ArticleNature structural & molecular biology2010
Hybrid molecular structure of the giant protease tripeptidyl peptidase II.
Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 30 citations in OpenAlex.
- Chameleon sequences-Structural effects.PloS one · 2025Article
- The protein organization of a red blood cell.Cell reports · 2022Article
- How metal cofactors drive dimer-dodecamer transition of the M42 aminopeptidase TmPep1050 ofThe Journal of biological chemistry · 2019Article
- Infinite Assembly of Folded Proteins in Evolution, Disease, and Engineering.Angewandte Chemie (International ed. in English) · 2019Review
- Quantifying the Limits of Detection of Surface-Enhanced Infrared Spectroscopy with Grating Order-Coupled Nanogap Antennas.ACS photonics · 2018Article
- In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Post-proteasomal and proteasome-independent generation of MHC class I ligands.Cellular and molecular life sciences : CMLS · 2011Review
- EMDataBank.org: unified data resource for CryoEM.Nucleic acids research · 2011Article
- Article
- Tripeptidyl Peptidase II Is Required for c-MYC-Induced Centriole Overduplication and a Novel Therapeutic Target in c-MYC-Associated Neoplasms.Genes & cancer · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Tripeptidyl peptidase II (TPP II) is the largest known eukaryotic protease (6 MDa). It is believed to act downstream of the 26S proteasome, cleaving tripeptides from the N termini of longer peptides, and it is implicated in numerous cellular processes. Here we report the structure of Drosophila TPP II determined by a hybrid approach. We solved the structure of the dimer by X-ray crystallography and docked it into the three-dimensional map of the holocomplex, which we obtained by single-particle cryo-electron microscopy. The resulting structure reveals the compartmentalization of the active sites inside a system of chambers and suggests the existence of a molecular ruler determining the size of the cleavage products. Furthermore, the structure suggests a model for activation of TPP II involving the relocation of a flexible loop and a repositioning of the active-site serine, coupling it to holocomplex assembly and active-site sequestration.
Indexed as
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.