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The unique paradigm of spirochete motility and chemotaxis.

The unique paradigm of spirochete motility and chemotaxis.

http://www.wikidata.org/entity/Q30544647

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Lessons in Fundamental Mechanisms and Diverse Adaptations from the 2015 Bacterial Locomotion and Signal Transduction Meeting Intravital Imaging of Vascular Transmigration by the Lyme Spirochete: Requirement for the Integrin Binding Residues of the B. burgdorferi P66 Protein Hypothetical Protein BB0569 Is Essential for Chemotaxis of the Lyme Disease Spirochete Borrelia burgdorferi.Opposite and Coordinated Rotation of Amphitrichous Flagella Governs Oriented Swimming and Reversals in a Magnetotactic Spirillum.Initial characterization of the FlgE hook high molecular weight complex of Borrelia burgdorferi Stage-specific global alterations in the transcriptomes of Lyme disease spirochetes during tick feeding and following mammalian host adaptation.Spirochaete flagella hook proteins self-catalyse a lysinoalanine covalent crosslink for motility Two CheW coupling proteins are essential in a chemosensory pathway of Borrelia burgdorferi.Helicobacter pylori strains vary cell shape and flagellum number to maintain robust motility in viscous environments Motility and Ultrastructure of Spirochaeta thermophila Biomechanics of Borrelia burgdorferi Vascular Interactions The cyclic-di-GMP signaling pathway in the Lyme disease spirochete, Borrelia burgdorferi A protein-protein interaction dictates Borrelial infectivity.Genetics of Borrelia burgdorferi Innate immunity networks during infection with Borrelia burgdorferi.Molecular architecture of the bacterial flagellar motor in cells Spirochetal motility and chemotaxis in the natural enzootic cycle and development of Lyme disease Periplasmic flagellar export apparatus protein, FliH, is involved in post-transcriptional regulation of FlaB, motility and virulence of the relapsing fever spirochete Borrelia hermsii.Co-feeding transmission in Lyme disease pathogens.BB0323 and novel virulence determinant BB0238: Borrelia burgdorferi proteins that interact with and stabilize each other and are critical for infectivity Motor rotation is essential for the formation of the periplasmic flagellar ribbon, cellular morphology, and Borrelia burgdorferi persistence within Ixodes scapularis tick and murine hosts.Gene inactivation of a chemotaxis operon in the pathogen Leptospira interrogans.Mutations in the Borrelia burgdorferi Flagellar Type III Secretion System Genes fliH and fliI Profoundly Affect Spirochete Flagellar Assembly, Morphology, Motility, Structure, and Cell Division.What Makes a Bacterial Species Pathogenic?:Comparative Genomic Analysis of the Genus Leptospira Motility of Spirochetes.Proteolysis of BB0323 results in two polypeptides that impact physiologic and infectious phenotypes in Borrelia burgdorferi.Review of evidence for immune evasion and persistent infection in Lyme disease.The HtrA protease of Borrelia burgdorferi degrades outer membrane protein BmpD and chemotaxis phosphatase CheX.Motility is crucial for the infectious life cycle of Borrelia burgdorferi.Borrelia burgdorferi CheD Promotes Various Functions in Chemotaxis and the Pathogenic Life Cycle of the Spirochete Cryoelectron tomography reveals the sequential assembly of bacterial flagella in Borrelia burgdorferi.Viscous dynamics of Lyme disease and syphilis spirochetes reveal flagellar torque and drag Direct measurement of helical cell motion of the spirochete leptospira.Borrelia burgdorferi CheY2 Is Dispensable for Chemotaxis or Motility but Crucial for the Infectious Life Cycle of the Spirochete.Borrelia burgdorferi Keeps Moving and Carries on: A Review of Borrelial Dissemination and Invasion.A tale of two machines: a review of the BLAST meeting, Tucson, AZ, 20-24 January 2013.Bacteria that glide with helical tracks.DhhP, a cyclic di-AMP phosphodiesterase of Borrelia burgdorferi, is essential for cell growth and virulence Spirochetes flagellar collar protein FlbB has astounding effects in orientation of periplasmic flagella, bacterial shape, motility, and assembly of motors in Borrelia burgdorferi.The Borrelia burgdorferi CheY3 response regulator is essential for chemotaxis and completion of its natural infection cycle.

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The unique paradigm of spirochete motility and chemotaxis.

http://www.wikidata.org/entity/Q30544647

description

2012 nî lūn-bûn

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2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2012 թվականի հունվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

The unique paradigm of spirochete motility and chemotaxis.

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The unique paradigm of spirochete motility and chemotaxis.

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The unique paradigm of spirochete motility and chemotaxis.

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The unique paradigm of spirochete motility and chemotaxis.

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The unique paradigm of spirochete motility and chemotaxis.

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The unique paradigm of spirochete motility and chemotaxis.

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ANNUREV-MICRO-092611-150145

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Annual Review of Microbiology

P1476

The unique paradigm of spirochete motility and chemotaxis

@en

P2093

Andrew Cockburn

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

Charles W Wolgemuth

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Chunhao Li

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Jun Liu

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Kelly A Miller

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Michael R Miller

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Nyles W Charon

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P2860

Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi

Biology of infection with Borrelia burgdorferi

Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain

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

Analysis of the Borrelia burgdorferi cyclic-di-GMP-binding protein PlzA reveals a role in motility and virulence

The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism.

A newly discovered cholesteryl galactoside from Borrelia burgdorferi

Molecular mechanisms involved in vascular interactions of the Lyme disease pathogen in a living host

Real-time high resolution 3D imaging of the lyme disease spirochete adhering to and escaping from the vasculature of a living host

Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate

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349-370

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scholarly article

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10.1146/ANNUREV-MICRO-092611-150145

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66

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MD Abdul Motaleb

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2012-01-01T00:00:00Z

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230893075

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22994496

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3771095

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