Conserved glycines in the C terminus of MinC proteins are implicated in their functionality as cell division inhibitors. - Wikidata - wikimedia - TriplyDB

Conserved glycines in the C terminus of MinC proteins are implicated in their functionality as cell division inhibitors.

Conserved glycines in the C terminus of MinC proteins are implicated in their functionality as cell division inhibitors.

http://www.wikidata.org/entity/Q37425484

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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 MinC Crystal structure of the N-terminal domain of MinC dimerized via domain swapping MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component.Maintenance of the cell morphology by MinC in Helicobacter pylori.The N terminus of MinD contains determinants which affect its dynamic localization and enzymatic activity.An Escherichia coli expression model reveals the species-specific function of FtsA from Neisseria gonorrhoeae in cell division.MinC/MinD copolymers are not required for Min function.Robust Min-system oscillation in the presence of internal photosynthetic membranes in cyanobacteria.The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide.

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Conserved glycines in the C terminus of MinC proteins are implicated in their functionality as cell division inhibitors.

http://www.wikidata.org/entity/Q37425484

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on May 2004

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vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

Conserved glycines in the C te ...... y as cell division inhibitors.

@en

Conserved glycines in the C te ...... y as cell division inhibitors.

@nl

type

label

Conserved glycines in the C te ...... y as cell division inhibitors.

@en

Conserved glycines in the C te ...... y as cell division inhibitors.

@nl

prefLabel

Conserved glycines in the C te ...... y as cell division inhibitors.

@en

Conserved glycines in the C te ...... y as cell division inhibitors.

@nl

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P356

JB.186.9.2841-2855.2004

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Journal of Bacteriology

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Conserved glycines in the C te ...... y as cell division inhibitors.

@en

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Dillon JR

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Douglas H

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Fan D

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Greco V

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Ramirez-Arcos S

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Szeto J

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Tessier D

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Wang J

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P2860

Recruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE.

Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles

Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus.

Crystal structure of the bacterial cell division inhibitor MinC.

Contribution of glycine 146 to a conserved folding module affecting stability and refolding of human glutathione transferase p1-1

Anatomy of hot spots in protein interfaces

Specific amino acid substitutions determine the differential contribution of the N- and C-terminal domains of insulin-like growth factor (IGF)-binding protein-5 in binding IGF-I.

Gonococcal MinD affects cell division in Neisseria gonorrhoeae and Escherichia coli and exhibits a novel self-interaction.

Stability of the Escherichia coli division inhibitor protein MinC requires determinants in the carboxy-terminal region of the protein.

The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization.

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2841-2855

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10.1128/JB.186.9.2841-2855.2004

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2004-05-01T00:00:00Z

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387809

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