| Year |
Citation |
Score |
| 2021 |
Park KT, Pichoff S, Du S, Lutkenhaus J. FtsA acts through FtsW to promote cell wall synthesis during cell division in . Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34453005 DOI: 10.1073/pnas.2107210118 |
0.579 |
|
| 2021 |
Li Y, Gong H, Zhan R, Ouyang S, Park KT, Lutkenhaus J, Du S. Genetic analysis of the septal peptidoglycan synthase FtsWI complex supports a conserved activation mechanism for SEDS-bPBP complexes. Plos Genetics. 17: e1009366. PMID 33857142 DOI: 10.1371/journal.pgen.1009366 |
0.59 |
|
| 2020 |
Park KT, Du S, Lutkenhaus J. Essential Role for FtsL in Activation of Septal Peptidoglycan Synthesis. Mbio. 11. PMID 33293384 DOI: 10.1128/mBio.03012-20 |
0.567 |
|
| 2020 |
Alcorlo M, Straume D, Lutkenhaus J, Håvarstein LS, Hermoso JA. Structural Characterization of the Essential Cell Division Protein FtsE and Its Interaction with FtsX in Streptococcus pneumoniae. Mbio. 11. PMID 32873757 DOI: 10.1128/Mbio.01488-20 |
0.447 |
|
| 2020 |
Du S, Pichoff S, Lutkenhaus J. Roles of ATP Hydrolysis by FtsEX and Interaction with FtsA in Regulation of Septal Peptidoglycan Synthesis and Hydrolysis. Mbio. 11. PMID 32636250 DOI: 10.1128/Mbio.01247-20 |
0.337 |
|
| 2019 |
Pichoff S, Du S, Lutkenhaus J. Roles of FtsEX in cell division. Research in Microbiology. PMID 31376483 DOI: 10.1016/J.Resmic.2019.07.003 |
0.31 |
|
| 2019 |
Du S, Henke W, Pichoff S, Lutkenhaus J. How FtsEX localizes to the Z ring and interacts with FtsA to regulate cell division. Molecular Microbiology. PMID 31175681 DOI: 10.1111/Mmi.14324 |
0.369 |
|
| 2019 |
Du S, Lutkenhaus J. At the Heart of Bacterial Cytokinesis: The Z Ring. Trends in Microbiology. PMID 31171437 DOI: 10.1016/J.Tim.2019.04.011 |
0.31 |
|
| 2018 |
Pichoff S, Du S, Lutkenhaus J. Disruption of divisome assembly rescued by FtsN-FtsA interaction in . Proceedings of the National Academy of Sciences of the United States of America. PMID 29967164 DOI: 10.1073/Pnas.1806450115 |
0.359 |
|
| 2018 |
Park KT, Dajkovic A, Wissel M, Du S, Lutkenhaus J. MinC and FtsZ mutant analysis provides insight into MinC/MinD-mediated Z Ring disassembly. The Journal of Biological Chemistry. PMID 29414773 DOI: 10.1074/Jbc.M117.815894 |
0.577 |
|
| 2017 |
Park KT, Villar MT, Artigues A, Lutkenhaus J. MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation. Proceedings of the National Academy of Sciences of the United States of America. PMID 28652337 DOI: 10.1073/Pnas.1707385114 |
0.581 |
|
| 2017 |
Lutkenhaus J, Du S. E. coli Cell Cycle Machinery. Sub-Cellular Biochemistry. 84: 27-65. PMID 28500522 DOI: 10.1007/978-3-319-53047-5_2 |
0.419 |
|
| 2017 |
Du S, Lutkenhaus J. The N-succinyl-L, L-diaminopimelic acid desuccinylase DapE acts through ZapB to promote septum formation in Escherichia coli. Molecular Microbiology. PMID 28470834 DOI: 10.1111/Mmi.13703 |
0.312 |
|
| 2017 |
Du S, Lutkenhaus J. Assembly and Activation of the Escherichia coli Divisome. Molecular Microbiology. PMID 28419603 DOI: 10.1111/Mmi.13696 |
0.328 |
|
| 2016 |
Du S, Pichoff S, Lutkenhaus J. FtsEX acts on FtsA to regulate divisome assembly and activity. Proceedings of the National Academy of Sciences of the United States of America. PMID 27503875 DOI: 10.1073/Pnas.1606656113 |
0.437 |
|
| 2015 |
Park KT, Du S, Lutkenhaus J. MinC/MinD copolymers are not required for Min function. Molecular Microbiology. PMID 26268537 DOI: 10.1111/Mmi.13164 |
0.61 |
|
| 2015 |
Pichoff S, Du S, Lutkenhaus J. The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring. Molecular Microbiology. 95: 971-87. PMID 25496259 DOI: 10.1111/Mmi.12907 |
0.429 |
|
| 2015 |
Du S, Park KT, Lutkenhaus J. Oligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA. Molecular Microbiology. 95: 173-88. PMID 25382687 DOI: 10.1111/Mmi.12854 |
0.538 |
|
| 2014 |
Du S, Lutkenhaus J. SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD. Plos Genetics. 10: e1004460. PMID 25078077 DOI: 10.1371/Journal.Pgen.1004460 |
0.482 |
|
| 2012 |
Park KT, Wu W, Lovell S, Lutkenhaus J. Mechanism of the asymmetric activation of the MinD ATPase by MinE. Molecular Microbiology. 85: 271-81. PMID 22651575 DOI: 10.1111/J.1365-2958.2012.08110.X |
0.562 |
|
| 2012 |
Pichoff S, Shen B, Sullivan B, Lutkenhaus J. FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins. Molecular Microbiology. 83: 151-67. PMID 22111832 DOI: 10.1111/J.1365-2958.2011.07923.X |
0.345 |
|
| 2011 |
Park KT, Wu W, Battaile KP, Lovell S, Holyoak T, Lutkenhaus J. The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis. Cell. 146: 396-407. PMID 21816275 DOI: 10.1016/J.Cell.2011.06.042 |
0.591 |
|
| 2011 |
Wu W, Park KT, Holyoak T, Lutkenhaus J. Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC. Molecular Microbiology. 79: 1515-28. PMID 21231967 DOI: 10.1111/J.1365-2958.2010.07536.X |
0.546 |
|
| 2011 |
Shen B, Lutkenhaus J. Differences in MinC/MinD sensitivity between polar and internal Z rings in Escherichia coli. Journal of Bacteriology. 193: 367-76. PMID 21097625 DOI: 10.1128/Jb.01095-10 |
0.317 |
|
| 2010 |
Dajkovic A, Pichoff S, Lutkenhaus J, Wirtz D. Cross-linking FtsZ polymers into coherent Z rings. Molecular Microbiology. 78: 651-68. PMID 20969647 DOI: 10.1111/J.1365-2958.2010.07352.X |
0.337 |
|
| 2010 |
Shen B, Lutkenhaus J. Examination of the interaction between FtsZ and MinCN in E. coli suggests how MinC disrupts Z rings. Molecular Microbiology. 75: 1285-98. PMID 20132438 DOI: 10.1111/J.1365-2958.2010.07055.X |
0.364 |
|
| 2010 |
Dajkovic A, Pichoff S, Lutkenhaus J, Wirtz D. ZAPA Controls the Scaffolding Function of FtsZ Through Three Synergistic Activities Biophysical Journal. 98: 9a. DOI: 10.1016/J.Bpj.2009.12.054 |
0.38 |
|
| 2009 |
Lutkenhaus J. FtsN--trigger for septation. Journal of Bacteriology. 191: 7381-2. PMID 19854895 DOI: 10.1128/Jb.01100-09 |
0.396 |
|
| 2009 |
Shen B, Lutkenhaus J. The conserved C-terminal tail of FtsZ is required for the septal localization and division inhibitory activity of MinC(C)/MinD. Molecular Microbiology. 72: 410-24. PMID 19415799 DOI: 10.1111/J.1365-2958.2009.06651.X |
0.417 |
|
| 2008 |
Dajkovic A, Lan G, Sun SX, Wirtz D, Lutkenhaus J. MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ. Current Biology : Cb. 18: 235-44. PMID 18291654 DOI: 10.1016/J.Cub.2008.01.042 |
0.367 |
|
| 2008 |
Dajkovic A, Mukherjee A, Lutkenhaus J. Investigation of regulation of FtsZ assembly by SulA and development of a model for FtsZ polymerization. Journal of Bacteriology. 190: 2513-26. PMID 18245292 DOI: 10.1128/Jb.01612-07 |
0.356 |
|
| 2007 |
Pichoff S, Lutkenhaus J. Identification of a region of FtsA required for interaction with FtsZ. Molecular Microbiology. 64: 1129-38. PMID 17501933 DOI: 10.1111/J.1365-2958.2007.05735.X |
0.431 |
|
| 2005 |
Zhou H, Lutkenhaus J. MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component. Journal of Bacteriology. 187: 2846-57. PMID 15805531 DOI: 10.1128/Jb.187.8.2846-2857.2005 |
0.431 |
|
| 2005 |
Pichoff S, Lutkenhaus J. Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Molecular Microbiology. 55: 1722-34. PMID 15752196 DOI: 10.1111/J.1365-2958.2005.04522.X |
0.373 |
|
| 2005 |
Zhou H, Schulze R, Cox S, Saez C, Hu Z, Lutkenhaus J. Analysis of MinD mutations reveals residues required for MinE stimulation of the MinD ATPase and residues required for MinC interaction. Journal of Bacteriology. 187: 629-38. PMID 15629934 DOI: 10.1128/Jb.187.2.629-638.2005 |
0.489 |
|
| 2004 |
Zhou H, Lutkenhaus J. The switch I and II regions of MinD are required for binding and activating MinC. Journal of Bacteriology. 186: 1546-55. PMID 14973039 DOI: 10.1128/Jb.186.5.1546-1555.2004 |
0.422 |
|
| 2003 |
Zhou H, Lutkenhaus J. Membrane binding by MinD involves insertion of hydrophobic residues within the C-terminal amphipathic helix into the bilayer. Journal of Bacteriology. 185: 4326-35. PMID 12867440 DOI: 10.1128/Jb.185.15.4326-4335.2003 |
0.41 |
|
| 2003 |
Lutkenhaus J, Sundaramoorthy M. MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation. Molecular Microbiology. 48: 295-303. PMID 12675792 DOI: 10.1046/J.1365-2958.2003.03427.X |
0.475 |
|
| 2003 |
Hu Z, Lutkenhaus J. A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum. Molecular Microbiology. 47: 345-55. PMID 12519187 DOI: 10.1046/J.1365-2958.2003.03321.X |
0.409 |
|
| 2003 |
Hu Z, Saez C, Lutkenhaus J. Recruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE. Journal of Bacteriology. 185: 196-203. PMID 12486056 DOI: 10.1128/Jb.185.1.196-203.2003 |
0.429 |
|
| 2002 |
Hu Z, Gogol EP, Lutkenhaus J. Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE. Proceedings of the National Academy of Sciences of the United States of America. 99: 6761-6. PMID 11983867 DOI: 10.1073/Pnas.102059099 |
0.331 |
|
| 2002 |
Pichoff S, Lutkenhaus J. Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli. The Embo Journal. 21: 685-93. PMID 11847116 DOI: 10.1093/Emboj/21.4.685 |
0.36 |
|
| 2001 |
Mukherjee A, Saez C, Lutkenhaus J. Assembly of an FtsZ mutant deficient in GTPase activity has implications for FtsZ assembly and the role of the Z ring in cell division. Journal of Bacteriology. 183: 7190-7. PMID 11717278 DOI: 10.1128/Jb.183.24.7190-7197.2001 |
0.379 |
|
| 2000 |
Hu Z, Lutkenhaus J. Analysis of MinC reveals two independent domains involved in interaction with MinD and FtsZ. Journal of Bacteriology. 182: 3965-71. PMID 10869074 DOI: 10.1128/Jb.182.14.3965-3971.2000 |
0.314 |
|
| 1999 |
Hu Z, Mukherjee A, Pichoff S, Lutkenhaus J. The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization. Proceedings of the National Academy of Sciences of the United States of America. 96: 14819-24. PMID 10611296 DOI: 10.1073/Pnas.96.26.14819 |
0.365 |
|
| 1999 |
Hu Z, Lutkenhaus J. Topological regulation of cell division in Escherichia coli involves rapid pole to pole oscillation of the division inhibitor MinC under the control of MinD and MinE. Molecular Microbiology. 34: 82-90. PMID 10540287 DOI: 10.1046/J.1365-2958.1999.01575.X |
0.402 |
|
| 1999 |
Liu Z, Mukherjee A, Lutkenhaus J. Recruitment of ZipA to the division site by interaction with FtsZ. Molecular Microbiology. 31: 1853-61. PMID 10209756 DOI: 10.1046/J.1365-2958.1999.01322.X |
0.474 |
|
| 1998 |
Lutkenhaus J. Organelle division: from coli to chloroplasts. Current Biology : Cb. 8: R619-21. PMID 9742393 DOI: 10.1016/S0960-9822(98)70391-4 |
0.301 |
|
| 1998 |
Mukherjee A, Cao C, Lutkenhaus J. Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 95: 2885-90. PMID 9501185 DOI: 10.1073/Pnas.95.6.2885 |
0.32 |
|
| 1998 |
Mukherjee A, Lutkenhaus J. Dynamic assembly of FtsZ regulated by GTP hydrolysis. The Embo Journal. 17: 462-9. PMID 9430638 DOI: 10.1093/Emboj/17.2.462 |
0.315 |
|
| 1997 |
Wang X, Huang J, Mukherjee A, Cao C, Lutkenhaus J. Analysis of the interaction of FtsZ with itself, GTP, and FtsA. Journal of Bacteriology. 179: 5551-9. PMID 9287012 DOI: 10.1128/Jb.179.17.5551-5559.1997 |
0.362 |
|
| 1997 |
Addinall SG, Cao C, Lutkenhaus J. FtsN, a late recruit to the septum in Escherichia coli. Molecular Microbiology. 25: 303-9. PMID 9282742 DOI: 10.1046/J.1365-2958.1997.4641833.X |
0.306 |
|
| 1996 |
Addinall SG, Lutkenhaus J. FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli. Molecular Microbiology. 22: 231-7. PMID 8930908 DOI: 10.1046/J.1365-2958.1996.00100.X |
0.369 |
|
| 1996 |
Wang X, Lutkenhaus J. FtsZ ring: the eubacterial division apparatus conserved in archaebacteria. Molecular Microbiology. 21: 313-9. PMID 8858586 DOI: 10.1046/J.1365-2958.1996.6421360.X |
0.311 |
|
| 1996 |
Addinall SG, Bi E, Lutkenhaus J. FtsZ ring formation in fts mutants. Journal of Bacteriology. 178: 3877-84. PMID 8682793 DOI: 10.1128/Jb.178.13.3877-3884.1996 |
0.311 |
|
| 1996 |
Dai K, Xu Y, Lutkenhaus J. Topological characterization of the essential Escherichia coli cell division protein FtsN. Journal of Bacteriology. 178: 1328-34. PMID 8631709 DOI: 10.1128/Jb.178.5.1328-1334.1996 |
0.3 |
|
| 1994 |
Dai K, Mukherjee A, Xu Y, Lutkenhaus J. Mutations in ftsZ that confer resistance to SulA affect the interaction of FtsZ with GTP. Journal of Bacteriology. 176: 130-6. PMID 8282688 DOI: 10.1128/Jb.176.1.130-136.1994 |
0.366 |
|
| 1994 |
Mukherjee A, Lutkenhaus J. Guanine nucleotide-dependent assembly of FtsZ into filaments. Journal of Bacteriology. 176: 2754-8. PMID 8169229 DOI: 10.1128/Jb.176.9.2754-2758.1994 |
0.399 |
|
| 1993 |
Mukherjee A, Dai K, Lutkenhaus J. Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein. Proceedings of the National Academy of Sciences of the United States of America. 90: 1053-7. PMID 8430073 DOI: 10.1073/Pnas.90.3.1053 |
0.396 |
|
| 1993 |
Wang X, Lutkenhaus J. The FtsZ protein of Bacillus subtilis is localized at the division site and has GTPase activity that is dependent upon FtsZ concentration. Molecular Microbiology. 9: 435-42. PMID 8412693 DOI: 10.1111/J.1365-2958.1993.Tb01705.X |
0.4 |
|
| 1993 |
Lutkenhaus J. FtsZ ring in bacterial cytokinesis. Molecular Microbiology. 9: 403-9. PMID 8412689 DOI: 10.1111/J.1365-2958.1993.Tb01701.X |
0.362 |
|
| 1991 |
Bi E, Lutkenhaus J. FtsZ ring structure associated with division in Escherichia coli Nature. 354: 161-164. PMID 1944597 DOI: 10.1038/354161A0 |
0.309 |
|
| Show low-probability matches. |