Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor. - Wikidata - awgldk - TriplyDB

Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor.

Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor.

http://www.wikidata.org/entity/Q40015520

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Architecture of the Flagellar Switch Complex of Escherichia coli: Conformational Plasticity of FliG and Implications for Adaptive Remodeling.Structural Analysis of the Flagellar Component Proteins in Solution by Small Angle X-Ray Scattering.The Gearbox of the Bacterial Flagellar Motor Switch.Length-dependent flagellar growth of Vibrio alginolyticus revealed by real time fluorescent imaging Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly.Domain-based biophysical characterization of the structural and thermal stability of FliG, an essential rotor component of the Na+-driven flagellar motor.Biogenesis of the Flagellar Switch Complex in Escherichia coli: Formation of Sub-Complexes Independently of the Basal-Body MS-Ring.Crystal structure of the FliF-FliG complex from Helicobacter pylori yields insight into the assembly of the motor MS-C ring in the bacterial flagellum.Design principles and optimal performance for molecular motors under realistic constraints.Characterization of C-ring component assembly in flagellar motors from amino acid coevolution.A coevolution-guided model for the rotor of the bacterial flagellar motor

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Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor.

http://www.wikidata.org/entity/Q40015520

description

2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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name

Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor.

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type

label

Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor.

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prefLabel

Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor.

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Nature Structural & Molecular Biology

P1476

Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor.

@en

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Anthony A Rey

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

Chu Wai Liew

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Daniela Stock

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

Judith P Armitage

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

Keiichi Namba

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

Lorraine A Ganuelas

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

Nasim Shah Mohammadi

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

Nicolas J Delalez

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

Richard M Berry

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

Robert M G Hynson

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

P2860

Protein 3D structure computed from evolutionary sequence variation

Sequence co-evolution gives 3D contacts and structures of protein complexes

How frequent are correlated changes in families of protein sequences?

Three-dimensional structures of membrane proteins from genomic sequencing

A mutational analysis of the interaction between FliG and FliM, two components of the flagellar motor of Escherichia coli

What macromolecular crowding can do to a protein

Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG

Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization

Cytochrome c polymerization by successive domain swapping at the C-terminal helix

Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching.

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197-203

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scholarly article

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10.1038/NSMB.3172

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3

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23

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Andrew E Whitten

Andrew Turberfield

Anthony P. Duff

Yusuke V Morimoto

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2016-02-08T00:00:00Z

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293634209

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26854663

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