Solution structure of ZipA, a crucial component of Escherichia coli cell division
about
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I databaseRecent contributions of structure-based drug design to the development of antibacterial compounds.FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.Cytokinesis in bacteriaThe transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ringPremature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli.Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stabilityZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coliStructural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain.Discovery of anti-TB agents that target the cell-division protein FtsZ.Domain architecture and structure of the bacterial cell division protein DivIBIdentification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymersExpression, purification and crystallization of the cell-division protein YgfE from Escherichia coli.Dynamic interaction of the Escherichia coli cell division ZipA and FtsZ proteins evidenced in nanodiscs.Targeting FtsZ for antibacterial therapy: a promising avenue.Therapeutic potential of FtsZ inhibition: a patent perspective.FtsZ ring stability: of bundles, tubules, crosslinks, and curves.The keepers of the ring: regulators of FtsZ assembly.FtsZ from divergent foreign bacteria can function for cell division in Escherichia coliThe essential role of SepF in mycobacterial division.FtsZ condensates: an in vitro electron microscopy study.Structure-based design of carboxybiphenylindole inhibitors of the ZipA-FtsZ interaction.Suppression of a Thermosensitive zipA Cell Division Mutant by Altering Amino Acid Metabolism.Monitoring structural changes in intrinsically disordered proteins using QCM-D: application to the bacterial cell division protein ZipA.Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly.Escherichia coli ZipA Organizes FtsZ Polymers into Dynamic Ring-Like Protofilament Structures.
P2860
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P2860
Solution structure of ZipA, a crucial component of Escherichia coli cell division
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2000 nî lūn-bûn
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2000 թվականի օգոստոսին հրատարակված գիտական հոդված
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Solution structure of ZipA, a crucial component of Escherichia coli cell division
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Solution structure of ZipA, a crucial component of Escherichia coli cell division
@en
Solution structure of ZipA, a crucial component of Escherichia coli cell division
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type
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Solution structure of ZipA, a crucial component of Escherichia coli cell division
@ast
Solution structure of ZipA, a crucial component of Escherichia coli cell division
@en
Solution structure of ZipA, a crucial component of Escherichia coli cell division
@nl
prefLabel
Solution structure of ZipA, a crucial component of Escherichia coli cell division
@ast
Solution structure of ZipA, a crucial component of Escherichia coli cell division
@en
Solution structure of ZipA, a crucial component of Escherichia coli cell division
@nl
P2093
P356
P1433
P1476
Solution structure of ZipA, a crucial component of Escherichia coli cell division
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P2093
P304
P356
10.1021/BI0009690
P407
P577
2000-08-08T00:00:00Z