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A22 Disrupts the Bacterial Actin Cytoskeleton by Directly Binding and Inducing a Low-Affinity State in MreB

https://doi.org/10.1021/bi900014d
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31/31 checkable references clean · checked 2026-08-29

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

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The 31 checked references that resolve
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Actin-like Proteins MreB and Mbl from Bacillus subtilis Are Required for Bipolar Positioning of Replication Origins
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Bacterial DNA segregation by the actin-like MreB protein
resolves10.1111/j.1365-2958.2003.03936.x
MreB, the cell shape‐determining bacterial actin homologue, co‐ordinates cell wall morphogenesis in <i>Caulobacter crescentus</i>
resolves10.1073/pnas.0402638101
An actin-like gene can determine cell polarity in bacteria
resolves10.1186/1471-2121-6-10
Bacillus subtilis actin-like protein MreB influences the positioning of the replication machinery and requires membrane proteins MreC/D and other actin-like proteins for proper localization
resolves10.1271/bbb.66.2658
Novel <i>S</i> -Benzylisothiourea Compound That Induces Spherical Cells in <i>Escherichia coli</i> Probably by Acting on a Rod-shape-determining Protein(s) Other Than Penicillin-binding Protein 2
resolves10.1016/j.cell.2005.01.007
MreB Actin-Mediated Segregation of a Specific Region of a Bacterial Chromosome
resolves10.1073/pnas.0507937102
The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in <i>Caulobacter crescentus</i>
resolves10.1073/pnas.0507708102
Two independent spiral structures control cell shape in <i>Caulobacter</i>
resolves10.1128/JB.187.17.6187-6196.2005
Presence of Multiple Sites Containing Polar Material in Spherical <i>Escherichia coli</i> Cells That Lack MreB
resolves10.1101/gad.366606
Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in <i>Escherichia coli</i>
resolves10.1111/j.1365-2958.2007.05910.x
The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes
resolves10.1271/bbb.60443
Structure-Activity Relationship Study of the Bacterial Actin-Like Protein MreB Inhibitors: Effects of Substitution of Benzyl Group in<i>S</i>-Benzylisothiourea
resolves10.1111/j.1365-2958.2007.05777.x
DNA and origin region segregation are not affected by the transition from rod to sphere after inhibition of <i>Escherichia coli</i> MreB by A22
resolves10.1038/sj.emboj.7601895
The structure of FtsZ filaments in vivo suggests a force‐generating role in cell division
resolves10.1128/JB.00805-07
A Novel Indole Compound That Inhibits <i>Pseudomonas aeruginosa</i> Growth by Targeting MreB Is a Substrate for MexAB-OprM
resolves10.1128/JB.00362-07
Changes in Nucleoid Morphology and Origin Localization upon Inhibition or Alteration of the Actin Homolog, MreB, of<i>Vibrio cholerae</i>
resolves10.1248/bpb.31.1327
Anti-infectious Effect of S-Benzylisothiourea Compound A22, Which Inhibits the Actin-Like Protein, MreB, in Shigella flexneri
resolves10.1128/JB.00207-08
Growth of<i>Escherichia coli</i>: Significance of Peptidoglycan Degradation during Elongation and Septation
resolves10.1021/bi701538e
Polymerization Properties of the <i>Thermotoga maritima</i> Actin MreB:  Roles of Temperature, Nucleotides, and Ions
resolves10.1002/(SICI)1521-3773(19990614)38:12<1784::AID-ANIE1784>3.0.CO;2-Q
Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy
resolves10.1038/35014075
Latrunculin alters the actin-monomer subunit interface to prevent polymerization
The 1 reference without a DOI — listed, not checked
no DOI — not checkedref31/cit31
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