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

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

Cell - 22 Aug 2003

Kenniston Jon A, Baker Tania A, Fernandez Julio M, Sauer Robert T

Abstract excerpt

Proteolytic machines powered by ATP hydrolysis bind proteins with specific peptide tags, denature these substrates, and translocate them into a sequestered compartment for degradation. To determine how ATP is used during individual reaction steps, we assayed ClpXP degradation of ssrA-tagged titin variants with different stabilities in native and denatured forms. The rate of ATP turnover was 4-fold slower during...

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

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Connectin

Share to Endopeptidase Clp

Share to Muscle Proteins

Share to Protein Denaturation

Share to Protein Kinases

Share to Serine Endopeptidases

Source

Identifiers

PMID: 12941278
DOI: 10.1016/s0092-8674(03)00612-3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine.PMID 12941278Read ↗

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

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

Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines.Semantic proximity Read ↗

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

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

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

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

The Intrinsically Disordered N-terminal Extension of the ClpS Adaptor Reprograms Its Partner AAA+ ClpAP Protease.Semantic proximity Read ↗

C-terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding.Semantic proximity Read ↗

ClpB chaperone passively threads soluble denatured proteins through its central pore.Semantic proximity Read ↗

Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine.Semantic proximity Read ↗

A mitochondrial insertion directs substrate selection and engagement by ClpXSemantic proximity Read ↗

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