The dimerization function of MinC resides in a structurally autonomous C-terminal domain
about
Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinERecruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE.Collaborative protein filamentsCrystal structure of the N-terminal domain of MinC dimerized via domain swappingCell age dependent concentration of Escherichia coli divisome proteins analyzed with ImageJ and ObjectJFtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.Cytokinesis in bacteriaMinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component.ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coliMin protein patterns emerge from rapid rebinding and membrane interaction of MinE.SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli.Location of dual sites in E. coli FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker.The C-terminal domain of MinC inhibits assembly of the Z ring in Escherichia coli.The switch I and II regions of MinD are required for binding and activating MinC.MinD and MinE interact with anionic phospholipids and regulate division plane formation in Escherichia coli.Conserved glycines in the C terminus of MinC proteins are implicated in their functionality as cell division inhibitors.Reconstitution of Protein Dynamics Involved in Bacterial Cell Division.Targeting of (D)MinC/MinD and (D)MinC/DicB complexes to septal rings in Escherichia coli suggests a multistep mechanism for MinC-mediated destruction of nascent FtsZ rings.ATP-dependent interactions between Escherichia coli Min proteins and the phospholipid membrane in vitro.MinC/MinD copolymers are not required for Min function.MinCD cell division proteins form alternating copolymeric cytomotive filaments.Propagation of MinCDE waves on free-standing membranes.
P2860
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P2860
The dimerization function of MinC resides in a structurally autonomous C-terminal domain
description
2001 nî lūn-bûn
@nan
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2001年の論文
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2001年論文
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2001年論文
@zh-hant
2001年論文
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2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
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name
The dimerization function of MinC resides in a structurally autonomous C-terminal domain
@ast
The dimerization function of MinC resides in a structurally autonomous C-terminal domain
@en
type
label
The dimerization function of MinC resides in a structurally autonomous C-terminal domain
@ast
The dimerization function of MinC resides in a structurally autonomous C-terminal domain
@en
prefLabel
The dimerization function of MinC resides in a structurally autonomous C-terminal domain
@ast
The dimerization function of MinC resides in a structurally autonomous C-terminal domain
@en
P2860
P1476
The dimerization function of MinC resides in a structurally autonomous C-terminal domain
@en
P2093
P2860
P304
P356
10.1128/JB.183.22.6684-6687.2001
P407
P577
2001-11-01T00:00:00Z