Observational studyScientific reports2021
Proteomic and molecular dynamic investigations of PTM-induced structural fluctuations in breast and ovarian cancer.
Observational study in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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.
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
13 citing papers in PubMed, 17 citations in OpenAlex.
- PTM encoding: decoding the mechanisms of exercise-induced metabolic memory through spatiotemporal modification networks.Frontiers in sports and active living · 2026Review
- Aberrant Sialylation in Ovarian Cancer: Orchestrating Progression, Metastasis, and Therapeutic Hurdles.Current medical science · 2025Review
- Peptide Biomarkers - An Emerging Diagnostic Tool and Current Applicable Assay.Current protein & peptide science · 2025Review
- Advances in Prediction of Posttranslational Modification Sites Known to Localize in Protein Supersecondary Structures.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Targeted inhibition of SUMOylation: treatment of tumors.Human cell · 2024Review
- Pronucleotide Probes Reveal a Diverging Specificity for AMPylation vs UMPylation of Human and Bacterial Nucleotide Transferases.Biochemistry · 2024Article
- Plasma proteome fingerprint in kidney diseases.Frontiers in molecular biosciences · 2024Article
- Circulating and non-circulating proteins and nucleic acids as biomarkers and therapeutic molecules in ovarian cancer.Genes & diseases · 2023Review
- Proteomics as a New-Generation Tool for Studying Moulds Related to Food Safety and Quality.International journal of molecular sciences · 2023Review
- PSSNet-An Accurate Super-Secondary Structure for Protein Segmentation.International journal of molecular sciences · 2022Article
- Identification of Dihydrolipoamide Dehydrogenase as Potential Target of Vemurafenib-Resistant Melanoma Cells.Molecules (Basel, Switzerland) · 2022Article
- Applications of Tandem Mass Spectrometry (MS/MS) in Protein Analysis for Biomedical Research.Molecules (Basel, Switzerland) · 2022Review
- Current Approaches in Supersecondary Structures Investigation.International journal of molecular sciences · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational processing leads to conformational changes in protein structure that modulate molecular functions and change the signature of metabolic transformations and immune responses. Some post-translational modifications (PTMs), such as phosphorylation and acetylation, are strongly related to oncogenic processes and malignancy. This study investigated a PTM pattern in patients with gender-specific ovarian or breast cancer. Proteomic profiling and analysis of cancer-specific PTM patterns were performed using high-resolution UPLC-MS/MS. Structural analysis, topology, and stability of PTMs associated with sex-specific cancers were analyzed using molecular dynamics modeling. We identified highly specific PTMs, of which 12 modified peptides from eight distinct proteins derived from patients with ovarian cancer and 6 peptides of three proteins favored patients from the group with breast cancer. We found that all defined PTMs were localized in the compact and stable structural motifs exposed outside the solvent environment. PTMs increase the solvent-accessible surface area of the modified moiety and its active environment. The observed conformational fluctuations are still inadequate to activate the structural degradation and enhance protein elimination/clearance; however, it is sufficient for the significant modulation of protein activity.
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.