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

Exploring long-range cooperativity in the 20S proteasome core particle from Thermoplasma acidophilum using methyl-TROSY-based NMR.

Proceedings of the National Academy of Sciences of the United States of America - 10 Mar 2020

Rennella Enrico, Huang Rui, Yu Zanlin, Kay Lewis E

Abstract excerpt

The 20S core particle (CP) proteasome is a molecular assembly catalyzing the degradation of misfolded proteins or proteins no longer required for function. It is composed of four stacked heptameric rings that form a barrel-like structure, sequestering proteolytic sites inside its lumen. Proteasome function is regulated by gates derived from the termini of α-rings and through binding of regulatory particles (RPs)...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Archaeal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Magnetic Resonance Spectroscopy

Share to Mutation

Share to Proteasome Endopeptidase Complex

Share to Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 32094174
DOI: 10.1073/pnas.1920770117
PMCID: PMC7071895

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exploring long-range cooperativity in the 20S proteasome core particle from Thermoplasma acidophilum using methyl-TROSY-based NMR.PMID 32094174Read ↗

Conformational maps of human 20S proteasomes reveal PA28- and immuno-dependent inter-ring crosstalksSemantic proximity Read ↗

A tetrahedral transition state at the active sites of the 20S proteasome is coupled to opening of the alpha-ring channel.Semantic proximity Read ↗

Minimal mechanistic component of proteasome activation and prevention of impairment by pathological oligomersSemantic proximity Read ↗

Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly.Semantic proximity Read ↗

Allosteric network of dynamic coupling within BAP1-UCH revealed by methyl NMR.Semantic proximity Read ↗

Dissecting the role of interprotomer cooperativity in the activation of oligomeric high-temperature requirement A2 protein.Semantic proximity Read ↗

NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function.Semantic proximity Read ↗

Minimal mechanistic component of HbYX-dependent proteasome activationSemantic proximity Read ↗

Chemical shift imprint of intersubunit communication in a symmetric homodimer.Semantic proximity Read ↗

The importance of proteasome grip depends on substrate stability.Semantic proximity Read ↗

ATPase and Protease Domain Movements in the Bacterial AAA+ Protease FtsH Are Driven by Thermal Fluctuations.Semantic proximity Read ↗

Genetic Encoding of N6-(((Trimethylsilyl)methoxy)carbonyl)-l-lysine for NMR Studies of Protein-Protein and Protein-Ligand Interactions.Semantic proximity Read ↗

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