Temperature-sensitive reaction intermediate of F1-ATPase. - Wikidata - wikimedia - TriplyDB

Temperature-sensitive reaction intermediate of F1-ATPase.

Temperature-sensitive reaction intermediate of F1-ATPase.

http://www.wikidata.org/entity/Q30481307

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Operation mechanism of F(o) F(1)-adenosine triphosphate synthase revealed by its structure and dynamics Comparison between single-molecule and X-ray crystallography data on yeast F1-ATPase A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis Single-molecule study on the temperature-sensitive reaction of F1-ATPase with a hybrid F1 carrying a single beta(E190D).High-resolution single-molecule characterization of the enzymatic states in Escherichia coli F1-ATPase Improving FRET-based monitoring of single chemomechanical rotary motors at work.Rotation and structure of FoF1-ATP synthase.Simple mechanism whereby the F1-ATPase motor rotates with near-perfect chemomechanical energy conversion.Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation Chemomechanical coupling of F1-ATPase under hydrolysis conditions.Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation.Simple dark-field microscopy with nanometer spatial precision and microsecond temporal resolution.Torque transmission mechanism via DELSEED loop of F1-ATPase.Single-molecule analysis of the rotation of F₁-ATPase under high hydrostatic pressure.Motor-substrate interactions in mycoplasma motility explains non-Arrhenius temperature dependence.Catalysis-enhancement via rotary fluctuation of F1-ATPase.Thermodynamic analysis of F1-ATPase rotary catalysis using high-speed imaging.Mechanism of the αβ conformational change in F1-ATPase after ATP hydrolysis: free-energy simulations.Torque generation mechanism of F1-ATPase upon NTP binding.Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase.Mechanical modulation of catalytic power on F1-ATPase.Acceleration of the ATP-binding rate of F1-ATPase by forcible forward rotation.Biophysical Characterization of a Thermoalkaliphilic Molecular Motor with a High Stepping Torque Gives Insight into Evolutionary ATP Synthase Adaptation.Giant Acceleration of Diffusion Observed in a Single-Molecule Experiment on F(1)-ATPase.A Specific Single Nucleotide Polymorphism in the ATP Synthase Gene Significantly Improves Environmental Stress Tolerance of Synechococcus elongatus PCC 7942

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Temperature-sensitive reaction intermediate of F1-ATPase.

http://www.wikidata.org/entity/Q30481307

description

2007 nî lūn-bûn

@nan

2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

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name

Temperature-sensitive reaction intermediate of F1-ATPase.

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Temperature-sensitive reaction intermediate of F1-ATPase.

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type

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Temperature-sensitive reaction intermediate of F1-ATPase.

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Temperature-sensitive reaction intermediate of F1-ATPase.

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Temperature-sensitive reaction intermediate of F1-ATPase.

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Temperature-sensitive reaction intermediate of F1-ATPase.

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SJ.EMBOR.7401135

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P1476

Temperature-sensitive reaction intermediate of F1-ATPase

@en

P2093

Hiroyuki Noji

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

Katsuya Shimabukuro

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

Masasuke Yoshida

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

Rikiya Watanabe

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

P2860

Catalytic and mechanical cycles in F-ATP synthases. Fourth in the Cycles Review Series

Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolution

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

The binding change mechanism for ATP synthase--some probabilities and possibilities

Direct observation of the rotation of F1-ATPase

Energy coupling, turnover, and stability of the F0F1 ATP synthase are dependent on the energy of interaction between gamma and beta subunits.

Temperature dependence and Arrhenius activation energy of F-actin velocity generated in vitro by skeletal myosin.

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

Activation of pausing F1 motor by external force

Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.

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scholarly article

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10.1038/SJ.EMBOR.7401135

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1

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18064048

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2246616

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