Year |
Citation |
Score |
2024 |
Zhao S, Makarova KS, Zheng W, Zhan L, Wan Q, Liu Y, Gong H, Krupovic M, Lutkenhaus J, Chen X, Koonin EV, Du S. Widespread photosynthesis reaction centre barrel proteins are necessary for haloarchaeal cell division. Nature Microbiology. 9: 712-726. PMID 38443574 DOI: 10.1038/s41564-024-01615-y |
0.576 |
|
2023 |
Zhao S, Makarova KS, Zheng W, Liu Y, Zhan L, Wan Q, Gong H, Krupovic M, Lutkenhaus J, Chen X, Koonin EV, Du S. Widespread PRC barrel proteins play critical roles in archaeal cell division. Biorxiv : the Preprint Server For Biology. PMID 37090588 DOI: 10.1101/2023.03.28.534520 |
0.585 |
|
2022 |
Li Y, Boes A, Cui Y, Zhao S, Liao Q, Gong H, Breukink E, Lutkenhaus J, Terrak M, Du S. Identification of the potential active site of the septal peptidoglycan polymerase FtsW. Plos Genetics. 18: e1009993. PMID 34986161 DOI: 10.1371/journal.pgen.1009993 |
0.582 |
|
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 |
0.592 |
|
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 |
0.615 |
|
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 |
0.61 |
|
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 |
0.592 |
|
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 |
0.634 |
|
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 |
0.681 |
|
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 |
0.653 |
|
2018 |
Du S, Pichoff S, Kruse K, Lutkenhaus J. FtsZ filaments have the opposite kinetic polarity of microtubules. Proceedings of the National Academy of Sciences of the United States of America. PMID 30275322 DOI: 10.1073/Pnas.1811919115 |
0.613 |
|
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 |
0.674 |
|
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 |
0.715 |
|
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 |
0.683 |
|
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 |
0.645 |
|
2017 |
Du S, Lutkenhaus J. Assembly and Activation of the Escherichia coli Divisome. Molecular Microbiology. PMID 28419603 DOI: 10.1111/Mmi.13696 |
0.654 |
|
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 |
0.686 |
|
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 |
0.672 |
|
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 |
0.685 |
|
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 |
0.599 |
|
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 |
0.661 |
|
2012 |
Lutkenhaus J, Pichoff S, Du S. Bacterial cytokinesis: From Z ring to divisome. Cytoskeleton (Hoboken, N.J.). 69: 778-90. PMID 22888013 DOI: 10.1002/Cm.21054 |
0.663 |
|
2012 |
Du S, Lutkenhaus J. MipZ: one for the pole, two for the DNA. Molecular Cell. 46: 239-40. PMID 22578537 DOI: 10.1016/J.Molcel.2012.04.024 |
0.565 |
|
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