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

Electron microscopic evidence in support of alpha-solenoid models of proteasomal subunits Rpn1 and Rpn2.

Journal of molecular biology - 13 Mar 2009

Effantin Grégory, Rosenzweig Rina, Glickman Michael H, Steven Alasdair C

Abstract excerpt

Rpn1 (109 kDa) and Rpn2 (104 kDa) are components of the 19S regulatory complex of the proteasome. The central portions of both proteins are predicted to have toroidal alpha-solenoid folds composed of 9-11 proteasome/cyclosome repeats, each approximately 40 residues long and containing two alpha-helices and turns [A. V. Kajava, J. Biol. Chem. 277, 49791-49798, 2002]. To evaluate this prediction, we examined the...

Read the complete abstract on PubMed

Topics

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

Share to Chromatography, Gel
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Electron, Transmission

Share to Models, Molecular

Share to Proteasome Endopeptidase Complex

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 19361443
DOI: 10.1016/j.jmb.2009.01.039
PMCID: PMC2671960

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Electron microscopic evidence in support of alpha-solenoid models of proteasomal subunits Rpn1 and Rpn2.PMID 19361443Read ↗

Classification of Single Particles from Human Cell Extract Reveals Distinct StructuresSemantic proximity Read ↗

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

Cryo-EM Structure of the Full-length hnRNPA1 Amyloid Fibril.Semantic proximity Read ↗

Structural basis of human 20S proteasome biogenesisSemantic proximity Read ↗

New crystal structure of the proteasome-dedicated chaperone Rpn14 at 1.6 Å resolution.Semantic proximity Read ↗

Visualizing chaperone-mediated multistep assembly of the human 20S proteasomeSemantic proximity Read ↗

Structural basis for proteasome formation controlled by an assembly chaperone nas2.Semantic proximity Read ↗

Identification of a Non-canonical Function of Prefoldin Subunit 5 in Proteasome AssemblySemantic proximity Read ↗

Crystal structure of yeast rpn14, a chaperone of the 19 S regulatory particle of the proteasome.Semantic proximity Read ↗

Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes.Semantic proximity Read ↗

Electron cryomicroscopy structure of a membrane-anchored mitochondrial AAA protease.Semantic proximity Read ↗

Dissection of the carboxyl-terminal domain of the proteasomal subunit Rpn11 in maintenance of mitochondrial structure and function.Semantic proximity Read ↗

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