ArticleEMBO reports2007
A novel cytosolic class I antigen-processing pathway for endoplasmic-reticulum-targeted proteins.
Article in EMBO reports, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Elimination of a signal sequence-uncleaved form of defective HLA protein through BAG6.Scientific reports · 2017Article
- UBQLN4 recognizes mislocalized transmembrane domain proteins and targets these to proteasomal degradation.EMBO reports · 2016Article
- Article
- Just one position-independent lysine residue can direct MelanA into proteasomal degradation following N-terminal fusion of ubiquitin.PloS one · 2013Article
- DRiPs solidify: progress in understanding endogenous MHC class I antigen processing.Trends in immunology · 2011Review
- Translating DRiPs: progress in understanding viral and cellular sources of MHC class I peptide ligands.Cellular and molecular life sciences : CMLS · 2011Review
- Hydrophobicity as a driver of MHC class I antigen processing.The EMBO journal · 2011Article
- Defective ribosomal products are the major source of antigenic peptides endogenously generated from influenza A virus neuraminidase.Journal of immunology (Baltimore, Md. : 1950) · 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 5 institutions in 3 countries.
Funding
Abstract
Proteins bearing an endoplasmic reticulum (ER) leader are inserted into the ER followed by cleavage of the signal peptide. Major histocompatibility complex class I-restricted T-cell epitopes can be generated from these proteins by the proteasome after retrotranslocation into the cytosol. Here, we show that an HLA-A(*)0201-restricted epitope from prostate stem cell antigen contains the cleavage site of the ER signal peptidase. The resulting cleavage products fail to bind to HLA-A(*)0201 and are not recognized by T lymphocytes. As processing of prostate stem cell antigen by signal peptidase occurs immediately after co-translational insertion, the epitope must be processed from polypeptides that have never reached the ER. The processing of this epitope depends on the proteasome and the transporter associated with antigen processing and shows a novel pathway of class I processing that relies on the failure of ER-targeted proteins to reach their target compartment.
Indexed as
Identifiers
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.