Evidence map›Paper›PMID 36961377›Full record

ArticleJournal of proteome research2023

OpenCustomDB: Integration of Unannotated Open Reading Frames and Genetic Variants to Generate More Comprehensive Customized Protein Databases.

Noé Guilloy, Marie A Brunet, Sébastien Leblanc, Jean-François Jacques, Marie-Pierre Hardy, Grégory Ehx, Joël Lanoix, Pierre Thibault, Claude Perreault, Xavier Roucou

Open access · hybridAbstract read
In one paragraph

Article in Journal of proteome research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
5.6field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 2 countries.

Noé GuilloyDepartment of Biochemistry and Functional Genomics, Université de Sherbrooke, Sherbrooke, Québec J1E 4K8, Canada.
Marie A BrunetDepartment of Pediatrics, Université de Sherbrooke, Sherbrooke, Québec J1E 4K8, Canada.
Sébastien LeblancDepartment of Biochemistry and Functional Genomics, Université de Sherbrooke, Sherbrooke, Québec J1E 4K8, Canada.
Jean-François JacquesDepartment of Biochemistry and Functional Genomics, Université de Sherbrooke, Sherbrooke, Québec J1E 4K8, Canada.
Marie-Pierre HardyInstitute for Research in Immunology and Cancer, Université de Montréal, Montreal, Québec H3C 3J7, Canada.
Grégory EhxInterdisciplinary Cluster for Applied Geno-Proteomics (GIGA-I3), University of Liège, Liège B-4000, Belgium.
Joël LanoixInstitute for Research in Immunology and Cancer, Université de Montréal, Montreal, Québec H3C 3J7, Canada.
Pierre ThibaultInstitute for Research in Immunology and Cancer, Université de Montréal, Montreal, Québec H3C 3J7, Canada.ORCID 0000-0001-5993-0331
Claude PerreaultInstitute for Research in Immunology and Cancer, Université de Montréal, Montreal, Québec H3C 3J7, Canada.ORCID 0000-0001-9453-7383
Xavier RoucouDepartment of Biochemistry and Functional Genomics, Université de Sherbrooke, Sherbrooke, Québec J1E 4K8, Canada.ORCID 0000-0001-9370-5584
Université de Sherbrooke · CAInstitute for Research in Immunology and Cancer · CAUniversity of Liège · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteomic diversity in biological samples can be characterized by mass spectrometry (MS)-based proteomics using customized protein databases generated from sets of transcripts previously detected by RNA-seq. This diversity has only been increased by the recent discovery that many translated alternative open reading frames rest unannotated at unsuspected locations of mRNAs and ncRNAs. These novel protein products, termed alternative proteins, have been left out of all previous custom database generation tools. Consequently, genetic variations that impact alternative open reading frames and variant peptides from their translated proteins are not detectable with current computational workflows. To fill this gap, we present OpenCustomDB, a bioinformatics tool that uses sample-specific RNaseq data to identify genomic variants in canonical and alternative open reading frames, allowing for more than one coding region per transcript. In a test reanalysis of a cohort of 16 patients with acute myeloid leukemia, 5666 peptides from alternative proteins were detected, including 201 variant peptides. We also observed that a significant fraction of peptide-spectrum matches previously assigned to peptides from canonical proteins got better scores when reassigned to peptides from alternative proteins. Custom protein libraries that include sample-specific sequence variations of all possible open reading frames are promising contributions to the development of proteomics and precision medicine. The raw and processed proteomics data presented in this study can be found in PRIDE repository with accession number PXD029240.

Indexed as

ProteinsProteomicsDatabases, ProteinHumansOpen Reading FramesPeptidesPeptidesProteinsalternative ORFsalternative proteinsdatabasemulticodingprecision medicineproteogenomicsvariants

Identifiers

PMID36961377
PMCPMC10167680
OpenAlexW4360812610

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.