Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics.

about

Inhibition of F1-ATPase rotational catalysis by the carboxyl-terminal domain of the ϵ subunit.Identification of a new Mpl-interacting protein, Atp5d.Ancient Systems of Sodium/Potassium Homeostasis as Predecessors of Membrane Bioenergetics.

P2860

Q30366884-EAABD53A-40B5-4F31-808A-C8660BC6F073 Q39016705-5465F8EA-C853-4C9D-8729-A42D62ADBE97 Q40838602-E508C7D2-E953-4C14-874B-D8D3E2030821

P2860

Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics.

Item

http://www.wikidata.org/entity/Q38084629

description

article científic

@ca

article scientifique

@fr

articol științific

@ro

articolo scientifico

@it

artigo científico

@gl

artigo científico

@pt

artigo científico

@pt-br

artikel ilmiah

@id

artikull shkencor

@sq

artículo científico

@es

name

Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics.

@en

type

Item

label

Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics.

@en

prefLabel

Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics.

@en

P1476

Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics.

@en

P2093

Masamitsu Futai

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

Mayumi Nakanishi-Matsui

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

Mizuki Sekiya

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

P2860

Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols

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

Direct observation of the rotation of F1-ATPase

The ATP synthase--a splendid molecular machine

Binding of phytopolyphenol piceatannol disrupts β/γ subunit interactions and rate-limiting step of steady-state rotational catalysis in Escherichia coli F1-ATPase.

Single molecule behavior of inhibited and active states of Escherichia coli ATP synthase F1 rotation.

Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell.

The ATP synthase gamma subunit. Suppressor mutagenesis reveals three helical regions involved in energy coupling.

Intergenic suppression of the gammaM23K uncoupling mutation in F0F1 ATP synthase by betaGlu-381 substitutions: the role of the beta380DELSEED386 segment in energy coupling.

High-resolution single-molecule characterization of the enzymatic states in Escherichia coli F1-ATPase

P304

247-254

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

P31

scholarly article

P356

10.1002/IUB.1134

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

P433

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

P478

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

P577

2013-03-01T00:00:00Z

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

P698

23441040

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

Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics.

about

P2860

P2860

Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698