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

Phylogenetic analysis predicts structural divergence for proteobacterial ClpC proteins.

Journal of structural biology - 1 Jan 2018

Miller Justin M, Chaudhary Hamza, Marsee Justin D

Abstract excerpt

Regulated proteolysis is required in all organisms for the removal of misfolded or degradation-tagged protein substrates in cellular quality control pathways. The molecular machines that catalyze this process are known as ATP-dependent proteases with examples that include ClpAP and ClpCP. Clp/Hsp100 subunits form ring-structures that couple the energy of ATP binding and hydrolysis to protein unfolding and...

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 Endopeptidase Clp

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

Share to Heat-Shock Proteins

Share to Hydrolysis

Share to Protein Domains

Share to Protein Unfolding

Share to Proteobacteria

Source

Identifiers

PMID: 29129755
DOI: 10.1016/j.jsb.2017.11.003

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

Phylogenetic analysis predicts structural divergence for proteobacterial ClpC proteins.PMID 29129755Read ↗

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

Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.Semantic proximity Read ↗

Hsp100 Molecular Chaperone ClpB and Its Role in Virulence of Bacterial PathogensSemantic 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 ↗

Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.Semantic proximity Read ↗

Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome.Semantic proximity Read ↗

The Bacterial ClpXP-ClpB Family is Enriched with RNA-Binding Protein ComplexesSemantic proximity Read ↗

Clp P represents a unique family of serine proteases.Semantic proximity Read ↗

The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureusSemantic proximity Read ↗

Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triadSemantic proximity Read ↗

ClpL is required for folding of CtsR in Streptococcus mutans.Semantic proximity Read ↗

Trapping and Identification of Cellular Substrates of the Staphylococcus aureus ClpC ChaperoneSemantic proximity Read ↗

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