The caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factor - Wikidata - awgldk - TriplyDB

The caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factor

The caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factor

http://www.wikidata.org/entity/Q34150858

about

Emergence and modular evolution of a novel motility machinery in bacteria Structural insight into the role of the Ton complex in energy transduction How bacteria maintain location and number of flagella?The YfiBNR signal transduction mechanism reveals novel targets for the evolution of persistent Pseudomonas aeruginosa in cystic fibrosis airways The periplasmic protein TolB as a potential drug target in Pseudomonas aeruginosa DipM is required for peptidoglycan hydrolysis during chloroplast division.From the regulation of peptidoglycan synthesis to bacterial growth and morphology.Thioesterase YbgC affects motility by modulating c-di-GMP levels in Shewanella oneidensis.Polar localization of Escherichia coli chemoreceptors requires an intact Tol-Pal complex Mapping the interactions between Escherichia coli TolQ transmembrane segments.Genes required for growth at high hydrostatic pressure in Escherichia coli K-12 identified by genome-wide screening.Probing the subcellular localization of hopanoid lipids in bacteria using NanoSIMS BB0323 and novel virulence determinant BB0238: Borrelia burgdorferi proteins that interact with and stabilize each other and are critical for infectivity An SMC ATPase mutant disrupts chromosome segregation in Caulobacter.Osmolality-dependent relocation of penicillin-binding protein PBP2 to the division site in Caulobacter crescentus PG1058 Is a Novel Multidomain Protein Component of the Bacterial Type IX Secretion System Cloning, purification and preliminary X-ray crystallographic analysis of the OmpA-like domain of peptidoglycan-associated lipoprotein from Acinetobacter baumannii Proteolysis of BB0323 results in two polypeptides that impact physiologic and infectious phenotypes in Borrelia burgdorferi.How do bacteria localize proteins to the cell pole?Outer-membrane vesicles from Gram-negative bacteria: biogenesis and functions.Advances in understanding E. coli cell fission.From individual cell motility to collective behaviors: insights from a prokaryote, Myxococcus xanthus.Decoding Caulobacter development.Colicin A binds to a novel binding site of TolA in the Escherichia coli periplasm.The physiology of bacterial cell division.Envelope control of outer membrane vesicle production in Gram-negative bacteria.Establishing polar identity in gram-negative rods.An essential tyrosine phosphatase homolog regulates cell separation, outer membrane integrity, and morphology in Caulobacter crescentus LytM factors affect the recruitment of autolysins to the cell division site in Caulobacter crescentus.Outer membrane vesicles in service as protein shuttles, biotic defenders, and immunological doppelgängers Shapeshifting to Survive: Shape Determination and Regulation in Caulobacter crescentus.The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division.Versatile effects of bacterium-released membrane vesicles on mammalian cells and infectious/inflammatory diseases.Electrostatic interactions between the CTX phage minor coat protein and the bacterial host receptor TolA drive the pathogenic conversion of Vibrio cholerae.Visualizing attack of Escherichia coli by the antimicrobial peptide human defensin 5.Increased Outer Membrane Vesicle Formation in a Helicobacter pylori tolB Mutant.Assembly of the Caulobacter cell division machine.Dual orientation of the outer membrane lipoprotein Pal in Escherichia coli.Localization of the outer membrane protein OmpA2 in Caulobacter crescentus depends on the position of the gene in the chromosome.A polarity factor takes the lead in chromosome segregation.

P2860

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P2860

The caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factor

http://www.wikidata.org/entity/Q34150858

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

The caulobacter Tol-Pal comple ...... of a polar localization factor

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The caulobacter Tol-Pal comple ...... of a polar localization factor

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The caulobacter Tol-Pal comple ...... of a polar localization factor

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The caulobacter Tol-Pal comple ...... of a polar localization factor

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The caulobacter Tol-Pal comple ...... of a polar localization factor

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The caulobacter Tol-Pal comple ...... of a polar localization factor

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The caulobacter Tol-Pal comple ...... of a polar localization factor

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The caulobacter Tol-Pal comple ...... of a polar localization factor

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Journal of Bacteriology

P1476

The caulobacter Tol-Pal comple ...... of a polar localization factor

@en

P2093

Kenneth H Downing

http://www.w3.org/2001/XMLSchema#string

Luis R Comolli

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Yi-Chun Yeh

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P2860

Complete genome sequence of Caulobacter crescentus

In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions

A self-associating protein critical for chromosome attachment, division, and polar organization in caulobacter

A polymeric protein anchors the chromosomal origin/ParB complex at a bacterial cell pole

A modular BAM complex in the outer membrane of the alpha-proteobacterium Caulobacter crescentus.

NagA-dependent uptake of N-acetyl-glucosamine and N-acetyl-chitin oligosaccharides across the outer membrane of Caulobacter crescentus.

The structure of FtsZ filaments in vivo suggests a force-generating role in cell division

A protein critical for cell constriction in the Gram-negative bacterium Caulobacter crescentus localizes at the division site through its peptidoglycan-binding LysM domains.

DipM links peptidoglycan remodelling to outer membrane organization in Caulobacter.

Distinct constrictive processes, separated in time and space, divide caulobacter inner and outer membranes.

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4847-4858

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scholarly article

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10.1128/JB.00607-10

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19

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192

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2010-08-06T00:00:00Z

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45537939

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20693330

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2944545

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