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

Turned on for degradation: ATPase-independent degradation by ClpP.

Journal of structural biology - 1 Feb 2009

Bewley Maria C, Graziano Vito, Griffin Kathleen, Flanagan John M

Abstract excerpt

Clp is a barrel-shaped hetero-oligomeric ATP-dependent protease comprising a hexameric ATPase (ClpX or ClpA) that unfolds protein substrates and translocates them into the central chamber of the tetradecameric proteolytic component (ClpP) where they are degraded processively to short peptides. Ch...

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 Caseins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Endopeptidase Clp

Share to Escherichia coli Proteins

Share to Hydrolysis

Share to Peptides

Source

Open in PubMed Open full text

Identifiers

PMID: 19038348
DOI: 10.1016/j.jsb.2008.10.005
PMCID: PMC3433037

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-19038348-2026-09-04.2. 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

Turned on for degradation: ATPase-independent degradation by ClpP.PMID 19038348Read ↗

The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes.Semantic proximity Read ↗

Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding.Semantic proximity Read ↗

Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli.Semantic proximity Read ↗

A conformational switch underlies ClpP protease function.Semantic proximity Read ↗

Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP.Semantic proximity Read ↗

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

The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.Semantic proximity Read ↗

AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.Semantic proximity Read ↗

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

Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations.Semantic proximity Read ↗

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

Substrate recognition and processing by a Walker B mutant of the human mitochondrial AAA+ protein CLPX.Semantic proximity Read ↗

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