ReviewMolecular biology reports1995
Proteasome and class I antigen processing and presentation.
Review in Molecular biology reports, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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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
9 citing papers in PubMed, 40 citations in OpenAlex.
- Residue 81 confers a restricted C-terminal peptide binding motif in HLA-B*44:09.Immunogenetics · 2012Article
- Comparative genomic analysis of the proteasome β5t subunit gene: implications for the origin and evolution of thymoproteasomes.Immunogenetics · 2012Article
- Interferon regulatory factor 7 mediates activation of Tap-2 by Epstein-Barr virus latent membrane protein 1.Journal of virology · 2001Article
- Mov34 protein from mouse brain interacts with the 3' noncoding region of Japanese encephalitis virus.Journal of virology · 2000Article
- Relationships between proteasomes and viral gene products.Molecular biology reports · 1999Review
- Involvement of proteasomal subunits zeta and iota in RNA degradation.The Biochemical journal · 1997Article
- Targeting of HIV-1 antigens for rapid intracellular degradation enhances cytotoxic T lymphocyte (CTL) recognition and the induction of de novo CTL responses in vivo after immunization.The Journal of experimental medicine · 1997Article
- Antigen processing by proteasomes: insights into the molecular basis of crypticity.Molecular biology reports · 1997Review
- Proteasome (prosome) associated endonuclease activity.Molecular biology reports · 1997Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recent discovery of two proteasome homologous genes, LMP2 and LMP7, in the class II region of the human MHC, has implicated this multi-subunit protease in an early step of the immune response; the degradation of intracellular and viral proteins. Short peptides produced by the proteasome are transported into the ER by the product of another set of MHC class II genes, TAP1 and TAP2, where they bind and stabilise HLA class I molecules. Antigenic peptides displayed at the cell surface by HLA class I molecules mark cells for destruction by cytotoxic T lymphocytes. The role of the proteasome in antigen processing was questioned when mutant cells, which lack the LMP genes, were able to process and present antigens normally. The discovery that two proteasome beta-subunits, delta and MB1, highly homologous to LMP2 and LMP7 and expressed in reciprocal manner, is now consistent with a role for the proteasome in antigen processing. The incorporation of different beta-subunits into the proteasome may be a mechanism to modulate catalytic activity of the proteasome complex, allowing production of peptides that are more suitable to enter into the ER by the TAP transporters and to bind HLA class I molecules. But, in the absence of the LMPs, the other subunits permit processing of most antigens reasonably efficiently.
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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.