Activation of cell division protein FtsZ. Control of switch loop T3 conformation by the nucleotide gamma-phosphate.
about
Site-specific mutations of FtsZ--effects on GTPase and in vitro assemblyFilament structure of bacterial tubulin homologue TubZFilament Formation of the FtsZ/Tubulin-like Protein TubZ from the Bacillus cereus pXO1 PlasmidTubulin homolog TubZ in a phage-encoded partition systemFtsZ Protofilaments Use a Hinge-Opening Mechanism for Constrictive Force GenerationIn the beginning, Escherichia coli assembled the proto-ring: an initial phase of divisionIntrinsic bending and structural rearrangement of tubulin dimer: molecular dynamics simulations and coarse-grained analysis.Cytokinesis in bacteriaThe polymerization mechanism of the bacterial cell division protein FtsZ.A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus.Discovery of anti-TB agents that target the cell-division protein FtsZ.Targeting cell division: small-molecule inhibitors of FtsZ GTPase perturb cytokinetic ring assembly and induce bacterial lethality.Peptide inhibitors of the essential cell division protein FtsA.Conformational changes of FtsZ reported by tryptophan mutants.Domain folding and flexibility of Escherichia coli FtsZ determined by tryptophan site-directed mutagenesis.A Polymerization-Associated Structural Switch in FtsZ That Enables Treadmilling of Model Filaments.Understanding nucleotide-regulated FtsZ filament dynamics and the monomer assembly switch with large-scale atomistic simulations.Mapping flexibility and the assembly switch of cell division protein FtsZ by computational and mutational approaches.Energetics of the cooperative assembly of cell division protein FtsZ and the nucleotide hydrolysis switch.Ring, helix, sphere and cylinder: the basic geometry of prokaryotic cell division.In vitro reconstitution of the initial stages of the bacterial cell division machinery.Immediate GTP hydrolysis upon FtsZ polymerization.Reversible unfolding of FtsZ cell division proteins from archaea and bacteria. Comparison with eukaryotic tubulin folding and assembly.Detection of an intermediate during unfolding of bacterial cell division protein FtsZ: loss of functional properties precedes the global unfolding of FtsZ.Assembly of archaeal cell division protein FtsZ and a GTPase-inactive mutant into double-stranded filaments.Polymerization of nucleotide-free, GDP- and GTP-bound cell division protein FtsZ: GDP makes the difference.FtsZ fiber bundling is triggered by a conformational change in bound GTP.The Tubulin Superfamily in Archaea.Influence of GTP/GDP and magnesium ion on the solvated structure of the protein FtsZ: a molecular dynamics study.
P2860
Q24799397-963918A6-D3F0-4595-A1E0-B3EB7DF7414CQ27665359-475B73A8-68CA-4FBE-846A-1876EAF0CC86Q27670975-8F704493-7CC1-4911-9727-576103260D77Q27678760-17D580A9-96DF-4EC3-BC07-D588A280BF54Q27679200-A0C0BA9E-0FBA-44C9-80EB-A06B2BE52BECQ27694716-26050907-02D9-475F-8A93-5ED830187684Q30483097-17868229-033B-4309-AE5C-14735A8A0048Q33186319-98D76EA0-4415-4A29-B63A-53B022AD10FFQ33955077-4D6D271A-6C64-43AC-AC39-190F9F9060DAQ34188556-01762264-4FC5-4C20-8A6D-20D26C816050Q34576179-1C24DFF7-0797-4481-9CAF-AAAFFD341418Q37416206-545E4C5F-5F42-41F1-A8F1-339194F72804Q40435544-38C690CE-4881-46D9-AA66-F8B0BDC4F473Q41834711-1E1A6717-61E8-4229-A8C4-408A218F38C2Q41976563-C5B1CD5A-5F9C-49DD-BF66-F4C913F79746Q42289849-EB38A7BF-65B0-4D48-B4AA-606F62406477Q42549545-105C7790-18A0-46D5-89B6-9F95AF1FDBBDQ42733822-F30540EC-658D-4D21-9C5D-E16B17E2D807Q43034163-AEA6064A-8669-4F2C-8466-9928C44BA928Q43153843-EFD9847C-B617-48B2-BA92-29248954BD03Q43247333-37CFB47D-4BFC-420B-A61B-0F9104AF0AB9Q43959203-B38A7A84-3A35-47A6-998C-771B619E1F85Q44127976-27DF2D64-92D4-43AB-BC3F-54443C7D2A18Q44370239-2D88435F-3C7B-457C-BF9B-B82A1575209BQ44478836-7922ACD9-A533-406E-B79E-409BAC1FB66DQ44957915-A25E5C89-4C82-4193-9AA9-33EDCBF3C986Q45029757-4503C3FE-3E38-4352-B61C-4D797F2A0616Q46366579-EBC950A4-EB63-4546-9E49-1D678DC80A15Q46674009-C394DF6F-19BE-4EFC-85D8-04D4154428AA
P2860
Activation of cell division protein FtsZ. Control of switch loop T3 conformation by the nucleotide gamma-phosphate.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Activation of cell division pr ...... he nucleotide gamma-phosphate.
@ast
Activation of cell division pr ...... he nucleotide gamma-phosphate.
@en
type
label
Activation of cell division pr ...... he nucleotide gamma-phosphate.
@ast
Activation of cell division pr ...... he nucleotide gamma-phosphate.
@en
prefLabel
Activation of cell division pr ...... he nucleotide gamma-phosphate.
@ast
Activation of cell division pr ...... he nucleotide gamma-phosphate.
@en
P2093
P2860
P356
P1476
Activation of cell division pr ...... he nucleotide gamma-phosphate.
@en
P2093
P2860
P304
17307-17315
P356
10.1074/JBC.M010920200
P407
P577
2001-01-25T00:00:00Z