Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization. - Test2 - elhamkhani - TriplyDB

Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization.

Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization.

http://www.wikidata.org/entity/Q24632784

about

BacM, an N-terminally processed bactofilin of Myxococcus xanthus, is crucial for proper cell shape.Colonize, evade, flourish: how glyco-conjugates promote virulence of Helicobacter pylori Molecular mechanisms for the evolution of bacterial morphologies and growth modes Disruption of TgPHIL1 alters specific parameters of Toxoplasma gondii motility measured in a quantitative, three-dimensional live motility assay Deformation of filamentous Escherichia coli cells in a microfluidic device: a new technique to study cell mechanics Multiple peptidoglycan modification networks modulate Helicobacter pylori's cell shape, motility, and colonization potential Bacillus subtilis Bactofilins Are Essential for Flagellar Hook- and Filament Assembly and Dynamically Localize into Structures of Less than 100 nm Diameter underneath the Cell Membrane Structure of the LdcB LD-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at theEscherichia colidivision site The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain Difluoromethylornithine is a novel inhibitor of Helicobacter pylori growth, CagA translocation, and interleukin-8 induction A novel insight into the oxidoreductase activity of Helicobacter pylori HP0231 protein The bactofilin cytoskeleton protein BacM of Myxococcus xanthus forms an extended β-sheet structure likely mediated by hydrophobic interactions Structural basis for the recognition of muramyltripeptide by Helicobacter pylori Csd4, a D,L-carboxypeptidase controlling the helical cell shape β-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.The Cell Shape-determining Csd6 Protein from Helicobacter pylori Constitutes a New Family of L,D-Carboxypeptidase.Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR.Mutations in the nucleotide binding pocket of MreB can alter cell curvature and polar morphology in Caulobacter.Neisseria gonorrhoeae metalloprotease NGO1686 is required for full piliation, and piliation is required for resistance to H2O2- and neutrophil-mediated killing Mechanisms for maintaining cell shape in rod-shaped Gram-negative bacteria The Rcs stress response and accessory envelope proteins are required for de novo generation of cell shape in Escherichia coli.The Influence of Mucus Microstructure and Rheology in Helicobacter pylori Infection.Helicobacter pylori strains vary cell shape and flagellum number to maintain robust motility in viscous environments Helical and rod-shaped bacteria swim in helical trajectories with little additional propulsion from helical shape.Factors that mediate colonization of the human stomach by Helicobacter pylori.From the regulation of peptidoglycan synthesis to bacterial growth and morphology.HelicoBase: a Helicobacter genomic resource and analysis platform.Ulcerogenic Helicobacter pylori strains isolated from children: a contribution to get insight into the virulence of the bacteria.Peptidoglycan-modifying enzyme Pgp1 is required for helical cell shape and pathogenicity traits in Campylobacter jejuni.Helicobacter pylori in the pathogenesis of gastric cancer and gastric lymphoma Helicobacter pylori: bacterial strategy for incipient stage and persistent colonization in human gastric niches.Mechanisms of bacterial morphogenesis: evolutionary cell biology approaches provide new insights.Growth medium-dependent glycine incorporation into the peptidoglycan of Caulobacter crescentus Robustness of Helicobacter pylori infection conferred by context-variable redundancy among cysteine-rich paralogs.Maintenance of the cell morphology by MinC in Helicobacter pylori.Flow cytometry-based enrichment for cell shape mutants identifies multiple genes that influence Helicobacter pylori morphology.Helical shape of Helicobacter pylori requires an atypical glutamine as a zinc ligand in the carboxypeptidase Csd4 Mechanical control of bacterial cell shape.High resolution electron microscopy of the Helicobacter pylori Cag type IV secretion system pili produced in varying conditions of iron availability.Structure of Csd3 from Helicobacter pylori, a cell shape-determining metallopeptidase.

P2860

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P2860

Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization.

http://www.wikidata.org/entity/Q24632784

description

2010 nî lūn-bûn

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2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2010 թվականի մայիսին 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

Peptidoglycan crosslinking rel ...... shape and stomach colonization

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Peptidoglycan crosslinking rel ...... hape and stomach colonization.

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Peptidoglycan crosslinking rel ...... hape and stomach colonization.

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type

label

Peptidoglycan crosslinking rel ...... shape and stomach colonization

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Peptidoglycan crosslinking rel ...... hape and stomach colonization.

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Peptidoglycan crosslinking rel ...... hape and stomach colonization.

@en

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Peptidoglycan crosslinking rel ...... shape and stomach colonization

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Peptidoglycan crosslinking rel ...... hape and stomach colonization.

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Peptidoglycan crosslinking rel ...... hape and stomach colonization.

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J.CELL.2010.03.046

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Peptidoglycan crosslinking rel ...... hape and stomach colonization.

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Chelsea A Stern

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Jacob Biboy

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Kimberley D Gutierrez

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Laura K Sycuro

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Nina R Salama

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Zachary Pincus

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P2860

A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori

The complete genome sequence of the gastric pathogen Helicobacter pylori

A novel membrane protein influencing cell shape and multicellular swarming of Proteus mirabilis

Borrelia burgdorferi swims with a planar waveform similar to that of eukaryotic flagella

The selective value of bacterial shape

Pathogenesis of Helicobacter pylori infection

Emergence of large-scale cell morphology and movement from local actin filament growth dynamics

Latent LytM at 1.3A resolution

Crystal structure of a putative lysostaphin peptidase from Vibrio cholerae

The bacterial cytoskeleton: an intermediate filament-like function in cell shape

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10.1016/J.CELL.2010.03.046

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5

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141

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Waldemar Vollmer

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44638435

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20510929

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Helicobacter pylori

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2920535

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