Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Characterization of domain interfaces in monomeric and dimeric ATP synthase.

Molecular & cellular proteomics : MCP - 1 May 2008

Wittig Ilka, Velours Jean, Stuart Rosemary, Schägger Hermann

Abstract excerpt

We disassembled monomeric and dimeric yeast ATP synthase under mild conditions to identify labile proteins and transiently stable subcomplexes that had not been observed before. Specific removal of subunits alpha, beta, oligomycin sensitivity conferring protein (OSCP), and h disrupted the ATP synthase at the gamma-alpha(3)beta(3) rotor-stator interface. Loss of two F(1)-parts from dimeric ATP synthase led to the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adaptor Proteins, Signal Transducing
Share to Adenosine Triphosphatases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Dimerization

Share to Mitochondrial Proteins

Share to Mitochondrial Proton-Translocating ATPases

Share to Multienzyme Complexes

Share to Protein Subunits

Share to Saccharomyces cerevisiae Proteins

Source

Identifiers

PMID: 18245802
DOI: 10.1074/mcp.M700465-MCP200

Genes

SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of domain interfaces in monomeric and dimeric ATP synthase.PMID 18245802Read ↗

TMEM70 forms oligomeric scaffolds within mitochondrial cristae promoting <i>in situ</i> assembly of mammalian ATP synthase proton channelSemantic proximity Read ↗

Stepwise assembly of dimeric F(1)F(o)-ATP synthase in mitochondria involves the small F(o)-subunits k and i.Semantic proximity Read ↗

Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase. Deletions disrupt function but not enzyme assembly.Semantic proximity Read ↗

Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits.Semantic proximity Read ↗

Bacterial F-type ATP synthases follow a well-choreographed assembly pathwaySemantic proximity Read ↗

Subunit δ is the key player for assembly of the H(+)-translocating unit of Escherichia coli F(O)F1 ATP synthase.Semantic proximity Read ↗

Construction and analyses of tetrameric forms of yeast NAD+-specific isocitrate dehydrogenase.Semantic proximity Read ↗

Assembly of the yeast vacuolar H+-ATPase and ATP hydrolysis occurs in the absence of subunit c''.Semantic proximity Read ↗

Role of α/β interface in F1 ATPase rotational catalysis probed by inhibitors and mutations.Semantic proximity Read ↗

Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex.Semantic proximity Read ↗

Reconstitution of the Fo complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit c after purification in organic solvent.Semantic proximity Read ↗

Structure of the yeast F1Fo-ATP synthase dimer and its role in shaping the mitochondrial cristae.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.