Force distribution reveals signal transduction in E. coli Hsp90. - Wikidata - wikimedia - TriplyDB

Force distribution reveals signal transduction in E. coli Hsp90.

Force distribution reveals signal transduction in E. coli Hsp90.

http://www.wikidata.org/entity/Q42209394

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Dynamic Allostery of the Catabolite Activator Protein Revealed by Interatomic Forces Access Path to the Ligand Binding Pocket May Play a Role in Xenobiotics Selection by AhR Differential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.Allosteric regulation of the Hsp90 dynamics and stability by client recruiter cochaperones: protein structure network modeling Computational modeling of allosteric regulation in the hsp90 chaperones: a statistical ensemble analysis of protein structure networks and allosteric communications.An allosteric signaling pathway of human 3-phosphoglycerate kinase from force distribution analysis Time-resolved force distribution analysis.Allosteric regulation of focal adhesion kinase by PIP₂ and ATP.Mapping Mechanical Force Propagation through Biomolecular Complexes.New Insights into the Formation of Viable but Nonculturable Escherichia coli O157:H7 Induced by High-Pressure CO2.ATP-driven molecular chaperone machines.One-Way Allosteric Communication between the Two Disulfide Bonds in Tissue Factor.Autoregulation of von Willebrand factor function by a disulfide bond switch.

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P2860

Force distribution reveals signal transduction in E. coli Hsp90.

http://www.wikidata.org/entity/Q42209394

description

2012 nî lūn-bûn

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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年论文

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2012年论文

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2012年论文

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name

Force distribution reveals signal transduction in E. coli Hsp90.

@en

Force distribution reveals signal transduction in E. coli Hsp90.

@nl

type

label

Force distribution reveals signal transduction in E. coli Hsp90.

@en

Force distribution reveals signal transduction in E. coli Hsp90.

@nl

prefLabel

Force distribution reveals signal transduction in E. coli Hsp90.

@en

Force distribution reveals signal transduction in E. coli Hsp90.

@nl

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J.BPJ.2012.09.008

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Biophysical Journal

P1476

Force distribution reveals signal transduction in E. coli Hsp90

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Christian Seifert

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P2860

Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms

In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

Corresponding functional dynamics across the Hsp90 Chaperone family: insights from a multiscale analysis of MD simulations

Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family members

Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer

WHAT IF: a molecular modeling and drug design program

GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation

ModLoop: automated modeling of loops in protein structures

Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

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2195-2202

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scholarly article

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Escherichia coli

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