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HaloTag technology: a versatile platform for biomedical applicationsStructural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ringBacterial actin and tubulin homologs in cell growth and divisionGenetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilisA flexible C-terminal linker is required for proper FtsZ assembly in vitro and cytokinetic ring formation in vivoMapZ marks the division sites and positions FtsZ rings in Streptococcus pneumoniae.Oligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA.Characterization of the FtsZ C-Terminal Variable (CTV) Region in Z-Ring Assembly and Interaction with the Z-Ring Stabilizer ZapD in E. coli CytokinesisStructural and Functional Analyses Reveal Insights into the Molecular Properties of the Escherichia coli Z Ring Stabilizing Protein, ZapC.A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein.Splitsville: structural and functional insights into the dynamic bacterial Z ring.FtsZ ring stability: of bundles, tubules, crosslinks, and curves.Intrinsic structural disorder in cytoskeletal proteins.Cell division in CorynebacterineaeThe keepers of the ring: regulators of FtsZ assembly.Current Experimental Methods for Characterizing Protein-Protein Interactions.FtsZ polymerization assays: simple protocols and considerations.Structure of the Z Ring-associated Protein, ZapD, Bound to the C-terminal Domain of the Tubulin-like Protein, FtsZ, Suggests Mechanism of Z Ring Stabilization through FtsZ Cross-linking.Antibacterial activity of alkyl gallates is a combination of direct targeting of FtsZ and permeabilization of bacterial membranes.The essential role of SepF in mycobacterial division.A function of DivIVA in Listeria monocytogenes division site selection.Cytoskeletal Proteins in Caulobacter crescentus: Spatial Orchestrators of Cell Cycle Progression, Development, and Cell Shape.Free SepF interferes with recruitment of late cell division proteins.
P2860
Q26997400-059865E4-61EB-478C-8869-E6F4FB503E75Q27680581-F82C9682-8450-4005-9492-2C0D7AE6E5FCQ28083563-18A67AEC-3172-4652-8510-6F7DD7C1DB9AQ28486034-72BBDAC2-4833-47DD-84A6-C71FCD16A3C5Q28679156-9BC61EC0-05FE-4C2E-B0DA-6640E6DAFCE6Q30608668-EB7F40EA-94CF-41D9-91FD-35578EB1396BQ35190227-E013E636-AD63-4465-9263-9499E49860FCQ35992216-4F2DAABF-74F8-4AB8-A3EC-4E4164583D31Q36518380-23DDB99E-67A2-4539-8DE4-ED56FE1712CFQ36579510-17EBFA98-5AC2-4CA3-9254-54B1BD2281B4Q37623180-55604975-4D03-49E6-A835-D4138C34E928Q38086221-FD4DCC25-6BCA-4EAD-B4AB-6B4C69851666Q38114023-B57C1273-4B52-4955-9F2C-28EA90E02EB8Q38208303-596964FC-1278-49F7-9BAA-78AD1175F776Q38588069-FD350101-3821-4CA9-8541-85C3D372A297Q38728681-B5D17DF7-7279-45F4-A549-E8D5FE9BB866Q38823070-0846DBA9-FDFC-4953-93A7-6F72A9DE4CD4Q39013722-31C8CE89-805C-4571-B78A-4915F67E176FQ40061326-493E43B4-BD42-461D-B4C1-C57CE54A1CA1Q40974615-3E2B7D1C-24E2-4252-84AB-3F3C44E6EDF1Q44025615-D2175AFB-7051-41DE-9A1B-42484F39E54DQ47109723-85645C49-E531-4602-B3F5-CE40E21DD7D9Q47155522-68F09B18-4DAB-477C-A3C7-2BE83E660C15
P2860
description
2012 nî lūn-bûn
@nan
2012 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
@ast
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
@en
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
@nl
type
label
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
@ast
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
@en
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
@nl
prefLabel
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
@ast
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
@en
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
@nl
P2093
P2860
P1433
P1476
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
@en
P2093
Dirk-Jan Scheffers
Egbert J Boekema
Laura S van Bezouwen
Neeraj Kumar
Sebastiaan P van Kessel
P2860
P304
P356
10.1371/JOURNAL.PONE.0043293
P407
P577
2012-08-13T00:00:00Z