A bacterial Ras-like small GTP-binding protein and its cognate GAP establish a dynamic spatial polarity axis to control directed motility. - Wikidata - awgldk - TriplyDB

A bacterial Ras-like small GTP-binding protein and its cognate GAP establish a dynamic spatial polarity axis to control directed motility.

A bacterial Ras-like small GTP-binding protein and its cognate GAP establish a dynamic spatial polarity axis to control directed motility.

http://www.wikidata.org/entity/Q33638426

about

Complex archaea that bridge the gap between prokaryotes and eukaryotes Novel transglutaminase-like peptidase and C2 domains elucidate the structure, biogenesis and evolution of the ciliary compartment Salmonella pathogenicity and host adaptation in chicken-associated serovars Evolution and Design Governing Signal Precision and Amplification in a Bacterial Chemosensory Pathway A dynamic response regulator protein modulates G-protein-dependent polarity in the bacterium Myxococcus xanthus Emergence and modular evolution of a novel motility machinery in bacteria Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity Molecular paleontology and complexity in the last eukaryotic common ancestor Effects of site-directed mutagenesis of mglA on motility and swarming of Myxococcus xanthus.Motor-driven intracellular transport powers bacterial gliding motility Cell division resets polarity and motility for the bacterium Myxococcus xanthus.A response regulator interfaces between the Frz chemosensory system and the MglA/MglB GTPase/GAP module to regulate polarity in Myxococcus xanthus Poles apart: prokaryotic polar organelles and their spatial regulation Dual biochemical oscillators may control cellular reversals in Myxococcus xanthus.The polarity of myxobacterial gliding is regulated by direct interactions between the gliding motors and the Ras homolog MglA Evolution and diversity of the Ras superfamily of small GTPases in prokaryotes Ras GTPase-like protein MglA, a controller of bacterial social-motility in Myxobacteria, has evolved to control bacterial predation by Bdellovibrio Effect of the Min system on timing of cell division in Escherichia coli.The small G-protein MglA connects to the MreB actin cytoskeleton at bacterial focal adhesions.Uncovering the mystery of gliding motility in the myxobacteria The TGFβ receptor-interacting protein km23-1/DYNLRB1 plays an adaptor role in TGFβ1 autoinduction via its association with Ras.Mycobacterium fluoroquinolone resistance protein B, a novel small GTPase, is involved in the regulation of DNA gyrase and drug resistance.Invasive cells in animals and plants: searching for LECA machineries in later eukaryotic life Phosphorylation-dependent localization of the response regulator FrzZ signals cell reversals in Myxococcus xanthus.De- and repolarization mechanism of flagellar morphogenesis during a bacterial cell cycle.Temporal and spatial oscillations in bacteria.From individual cell motility to collective behaviors: insights from a prokaryote, Myxococcus xanthus.Chemosensory signaling controls motility and subcellular polarity in Myxococcus xanthus.Establishing polar identity in gram-negative rods.Regulation of cell polarity in bacteria.Open and Lys-His Hexacoordinated Closed Structures of a Globin with Swapped Proximal and Distal Sites Outside-in assembly pathway of the type IV pilus system in Myxococcus xanthus.MglC, a Paralog of Myxococcus xanthus GTPase-Activating Protein MglB, Plays a Divergent Role in Motility Regulation.Role of km23-1 in RhoA/actin-based cell migration.Are There Rab GTPases in Archaea?Longin and GAF domains: structural evolution and adaptation to the subcellular trafficking machinery.Regulation of cell reversal frequency in Myxococcus xanthus requires the balanced activity of CheY-like domains in FrzE and FrzZ.PlpA, a PilZ-like protein, regulates directed motility of the bacterium Myxococcus xanthus.Exopolysaccharides promote Myxococcus xanthus social motility by inhibiting cellular reversals.Subcellular Organization: A Critical Feature of Bacterial Cell Replication.

P2860

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P2860

A bacterial Ras-like small GTP-binding protein and its cognate GAP establish a dynamic spatial polarity axis to control directed motility.

http://www.wikidata.org/entity/Q33638426

description

2010 nî lūn-bûn

@nan

2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

A bacterial Ras-like small GTP ...... to control directed motility.

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A bacterial Ras-like small GTP ...... to control directed motility.

@en

type

label

A bacterial Ras-like small GTP ...... to control directed motility.

@ast

A bacterial Ras-like small GTP ...... to control directed motility.

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prefLabel

A bacterial Ras-like small GTP ...... to control directed motility.

@ast

A bacterial Ras-like small GTP ...... to control directed motility.

@en

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A bacterial Ras-like small GTP ...... to control directed motility.

@en

P2093

Adrien Ducret

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

Michel Franco

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

Tâm Mignot

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

Yong Zhang

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

P2860

A microscope automated fluidic system to study bacterial processes in real time

Adjacent positioning of cellular structures enabled by a Cdc42 GTPase-activating protein-mediated zone of inhibition.

GAP control: regulating the regulators of small GTPases

GEFs and GAPs: critical elements in the control of small G proteins

The influence of bound GDP on the kinetics of guanine nucleotide binding to G proteins

Bacterial motility complexes require the actin-like protein, MreB and the Ras homologue, MglA

Making sense of it all: bacterial chemotaxis

Drosophila roadblock and Chlamydomonas LC7: a conserved family of dynein-associated proteins involved in axonal transport, flagellar motility, and mitosis.

Evidence that focal adhesion complexes power bacterial gliding motility.

Dynein light chains of the Roadblock/LC7 group belong to an ancient protein superfamily implicated in NTPase regulation.

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e1000430

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scholarly article

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10.1371/JOURNAL.PBIO.1000430

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7

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