Appropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinE
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Membrane-bound MinDE complex acts as a toggle switch that drives Min oscillation coupled to cytoplasmic depletion of MinD.Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinCThe Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate CytokinesisThe N-terminal amphipathic helix of the topological specificity factor MinE is associated with shaping membrane curvatureRegulation of symmetric bacterial cell division by MinE: What is the role of conformational dynamics?Self-assembly of MinE on the membrane underlies formation of the MinE ring to sustain function of the Escherichia coli Min system.Mechanism of the asymmetric activation of the MinD ATPase by MinE.Spatial control of the cell division site by the Min system in Escherichia coli.Toward Spatially Regulated Division of Protocells: Insights into the E. coli Min System from in Vitro Studies.FtsZ-ring Architecture and Its Control by MinCD.Reconstitution of Protein Dynamics Involved in Bacterial Cell Division.MinC/MinD copolymers are not required for Min function.Mechanistic insights of the Min oscillator via cell-free reconstitution and imaging.Dissecting the role of conformational change and membrane binding by the bacterial cell division regulator MinE in the stimulation of MinD ATPase activity.MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation.MinE conformational switching confers robustness on self-organized Min protein patterns.The Min-protein oscillations in Escherichia coli: an example of self-organized cellular protein waves.
P2860
Q27316432-A5DDA144-3B54-45F7-9148-1050842B3C0BQ27666570-81BCC5F2-8AE0-473B-BB67-5CEADAAC5983Q27671525-57B12D38-5277-4A03-865C-B8F75C6CC3DBQ28478761-2054A310-C0DD-4388-9F9B-5CB030E6664AQ30402057-3C41C682-623E-4F8D-9EB3-49FEA6C678DEQ33985211-A0BDFCCE-009C-4826-A9C8-F86E40537399Q36038208-991E2AE9-53AF-4C86-9EEB-4157764A9AD6Q38097923-7C403078-DB5B-4A2E-9E18-03511F1C7684Q38290250-A3830E92-FB9C-48EC-9482-16758DFB29DAQ38788436-C445C942-164A-473D-9DE7-A2470EB498F9Q39303537-67B47367-F1E9-4945-9F01-8944EB187C50Q41773713-3E75F8C1-95F0-4929-BE7A-F5551794E6BCQ47348572-6BB0DFDA-1480-4AEE-AD6E-CCC894745A4DQ47608185-22A70C13-483F-4AF9-9496-5701B060D70CQ49226559-9D19D9F0-E5E6-47BD-A302-BC1FD31E116BQ52318676-007DBD16-C0B4-454F-A63D-52758D659DF5Q52720518-03452853-7528-44DB-8A9F-805F57CCFDD7
P2860
Appropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinE
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2010 nî lūn-bûn
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2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
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2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
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Appropriation of the MinD prot ...... l cell division regulator MinE
@ast
Appropriation of the MinD prot ...... l cell division regulator MinE
@en
Appropriation of the MinD prot ...... l cell division regulator MinE
@nl
type
label
Appropriation of the MinD prot ...... l cell division regulator MinE
@ast
Appropriation of the MinD prot ...... l cell division regulator MinE
@en
Appropriation of the MinD prot ...... l cell division regulator MinE
@nl
prefLabel
Appropriation of the MinD prot ...... l cell division regulator MinE
@ast
Appropriation of the MinD prot ...... l cell division regulator MinE
@en
Appropriation of the MinD prot ...... l cell division regulator MinE
@nl
P2093
P2860
P356
P1476
Appropriation of the MinD prot ...... l cell division regulator MinE
@en
P2093
Ali Al-Baldawi
Chris T Hart
Fatima Hafizi
Jo-Anne R Dillon
Natalie K Goto
Nina Chang
Patrik Lundström
Saud H Ayed
Thierry Ducat
P2860
P304
18416-18421
P356
10.1073/PNAS.1007141107
P407
P577
2010-10-11T00:00:00Z