About: The epsilon subunit of the F(1)F(0) complex of Escherichia coli. cross-linking studies show the same structure in situ as when isolated

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About: The epsilon subunit of the F(1)F(0) complex of Escherichia coli. cross-linking studies show the same structure in situ as when isolated Goto Sponge NotDistinct Permalink

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scientific article published on 01 October 1999

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 1999 (uk) im Oktober 1999 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'ochobre de 1999 (ast) scientific article published on 01 October 1999 (en)
publication date	wds:Q73019327-B790C9DA-8961-4081-8A54-02177D94EDD8
publication date	1999-10-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73019327-D0A82859-E8B2-4051-8724-6C0AE7266639
language of work or name	English
cites work	wds:Q73019327-082FDE1E-B31A-4436-B5BE-DD856BCFDA55 wds:Q73019327-0B42AF42-58A7-4F59-AFDE-4D6EA49D2853 wds:Q73019327-0C2E9B9A-80DE-4E29-B8B2-CB205D1B919B wds:Q73019327-10A8AAAD-ED33-43C5-BF83-6198C62B9ABB wds:Q73019327-1638170D-B3D0-442E-A637-31EE707D8A42 wds:Q73019327-1922FBBB-9254-4ABC-A690-338F07C2CC2D wds:Q73019327-1A5D2B96-DA2E-432A-A85E-D299D81CD2F8 wds:Q73019327-27495B1B-C4BA-4952-83EE-8CCA323B5014 wds:Q73019327-2EF9ED9B-5D6D-4898-801F-C59F77911370 wds:Q73019327-3A235B16-1680-4937-BA73-8376BC2506DA wds:Q73019327-41112AC2-FECF-4438-A114-F3C74E47DAEE wds:Q73019327-41684D97-DDED-45B7-8324-1A5FA13961D1 wds:Q73019327-43FB2AD9-0C68-4B14-98A8-FD3885EB4D05 wds:Q73019327-4AB36538-50F0-4590-B5DA-9CA871604209 wds:Q73019327-4B95E212-CCE8-4178-A2E6-9DD356754390 wds:Q73019327-6510B9C0-7A31-4881-B1FC-FBDF8F0E22D7 wds:Q73019327-65749A46-C39C-4E2C-A381-25DD00269CF9 wds:Q73019327-7C6CB1C5-E344-4AAA-AAAD-5DFBBFBB594B wds:Q73019327-7C8189A2-7EE9-422E-BE4C-67A87AEDC4B2 wds:Q73019327-846C39C3-C05A-4552-B3D6-FD913EE1CBD2 wds:Q73019327-8D16ADAF-020F-4639-81EA-2B29B80F35BE wds:Q73019327-91754DF9-8C0E-4E19-9326-095570E72294 wds:Q73019327-9246F04C-5822-425F-862F-96F298E056C4 wds:Q73019327-963FD0B2-D37E-4363-B723-FEB415352D13 wds:Q73019327-9D7E8116-643F-4E26-9415-20F47BDEC5D0 wds:Q73019327-A16AD86E-39EE-447F-8FEE-B70DFBA6B7E9 wds:Q73019327-A446AADF-ED49-4A45-ABE8-23CD9F1526B2 wds:Q73019327-AD6C7B8B-9A74-4D92-AF7C-8C750062D146 wds:Q73019327-AF848A8A-013F-44A1-92F1-6DFFF4A424B1 wds:Q73019327-B7064162-9CCF-4087-BCD2-3798EBE27411 wds:Q73019327-C12051DA-8D9D-4620-9DF5-BA921728248C wds:Q73019327-C581DCED-2810-4FFE-8368-8BFF115DF1A0 wds:Q73019327-C6699238-23F1-49D2-8D30-3BEF3BE96EE3 wds:Q73019327-D52EB181-3279-475F-B528-E8DACEC299D5 wds:Q73019327-DFC2D5D7-8BA8-469A-99D8-68FCE7AAE681 wds:Q73019327-F1C01B78-3969-448D-B923-1AAF5875D596 wds:Q73019327-FFB6DFE3-0E95-4416-BCD2-405BD9A19478
cites work	The UNC operon nucleotide sequence, regulation and structure of ATP-synthase The proton-translocating ATPase of Escherichia coli Interconversion of high and low adenosinetriphosphatase activity forms of Escherichia coli F1 by the detergent lauryldimethylamine oxide Energy transduction in ATP synthase The ATP synthase--a splendid molecular machine Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Direct observation of the rotation of F1-ATPase Energy transduction in the sodium F-ATPase of Propionigenium modestum Rapid and efficient site-specific mutagenesis without phenotypic selection Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase. Cys-Cys cross-linking of F1 subunit epsilon to the polar loop of F0 subunit c. Nucleotide-dependent movement of the epsilon subunit between alpha and beta subunits in the Escherichia coli F1F0-type ATPase Disulfide bond formation between the COOH-terminal domain of the beta subunits and the gamma and epsilon subunits of the Escherichia coli F1-ATPase. Structural implications and functional consequences. Intersubunit rotation in active F-ATPase Characterization of the interface between gamma and epsilon subunits of Escherichia coli F1-ATPase Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis The second stalk composed of the b- and delta-subunits connects F0 to F1 via an alpha-subunit in the Escherichia coli ATP synthase Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy Rotation of the epsilon subunit during catalysis by Escherichia coli FOF1-ATP synthase A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250. Electron microscopic evidence of two stalks linking the F1 and F0 parts of the Escherichia coli ATP synthase. Cross-linking of the delta subunit to one of the three alpha subunits has no effect on functioning, as expected if delta is a part of the stator that links the F1 and F0 parts of the Escherichia coli ATP synthase. Direct indication for the existence of a double stalk in CF 0 F 1 1 1Edited by J. Karn Genetic fusions of subunit c in the F0 sector of H+-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis Molecular dissection of the epsilon subunit of the chloroplast ATP synthase of spinach Subunit epsilon of the Escherichia coli ATP synthase: novel insights into structure and function by analysis of thirteen mutant forms Components of the mitochondrial inner membrane. 3. Characterization of a seventh different subunit of beef heart cytochrome c oxidase. Similarities between the beef heart enzyme and that from other species Binding stoichiometry and structural mapping of the epsilon polypeptide of chloroplast coupling factor 1 Rotation of a gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. The gamma-epsilon subunits are essentially randomly distributed relative to the alpha3beta3delta domain in the intact complex. Nucleotide-dependent and dicyclohexylcarbodiimide-sensitive conformational changes in the .epsilon. subunit of Escherichia coli ATP synthase Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the .epsilon. subunit in the Escherichia coli adenosinetriphosphatase Introduction of reactive cysteine residues in the epsilon subunit of Escherichia coli F1 ATPase, modification of these sites with tetrafluorophenyl azide-maleimides, and examination of changes in the binding of the epsilon subunit when different nuc A mutation in the Escherichia coli F0F1-ATP synthase rotor, gammaE208K, perturbs conformational coupling between transport and catalysis Labeling of the ATP synthase of Escherichia coli from the head-group region of the lipid bilayer Characterization of the inhibitory (epsilon) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli Cross-linking of chloroplast F0F1-ATPase subunit epsilon to gamma without effect on activity. Epsilon and gamma are parts of the rotor
author name string	wds:Q73019327-9630FC92-6B50-4EC2-9C82-E6D1548C3EB4 wds:Q73019327-E223DFE4-0107-4AEF-B173-5C7DD2C8A073
author name string	R A Capaldi B Schulenberg
rdfs:label	The epsilon subunit of the F (nl) The epsilon subunit of the F(1)F(0) complex of Escherichia coli. cross-linking studies show the same structure in situ as when isolated (en)
skos:prefLabel	The epsilon subunit of the F (nl) The epsilon subunit of the F(1)F(0) complex of Escherichia coli. cross-linking studies show the same structure in situ as when isolated (en)
name	The epsilon subunit of the F (nl) The epsilon subunit of the F(1)F(0) complex of Escherichia coli. cross-linking studies show the same structure in situ as when isolated (en)
title	wds:Q73019327-960287BE-32FB-448E-9629-18D34C2BF437
title	The epsilon subunit of the F(1)F(0) complex of Escherichia coli. cross-linking studies show the same structure in situ as when isolated (en)
page(s)	wds:Q73019327-06C0FB2F-D15F-49A3-A4E7-D46A88C14721
page(s)	28351-28355
instance of	wds:Q73019327-F287E898-8A29-49F1-B77C-EA00B2E5D090
instance of	scholarly article

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