Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase. - Wikidata - awgldk - TriplyDB

Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.

Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.

http://www.wikidata.org/entity/Q43018352

about

Structures of the thermophilic F1-ATPase subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1 Structural and functional analysis of the intrinsic inhibitor subunit epsilon of F1-ATPase from photosynthetic organisms The regulator of the F1 motor: inhibition of rotation of cyanobacterial F1-ATPase by the epsilon subunit.Rotation and structure of FoF1-ATP synthase.Visualization and measurement of ATP levels in living cells replicating hepatitis C virus genome RNA.Inhibition of ATP hydrolysis by thermoalkaliphilic F1Fo-ATP synthase is controlled by the C terminus of the epsilon subunit.Characterization of the relationship between ADP- and epsilon-induced inhibition in cyanobacterial F1-ATPase ε subunit of Bacillus subtilis F1-ATPase relieves MgADP inhibition.Genetically encodable fluorescent biosensors for tracking signaling dynamics in living cells.Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators.ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis Regulation of the F1F0-ATP synthase rotary nanomotor in its monomeric-bacterial and dimeric-mitochondrial forms Microscopy of single F(o) F(1) -ATP synthases--the unraveling of motors, gears, and controls.Activation and stiffness of the inhibited states of F1-ATPase probed by single-molecule manipulation.Inhibition of thermophilic F1-ATPase by the ε subunit takes different path from the ADP-Mg inhibition.Modulation of nucleotide specificity of thermophilic F(o)F(1)-ATP Synthase by epsilon-subunit Conformational transitions of subunit epsilon in ATP synthase from thermophilic Bacillus PS3 Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase.Regulatory interplay between proton motive force, ADP, phosphate, and subunit epsilon in bacterial ATP synthase.Role of the epsilon subunit of thermophilic F1-ATPase as a sensor for ATP.Effect of epsilon subunit on the rotation of thermophilic Bacillus F1-ATPase.ATP binding to the ϵ subunit of thermophilic ATP synthase is crucial for efficient coupling of ATPase and H+ pump activities.Dynamic mechanisms driving conformational conversions of the β and ε subunits involved in rotational catalysis of F1-ATPase.Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.Single mutations in the ε subunit from thermophilic PS3 generate a high binding affinity site for ATP

P2860

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P2860

Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.

http://www.wikidata.org/entity/Q43018352

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh-hant

name

Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.

@en

Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.

@nl

type

label

Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.

@en

Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.

@nl

prefLabel

Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.

@en

Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.

@nl

P1433

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P1433

Journal of Biological Chemistry

P1476

Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.

@en

P2093

Masasuke Yoshida

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

Ryota Iino

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

Satoshi Iizuka

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

Tomoe Murakami

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

Toshiharu Suzuki

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

Yasuyuki Kato-Yamada

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

P2860

Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride

Structure of the gamma-epsilon complex of ATP synthase

The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution

The conformation of the epsilon- and gamma-subunits within the Escherichia coli F(1) ATPase

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

Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli

The ATP synthase--a splendid molecular machine

Purine but not pyrimidine nucleotides support rotation of F(1)-ATPase.

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

Pause and rotation of F(1)-ATPase during catalysis

P304

40130-40134

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scholarly article

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10.1074/JBC.M506160200

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48

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280

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2005-10-03T00:00:00Z

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P698

16203732

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