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Volumn 11, Issue , 2011, Pages

A model for the Escherichia coli FtsB/FtsL/FtsQ cell division complex

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; FTSB PROTEIN; FTSL PROTEIN; FTSQ PROTEIN; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN; ESCHERICHIA COLI PROTEIN; FTSB PROTEIN, E COLI; FTSL PROTEIN, E COLI; FTSQ PROTEIN, E COLI; MEMBRANE PROTEIN;

EID: 79958292223     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-11-28     Document Type: Article
Times cited : (37)

References (69)
  • 2
    • 33644920433 scopus 로고    scopus 로고
    • Septum enlightenment: Assembly of bacterial division proteins
    • 10.1128/JB.188.1.19-27.2006 16352817
    • Septum enlightenment: assembly of bacterial division proteins. M Vicente, IA Rico, R Martinez-Arteaga, J Mingrorance, J Bacteriol 2006 188 19 27 10.1128/JB.188.1.19-27.2006 16352817
    • (2006) J Bacteriol , vol.188 , pp. 19-27
    • Vicente, M.1    Rico, I.A.2    Martinez-Arteaga, R.3    Mingrorance, J.4
  • 3
    • 0346252349 scopus 로고    scopus 로고
    • Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: Bacterial septosome differentiation
    • Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacteria septosome differentiation. G Di Lallo, GM Fagioli, D Barionovi, P Ghelardini, L Paolozzi, Microbiology 2003 149 3353 3359 10.1099/mic.0.26580-0 14663069 (Pubitemid 38016664)
    • (2003) Microbiology , vol.149 , Issue.12 , pp. 3353-3359
    • Di Lallo, G.1    Fagioli, M.2    Barionovi, D.3    Ghelardini, P.4    Paolozzi, L.5
  • 4
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • DOI 10.1128/JB.187.7.2233-2243.2005
    • Interaction network among Escherichia coli membrane proteins inved in cell division as revealed by bacterial two-hybrid analysis. G Karimova, N Dautin, D Ladant, J Bacteriol 2005 187 2233 2243 10.1128/JB.187.7.2233-2243.2005 15774864 (Pubitemid 40389120)
    • (2005) Journal of Bacteriology , vol.187 , Issue.7 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 5
    • 33745195461 scopus 로고    scopus 로고
    • Premature targeting of a cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly
    • 10.1111/j.1365-2958.2006.05206.x 16824093
    • Premature targeting of a cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly. NW Goehring, MD Gonzalez, J Beckwith, Mol Microbiol 2006 61 33 45 10.1111/j.1365-2958.2006. 05206.x 16824093
    • (2006) Mol Microbiol , vol.61 , pp. 33-45
    • Goehring, N.W.1    Gonzalez, M.D.2    Beckwith, J.3
  • 6
    • 0025803531 scopus 로고
    • The FtsQ protein of Escherichia coli: Membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations
    • 2007547
    • The FtsQ protein of Escherichia coli: membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations. MJ Carson, J Barondess, J Beckwith, J Bacteriol 1991 173 2187 2195 2007547
    • (1991) J Bacteriol , vol.173 , pp. 2187-2195
    • Carson, M.J.1    Barondess, J.2    Beckwith, J.3
  • 7
    • 0030756250 scopus 로고    scopus 로고
    • Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli
    • Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli. LM Guzman, DS Weiss, J Beckwith, J Bacteriol 1997 179 5094 5103 9260951 (Pubitemid 27340543)
    • (1997) Journal of Bacteriology , vol.179 , Issue.16 , pp. 5094-5103
    • Guzman, L.M.1    Weiss, D.S.2    Beckwith, J.3
  • 8
    • 0032953197 scopus 로고    scopus 로고
    • Septal localization of FtsQ, an essential cell division protein in Escherichia coli
    • Septal localization of FtsQ, an essential cell division protein in Escherichia coli. JC Chen, DS Weiss, JM Ghigo, J Beckwith, J Bacteriol 1999 181 521 530 9882666 (Pubitemid 29045143)
    • (1999) Journal of Bacteriology , vol.181 , Issue.2 , pp. 521-530
    • Chen, J.C.1    Weiss, D.S.2    Ghigo, J.-M.3    Beckwith, J.4
  • 9
    • 0034740520 scopus 로고    scopus 로고
    • FtsQ, FtsL and Ftsl require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division
    • DOI 10.1046/j.1365-2958.2001.02640.x
    • FtsQ, FtsL, and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division. JC Chen, J Beckwith, Mol Microbiol 2001 42 395 413 10.1046/j.1365-2958.2001.02640.x 11703663 (Pubitemid 32990129)
    • (2001) Molecular Microbiology , vol.42 , Issue.2 , pp. 395-413
    • Chen, J.C.1    Beckwith, J.2
  • 11
    • 0032957011 scopus 로고    scopus 로고
    • Localization of FtsL to the Escherichia coli septal ring
    • DOI 10.1046/j.1365-2958.1999.01213.x
    • Localization of FtsL to the Escherichia coli septal ring. JM Ghigo, DS Weiss, JC Chen, JC Yarrow, J Beckwith, Mol Microbiol 1999 31 725 737 10.1046/j.1365-2958.1999.01213.x 10027987 (Pubitemid 29046112)
    • (1999) Molecular Microbiology , vol.31 , Issue.2 , pp. 725-737
    • Ghigo, J.-M.1    Weiss, D.S.2    Chen, J.C.3    Yarrow, J.C.4    Beckwith, J.5
  • 13
    • 0032932435 scopus 로고    scopus 로고
    • Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL
    • Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL. DS Weiss, JC Chen, JM Ghigo, D Boyd, J Beckwith, J Bacteriol 1999 181 508 520 9882665 (Pubitemid 29045142)
    • (1999) Journal of Bacteriology , vol.181 , Issue.2 , pp. 508-520
    • Weiss, D.S.1    Chen, J.C.2    Ghigo, J.-M.3    Boyd, D.4    Beckwith, J.5
  • 14
    • 0030856502 scopus 로고    scopus 로고
    • FtsN, a late recruit to the septum in Escherichia coil
    • FtsN, a late recruit to the septum in Escherichia coli. SG Addinall, C Cao, J Lutkenhaus, Mol Microbiol 1997 25 303 309 10.1046/j.1365-2958.1997. 4641833.x 9282742 (Pubitemid 27351581)
    • (1997) Molecular Microbiology , vol.25 , Issue.2 , pp. 303-309
    • Addinall, S.G.1    Cao, C.2    Lutkenhaus, J.3
  • 16
    • 0642377467 scopus 로고    scopus 로고
    • POTRA: A conserved domain in the FtsQ family and a class of β-barrel outer membrane proteins
    • DOI 10.1016/j.tibs.2003.08.003, PII S0968000403002123
    • POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins. L Sánchez-Pulido, D Devos, S Genevrois, M Vicente, A Valencia, Trends Biochem Sci 2003 2 523 526 (Pubitemid 38366276)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.10 , pp. 523-526
    • Sanchez-Pulido, L.1    Devos, D.2    Genevrois, S.3    Vicente, M.4    Valencia, A.5
  • 17
    • 33646269969 scopus 로고    scopus 로고
    • Domain architecture and structure of the bacterial cell division protein DivIB
    • 10.1073/pnas.0601397103 16618922
    • Domain architecture and structure of the bacterial cell division protein DivIB. SA Robson, GF King, Proc Natl Acad Sci USA 2006 103 6700 6705 10.1073/pnas.0601397103 16618922
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6700-6705
    • Robson, S.A.1    King, G.F.2
  • 18
    • 70350437278 scopus 로고    scopus 로고
    • Central domain of DivIB caps the C-terminal region of the FtsL/DivIC coiled-coil rod
    • 10.1074/jbc.M109.019471 19635793
    • Central domain of DivIB caps the C-terminal region of the FtsL/DivIC coiled-coil rod. S Masson, T Kern, A Le Goullec, C Guistini, JP Simorre, P Cllow, T Vernet, F Gabel, A Zapun, J Biol Chem 2009 284 40 27687 27700 10.1074/jbc.M109.019471 19635793
    • (2009) J Biol Chem , vol.284 , Issue.40 , pp. 27687-27700
    • Masson, S.1    Kern, T.2    Le Goullec, A.3    Guistini, C.4    Simorre, J.P.5    Cllow, P.6    Vernet, T.7    Gabel, F.8    Zapun, A.9
  • 19
    • 33846299252 scopus 로고    scopus 로고
    • Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins
    • DOI 10.1099/mic.0.2006/000265-0
    • Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins. V D'Ulisse, M Fagioli, P Ghelardini, L Paolozzi, Microbiology 2007 153 124 138 10.1099/mic.0.2006/000265-0 17185541 (Pubitemid 46111827)
    • (2007) Microbiology , vol.153 , Issue.1 , pp. 124-138
    • D'Ulisse, V.1    Fagioli, M.2    Ghelardini, P.3    Paolozzi, L.4
  • 20
    • 0036176969 scopus 로고    scopus 로고
    • Analysis of ftsQ mutant alleles in Escherichia coli: Complementation, septal localization, and recruitment of downstream cell division proteins
    • Analysis of ftsQ mutant alleles in Escherichia coli: complementation, septal localization, and recruitment of downstream cell division proteins. JC Chen, M Minev, J Beckwith, J Bacteriol 2002 184 695 705 10.1128/JB.184.3.695- 705.2002 11790739 (Pubitemid 34150216)
    • (2002) Journal of Bacteriology , vol.184 , Issue.3 , pp. 695-705
    • Chen, J.C.1    Minev, M.2    Beckwith, J.3
  • 21
    • 78649338546 scopus 로고    scopus 로고
    • FtsQ interaction mutants: A way to identify new antibacterial targets
    • 10.1016/j.nbt.2010.05.002
    • FtsQ interaction mutants: a way to identify new antibacterial targets. L Grenga, G Guglielmi, S Melino, P Ghelardini, L Paolozzi, New Biotechnol 2010 27 870 881 10.1016/j.nbt.2010.05.002
    • (2010) New Biotechnol , vol.27 , pp. 870-881
    • Grenga, L.1    Guglielmi, G.2    Melino, S.3    Ghelardini, P.4    Paolozzi, L.5
  • 22
    • 33846237649 scopus 로고    scopus 로고
    • Mutants, suppressors, and wrinkled colonies: Mutant alleles of the cell division gene ftsQ point to functional domains in FtsQ and a role for domain 1C of FtsA in divisome assembly
    • DOI 10.1128/JB.00991-06
    • Mutants, suppressors, and wrinkled colonies: mutant alleles of the cell division gene ftsQ point to functional domains in FtsQ and a role for the domain 1C of FtsA in divisome assembly. NW Goehring, I Petrovska, D Boyd, K Beckwith, J Bacteriol 2007 189 633 645 10.1128/JB.00991-06 16980443 (Pubitemid 46106396)
    • (2007) Journal of Bacteriology , vol.189 , Issue.2 , pp. 633-645
    • Goehring, N.W.1    Petrovska, I.2    Boyd, D.3    Beckwith, J.4
  • 23
    • 0033986953 scopus 로고    scopus 로고
    • Cell division in Escherichia coli: Role of FtsL domains in septal localization, function, and oligomerization
    • Cell division in Escherichia coli: role of FtsL domains in septal localization, function, and oligomerization. JM Ghigo, J Beckwith, J Bacteriol 2000 182 116 129 10.1128/JB.182.1.116-129.2000 10613870 (Pubitemid 30004565)
    • (2000) Journal of Bacteriology , vol.182 , Issue.1 , pp. 116-129
    • Ghigo, J.-M.1    Beckwith, J.2
  • 24
    • 0031824694 scopus 로고    scopus 로고
    • Characterization of the essential cell division gene ftsL(yIID) of Bacillus subtilis and its role in the assembly of the division apparatus
    • DOI 10.1046/j.1365-2958.1998.00954.x
    • Characterization of the essential cell division gene ftsL (yllD) of Bacillus subtilis and its role in the assembly of the division apparatus. RA Daniel, EJ Harry, VL Katis, RG Wake, J Errington, Mol Microbiol 1998 29 593 604 10.1046/j.1365-2958.1998.00954.x 9720875 (Pubitemid 28330791)
    • (1998) Molecular Microbiology , vol.29 , Issue.2 , pp. 593-604
    • Daniel, R.A.1    Harry, E.J.2    Katis, V.L.3    Wake, R.G.4    Errington, J.5
  • 25
    • 0030662451 scopus 로고    scopus 로고
    • The Bacillus subtilis division protein DivlC is a highly abundant membrane-bound protein that localizes to the division site
    • The Bacillus subtulis division protein DivIC is a highly abundant membrane-bound protein that localizes to the division site. VL Katis, EJ Harry, RG Wake, Mol Microbiol 1997 26 1047 1055 10.1046/j.1365-2958.1997.6422012.x 9426141 (Pubitemid 27507888)
    • (1997) Molecular Microbiology , vol.26 , Issue.5 , pp. 1047-1055
    • Katis, V.L.1    Harry, E.J.2    Wake, R.G.3
  • 26
    • 2942570076 scopus 로고    scopus 로고
    • A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region
    • DOI 10.1111/j.1365-2958.2004.04044.x
    • A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region. N Buddelmeijer, J Beckwith, Mol Microbiol 2004 52 1315 1327 10.1111/j.1365-2958. 2004.04044.x 15165235 (Pubitemid 38746306)
    • (2004) Molecular Microbiology , vol.52 , Issue.5 , pp. 1315-1327
    • Buddelmeijer, N.1    Beckwith, J.2
  • 27
    • 65249155295 scopus 로고    scopus 로고
    • Divisome under construction: Distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins
    • 10.1128/JB.01597-08 19233928
    • Divisome under construction: Distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins. MD Gonzalez, J Beckwith, J Bacteriol 2009 191 8 2815 2825 10.1128/JB.01597-08 19233928
    • (2009) J Bacteriol , vol.191 , Issue.8 , pp. 2815-2825
    • Gonzalez, M.D.1    Beckwith, J.2
  • 28
    • 77952577603 scopus 로고    scopus 로고
    • Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex
    • 10.1128/JB.01609-09 20363951
    • Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex. MD Gonzalez, EA Akbay, D Boyd, J Beckwith, J Bacteriol 2010 192 2757 2768 10.1128/JB.01609-09 20363951
    • (2010) J Bacteriol , vol.192 , pp. 2757-2768
    • Gonzalez, M.D.1    Akbay, E.A.2    Boyd, D.3    Beckwith, J.4
  • 29
    • 0034107581 scopus 로고    scopus 로고
    • Intrinsic instability of the essential cell division protein FtsL of Bacillus subtilis and a role for DivlB protein in FtsL turnover
    • DOI 10.1046/j.1365-2958.2000.01857.x
    • Intrinsic instability of the essential cell division protein FtsL of Bacillus subtilis and a role for DivIB protein in FtsL turnover. RA Daniel, J Errington, Mol Microbiol 2000 36 278 289 10.1046/j.1365-2958.2000.01857.x 10792716 (Pubitemid 30229475)
    • (2000) Molecular Microbiology , vol.36 , Issue.2 , pp. 278-289
    • Daniel, R.A.1    Errington, J.2
  • 30
    • 0036096858 scopus 로고    scopus 로고
    • The Bacillus subtilis cell division proteins FtsL and DivIC are intrinsically unstable and do not interact with one another in the absence of other septasomal components
    • DOI 10.1046/j.1365-2958.2002.02920.x
    • The Bacillus subtilis cell division proteins FtsL and DivIC are intrinsically unstable and do not interact with one another in the absence of other septasomal components. SA Robson, KA Michie, JP Mackay, E Harry, GF King, Mol Microbiol 2002 44 663 674 10.1046/j.1365-2958.2002.02920.x 11994149 (Pubitemid 34526578)
    • (2002) Molecular Microbiology , vol.44 , Issue.3 , pp. 663-674
    • Robson, S.A.1    Michie, K.A.2    Mackay, J.P.3    Harry, E.4    King, G.F.5
  • 31
    • 33749183115 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of FtsL protein and the control of cell division in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2006.05402.x
    • Regulated intramembrane proteolysis of FtsL protein and the control of cell division in Bacillus subtilis. M Bramkamp, L Weston, RA Daniel, J Errington, Mol Microbiol 2006 62 2 580 91 10.1111/j.1365-2958.2006.05402.x 17020588 (Pubitemid 44477243)
    • (2006) Molecular Microbiology , vol.62 , Issue.2 , pp. 580-591
    • Bramkamp, M.1    Weston, L.2    Daniel, R.A.3    Errington, J.4
  • 32
    • 10044241602 scopus 로고    scopus 로고
    • RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences
    • DOI 10.1038/sj.emboj.7600449
    • RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences. Y Akiyama, K Kanehara, K Ito, EMBO J 2004 23 4434 4442 10.1038/sj.emboj.7600449 15496982 (Pubitemid 39601968)
    • (2004) EMBO Journal , vol.23 , Issue.22 , pp. 4434-4442
    • Akiyama, Y.1    Kanehara, K.2    Ito, K.3
  • 33
    • 44349189894 scopus 로고    scopus 로고
    • Substrate recognition and binding by RseP, en Escherichia coli intramembrane protease
    • 10.1074/jbc.M709984200 18268014
    • Substrate recognition and binding by RseP, en Escherichia coli intramembrane protease. K Koide, K Ito, Y Akiyama, J Biol Chem 2008 283 9562 9570 10.1074/jbc.M709984200 18268014
    • (2008) J Biol Chem , vol.283 , pp. 9562-9570
    • Koide, K.1    Ito, K.2    Akiyama, Y.3
  • 34
    • 13144257721 scopus 로고    scopus 로고
    • In vitro reconstitution of a trimeric complex of DivIB, DivIC and FtsL, and their transient co-localization at the division site in Streptococcus pneumoniae
    • DOI 10.1111/j.1365-2958.2004.04408.x
    • In vitro reconstruction of a trimeric complex of DivIB, DivIC and FtsL, and their transcient co-localization at the division site in Streptococcus pneumoniae. M Noirclerc-Savoye, A Le Gouellec, C Morlot, O Dideberg, T Vernet, A Zapun, Mol Microbiol 2005 55 413 424 15659160 (Pubitemid 40179377)
    • (2005) Molecular Microbiology , vol.55 , Issue.2 , pp. 413-424
    • Noirclerc-Savoye, M.1    Le Gouellec, A.2    Morlot, C.3    Dideberg, O.4    Vernet, T.5    Zapun, A.6
  • 35
    • 33750458379 scopus 로고    scopus 로고
    • Multiple interactions between the transmembrane division proteins of Bacillus subtilis and the role of FtsL instability in divisome assembly
    • DOI 10.1128/JB.01031-06
    • Multiple interactions between the transmembrane division proteins of Bacillus subtilis and role of FtsL instability in divisome assembly. RA Daniel, MF Noirot-Gros, P Noirot, J Errington, J Bacteriol 2006 188 7396 7404 10.1128/JB.01031-06 16936019 (Pubitemid 44646238)
    • (2006) Journal of Bacteriology , vol.188 , Issue.21 , pp. 7396-7404
    • Daniel, R.A.1    Noirot-Gros, M.-F.2    Noirot, P.3    Errington, J.4
  • 37
    • 33745878561 scopus 로고    scopus 로고
    • Conformational Transition between Four and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction
    • DOI 10.1016/j.jmb.2006.05.063, PII S0022283606006759
    • Conformational transition between four and five-stranded phenylalanine zippers determined by a local packing interaction. J Liu, Q Zheng, Y Deng, NR Kallenbach, M Lu, J Mol Biol 2006 361 1 168 79 10.1016/j.jmb.2006.05.063 16828114 (Pubitemid 44041450)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.1 , pp. 168-179
    • Liu, J.1    Zheng, Q.2    Deng, Y.3    Kallenbach, N.R.4    Lu, M.5
  • 38
    • 0028303384 scopus 로고
    • A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions
    • A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions. D Krylov, I Mikhailenko, C Vinson, EMBO J 1994 13 12 2849 2861 8026470 (Pubitemid 24191695)
    • (1994) EMBO Journal , vol.13 , Issue.12 , pp. 2849-2861
    • Krylov, D.1    Mikhailenko, I.2    Vinson, C.3
  • 39
    • 0029919832 scopus 로고    scopus 로고
    • + ion pair interactions
    • DOI 10.1021/bi952784c
    • Design of heterotetrameric coiled coils: Evidence of increased stabilization by Glu-Lys ion pair interaction. R Fairman, H Chao, TB Lovoie, JJ Villafranca, GR Matsueda, J Novotny, Biochemistry 1996 35 2824 2829 10.1021/bi952784c 8608117 (Pubitemid 26086790)
    • (1996) Biochemistry , vol.35 , Issue.9 , pp. 2824-2829
    • Fairman, R.1    Chao, H.-G.2    Lavoie, T.B.3    Villafranca, J.J.4    Matsueda, G.R.5    Novotny, J.6
  • 40
    • 0035100686 scopus 로고    scopus 로고
    • Effects of charged amino acids at b and c heptad positions on specificity and stability of four-chain coiled coils
    • DOI 10.1110/ps.41101
    • Effect of changed aminoacid at b and c heptad positions on specificity and stability of four-chain coiled coils. C Vu, J Robblee, KM Werner, R Fairman, Prot Sci 2001 10 631 637 10.1110/ps.41101 (Pubitemid 32221151)
    • (2001) Protein Science , vol.10 , Issue.3 , pp. 631-637
    • Vu, C.1    Robblee, J.2    Werner, K.M.3    Fairman, R.4
  • 41
    • 0035967522 scopus 로고    scopus 로고
    • Buried polar residues in coiled-coil interfaces
    • DOI 10.1021/bi002829w
    • Buried polar residues in coiled-coil interfaces. DL Akey, VN Malashkevich, PS Kim, Biochemistry 2001 40 6352 6360 10.1021/bi002829w 11371197 (Pubitemid 32472724)
    • (2001) Biochemistry , vol.40 , Issue.21 , pp. 6352-6360
    • Akey, D.L.1    Malashkevich, V.N.2    Kim, P.S.3
  • 44
    • 0034029042 scopus 로고    scopus 로고
    • The Bacillus subtilis cell division protein FtsL localizes to sites of septation and interacts with DivIC
    • DOI 10.1046/j.1365-2958.2000.01895.x
    • The Bacillus subtilis cell division protein FtsL localizes to sites of septation and interacts with DivIC. J Sievers, J Errington, Mol Microbiol 2000 36 846 855 10.1046/j.1365-2958.2000.01895.x 10844672 (Pubitemid 30326530)
    • (2000) Molecular Microbiology , vol.36 , Issue.4 , pp. 846-855
    • Sievers, J.1    Errington, J.2
  • 45
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • DOI 10.1016/S0022-2836(02)01281-0
    • Structural characterisation and functional significance of transient protein-protein interactions. IM Nooren, JM Thornton, J Mol Biol 2003 325 5 991 1018 10.1016/S0022-2836(02)01281-0 12527304 (Pubitemid 36263408)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.5 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 46
    • 24044457630 scopus 로고    scopus 로고
    • Amino acid architecture and the distribution of polar atoms on the surfaces of proteins
    • DOI 10.1002/bip.20295
    • Amino acid architecture and the distribution of polar atoms on the surfaces of proteins. HP Shanahan, JM Thornton, Biopolymers 2005 78 6 318 28 10.1002/bip.20295 15898105 (Pubitemid 41225228)
    • (2005) Biopolymers , vol.78 , Issue.6 , pp. 318-328
    • Shanahan, H.P.1    Thornton, J.M.2
  • 47
    • 0035178383 scopus 로고    scopus 로고
    • Protein-protein interfaces: Analysis of amino acid conservation in homodimers
    • 10.1002/1097-0134(20010101)42:1<108: AID-PROT110>3.0.CO;2-O 11093265
    • Protein-protein interfaces: analysis of amino acid conservation in homodimers. WS Valdar, JM Thornton, Proteins 2001 42 1 108 24 10.1002/1097-0134(20010101)42:1<108::AID-PROT110>3.0.CO;2-O 11093265
    • (2001) Proteins , vol.42 , Issue.1 , pp. 108-124
    • Valdar, W.S.1    Thornton, J.M.2
  • 48
    • 78649375524 scopus 로고    scopus 로고
    • Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B
    • 10.1128/JB.00783-10 20870765
    • Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B. SL Rowland, KD worth, SA Robson, C Robichon, J Beckwith, GF King, J Bacteriol 2010 192 6116 6125 10.1128/JB.00783-10 20870765
    • (2010) J Bacteriol , vol.192 , pp. 6116-6125
    • Rowland, S.L.1    Worth, K.D.2    Robson, S.A.3    Robichon, C.4    Beckwith, J.5    King, G.F.6
  • 50
    • 38549141229 scopus 로고    scopus 로고
    • Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre
    • DOI 10.1002/prot.21688
    • Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre. RM Bennett-Lovsey, AD Hebert, MJE Sternberg, LA Kelley, Proteins: structure, function, bioinformatics 2008 70 3 611 625 (Pubitemid 351161924)
    • (2008) Proteins: Structure, Function and Genetics , vol.70 , Issue.3 , pp. 611-625
    • Bennett-Lovsey, R.M.1    Herbert, A.D.2    Sternberg, M.J.E.3    Kelley, L.A.4
  • 51
    • 0030310296 scopus 로고    scopus 로고
    • Fast protein fold recognition via sequence to structure alignment and contact capacity potentials
    • World Scientific Publishing Co 21304719
    • Fast protein fold recognition via sequence to structure alignment and contact capacity potentials. NN Alexandrov, R Nussinov, RM Zimmer, Pacific Symposium on Biocomputing; Singapore World Scientific Publishing Co 1996 53 72 21304719
    • (1996) Pacific Symposium on Biocomputing; Singapore , pp. 53-72
    • Alexandrov, N.N.1    Nussinov, R.2    Zimmer, R.M.3
  • 52
    • 0032438987 scopus 로고    scopus 로고
    • Hidden Markov models for detecting remote protein homologies
    • DOI 10.1093/bioinformatics/14.10.846
    • Hidden Markov models for detecting remote protein homologies. K Karplus, C Barrett, R Hughey, Bioinformatics 1998 14 10 846 56 10.1093/bioinformatics/14. 10.846 9927713 (Pubitemid 29041540)
    • (1998) Bioinformatics , vol.14 , Issue.10 , pp. 846-856
    • Karplus, K.1    Barrett, C.2    Hughey, R.3
  • 53
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • 10.1093/nar/gkn238 18463136
    • The Jpred 3 secondary structure prediction server. C Cole, JD Barber, GJ Barton, Nucleic Acids Res 2008 36 197 W201 10.1093/nar/gkn238 18463136
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 54
    • 0029595442 scopus 로고
    • SOPMA: Significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • SOPMA: Significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. C Geourjon, G Deleage, Comput Appl Biosci 1995 11 6 681 684 8808585 (Pubitemid 26032758)
    • (1995) Computer Applications in the Biosciences , vol.11 , Issue.6 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 55
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • The PSIPRED protein structure prediction server. LJ McGuffin, K Bryson, DT Jones, Bioinformatics 2000 16 4 404 5 10.1093/bioinformatics/16.4.404 10869041 (Pubitemid 30417087)
    • (2000) Bioinformatics , vol.16 , Issue.4 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 56
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • DOI 10.1110/ps.062416606
    • Statistical potential for assessment and prediction of protein structures. MY Shen, A Sali, Protein Sci 2006 15 11 2507 24 10.1110/ps.062416606 17075131 (Pubitemid 44771688)
    • (2006) Protein Science , vol.15 , Issue.11 , pp. 2507-2524
    • Shen, M.-Y.1    Sali, A.2
  • 57
    • 0033562633 scopus 로고    scopus 로고
    • Use of pair potentials across protein interfaces in screening predicted docked complexes
    • DOI 10.1002/(SI CI)1097-0134(19990 515)35:3<364::AID-P ROT11>3.0.CO;2-4
    • Use of Pair Potentials Across Protein Interfaces in Screening Predicted Docked Complexes. G Moont, HA Gabb, MJ Sternberg, Proteins 1999 35 3 364 73 10.1002/(SICI)1097-0134(19990515)35:3<364::AID-PROT11>3.0.CO;2-4 10328272 (Pubitemid 29200974)
    • (1999) Proteins: Structure, Function and Genetics , vol.35 , Issue.3 , pp. 364-373
    • Moont, G.1    Gabb, H.A.2    Sternberg, M.J.E.3
  • 58
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • 10.1038/356083a0 1538787
    • Assessment of protein models with three-dimensional profiles. R Lüthy, JU Bowie, D Eisenberg, Nature 1992 356 6364 83 5 10.1038/356083a0 1538787
    • (1992) Nature , vol.356 , Issue.6364 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 59
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • DOI 10.1006/jmbi.1993.1351
    • Main-chain bond lengths and bond angles in protein structures. RA Laskowski, DS Moss, JM Thornton, J Mol Biol 1993 231 4 1049 67 10.1006/jmbi.1993.1351 8515464 (Pubitemid 23209879)
    • (1993) Journal of Molecular Biology , vol.231 , Issue.4 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 60
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins
    • 10.1093/nar/gkm290 17517781
    • ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. M Wiederstein, MJ Sippl, Nucleic Acids Res 2007 35 407 10 10.1093/nar/gkm290 17517781
    • (2007) Nucleic Acids Res , vol.35 , pp. 23407-23410
    • Wiederstein, M.1    Sippl, M.J.2
  • 61
    • 0031565730 scopus 로고    scopus 로고
    • Modelling protein docking using shape complementarity, electrostatics and biochemical information
    • DOI 10.1006/jmbi.1997.1203
    • Modelling protein docking using shape complementarity, electrostatics and biochemical information. HA Gabb, RM Jackson, MJ Sternberg, J Mol Biol 1997 272 1 106 20 10.1006/jmbi.1997.1203 9299341 (Pubitemid 27395541)
    • (1997) Journal of Molecular Biology , vol.272 , Issue.1 , pp. 106-120
    • Gabb, H.A.1    Jackson, R.M.2    Sternberg, M.J.E.3
  • 63
    • 23144457576 scopus 로고    scopus 로고
    • as and adding missing hydrogens to macromolecules
    • DOI 10.1093/nar/gki464
    • H++: a server for estimating pKas and adding missing hydrogens to macromolecules. JC Gordon, JB Myers, T Folta, V Shoja, LS Heath, A Onufriev, Nucleic Acids Res 2005 33 368 71 10.1093/nar/gki464 15980491 (Pubitemid 44529945)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS.
    • Gordon, J.C.1    Myers, J.B.2    Folta, T.3    Shoja, V.4    Heath, L.S.5    Onufriev, A.6
  • 64
    • 4944226552 scopus 로고    scopus 로고
    • A new hydrogen-bonding potential for the design of protein-RNA interactions predicts specific contacts and discriminates decoys
    • DOI 10.1093/nar/gkh785
    • Computational alanine scanning of protein-protein interfaces. T Kortemme, DE Kim, D Baker, Nucleic Acids Res 2004 32 17 5147 62 10.1093/nar/gkh785 15459285 (Pubitemid 39445502)
    • (2004) Nucleic Acids Research , vol.32 , Issue.17 , pp. 5147-5162
    • Chen, Y.1    Kortemme, T.2    Robertson, T.3    Baker, D.4    Varani, G.5
  • 65
    • 59549088662 scopus 로고    scopus 로고
    • ProtorP: A protein-protein interaction analysis server
    • 19001476
    • ProtorP: a protein-protein interaction analysis server. C Reynolds, D Damerell, S Jones, Bioinformatics 2008 25 3 413 4 19001476
    • (2008) Bioinformatics , vol.25 , Issue.3 , pp. 413-414
    • Reynolds, C.1    Damerell, D.2    Jones, S.3
  • 66
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • DOI 10.1006/jmbi.1994.1334
    • Satisfying hydrogen bonding potential in proteins. IK McDonald, JM Thornton, J Mol Biol 1994 238 5 777 93 10.1006/jmbi.1994.1334 8182748 (Pubitemid 24168633)
    • (1994) Journal of Molecular Biology , vol.238 , Issue.5 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 67
    • 0021112481 scopus 로고
    • Ion-pairs in proteins
    • 10.1016/S0022-2836(83)80079-5 6887253
    • Ion-pairs in proteins. DJ Barlow, JM Thornton, J Mol Biol 1983 168 4 867 885 10.1016/S0022-2836(83)80079-5 6887253
    • (1983) J Mol Biol , vol.168 , Issue.4 , pp. 867-885
    • Barlow, D.J.1    Thornton, J.M.2
  • 69
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • DOI 10.1093/nar/gkh381
    • PDB2PQR: an automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations. TJ Dolinsky, JE Nielsen, JA McCammon, NA Baker, Nucleic Acids Res 2004 32 665 W667 10.1093/nar/gkh381 15215472 (Pubitemid 38997419)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4


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