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ProteomicsAnti-tumor immunity induces the presentation of aberrant peptides in melanoma
Many tumors escape by activating multiple cellular pathways that induce immunosuppression. One pivotal immune-suppressive mechanism is the production of tryptophan metabolites along the kynurenine pathway by IFNγ-induced IDO1 enzyme production 4-8. Phase III clinical trials using chemical inhibition...
ORGANISM(S): Homo sapiens (Human) 
2020-12-04 | PXD020224 | Pride
Immune recognition Proteomics Melanoma Tryptophan depletion Immunopeptidomics Aberrant peptides Lc-ms/ms 
TranscriptomicsAtypical DNA methylation of genes encoding cysteine-rich peptides in Arabidopsis thaliana
In plants, transposons and non-protein-coding repeats are epigenetically silenced by CG and non-CG methylation. This pattern of methylation is mediated in part by small RNAs and two specialized RNA polymerases, Pol IV and Pol V, in a process called RNA-directed DNA methylation. By contrast, many pr...
ORGANISM(S): Arabidopsis thaliana 
2012-11-22 | E-GEOD-34207 | biostudies-arrayexpress
GenomicsAnti-tumor immunity induces the presentation of aberrant peptides in melanoma
Anti-tumor immunity induces the presentation of aberrant peptides in melanoma
PRJNA598557 | ENA
ProteomicsThe effect of interferons on presentation of defective ribosome products as HLA peptides
The class I major histocompatibility complex (MHC) bound peptides, produced from immature proteins that are degraded rapidly are called defective ribosome products (DRiPs). Such DRiPs are possibly involved with early alerting of the immune system about impeding infections, thus bringing about faster...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-10-25 | MSV000096209 | MassIVE
ProteomicsChemotherapy-induced codon-specific immunopeptidome diversification
Deregulated mRNA translation in cancer is a source of aberrant protein production when tryptophan shortage is induced by anti-tumor immunity (refs). Tryptophan is decoded by only one codon, and currently the consequences of aberrant protein production in conditions of a shortage of amino acids decod...
ORGANISM(S): Homo sapiens (Human) 
2025-05-06 | PXD044085 | Pride
Aberrant protein Mrna translation Tryptophan Leucine Ribosomal stalling Immunopeptidomics Neoepitopes 
TranscriptomicsAnti-tumor immunity induces the presentation of aberrant peptides in melanoma
Extensive tumor inflammation, reflected by high levels of infiltrating T-cells and Interferon gamma (IFNγ) signaling, is thought to improve checkpoint immunotherapy response. However, many tumors escape by activating multiple cellular pathways that induce immunosuppression. One pivotal immune-suppre...
ORGANISM(S): Homo sapiens 
2020-10-18 | GSE142822 | GEO
TranscriptomicsDifferent gene expressions in root tips between CLE10 and CLE25 treatment
Cell–cell communication is critical for tissue and organ development. In plants, secretory CLAVATA3/EMBRYO SURROUNDING REGION-related (CLE) peptides function as intercellular signaling molecules in various aspects of tissue development. However, little is known about intracellular signaling pathways...
ORGANISM(S): Arabidopsis thaliana 
2010-09-03 | E-GEOD-19978 | biostudies-arrayexpress
UnknownAberrant phase separation is a common killing strategy of positively charged peptides in biology and human disease.
Not available
S-EPMC10028949 | biostudies-literature
TranscriptomicsA genomic approach highlights common and diverse effects and determinants of susceptibility on the yeast Saccharomyces cerevisiae exposed to distinct antimicrobial peptides
The mechanism of action of antimicrobial peptides (AMPs) was initially correlated with peptide membrane permeation properties. However, recent evidences indicate that action of a number of AMPs is more complex and involves specific interactions at cell envelopes or with intracellular targets. In thi...
ORGANISM(S): Saccharomyces cerevisiae 
2010-11-11 | E-GEOD-25279 | biostudies-arrayexpress
UnknownThe ribosome-bound quality control complex remains associated to aberrant peptides during their proteasomal targeting and interacts with Tom1 to limit protein aggregation.
Not available
S-EPMC5415013 | biostudies-literature
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