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

Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines.

Nature - 20 Oct 2005

Martin Andreas, Baker Tania A, Sauer Robert T

Abstract excerpt

Hexameric ring-shaped ATPases of the AAA + (for ATPases associated with various cellular activities) superfamily power cellular processes in which macromolecular structures and complexes are dismantled or denatured, but the mechanisms used by these machine-like enzymes are poorly understood. By covalently linking active and inactive subunits of the ATPase ClpX to form hexamers, here we show that diverse geometric...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Adenosine Triphosphate
Share to Helicobacter pylori

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

Share to Hydrolysis

Share to Molecular Motor Proteins

Share to Protein Denaturation

Share to Protein Structure, Quaternary

Share to Protein Subunits

Source

Identifiers

PMID: 16237435
DOI: 10.1038/nature04031

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

Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines.PMID 16237435Read ↗

Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine.Semantic proximity Read ↗

Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding.Semantic proximity Read ↗

Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease.Semantic proximity Read ↗

Modular and coordinated activity of AAA+ active sites in the double-ring ClpA unfoldase of the ClpAP protease.Semantic proximity Read ↗

Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysisSemantic proximity Read ↗

Coordinated gripping of substrate by subunits of a AAA+ proteolytic machine.Semantic proximity Read ↗

Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.Semantic proximity Read ↗

A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinerySemantic proximity Read ↗

Dynamic structural states of ClpB involved in its disaggregation function.Semantic proximity Read ↗

Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine.Semantic proximity Read ↗

A tightly regulated molecular toggle controls AAA+ disaggregase.Semantic proximity Read ↗

Structural and kinetic basis for the regulation and potentiation of Hsp104 function.Semantic proximity Read ↗

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