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

Computer simulation of assembly and co-operativity of hexameric AAA ATPases.

PloS one - 1 Jan 2013

Le Doan Tuong-Van, Eckert Thomas, Woehlke Günther

Abstract excerpt

AAA ATPases form a functionally diverse superfamily of proteins. Most members form homo-hexameric ring complexes, are catalytically active only in the fully assembled state, and show co-operativity among the six subunits. The mutual dependence among the subunits is clearly evidenced by the fact t...

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 Computer Simulation
Share to Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Monte Carlo Method

Share to Mutation

Share to Protein Subunits

Source

Open in PubMed Open full text

Identifiers

PMID: 23869207
DOI: 10.1371/journal.pone.0067815
PMCID: PMC3711915

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-23869207-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Computer simulation of assembly and co-operativity of hexameric AAA ATPases.PMID 23869207Read ↗

Asymmetric configurations in a reengineered homodimer reveal multiple subunit communication pathways in protein allostery.Semantic proximity Read ↗

Evolutionary relationships and structural mechanisms of AAA+ proteins.Semantic proximity Read ↗

AAA+ ATPases: achieving diversity of function with conserved machinery.Semantic proximity Read ↗

Exploring signal transduction in heteromultimeric protein based on energy dissipation model.Semantic proximity Read ↗

Models of buffering of dosage imbalances in protein complexes.Semantic proximity Read ↗

Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.Semantic proximity Read ↗

Proteomics and models for enzyme cooperativity.Semantic proximity Read ↗

An asparagine residue mediates intramolecular communication in nucleotide-regulated pyrophosphatase.Semantic proximity Read ↗

In the multi-domain protein adenylate kinase, domain insertion facilitates cooperative folding while accommodating function at domain interfaces.Semantic proximity Read ↗

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ MachineSemantic proximity Read ↗

Distinct Allosteric Networks Underlie Mechanistic Speciation of ABC Transporters.Semantic proximity Read ↗

Modelling the evolution of biological complexity with a two-dimensional lattice self-assembly processSemantic proximity Read ↗

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