal , vol.11 , pp. 441-447
    • Benedetti, H.1    Lloubes, R.2    Lazdunski, C.3    Letellier, L.4
  • 12
    • 0015333430 scopus 로고
    • Specific inhibition of cell division by colicin E2 without degradation of deoxyribonucleic acid in a new colicin sensitivity mutant of Escherichia coli
    • BEPPU, T., KAWABATA, K. & ARIMA, K. (1972). Specific inhibition of cell division by colicin E2 without degradation of deoxyribonucleic acid in a new colicin sensitivity mutant of Escherichia coli. Journal of Bacteriology 110, 485-493.
    • (1972) Journal of Bacteriology , vol.110 , pp. 485-493
    • Beppu, T.1    Kawabata, K.2    Arima, K.3
  • 13
    • 11844273937 scopus 로고    scopus 로고
    • Directed evolution of protein inhibitors of DNA-nucleases by in vitro compartmentalization (IVC) and nano-droplet delivery
    • DOI 10.1016/j.jmb.2004.11.017, PII S0022283604014573
    • BERNATH, K., MAGDASSI, S. & TAWFIK, D. S. (2005). Directed evolution of protein inhibitors of DNAnucleases by in vitro compartmentalization (IVC) and nano-droplet delivery. Journal of Molecular Biology 345, 1015-1026. (Pubitemid 40092221)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.5 , pp. 1015-1026
    • Bernath, K.1    Magdassi, S.2    Tawfik, D.S.3
  • 14
    • 34247473840 scopus 로고    scopus 로고
    • Molecular mimicry enables competitive recruitment by a natively disordered protein
    • DOI 10.1021/ja070153n
    • BONSOR, D. A., GRISHKOVSKAYA, I., DODSON, E.J. & KLEANTHOUS, C. (2007). Molecular mimicry enables competitive recruitment by a natively disordered protein. Journal of the American Chemical Society 15, 4800-4807. (Pubitemid 46648779)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.15 , pp. 4800-4807
    • Bonsor, D.A.1    Grishkovskaya, I.2    Dodson, E.J.3    Kleanthous, C.4
  • 18
    • 0025114009 scopus 로고
    • Involvement of OmpF during reception and translocation steps of colicin N entry
    • BOURDINEAUD, J. P., FIEROBE, H. P., LAZDUNSKI, C. & PAGES, J. M. (1990b). Involvement of OmpF during reception and translocation steps of colicin N entry. Molecular Microbiology 4, 1737-1743.
    • (1990) Molecular Microbiology , vol.4 , pp. 1737-1743
    • Bourdineaud, J.P.1    Fierobe, H.P.2    Lazdunski, C.3    Pages, J.M.4
  • 19
    • 0344631755 scopus 로고    scopus 로고
    • In vitro characterization of peptidoglycan-associated lipoprotein (PAL)- peptidoglycan and PAL-TolB interactions
    • BOUVERET, E., BENEDETTI, H., RIGAL, A., LORET, E. & LAZDUNSKI, C. (1999). In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions. Journal of Bacteriology 181, 6306-6311. (Pubitemid 29512939)
    • (1999) Journal of Bacteriology , vol.181 , Issue.20 , pp. 6306-6311
    • Bouveret, E.1    Benedetti, H.2    Rigal, A.3    Loret, E.4    Lazdunski, C.5
  • 20
    • 0031983893 scopus 로고    scopus 로고
    • Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli
    • DOI 10.1046/j.1365-2958.1998.00667.x
    • BOUVERET, E., RIGAL, A., LAZDUNSKI, C. & BENEDETTI, H. (1998). Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli. Molecular Microbiology 27, 143-157. (Pubitemid 28022584)
    • (1998) Molecular Microbiology , vol.27 , Issue.1 , pp. 143-157
    • Bouveret, E.1    Rigal, A.2    Lazdunski, C.3    Benedetti, H.4
  • 21
    • 34249095469 scopus 로고    scopus 로고
    • Structure of colicin I receptor bound to the R-domain of colicin Ia: Implications for protein import
    • DOI 10.1038/sj.emboj.7601693, PII 7601693
    • BUCHANAN, S. K., LUKACIK, P., GRIZOT, S., GHIRLANDO, R., ALI, M. M., BARNARD, T. J., JAKES, K. S., KIENKER, P. K. & ESSER, L. (2007). Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import. EMBO Journal 26, 2594-2604. (Pubitemid 46788319)
    • (2007) EMBO Journal , vol.26 , Issue.10 , pp. 2594-2604
    • Buchanan, S.K.1    Lukacik, P.2    Grizot, S.3    Ghirlando, R.4    Ali, M.M.U.5    Barnard, T.J.6    Jakes, K.S.7    Kienker, P.K.8    Esser, L.9
  • 23
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: Misfolding on a path to the native state
    • DOI 10.1038/nsb757
    • CAPALDI, A. P., KLEANTHOUS, C. & RADFORD, S. E. (2002). Im7 folding mechanism: misfolding on a path to the native state. Nature Structural Biology 9, 209-216. (Pubitemid 34171314)
    • (2002) Nature Structural Biology , vol.9 , Issue.3 , pp. 209-216
    • Capaldi, A.P.1    Kleanthous, C.2    Radford, S.E.3
  • 24
    • 0035170463 scopus 로고    scopus 로고
    • Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate
    • DOI 10.1038/83074
    • CAPALDI, A. P., SHASTRY, M. C., KLEANTHOUS, C., RODER, H. & RADFORD, S. E. (2001). Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate. Nature Structural Biology 8, 68-72. (Pubitemid 32043031)
    • (2001) Nature Structural Biology , vol.8 , Issue.1 , pp. 68-72
    • Capaldi, A.P.1    Shastry, M.C.R.2    Kleanthous, C.3    Roder, H.4    Radford, S.E.5
  • 25
    • 0034520580 scopus 로고    scopus 로고
    • Crystallization of the cytotoxic domain of a ribosome-inactivating colicin in complex with its immunity protein
    • DOI 10.1107/S0907444900010726
    • CARR, S., WALKER, D., JAMES, R., KLEANTHOUS, C. & HEMMINGS, A. M. (2000). Crystallization of the cytotoxic domain of a ribosome-inactivating colicin in complex with its immunity protein. Acta Crystallographica. Section D, Biological Crystallography 56, 1630-1633. (Pubitemid 32040022)
    • (2000) Acta Crystallographica Section D: Biological Crystallography , vol.56 , Issue.12 , pp. 1630-1633
    • Carr, S.1    Walker, D.2    James, R.3    Kleanthous, C.4    Hemmings, A.M.5
  • 27
    • 0033637616 scopus 로고    scopus 로고
    • Proton motive force drives the interaction of the inner membrane TolA and outer membrane pal proteins in Escherichia coli
    • CASCALES, E., GAVIOLI, M., STURGIS, J.N. & LLOUBES, R. (2000). Proton motive force drives the interaction of the inner membrane TolA and outer membrane pal proteins in Escherichia coli. Molecular Microbiology 38, 904-915.
    • (2000) Molecular Microbiology , vol.38 , pp. 904-915
    • Cascales, E.1    Gavioli, M.2    Sturgis, J.N.3    Lloubes, R.4
  • 28
    • 0035163972 scopus 로고    scopus 로고
    • The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB
    • DOI 10.1046/j.1365-2958.2001.02673.x
    • CASCALES, E., LLOUBES, R. & STURGIS, J. N. (2001). The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB. Molecular Microbiology 42, 795-807. (Pubitemid 33064487)
    • (2001) Molecular Microbiology , vol.42 , Issue.3 , pp. 795-807
    • Cascales, E.1    Lloubes, R.2    Sturgis, J.N.3
  • 29
    • 0025181658 scopus 로고
    • Colicin cleavage by ompT protease during both entry into and release from Escherichia coli cells
    • CAVARD, D. & LAZDUNSKI, C. (1990). Colicin cleavage by OmpT protease during both entry into and release from Escherichia coli cells. Journal of Bacteriology 172, 648-652. (Pubitemid 20070372)
    • (1990) Journal of Bacteriology , vol.172 , Issue.2 , pp. 648-652
    • Cavard, D.1    Lazdunski, C.2
  • 30
    • 80051681504 scopus 로고    scopus 로고
    • FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm
    • CHAULEAU, M., MORA, L., SERBA, J. & DE ZAMAROCZY, M. (2011). FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm. Journal of Biological Chemistry 286, 29397-29407.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 29397-29407
    • Chauleau, M.1    Mora, L.2    Serba, J.3    De Zamaroczy, M.4
  • 31
    • 33144462415 scopus 로고    scopus 로고
    • Sulfate-induced effects in the on-pathway intermediate of the bacterial immunity protein Im7*
    • DOI 10.1021/bi0521238
    • COBOS, E. S. & RADFORD, S. E. (2006). Sulfate-induced effects in the on-pathway intermediate of the bacterial immunity protein Im7. Biochemistry 45, 2274-2282. (Pubitemid 43271327)
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2274-2282
    • Cobos, E.S.1    Radford, S.E.2
  • 34
    • 17144389864 scopus 로고    scopus 로고
    • Helix stability and hydrophobicity in the folding mechanism of the bacterial immunity protein Im9
    • DOI 10.1093/protein/gzi002
    • CRANZ-MILEVA, S., FRIEL, C. T. & RADFORD, S. E. (2005). Helix stability and hydrophobicity in the folding mechanism of the bacterial immunity protein Im9. Protein Engineering, Design and Selection 18, 41-50. (Pubitemid 40516990)
    • (2005) Protein Engineering, Design and Selection , vol.18 , Issue.1 , pp. 41-50
    • Cranz-Mileva, S.1    Friel, C.T.2    Radford, S.E.3
  • 35
    • 0016524407 scopus 로고
    • Genetics of resistance to colicins in Escherichia coli K-12: Cross-resistance among colicins of group A
    • DAVIES, J.K. & REEVES, P. (1975a). Genetics of resistance to colicins in Escherichia coli K-12: cross-resistance among colicins of group A. Journal of Bacteriology 123, 102-117.
    • (1975) Journal of Bacteriology , vol.123 , pp. 102-117
    • Davies, J.K.1    Reeves, P.2
  • 36
    • 0016524407 scopus 로고
    • Genetics of resistance to colicins in Escherichia coli K-12: Cross-resistance among colicins of group B
    • DAVIES, J. K. & REEVES, P. (1975b). Genetics of resistance to colicins in Escherichia coli K-12: cross-resistance among colicins of group B. Journal of Bacteriology 123, 96-101.
    • (1975) Journal of Bacteriology , vol.123 , pp. 96-101
    • Davies, J.K.1    Reeves, P.2
  • 37
    • 0036589208 scopus 로고    scopus 로고
    • Importation of nuclease colicins into E. coli cells: Endoproteolytic cleavage and its prevention by the immunity protein
    • DOI 10.1016/S0300-9084(02)01426-8, PII S0300908402014268
    • DE ZAMAROCZY, M. & BUCKINGHAM, R. H. (2002). Importation of nuclease colicins into E coli cells: endoproteolytic cleavage and its prevention by the immunity protein. Biochimie 84, 423-432. (Pubitemid 35350872)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 423-432
    • De Zamaroczy, M.1    Buckingham, R.H.2
  • 38
    • 0034881923 scopus 로고    scopus 로고
    • Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB
    • DOI 10.1016/S1097-2765(01)00276-3
    • DE ZAMAROCZY, M., MORA, L., LECUYER, A., GELI, V. & BUCKINGHAM, R. H. (2001). Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB. Molecular Cell 8, 159-168. (Pubitemid 32772914)
    • (2001) Molecular Cell , vol.8 , Issue.1 , pp. 159-168
    • De Zamaroczy, M.1    Mora, L.2    Lecuyer, A.3    Geli, V.4    Buckingham, R.H.5
  • 39
    • 0032127769 scopus 로고    scopus 로고
    • A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity
    • DENNIS, C. A., VIDELER, H., PAUPTIT, R. A., WALLIS, R., JAMES, R., MOORE, G.R. & KLEANTHOUS, C. (1998). A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity. Biochemistry Journal 333, 183-191. (Pubitemid 28342508)
    • (1998) Biochemical Journal , vol.333 , Issue.1 , pp. 183-191
    • Dennis, C.A.1    Videler, H.2    Pauptit, R.A.3    Wallis, R.4    James, R.5    Moore, G.R.6    Kleanthous, C.7
  • 40
    • 0037176873 scopus 로고    scopus 로고
    • Macromolecular import into Escherichia coli: The TolA C-terminal domain changes conformation when interacting with the colicin A toxin
    • DOI 10.1021/bi0157262
    • DEPREZ, C., BLANCHARD, L., GUERLESQUIN, F., GAVIOLI, M., SIMORRE, J. P., LAZDUNSKI, C., MARION, D. & LLOUBES, R. (2002). Macromolecular import into Escherichia coli: the TolA C-terminal domain changes conformation when interacting with the colicin A toxin. Biochemistry 41, 2589-2598. (Pubitemid 34168928)
    • (2002) Biochemistry , vol.41 , Issue.8 , pp. 2589-2598
    • Deprez, C.1    Blanchard, L.2    Guerlesquin, F.3    Gavioli, M.4    Simorre, J.-P.5    Lazdunski, C.6    Marion, D.7    Lloubes, R.8
  • 42
    • 31344461104 scopus 로고    scopus 로고
    • 2+
    • DOI 10.1110/ps.051903406
    • DOUDEVA, L. G., HUANG, H., HSIA, K. C., SHI, Z., LI, C. L., SHEN, Y., CHENG, Y. S. & YUAN, H. S. (2006). Crystal structural analysis and metal-dependent stability and activity studies of the ColE7 endonuclease domain in complex with DNA/Zn2+ or inhibitor/Ni2+. Protein Science 15, 269-280. (Pubitemid 43144999)
    • (2006) Protein Science , vol.15 , Issue.2 , pp. 269-280
    • Doudeva, L.G.1    Huang, H.2    Hsia, K.-C.3    Shi, Z.4    Li, C.-L.5    Shen, Y.6    Cheng, Y.-S.7    Yuan, H.S.8
  • 43
    • 0027938907 scopus 로고
    • Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering
    • DUCHE, D., BATY, D., CHARTIER, M. & LETELLIER, L. (1994). Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering. Journal of Biological Chemistry 269, 24820.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 24820
    • Duche, D.1    Baty, D.2    Chartier, M.3    Letellier, L.4
  • 44
    • 33845456098 scopus 로고    scopus 로고
    • Release of immunity protein requires functional endonuclease colicin import machinery
    • DOI 10.1128/JB.00941-06
    • DUCHE, D., FRENKIAN, A., PRIMA, V. & LLOUBES, R. (2006). Release of immunity protein requires functional endonuclease colicin import machinery. Journal of Bacteriology 188, 8593-8600. (Pubitemid 44894060)
    • (2006) Journal of Bacteriology , vol.188 , Issue.24 , pp. 8593-8600
    • Duche, D.1    Frenkian, A.2    Prima, V.3    Lloubes, R.4
  • 45
    • 58149133744 scopus 로고    scopus 로고
    • Immunity protein protects colicin E2 from OmpT protease
    • DUCHE, D., ISSOUF, M. & LLOUBES, R. (2009). Immunity protein protects colicin E2 from OmpT protease. Journal of Biochemistry 145, 95-101.
    • (2009) Journal of Biochemistry , vol.145 , pp. 95-101
    • Duche, D.1    Issouf, M.2    Lloubes, R.3
  • 46
    • 33747354636 scopus 로고    scopus 로고
    • Colicin M exerts its bacteriolytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors
    • EL GHACHI, M., BOUHSS, A., BARRETEAU, H., TOUZE, T., AUGER, G., BLANOT, D. & MENGIN-LECREULX, D. (2006). Colicin M exerts its bacteriolytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors. Journal of Biological Chemistry 281, 22761-22772.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 22761-22772
    • Ghachi, M.E.L.1    Bouhss, A.2    Barreteau, H.3    Touze, T.4    Auger, G.5    Blanot, D.6    Mengin-Lecreulx, D.7
  • 48
    • 0033548553 scopus 로고    scopus 로고
    • Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9
    • DOI 10.1006/jmbi.1998.2548
    • FERGUSON, N., CAPALDI, A. P., JAMES, R., KLEANTHOUS, C. & RADFORD, S. E. (1999). Rapid folding with and without populated intermediates in the homologous fourhelix proteins Im7 and Im9. Journal of Molecular Biology 286, 1597-1608. (Pubitemid 29121737)
    • (1999) Journal of Molecular Biology , vol.286 , Issue.5 , pp. 1597-1608
    • Ferguson, N.1    Capaldi, A.P.2    James, R.3    Kleanthous, C.4    Radford, S.E.5
  • 49
    • 0035896036 scopus 로고    scopus 로고
    • Using chimeric immunity proteins to explore the energy landscape for α-helical protein folding
    • DOI 10.1006/jmbi.2000.4492
    • FERGUSON, N., LI, W., CAPALDI, A. P., KLEANTHOUS, C. & RADFORD, S. E. (2001). Using chimeric immunity proteins to explore the energy landscape for alpha-helical protein folding. Journal of Molecular Biology 307, 393-405. (Pubitemid 33029989)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.1 , pp. 393-405
    • Ferguson, N.1    Li, W.2    Capaldi, A.P.3    Kleanthous, C.4    Radford, S.E.5
  • 51
    • 4143061715 scopus 로고    scopus 로고
    • Switching two-state to three-state kinetics in the helical protein Im9 via the optimisation of stabilising non-native interactions by design
    • DOI 10.1016/j.jmb.2004.06.076, PII S0022283604007818
    • FRIEL, C. T., BEDDARD, G. S. & RADFORD, S. E. (2004). Switching two-state to three-state kinetics in the helical protein Im9 via the optimisation of stabilising nonnative interactions by design. Journal of Molecular Biology 342, 261-273. (Pubitemid 39099289)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.1 , pp. 261-273
    • Friel, C.T.1    Beddard, G.S.2    Radford, S.E.3
  • 52
    • 0037423705 scopus 로고    scopus 로고
    • Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: Similarities and differences in the folding of homologous proteins
    • DOI 10.1016/S0022-2836(02)01249-4
    • FRIEL, C. T., CAPALDI, A.P. & RADFORD, S. E. (2003). Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. Journal of Molecular Biology 326, 293-305. (Pubitemid 36279376)
    • (2003) Journal of Molecular Biology , vol.326 , Issue.1 , pp. 293-305
    • Friel, C.T.1    Capaldi, A.P.2    Radford, S.E.3
  • 53
  • 54
    • 0037180394 scopus 로고    scopus 로고
    • Catalytic mechanisms of restriction and homing endonucleases
    • DOI 10.1021/bi020467h
    • GALBURT, E.A. & STODDARD, B. L. (2002). Catalytic mechanisms of restriction and homing endonucleases. Biochemistry 41, 13851-13860. (Pubitemid 35364858)
    • (2002) Biochemistry , vol.41 , Issue.47 , pp. 13851-13860
    • Galburt, E.A.1    Stoddard, B.L.2
  • 57
    • 33846650968 scopus 로고    scopus 로고
    • The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli
    • DOI 10.1111/j.1365-2958.2006.05571.x
    • GERDING, M. A., OGATA, Y., PECORA, N. D., NIKI, H. & DE BOER, P. A. (2007). The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Molecular Microbiology 63, 1008-1025. (Pubitemid 46188263)
    • (2007) Molecular Microbiology , vol.63 , Issue.4 , pp. 1008-1025
    • Gerding, M.A.1    Ogata, Y.2    Pecora, N.D.3    Niki, H.4    De Boer, P.A.J.5
  • 58
    • 33846839298 scopus 로고    scopus 로고
    • Mutational Analyses Define Helix Organization and Key Residues of a Bacterial Membrane Energy-transducing Complex
    • DOI 10.1016/j.jmb.2006.12.020, PII S0022283606016950
    • GOEMAERE, E. L., CASCALES, E. & LLOUBES, R. (2007). Mutational analyses define helix organization and key residues of a bacterial membrane energy-transducing complex. Journal of Molecular Biology 366, 1424-1436. (Pubitemid 46215605)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.5 , pp. 1424-1436
    • Goemaere, E.L.1    Cascales, E.2    Lloubes, R.3
  • 59
    • 0034623946 scopus 로고    scopus 로고
    • The TolA-recognition site of colicin N. ITC, SPR and stopped-flow fluorescence define a crucial 27-residue segment
    • DOI 10.1006/jmbi.2000.4232
    • GOKCE, I., RAGGETT, E. M., HONG, Q., VIRDEN, R., COOPER, A. & LAKEY, J. H. (2000). The TolArecognition site of colicin N. ITC, SPR and stoppedflow fluorescence define a crucial 27-residue segment. Journal of Molecular Biology 304, 621-632. (Pubitemid 32006194)
    • (2000) Journal of Molecular Biology , vol.304 , Issue.4 , pp. 621-632
    • Gokce, I.1    Raggett, E.M.2    Hong, Q.3    Virden, R.4    Cooper, A.5    Lakey, J.H.6
  • 60
    • 0028309650 scopus 로고
    • Self-splicing group I and group II introns encode homologous (putative) DNA endonucleases of a new family
    • GORBALENYA, A. E. (1994). Self-splicing group I and group II introns encode homologous (putative) DNA endonucleases of a new family. Protein Science 3, 1117-1120. (Pubitemid 24209906)
    • (1994) Protein Science , vol.3 , Issue.7 , pp. 1117-1120
    • Gorbalenya, A.E.1
  • 61
    • 0035965128 scopus 로고    scopus 로고
    • Acidic conditions stabilise intermediates populated during the folding of Im7 and Im9
    • DOI 10.1006/jmbi.2001.5001
    • GORSKI, S. A., CAPALDI, A. P., KLEANTHOUS, C. & RADFORD, S. E. (2001). Acidic conditions stabilise intermediates populated during the folding of Im7 and Im9. Journal of Molecular Biology 312, 849-863. (Pubitemid 33116745)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.4 , pp. 849-863
    • Gorski, S.A.1    Capaldi, A.P.2    Kleanthous, C.3    Radford, S.E.4
  • 62
    • 1442351134 scopus 로고    scopus 로고
    • Equilibrium Hydrogen Exchange Reveals Extensive Hydrogen Bonded Secondary Structure in the On-pathway Intermediate of Im7
    • DOI 10.1016/j.jmb.2004.01.004
    • GORSKI, S. A., LE DUFF, C. S., CAPALDI, A. P., KALVERDA, A. P., BEDDARD, G. S., MOORE, G. R. & RADFORD, S. E. (2004). Equilibrium hydrogen exchange reveals extensive hydrogen bonded secondary structure in the onpathway intermediate of Im7. Journal of Molecular Biology 337, 183-193. (Pubitemid 38270256)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.1 , pp. 183-193
    • Gorski, S.A.1    Le Duff, C.S.2    Capaldi, A.P.3    Kalverda, A.P.4    Beddard, G.S.5    Moore, G.R.6    Radford, S.E.7
  • 63
    • 2342447390 scopus 로고    scopus 로고
    • Structural inhibition of the colicin D tRNase by the tRNA-mimicking immunity protein
    • DOI 10.1038/sj.emboj.7600162
    • GRAILLE, M., MORA, L., BUCKINGHAM, R. H., VAN TILBEURGH, H. & DE ZAMAROCZY, M. (2004). Structural inhibition of the colicin D tRNase by the tRNAmimicking immunity protein. EMBO Journal 23, 1474-1482. (Pubitemid 38579508)
    • (2004) EMBO Journal , vol.23 , Issue.7 , pp. 1474-1482
    • Graille, M.1    Mora, L.2    Buckingham, R.H.3    Van Tilbeurgh, H.4    De Zamaroczy, M.5
  • 65
    • 33747378313 scopus 로고    scopus 로고
    • Therapeutic antibodies - Delivering the promise?
    • DOI 10.1016/j.addr.2006.03.010, PII S0169409X0600086X
    • HALE, G. (2006). Therapeutic antibodies - delivering the promise? Advanced Drug Delivery Review 58(5-6), 633-639. (Pubitemid 44247224)
    • (2006) Advanced Drug Delivery Reviews , vol.58 , Issue.5-6 , pp. 633-639
    • Hale, G.1
  • 68
    • 67349151629 scopus 로고    scopus 로고
    • A common interaction for the entry of colicin N and filamentous phage into Escherichia coli
    • HECHT, O., RIDLEY, H., LAKEY, J.H. & MOORE, G.R. (2009a). A common interaction for the entry of colicin N and filamentous phage into Escherichia coli. Journal of Molecular Biology 388, 880-893.
    • (2009) Journal of Molecular Biology , vol.388 , pp. 880-893
    • Hecht, O.1    Ridley, H.2    Lakey, J.H.3    Moore, G.R.4
  • 69
    • 67349151629 scopus 로고    scopus 로고
    • A common interaction for the entry of colicin N and filamentous phage into Escherichia coli
    • HECHT, O., RIDLEY, H., LAKEY, J.H. & MOORE, G.R. (2009b). A common interaction for the entry of colicin N and filamentous phage into Escherichia coli. Journal of Molecular Biology 388, 880-893.
    • (2009) Journal of Molecular Biology , vol.388 , pp. 880-893
    • Hecht, O.1    Ridley, H.2    Lakey, J.H.3    Moore, G.R.4
  • 70
    • 77952957038 scopus 로고    scopus 로고
    • Characterisation of the interaction of colicin A with its co-receptor TolA
    • HECHT, O., ZHANG, Y., LI, C., PENFOLD, C. N., JAMES, R.& MOORE, G. R. (2010). Characterisation of the interaction of colicin A with its co-receptor TolA. FEBS Letters 584, 2249-2252.
    • (2010) FEBS Letters , vol.584 , pp. 2249-2252
    • Hecht, O.1    Zhang, Y.2    I, C.L.3    Penfold, C.N.4    James, R.5    Moore, G.R.6
  • 71
    • 0014217347 scopus 로고
    • Purification and characterization of colicin E2 and colicin E3
    • HERSCHMAN, H. R. & HELINSKI, D. R. (1967). Purification and characterization of colicin E2 and colicin E3. Journal of Biological Chemistry 242, 5360-5368.
    • (1967) Journal of Biological Chemistry , vol.242 , pp. 5360-5368
    • Herschman, H.R.1    Helinski, D.R.2
  • 72
    • 1242297815 scopus 로고    scopus 로고
    • Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 Å resolution
    • DOI 10.1111/j.1365-2958.2003.03884.x
    • HILSENBECK, J. L., PARK, H., CHEN, G., YOUN, B., POSTLE, K. & KANG, C. (2004). Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution. Molecular Microbiology 51, 711-720. (Pubitemid 38233938)
    • (2004) Molecular Microbiology , vol.51 , Issue.3 , pp. 711-720
    • Hilsenbeck, J.L.1    Park, H.2    Chen, G.3    Youn, B.4    Postle, K.5    Kang, C.6
  • 73
    • 78650943856 scopus 로고    scopus 로고
    • Thermodynamic dissection of colicin interactions
    • HOUSDEN, N.G. & KLEANTHOUS, C. (2011). Thermodynamic dissection of colicin interactions. Methods in Enzymology 488, 123-145.
    • (2011) Methods in Enzymology , vol.488 , pp. 123-145
    • Housden, N.G.1    Kleanthous, C.2
  • 76
    • 1242306189 scopus 로고    scopus 로고
    • DNA Binding and Degradation by the HNH Protein ColE7
    • DOI 10.1016/S0969-2126(04)00006-1
    • HSIA, K. C., CHAK, K. F., LIANG, P. H., CHENG, Y. S., KU, W. Y. & YUAN, H. S. (2004). DNA binding and degradation by the HNH protein ColE7. Structure 12, 205-214. (Pubitemid 38224544)
    • (2004) Structure , vol.12 , Issue.2 , pp. 205-214
    • Hsia, K.-C.1    Chak, K.-F.2    Liang, P.-H.3    Cheng, Y.-S.4    Ku, W.-Y.5    Yuan, H.S.6
  • 77
    • 47749139311 scopus 로고    scopus 로고
    • Periplasmic chaperone FkpA is essential for imported colicin M toxicity
    • DOI 10.1111/j.1365-2958.2008.06327.x
    • HULLMANN, J., PATZER, S. I., ROMER, C., HANTKE, K. & BRAUN, V. (2008). Periplasmic chaperone FkpA is essential for imported colicin M toxicity. Molecular Microbiology 69, 926-937. (Pubitemid 352033311)
    • (2008) Molecular Microbiology , vol.69 , Issue.4 , pp. 926-937
    • Hullmann, J.1    Patzer, S.I.2    Romer, C.3    Hantke, K.4    Braun, V.5
  • 78
    • 45449117125 scopus 로고    scopus 로고
    • Pore formation: An ancient yet complex form of attack
    • IACOVACHE, I., VAN DER GOOT, F.G. & PERNOT, L. (2008). Pore formation: an ancient yet complex form of attack. Biochimica Biophysica Acta 1778(7-8), 1611-1623.
    • (2008) Biochimica Biophysica Acta , vol.1778 , Issue.7-8 , pp. 1611-1623
    • Iacovache, I.1    Van Der Goot, F.G.2    Pernot, L.3
  • 79
    • 25844525796 scopus 로고    scopus 로고
    • Cellular functions, mechanism of action, and regulation of FtsH protease
    • DOI 10.1146/annurev.micro.59.030804.121316
    • ITO, K. & AKIYAMA, Y. (2005). Cellular functions, mechanism of action, and regulation of FtsH protease. Annual Review of Microbiology 59, 211-231. (Pubitemid 41507430)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 211-231
    • Ito, K.1    Akiyama, Y.2
  • 80
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • DOI 10.1016/S1359-0278(98)00033-9
    • JACKSON, S. E. (1998). How do small single-domain proteins fold? Fold Design 3, R81-91. (Pubitemid 28366044)
    • (1998) Folding and Design , vol.3 , Issue.4
    • Jackson, S.E.1
  • 81
    • 0023697146 scopus 로고
    • A hybrid toxin from bacteriophage f1 attachment protein and colicin E3 has altered cell receptor specificity
    • JAKES, K. S., DAVIS, N.G. & ZINDER, N. D. (1988). A hybrid toxin from bacteriophage f1 attachment protein and colicin E3 has altered cell receptor specificity. Journal of Bacteriology 170, 4231-4238.
    • (1988) Journal of Bacteriology , vol.170 , pp. 4231-4238
    • Jakes, K.S.1    Davis, N.G.2    Zinder, N.D.3
  • 82
    • 75149196290 scopus 로고    scopus 로고
    • The colicin Ia receptor, Cir, is also the translocator for colicin Ia
    • JAKES, K.S. & FINKELSTEIN, A. (2010). The colicin Ia receptor, Cir, is also the translocator for colicin Ia. Molecular Microbiology 75, 567-578.
    • (2010) Molecular Microbiology , vol.75 , pp. 567-578
    • Jakes, K.S.1    Finkelstein, A.2
  • 83
    • 33745927413 scopus 로고    scopus 로고
    • Computational Design of a New Hydrogen Bond Network and at Least a 300-fold Specificity Switch at a Protein-Protein Interface
    • DOI 10.1016/j.jmb.2006.05.022, PII S0022283606006048
    • JOACHIMIAK, L. A., KORTEMME, T., STODDARD, B.L. & BAKER, D. (2006). Computational design of a new hydrogen bond network and at least a 300-fold specificity switch at a protein-protein interface. Journal of Molecular Biology 361, 195-208. (Pubitemid 44041449)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.1 , pp. 195-208
    • Joachimiak, L.A.1    Kortemme, T.2    Stoddard, B.L.3    Baker, D.4
  • 84
    • 0033281074 scopus 로고    scopus 로고
    • The translocon: A dynamic gateway at the ER membrane
    • DOI 10.1146/annurev.cellbio.15.1.799
    • JOHNSON, A. E. & VAN WAES, M. A. (1999). The translocon: a dynamic gateway at the ER membrane. Annual Review of Cell Development Biology 15, 799-842. (Pubitemid 32250392)
    • (1999) Annual Review of Cell and Developmental Biology , vol.15 , pp. 799-842
    • Johnson, A.E.1    Van Waes, M.A.2
  • 85
    • 0034767924 scopus 로고    scopus 로고
    • Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm
    • DOI 10.1046/j.1365-2958.2001.02592.x
    • JOURNET, L., BOUVERET, E., RIGAL, A., LLOUBES, R., LAZDUNSKI, C. & BENEDETTI, H. (2001). Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm. Molecular Microbiology 42, 331-344. (Pubitemid 32990124)
    • (2001) Molecular Microbiology , vol.42 , Issue.2 , pp. 331-344
    • Journet, L.1    Bouveret, E.2    Rigal, A.3    Lloubes, R.4    Lazdunski, C.5    Benedetti, H.6
  • 86
    • 44149113954 scopus 로고    scopus 로고
    • Experimental and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases
    • KEEBLE, A. H., JOACHIMIAK, L. A., MATE, M. J., MEENAN, N., KIRKPATRICK, N., BAKER, D. & KLEANTHOUS, C. (2008). Experimental and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases. Journal of Molecular Biology 379, 745-759.
    • (2008) Journal of Molecular Biology , vol.379 , pp. 745-759
    • Keeble, A.H.1    Joachimiak, L.A.2    Mate, M.J.3    Meenan, N.4    Kirkpatrick, N.5    Baker, D.6    Kleanthous, C.7
  • 87
    • 33644857694 scopus 로고    scopus 로고
    • Calorimetric dissection of colicin DNase-immunity protein complex specificity
    • DOI 10.1021/bi052373o
    • KEEBLE, A. H., KIRKPATRICK, N., SHIMIZU, S. & KLEANTHOUS, C. (2006). Calorimetric dissection of colicin DNase-immunity protein complex specificity. Biochemistry 45, 3243-3254. (Pubitemid 43376343)
    • (2006) Biochemistry , vol.45 , Issue.10 , pp. 3243-3254
    • Keeble, A.H.1    Kirkpatrick, N.2    Shimizu, S.3    Kleanthous, C.4
  • 88
    • 24044523202 scopus 로고    scopus 로고
    • The kinetic basis for dual recognition in colicin endonuclease-immunity protein complexes
    • DOI 10.1016/j.jmb.2005.07.035, PII S0022283605008235
    • KEEBLE, A. H. & KLEANTHOUS, C. (2005). The kinetic basis for dual recognition in colicin endonuclease-immunity protein complexes. Journal of Molecular Biology 352, 656-671. (Pubitemid 41225476)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.3 , pp. 656-671
    • Keeble, A.H.1    Kleanthous, C.2
  • 89
    • 33751098280 scopus 로고    scopus 로고
    • HNH endonucleases
    • (eds. M. Belfort, V. Derbyshire, B. Stoddard & D. Wood), Berlin: Springer-Verlag
    • KEEBLE, A. H., MATÉ, M. J. & KLEANTHOUS, C. (2005). HNH endonucleases. In Homing Endonucleases and Inteins, vol. 16 (eds. M. Belfort, V. Derbyshire, B. Stoddard & D. Wood), pp. 49-65. Berlin: Springer-Verlag.
    • (2005) Homing Endonucleases and Inteins , vol.16 , pp. 49-65
    • Keeble, A.H.1    Maté, M.J.2    Kleanthous, C.3
  • 91
    • 33748525883 scopus 로고    scopus 로고
    • Enzyme promiscuity: evolutionary and mechanistic aspects
    • DOI 10.1016/j.cbpa.2006.08.011, PII S1367593106001189, Analytical Techniques/Mechanisms
    • KHERSONSKY, O., ROODVELDT, C. & TAWFIK, D. S. (2006). Enzyme promiscuity: evolutionary and mechanistic aspects. Current Opinion in Chemical Biology 10, 498-508. (Pubitemid 44375065)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 498-508
    • Khersonsky, O.1    Roodveldt, C.2    Tawfik, D.S.3
  • 92
    • 0036274556 scopus 로고    scopus 로고
    • Infliximab and leflunomide combination therapy in rheumatoid arthritis: An open-label study
    • KIELY, P.D. & JOHNSON, D. M. (2002). Infliximab and leflunomide combination therapy in rheumatoid arthritis: an open-label study. Rheumatology (Oxford) 41, 631-637. (Pubitemid 34618880)
    • (2002) Rheumatology , vol.41 , Issue.6 , pp. 631-637
    • Kiely, P.D.W.1    Johnson, D.M.2
  • 93
    • 1842525243 scopus 로고    scopus 로고
    • Antibiotic-mediated antagonism leads to a bacterial game of rock-paperscissors in vivo
    • KIRKUP, B. C. & RILEY, M. A. (2004). Antibiotic-mediated antagonism leads to a bacterial game of rock-paperscissors in vivo. Nature 428, 412.
    • (2004) Nature , vol.428 , pp. 412
    • Kirkup, B.C.1    Riley, M.A.2
  • 94
    • 78449293752 scopus 로고    scopus 로고
    • Swimming against the tide: Progress and challenges in our understanding of colicin translocation
    • KLEANTHOUS, C. (2010). Swimming against the tide: progress and challenges in our understanding of colicin translocation. Nature Reviews Microbiology 8, 843-848.
    • (2010) Nature Reviews Microbiology , vol.8 , pp. 843-848
    • Kleanthous, C.1
  • 96
    • 0035478958 scopus 로고    scopus 로고
    • Immunity proteins: Enzyme inhibitors that avoid the active site
    • DOI 10.1016/S0968-0004(01)01941-7, PII S0968000401019417
    • KLEANTHOUS, C. & WALKER, D. (2001). Immunity proteins: enzyme inhibitors that avoid the active site. Trends in Biochemical Sciences 26, 624-631. (Pubitemid 32925193)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.10 , pp. 624-631
    • Kleanthous, C.1    Walker, D.2
  • 97
    • 69749123006 scopus 로고    scopus 로고
    • Amino acid insertion reveals a necessary three-helical intermediate in the folding pathway of the colicin E7 immunity protein Im7
    • KNOWLING, S. E., FIGUEIREDO, A. M., WHITTAKER, S. B., MOORE, G.R. & RADFORD, S. E. (2009). Amino acid insertion reveals a necessary three-helical intermediate in the folding pathway of the colicin E7 immunity protein Im7. Journal of Molecular Biology 392, 1074-1086.
    • (2009) Journal of Molecular Biology , vol.392 , pp. 1074-1086
    • Knowling, S.E.1    Figueiredo, A.M.2    Whittaker, S.B.3    Moore, G.R.4    Radford, S.E.5
  • 98
    • 0002347541 scopus 로고    scopus 로고
    • The crystal structure of the DNase domain of colicin E7 in complex with its inhibitor Im7 protein
    • DOI 10.1016/S0969-2126(99)80012-4
    • KO, T. P., LIAO, C. C., KU, W. Y., CHAK, K. F. & YUAN, H. S. (1999). The crystal structure of the DNase domain of colicin E7 in complex with its inhibitor Im7 protein. Structure 7, 91-102. (Pubitemid 29159185)
    • (1999) Structure , vol.7 , Issue.1 , pp. 91-102
    • Ko, T.-P.1    Liao, C.-C.2    Ku, W.-Y.3    Chak, K.-F.4    Yuan, H.S.5
  • 101
    • 0033459467 scopus 로고    scopus 로고
    • Structural parsimony in endonuclease active sites: Should the number of homing endonuclease families be redefined?
    • KUHLMANN, U. C., MOORE, G. R., JAMES, R., KLEANTHOUS, C. & HEMMINGS, A. M. (1999). Structural parsimony in endonuclease active sites: should the number of homing endonuclease families be redefined? FEBS Letters 463, 1.
    • (1999) FEBS Letters , vol.463 , pp. 1
    • Kuhlmann, U.C.1    Moore, G.R.2    James, R.3    Kleanthous, C.4    Hemmings, A.M.5
  • 102
    • 0034283147 scopus 로고    scopus 로고
    • Specificity in protein-protein interactions: The structural basis for dual recognition in endonuclease colicin-immunity protein complexes
    • KUHLMANN, U. C., POMMER, A. J., MOORE, G. R., JAMES, R. & KLEANTHOUS, C. (2000). Specificity in protein-protein interactions: the structural basis for dual recognition in endonuclease colicin-immunity protein complexes. Journal of Molecular Biology 301, 1163.
    • (2000) Journal of Molecular Biology , vol.301 , pp. 1163
    • Kuhlmann, U.C.1    Pommer, A.J.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 104
    • 47249132914 scopus 로고    scopus 로고
    • Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes
    • DOI 10.1111/j.1365-2958.2008.06283.x
    • LANCASTER, L. E., SAVELSBERGH, A., KLEANTHOUS, C., WINTERMEYER, W. & RODNINA, M. V. (2008). Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes. Molecular Microbiology 69, 390-401. (Pubitemid 351988012)
    • (2008) Molecular Microbiology , vol.69 , Issue.2 , pp. 390-401
    • Lancaster, L.E.1    Savelsbergh, A.2    Kleanthous, C.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 105
    • 0036589166 scopus 로고    scopus 로고
    • The Tol proteins of Escherichia coli and their involvement in the translocation of group A colicins
    • DOI 10.1016/S0300-9084(02)01419-0, PII S0300908402014190
    • LAZZARONI, J. C., DUBUISSON, J. F. & VIANNEY, A. (2002). The Tol proteins of Escherichia coli and their involvement in the translocation of group A colicins. Biochimie 84, 391-397. (Pubitemid 35350869)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 391-397
    • Lazzaroni, J.-C.1    Dubuisson, J.-F.2    Vianney, A.3
  • 106
    • 33750962168 scopus 로고    scopus 로고
    • Characterisation of the Conformational Properties of Urea-unfolded Im7: Implications for the Early Stages of Protein Folding
    • DOI 10.1016/j.jmb.2006.09.037, PII S0022283606012447
    • LE DUFF, C. S., WHITTAKER, S. B., RADFORD, S.E. & MOORE, G. R. (2006). Characterisation of the conformational properties of urea-unfolded Im7: implications for the early stages of protein folding. Journal of Molecular Biology 364, 824-835. (Pubitemid 44737830)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.4 , pp. 824-835
    • Le Duff, C.S.1    Whittaker, S.B.-M.2    Radford, S.E.3    Moore, G.R.4
  • 108
    • 0032566286 scopus 로고    scopus 로고
    • Dual recognition and the role of specificity-determining residues in colicin E9 DNase-immunity protein interactions
    • DOI 10.1021/bi9808621
    • LI, W., HAMILL, S. J., HEMMINGS, A. M., MOORE, G. R., JAMES, R. & KLEANTHOUS, C. (1998). Dual recognition and the role of specificity-determining residues in colicin E9 DNase-immunity protein interactions. Biochemistry 37, 11771-11779. (Pubitemid 28400048)
    • (1998) Biochemistry , vol.37 , Issue.34 , pp. 11771-11779
    • Li, W.1    Hamill, S.J.2    Hemmings, A.M.3    Moore, G.R.4    James, R.5    Kleanthous, C.6
  • 109
    • 1542358785 scopus 로고    scopus 로고
    • Highly Discriminating Protein-Protein Interaction Specificities in the Context of a Conserved Binding Energy Hotspot
    • DOI 10.1016/j.jmb.2004.02.005, PII S0022283604001512
    • LI, W., KEEBLE, A. H., GIFFARD, C., JAMES, R., MOORE, G. R. & KLEANTHOUS, C. (2004). Highly discriminating protein-protein interaction specificities in the context of a conserved binding energy hotspot. Journal of Molecular Biology 337, 743-759. (Pubitemid 38326888)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.3 , pp. 743-759
    • Li, W.1    Keeble, A.H.2    Giffard, C.3    James, R.4    Moore, G.R.5    Kleanthous, C.6
  • 110
    • 23244431996 scopus 로고    scopus 로고
    • Structural and mutational studies of the catalytic domain of colicin E5: A tRNA-specific ribonuclease
    • DOI 10.1021/bi050749s
    • LIN, Y. L., ELIAS, Y. & HUANG, R. H. (2005). Structural and mutational studies of the catalytic domain of colicin E5: a tRNA-specific ribonuclease. Biochemistry 44, 10494-10500. (Pubitemid 41098226)
    • (2005) Biochemistry , vol.44 , Issue.31 , pp. 10494-10500
    • Lin, Y.-L.1    Elias, Y.2    Huang, R.H.3
  • 112
    • 0000046526 scopus 로고    scopus 로고
    • Filamentous phage infection: Crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA
    • DOI 10.1016/S0969-2126(99)80092-6
    • LUBKOWSKI, J., HENNECKE, F., PLUCKTHUN, A. & WLODAWER, A. (1999). Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA. Structure 7, 711-722. (Pubitemid 29277424)
    • (1999) Structure , vol.7 , Issue.6 , pp. 711-722
    • Lubkowski, J.1    Hennecke, F.2    Pluckthun, A.3    Wlodawer, A.4
  • 113
    • 33646092552 scopus 로고    scopus 로고
    • Molecular basis of inhibition of the ribonuclease activity in colicin E5 by its cognate immunity protein
    • LUNA-CHAVEZ, C., LIN, Y.L. & HUANG, R. H. (2006). Molecular basis of inhibition of the ribonuclease activity in colicin E5 by its cognate immunity protein. Journal of Molecular Biology 358, 571-579.
    • (2006) Journal of Molecular Biology , vol.358 , pp. 571-579
    • Luna-Chavez, C.1    Lin, Y.L.2    Huang, R.H.3
  • 114
    • 4544287623 scopus 로고    scopus 로고
    • Structure-based analysis of the metal-dependent mechanism of H-N-H endonucleases
    • DOI 10.1074/jbc.M403719200
    • MATE, M. J. & KLEANTHOUS, C. (2004). Structure-based analysis of the metal-dependent mechanism of H-N-H endonucleases. Journal of Biological Chemistry 279, 34763-34769. (Pubitemid 39318108)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34763-34769
    • Mate, M.J.1    Kleanthous, C.2
  • 116
    • 33745743311 scopus 로고    scopus 로고
    • Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter
    • DOI 10.1038/sj.emboj.7601132, PII 7601132
    • MENG, G., SURANA, N. K., ST GEME, III, J. W. & WAKSMAN, G. (2006). Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter. EMBO Journal 25, 2297-2304. (Pubitemid 44012213)
    • (2006) EMBO Journal , vol.25 , Issue.11 , pp. 2297-2304
    • Meng, G.1    Surana, N.K.2    St Geme III, J.W.3    Waksman, G.4
  • 117
    • 56749151048 scopus 로고    scopus 로고
    • Structure determination of protein-protein complexes using NMR chemical shifts: Case of an endonuclease colicin-immunity protein complex
    • MONTALVAO, R. W., CAVALLI, A., SALVATELLA, X., BLUNDELL, T. L. & VENDRUSCOLO, M. (2008). Structure determination of protein-protein complexes using NMR chemical shifts: case of an endonuclease colicin-immunity protein complex. Journal of the American Chemical Society 130, 15990-15996.
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 15990-15996
    • Montalvao, R.W.1    Cavalli, A.2    Salvatella, X.3    Blundell, T.L.4    Vendruscolo, M.5
  • 119
    • 33644512106 scopus 로고    scopus 로고
    • Global structural rearrangement of the cell penetrating ribonuclease colicin E3 on interaction with phospholipid membranes
    • MOSBAHI, K., WALKER, D., JAMES, R., MOORE, G.R. & KLEANTHOUS, C. (2006). Global structural rearrangement of the cell penetrating ribonuclease colicin E3 on interaction with phospholipid membranes. Protein Science 15, 620-627.
    • (2006) Protein Science , vol.15 , pp. 620-627
    • Mosbahi, K.1    Walker, D.2    James, R.3    Moore, G.R.4    Kleanthous, C.5
  • 120
    • 2542441795 scopus 로고    scopus 로고
    • Destabilization of the colicin E9 endonuclease domain by interaction with negatively charged phospholipids: Implications for colicin translocation into bacteria
    • DOI 10.1074/jbc.M400402200
    • MOSBAHI, K., WALKER, D., LEA, E., MOORE, G. R., JAMES, R. & KLEANTHOUS, C. (2004). Destabilization of the colicin E9 Endonuclease domain by interaction with negatively charged phospholipids: implications for colicin translocation into bacteria. Journal of Biological Chemistry 279, 22145-22151. (Pubitemid 38684139)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , pp. 22145-22151
    • Mosbahi, K.1    Walker, D.2    Lea, E.3    Moore, G.R.4    Jamesll, R.5    Kleanthous, C.6
  • 123
    • 0014303959 scopus 로고
    • Degradation of ribosomes in Escherichia coli cells treated with colicin E2
    • NOSE, K. & MIZUNO, D. (1968). Degradation of ribosomes in Escherichia coli cells treated with colicin E2. Journal of Biochemistry 64, 1-6.
    • (1968) Journal of Biochemistry , vol.64 , pp. 1-6
    • Nose, K.1    Mizuno, D.2
  • 124
    • 33845669124 scopus 로고    scopus 로고
    • Sequence-specific recognition of colicin E5, a tRNA-targeting ribonuclease
    • DOI 10.1093/nar/gkl629
    • OGAWA, T., INOUE, S., YAJIMA, S., HIDAKA, M. & MASAKI, H. (2006). Sequence-specific recognition of colicin E5, a tRNA-targeting ribonuclease. Nucleic Acids Research 34, 6065-6073. (Pubitemid 44942728)
    • (2006) Nucleic Acids Research , vol.34 , Issue.21 , pp. 6065-6073
    • Ogawa, T.1    Inoue, S.2    Yajima, S.3    Hidaka, M.4    Masaki, H.5
  • 125
    • 0033605708 scopus 로고    scopus 로고
    • A cytotoxic ribonuclease targeting specific transfer RNA anticodons
    • OGAWA, T., TOMITA, K., UEDA, T., WATANABE, K., UOZUMI, T. & MASAKI, H. (1999). A cytotoxic ribonuclease targeting specific transfer RNA anticodons. Science 283, 2097-2100.
    • (1999) Science , vol.283 , pp. 2097-2100
    • Ogawa, T.1    Tomita, K.2    Ueda, T.3    Watanabe, K.4    Uozumi, T.5    Masaki, H.6
  • 126
    • 42949106166 scopus 로고    scopus 로고
    • Monoclonal antibodies in cancer therapy: 25 years of progress
    • OLDHAM, R.K. & DILLMAN, R. O. (2008). Monoclonal antibodies in cancer therapy: 25 years of progress. Journal of Clinical Oncology 26, 1774-1777.
    • (2008) Journal of Clinical Oncology , vol.26 , pp. 1774-1777
    • Oldham, R.K.1    Dillman, R.O.2
  • 127
    • 1042279571 scopus 로고    scopus 로고
    • Comparison of the Transition State Ensembles for Folding of Im7 and Im9 Determined Using All-Atom Molecular Dynamics Simulations with π Value Restraints
    • DOI 10.1002/prot.10595
    • PACI, E., FRIEL, C. T., LINDORFF-LARSEN, K., RADFORD, S. E., KARPLUS, M. & VENDRUSCOLO, M. (2004). Comparison of the transition state ensembles for folding of Im7 and Im9 determined using all-atom molecular dynamics simulations with phi value restraints. Proteins 54, 513-525. (Pubitemid 38197363)
    • (2004) Proteins: Structure, Function and Genetics , vol.54 , Issue.3 , pp. 513-525
    • Paci, E.1    Friel, C.T.2    Lindorff-Larsen, K.3    Radford, S.E.4    Karplus, M.5    Vendruscolo, M.6
  • 128
    • 33144490288 scopus 로고    scopus 로고
    • Peptidoglycan recognition by Pal, an outer membrane lipoprotein
    • DOI 10.1021/bi052227i
    • PARSONS, L. M., LIN, F. & ORBAN, J. (2006). Peptidoglycan recognition by Pal, an outer membrane lipoprotein. Biochemistry 45, 2122-2128. (Pubitemid 43271312)
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2122-2128
    • Parsons, L.M.1    Lin, F.2    Orban, J.3
  • 129
    • 3042855401 scopus 로고    scopus 로고
    • Flexibility in the receptor-binding domain of the enzymatic colicin E9 is required for toxicity against Escherichia coli cells
    • DOI 10.1128/JB.186.14.4520-4527.2004
    • PENFOLD, C. N., HEALY, B., HOUSDEN, N. G., BOETZEL, R., VANKEMMELBEKE, M., MOORE, G. R., KLEANTHOUS, C.& JAMES, R. (2004a). Flexibility in the receptor-binding domain of the enzymatic colicin E9 is required for toxicity against Escherichia coli cells. Journal of Bacteriology 186, 4520-4527. (Pubitemid 38891015)
    • (2004) Journal of Bacteriology , vol.186 , Issue.14 , pp. 4520-4527
    • Penfold, C.N.1    Healy, B.2    Housden, N.G.3    Boetzel, R.4    Vankemmelbeke, M.5    Moore, G.R.6    Kleanthous, C.7    James, R.8
  • 130
    • 3042855401 scopus 로고    scopus 로고
    • Flexibility in the receptor-binding domain of the enzymatic colicin E9 is required for toxicity against Escherichia coli cells
    • DOI 10.1128/JB.186.14.4520-4527.2004
    • PENFOLD, C. N., HEALY, B., HOUSDEN, N. G., BOETZEL, R., VANKEMMELBEKE, M., MOORE, G. R., KLEANTHOUS, C. & JAMES, R. (2004b). Flexibility in the receptor-binding domain of the enzymatic colicin E9 is required for toxicity against Escherichia coli cells. Journal of Bacteriology 186, 4520-4527. (Pubitemid 38891015)
    • (2004) Journal of Bacteriology , vol.186 , Issue.14 , pp. 4520-4527
    • Penfold, C.N.1    Healy, B.2    Housden, N.G.3    Boetzel, R.4    Vankemmelbeke, M.5    Moore, G.R.6    Kleanthous, C.7    James, R.8
  • 131
    • 0032527793 scopus 로고    scopus 로고
    • The Ton system can functionally replace the TolB protein in the uptake of mutated colicin U
    • DOI 10.1016/S0378-1097(98)00240-7, PII S0378109798002407
    • PILSL, H. & BRAUN, V. (1998). The Ton system can functionally replace the TolB protein in the uptake of mutated colicin U. FEMS Microbiology Letters 164, 363-367. (Pubitemid 28321557)
    • (1998) FEMS Microbiology Letters , vol.164 , Issue.2 , pp. 363-367
    • Pilsl, H.1    Braun, V.2
  • 132
    • 0033000807 scopus 로고    scopus 로고
    • Characterization of colicin S4 and its receptor, OmpW, a minor protein of the Escherichia coli outer membrane
    • PILSL, H., SMAJS, D. & BRAUN, V. (1999). Characterization of colicin S4 and its receptor, OmpW, a minor protein of the Escherichia coli outer membrane. Journal of Bacteriology 181, 3578-3581. (Pubitemid 29259310)
    • (1999) Journal of Bacteriology , vol.181 , Issue.11 , pp. 3578-3581
    • Pilsl, H.1    Smajs, D.2    Braun, V.3
  • 133
    • 0038415649 scopus 로고    scopus 로고
    • Protein translocation in the three domains of life: Variations on a theme
    • POHLSCHRODER, M., PRINZ, W. A., HARTMANN, E. & BECKWITH, J. (1997). Protein translocation in the three domains of life: variations on a theme. Cell 91, 563-566. (Pubitemid 27513647)
    • (1997) Cell , vol.91 , Issue.5 , pp. 563-566
    • Pohlschroder, M.1    Prinz, W.A.2    Hartmann, E.3    Beckwith, J.4
  • 134
    • 0035782661 scopus 로고    scopus 로고
    • Review: Protein design - Where we were, where we are, where we're going
    • POKALA, N. & HANDEL, T. M. (2001). Review: protein design - where we were, where we are, where we're going. Journal of Structural Biology 134, 269-281.
    • (2001) Journal of Structural Biology , vol.134 , pp. 269-281
    • Pokala, N.1    Handel, T.M.2
  • 136
    • 0042065285 scopus 로고    scopus 로고
    • Touch and go: Tying TonB to transport
    • DOI 10.1046/j.1365-2958.2003.03629.x
    • POSTLE, K. & KADNER, R. J. (2003). Touch and go: tying TonB to transport. Molecular Microbiology 49, 869-882. (Pubitemid 36981335)
    • (2003) Molecular Microbiology , vol.49 , Issue.4 , pp. 869-882
    • Postle, K.1    Kadner, R.J.2
  • 138
    • 0031799096 scopus 로고    scopus 로고
    • Discovery of critical Tol A-binding residues in the bactericidal toxin colicin N: A biophysical approach
    • DOI 10.1046/j.1365-2958.1998.00899.x
    • RAGGETT, E. M., BAINBRIDGE, G., EVANS, L. J., COOPER, A. & LAKEY, J. H. (1998). Discovery of critical Tol A-binding residues in the bactericidal toxin colicin N: a biophysical approach. Molecular Microbiology 28, 1335-1343. (Pubitemid 28293555)
    • (1998) Molecular Microbiology , vol.28 , Issue.6 , pp. 1335-1343
    • Raggett, E.M.1    Bainbridge, G.2    Evans, L.J.A.3    Cooper, A.4    Lakey, J.H.5
  • 140
    • 0032425481 scopus 로고    scopus 로고
    • Molecular mechanisms of bacteriocin evolution
    • DOI 10.1146/annurev.genet.32.1.255
    • RILEY, M. A. (1998). Molecular mechanisms of bacteriocin evolution. Annual Review of Genetics 32, 255-278. (Pubitemid 29045314)
    • (1998) Annual Review of Genetics , vol.32 , pp. 255-278
    • Riley, M.A.1
  • 141
    • 13844281394 scopus 로고    scopus 로고
    • Directed evolution of proteins for heterologous expression and stability
    • DOI 10.1016/j.sbi.2005.01.001
    • ROODVELDT, C., AHARONI, A. & TAWFIK, D. S. (2005). Directed evolution of proteins for heterologous expression and stability. Current Opinion in Structural Biology 15, 50-56. (Pubitemid 40249509)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.1 SPEC. ISSUE , pp. 50-56
    • Roodveldt, C.1    Aharoni, A.2    Tawfik, D.S.3
  • 145
    • 21644453615 scopus 로고    scopus 로고
    • Identification of an essential cleavage site in ColE7 required for import and killing of cells
    • DOI 10.1074/jbc.M501216200
    • SHI, Z., CHAK, K. F. & YUAN, H. S. (2005). Identification of an essential cleavage site in ColE7 required for import and killing of cells. Journal of Biological Chemistry 280, 24663-24668. (Pubitemid 40934555)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24663-24668
    • Shi, Z.1    Chak, K.-F.2    Yuan, H.S.3
  • 146
    • 0028151655 scopus 로고
    • Amino acid sequence motif of group I intron endonucleases is conserved in open reading frames of group II introns
    • DOI 10.1016/0968-0004(94)90086-8
    • SHUB, D. A., GOODRICH-BLAIR, H. & EDDY, S. R. (1994). Amino acid sequence motif of group I intron endonucleases is conserved in open reading frames of group II introns. Trends in Biochemical Sciences 19, 402-404. (Pubitemid 24320127)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.10 , pp. 402-404
    • Shub, D.A.1    Goodrich-Blair, H.2    Eddy, S.R.3
  • 147
    • 65949115310 scopus 로고    scopus 로고
    • Fluoresceination of FepA during colicin B killing: Effects of temperature, toxin and TonB
    • SMALLWOOD, C. R., MARCO, A. G., XIAO, Q., TRINH, V., NEWTON, S.M. & KLEBBA, P. E. (2009). Fluoresceination of FepA during colicin B killing: effects of temperature, toxin and TonB. Molecular Microbiology 72, 1171-1180.
    • (2009) Molecular Microbiology , vol.72 , pp. 1171-1180
    • Smallwood, C.R.1    Marco, A.G.2    Xiao, Q.3    Trinh, V.4    Newton, S.M.5    Klebba, P.E.6
  • 148
    • 0035930345 scopus 로고    scopus 로고
    • Crystal structure of colicin E3: Implications for cell entry and ribosome inactivation
    • DOI 10.1016/S1097-2765(01)00396-3
    • SOELAIMAN, S., JAKES, K., WU, N., LI, C. & SHOHAM, M. (2001). Crystal structure of colicin E3: implications for cell entry and ribosome inactivation. Molecular Cell 8, 1053-1062. (Pubitemid 34031807)
    • (2001) Molecular Cell , vol.8 , Issue.5 , pp. 1053-1062
    • Soelaiman, S.1    Jakes, K.2    Wu, N.3    Li, C.4    Shoham, M.5
  • 149
    • 78650215348 scopus 로고    scopus 로고
    • Mobility of BtuB and OmpF in the Escherichia coli outer membrane: Implications for dynamic formation of a translocon complex
    • SPECTOR, J., ZAKHAROV, S., LILL, Y., SHARMA, O., CRAMER, W. A. & RITCHIE, K. (2010). Mobility of BtuB and OmpF in the Escherichia coli outer membrane: implications for dynamic formation of a translocon complex. Biophysical Journal 99, 3880-3886.
    • (2010) Biophysical Journal , vol.99 , pp. 3880-3886
    • Spector, J.1    Zakharov, S.2    Lill, Y.3    Sharma, O.4    Cramer, W.A.5    Ritchie, K.6
  • 150
    • 4143080376 scopus 로고    scopus 로고
    • Trapping the on-pathway folding intermediate of Im7 at equilibrium
    • DOI 10.1016/j.jmb.2004.05.049, PII S0022283604006291
    • SPENCE, G. R., CAPALDI, A. P. & RADFORD, S. E. (2004). Trapping the on-pathway folding intermediate of Im7 at equilibrium. Journal of Molecular Biology 341, 215-226. (Pubitemid 39090646)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.1 , pp. 215-226
    • Spence, G.R.1    Capaldi, A.P.2    Radford, S.E.3
  • 153
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • TOKURIKI, N. & TAWFIK, D. S. (2009). Protein dynamism and evolvability. Science 324, 203-207.
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2
  • 156
    • 21844450835 scopus 로고    scopus 로고
    • Rapid detection of colicin E9-induced DNA damage using Escherichia coli cells carrying SOS promoter-lux fusions
    • DOI 10.1128/JB.187.14.4900-4907.2005
    • VANKEMMELBEKE, M., HEALY, B., MOORE, G. R., KLEANTHOUS, C., PENFOLD, C.N. & JAMES, R. (2005). Rapid detection of colicin E9-induced DNA damage using Escherichia coli cells carrying SOS promoter-lux fusions. Journal of Bacteriology 187, 4900-4907. (Pubitemid 40962207)
    • (2005) Journal of Bacteriology , vol.187 , Issue.14 , pp. 4900-4907
    • Vankemmelbeke, M.1    Healy, B.2    Moore, G.R.3    Kleanthous, C.4    Penfold, C.N.5    James, R.6
  • 158
    • 0032528046 scopus 로고    scopus 로고
    • Crystal structure of a colicin N fragment suggests a model for toxicity
    • VETTER, I. R., PARKER, M. W., TUCKER, A. D., LAKEY, J. H., PATTUS, F. & TSERNOGLOU, D. (1998). Crystal structure of a colicin N fragment suggests a model for toxicity. Structure 6, 863-874. (Pubitemid 28348649)
    • (1998) Structure , vol.6 , Issue.7 , pp. 863-874
    • Vetter, I.R.1    Parker, M.W.2    Tucker, A.D.3    Lakey, J.H.4    Pattus, F.5    Tsernoglou, D.6
  • 159
    • 2442713814 scopus 로고    scopus 로고
    • Identification of the catalytic motif of the microbial ribosome inactivating cytotoxin colicin E3
    • DOI 10.1110/ps.04658504
    • WALKER, D., LANCASTER, L., JAMES, R. & KLEANTHOUS, C. (2004a). Identification of the catalytic motif of the microbial ribosome inactivating cytotoxin colicin E3. Protein Science 13, 1603-1611. (Pubitemid 38669248)
    • (2004) Protein Science , vol.13 , Issue.6 , pp. 1603-1611
    • Walker, D.1    Lancaster, L.2    James, R.3    Kleanthous, C.4
  • 160
    • 0345701261 scopus 로고    scopus 로고
    • Thermodynamic consequences of bipartite immunity protein binding to the ribosomal ribonuclease colicin E3
    • WALKER, D., MOORE, G. R., JAMES, R. & KLEANTHOUS, C. (2003). Thermodynamic consequences of bipartite immunity protein binding to the ribosomal ribonuclease colicin E3. Biochemistry 42, 4161.
    • (2003) Biochemistry , vol.42 , pp. 4161
    • Walker, D.1    Moore, G.R.2    James, R.3    Kleanthous, C.4
  • 161
    • 35748954062 scopus 로고    scopus 로고
    • The role of electrostatics in colicin nuclease domain translocation into bacterial cells
    • DOI 10.1074/jbc.M705883200
    • WALKER, D., MOSBAHI, K., VANKEMMELBEKE, M., JAMES, R. & KLEANTHOUS, C. (2007). The role of electrostatics in colicin nuclease domain translocation into bacterial cells. Journal of Biological Chemistry 282, 31389-31397. (Pubitemid 350044876)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.43 , pp. 31389-31397
    • Walker, D.1    Mosbahi, K.2    Vankemmelbeke, M.3    James, R.4    Kleanthous, C.5
  • 162
    • 1542275259 scopus 로고    scopus 로고
    • Transcriptional profiling of colicin-induced cell death of Escherichia coli MG1655 identifies potential mechanisms by which bacteriocins promote bacterial diversity
    • WALKER, D., ROLFE, M., THOMPSON, A., MOORE, G. R., JAMES, R., HINTON, J.C. & KLEANTHOUS, C. (2004b). Transcriptional profiling of colicin-induced cell death of Escherichia coli MG1655 identifies potential mechanisms by which bacteriocins promote bacterial diversity. Journal of Bacteriology 186, 866.
    • (2004) Journal of Bacteriology , vol.186 , pp. 866
    • Walker, D.1    Rolfe, M.2    Thompson, A.3    Moore, G.R.4    James, R.5    Hinton, J.C.6    Kleanthous, C.7
  • 163
    • 0032512424 scopus 로고    scopus 로고
    • Specificity in protein-protein recognition: Conserved Im9 residues are the major determinants of stability in the colicin E9 DNase-Im9 complex
    • WALLIS, R., LEUNG, K. Y., OSBORNE, M. J., JAMES, R., MOORE, G. R. & KLEANTHOUS, C. (1998). Specificity in protein-protein recognition: conserved Im9 residues are the major determinants of stability in the colicin E9 DNase-Im9 complex. Biochemistry 37, 476.
    • (1998) Biochemistry , vol.37 , pp. 476
    • Wallis, R.1    Leung, K.Y.2    Osborne, M.J.3    James, R.4    Moore, G.R.5    Kleanthous, C.6
  • 164
    • 0028866770 scopus 로고
    • Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 1. Diffusioncontrolled association and femtomolar binding for the cognate complex
    • WALLIS, R., MOORE, G. R., JAMES, R. & KLEANTHOUS, C. (1995). Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 1. Diffusioncontrolled association and femtomolar binding for the cognate complex. Biochemistry 34, 13743-13750.
    • (1995) Biochemistry , vol.34 , pp. 13743-13750
    • Wallis, R.1    Moore, G.R.2    James, R.3    Kleanthous, C.4
  • 166
    • 0025897173 scopus 로고
    • The tol gene products and the import of macromolecules into Escherichia coli
    • WEBSTER, R. E. (1991). The tol gene products and the import of macromolecules into Escherichia coli. Molecular Microbiology 5, 1005-1011. (Pubitemid 21896126)
    • (1991) Molecular Microbiology , vol.5 , Issue.5 , pp. 1005-1011
    • Webster, R.E.1
  • 167
    • 33846577660 scopus 로고    scopus 로고
    • NMR Analysis of the Conformational Properties of the Trapped on-pathway Folding Intermediate of the Bacterial Immunity Protein Im7
    • DOI 10.1016/j.jmb.2006.11.012, PII S0022283606015415
    • WHITTAKER, S. B., SPENCE, G. R., GUNTER GROSSMANN, J., RADFORD, S. E. & MOORE, G. R. (2007). NMR analysis of the conformational properties of the trapped onpathway folding intermediate of the bacterial immunity protein Im7. Journal of Molecular Biology 366, 1001-1015. (Pubitemid 46175862)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.3 , pp. 1001-1015
    • Whittaker, S.B.-M.1    Spence, G.R.2    Gunter Grossmann, J.3    Radford, S.E.4    Moore, G.R.5
  • 168
    • 0031022750 scopus 로고    scopus 로고
    • Crystal structure of colicin Ia
    • DOI 10.1038/385461a0
    • WIENER, M., FREYMANN, D., GHOSH, P. & STROUD, R.M. (1997). Crystal structure of colicin Ia. Nature 385, 461-464. (Pubitemid 27065935)
    • (1997) Nature , vol.385 , Issue.6615 , pp. 461-464
    • Wiener, M.1    Freymann, D.2    Ghosh, P.3    Stroud, R.M.4
  • 169
    • 23044489264 scopus 로고    scopus 로고
    • TonB-dependent outer membrane transport: Going for Baroque?
    • DOI 10.1016/j.sbi.2005.07.001, PII S0959440X05001247, Membranes/Engineering and Desing
    • WIENER, M. C. (2005). TonB-dependent outer membrane transport: going for Baroque? Current Opinion in Structural Biology 15, 394-400. (Pubitemid 41073829)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.4 , pp. 394-400
    • Wiener, M.C.1
  • 170
    • 49149127813 scopus 로고    scopus 로고
    • Crystal structures of the OmpF porin: Function in a colicin translocon
    • YAMASHITA, E., ZHALNINA, M. V., ZAKHAROV, S. D., SHARMA, O. & CRAMER, W. A. (2008). Crystal structures of the OmpF porin: function in a colicin translocon. EMBO Journal 27, 2171-2180.
    • (2008) EMBO Journal , vol.27 , pp. 2171-2180
    • Yamashita, E.1    Zhalnina, M.V.2    Zakharov, S.D.3    Sharma, O.4    Cramer, W.A.5
  • 171
    • 2442666884 scopus 로고    scopus 로고
    • On the mechanism and pathway of colicin import across the E. coli outer membrane
    • d1000-1499
    • ZAKHAROV, S.D. & CRAMER, W. A. (2004). On the mechanism and pathway of colicin import across the E. Coli outer membrane. Frontiers in Bioscience 9, 1311-1317. (Pubitemid 39060844)
    • (2004) Frontiers in Bioscience , vol.9 , pp. 1311-1317
    • Zakharov, S.D.1    Cramer, W.A.2
  • 174
    • 57049103480 scopus 로고    scopus 로고
    • Primary events in the colicin translocon: FRET analysis of colicin unfolding initiated by binding to BtuB and OmpF
    • ZAKHAROV, S. D., SHARMA, O., ZHALNINA, M.V. & CRAMER, W. A. (2008). Primary events in the colicin translocon: FRET analysis of colicin unfolding initiated by binding to BtuB and OmpF. Biochemistry 47, 12802-12809.
    • (2008) Biochemistry , vol.47 , pp. 12802-12809
    • Zakharov, S.D.1    Sharma, O.2    Zhalnina, M.V.3    Cramer, W.A.4
  • 175
    • 33748667290 scopus 로고    scopus 로고
    • The colicin E3 outer membrane translocon: Immunity protein release allows interaction of the cytotoxic domain with OmpF porin
    • DOI 10.1021/bi060694+
    • ZAKHAROV, S. D., ZHALNINA, M. V., SHARMA, O. & CRAMER, W. A. (2006). The colicin E3 outer membrane translocon: immunity protein release allows interaction of the cytotoxic domain with OmpF porin. Biochemistry 45, 10199-10207. (Pubitemid 44384795)
    • (2006) Biochemistry , vol.45 , Issue.34 , pp. 10199-10207
    • Zakharov, S.D.1    Zhalnina, M.V.2    Sharma, O.3    Cramer, W.A.4
  • 176
    • 54449087613 scopus 로고    scopus 로고
    • Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli
    • ZETH, K., ROMER, C., PATZER, S. I. & BRAUN, V. (2008). Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli. Journal of Biological Chemistry 283, 25324-25331.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 25324-25331
    • Zeth, K.1    Romer, C.2    Patzer, S.I.3    Braun, V.4
  • 178
    • 63249134496 scopus 로고    scopus 로고
    • Mapping the interactions between Escherichia coli tol subunits: Rotation of the TolR transmembrane helix
    • ZHANG, X. Y., GOEMAERE, E. L., THOME, R., GAVIOLI, M., CASCALES, E. & LLOUBES, R. (2009a). Mapping the interactions between Escherichia coli tol subunits: rotation of the TolR transmembrane helix. Journal of Biological Chemistry 284, 4275-4282.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 4275-4282
    • Zhang, X.Y.1    Goemaere, E.L.2    Thome, R.3    Gavioli, M.4    Cascales, E.5    Lloubes, R.6
  • 179
    • 75149149839 scopus 로고    scopus 로고
    • The crystal structure of the TolB box of Colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins
    • ZHANG, Y., VANKEMMELBEKE, M., BAARDELANG, P., PAOLI, M., PENFOLD, C.N. & JAMES, R. (2009b). The crystal structure of the TolB box of Colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins. Molecular Microbiology 75, 623-636.
    • (2009) Molecular Microbiology , vol.75 , pp. 623-636
    • Zhang, Y.1    Vankemmelbeke, M.2    Baardelang, P.3    Paoli, M.4    Penfold, C.N.5    James, R.6
  • 180
    • 44949113393 scopus 로고    scopus 로고
    • Investigating early events in receptor binding and translocation of colicin E9 using synchronized cell killing and proteolytic cleavage
    • DOI 10.1128/JB.00047-08
    • ZHANG, Y., VANKEMMELBEKE, M. N., HOLLAND, L. E., WALKER, D. C., JAMES, R. & PENFOLD, C. N. (2008). Investigating early events in receptor binding and translocation of colicin E9 using synchronized cell killing and proteolytic cleavage. Journal of Bacteriology 190, 4342-4350. (Pubitemid 351812882)
    • (2008) Journal of Bacteriology , vol.190 , Issue.12 , pp. 4342-4350
    • Zhang, Y.1    Vankemmelbeke, M.N.2    Holland, L.E.3    Walker, D.C.4    James, R.5    Penfold, C.N.6
  • 181
    • 0027105109 scopus 로고
    • Constraints imposed by protease accessibility on the trans-membrane and surface topography of the colicin E1 ion channel
    • ZHANG, Y.L. & CRAMER, W. A. (1992). Constraints imposed by protease accessibility on the trans-membrane and surface topography of the colicin E1 ion channel. Protein Science 1, 1666-1676. (Pubitemid 23047483)
    • (1992) Protein Science , vol.1 , Issue.12 , pp. 1666-1676
    • Zhang, Y.-L.1    Cramer, W.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.