ReviewJournal of molecular medicine (Berlin, Germany)2005
Targeting protein-protein interactions for cancer therapy.
Review in Journal of molecular medicine (Berlin, Germany), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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
54 citing papers in PubMed.
- Engineering selective amyloid precursor protein inhibitors by machine learning and deep mutational scanning.Protein science : a publication of the Protein Society · 2026Article
- Enhancing mutation impact prediction in protein-protein interactions through interpretable graph-based multi-level feature interactions.Bioinformatics (Oxford, England) · 2026Article
- Orally Bioavailable Cyclin A/B RxL Inhibitors: Optimization of a Novel Class of Macrocyclic Peptides That Target E2F-High and G1-S-Checkpoint-Compromised Cancers.Journal of medicinal chemistry · 2026Article
- A tethered yeast surface display system facilitates enriching epitope-specific binding interactions.Protein engineering, design & selection : PEDS · 2026Article
- Reliable prediction of protein-protein binding affinity changes upon mutations with Pythia-PPI.National science review · 2025Article
- Rational design of small-sized peptidomimetic inhibitors disrupting protein-protein interaction.RSC medicinal chemistry · 2024Review
- Identification, characterization, and prognosis investigation of pivotal genes shared in different stages of breast cancer.Scientific reports · 2023Article
- Using the Cyclotide Scaffold for Targeting Biomolecular Interactions in Drug Development.Molecules (Basel, Switzerland) · 2022Review
- Functional inhibition of c-Myc using novel inhibitors identified through "hot spot" targeting.The Journal of biological chemistry · 2022Article
- Selective Disruption of Survivin's Protein-Protein Interactions: A Supramolecular Approach Based on Guanidiniocarbonylpyrrole.Chembiochem : a European journal of chemical biology · 2022Article
- Engineered variants of the Ras effector protein RASSF5 (NORE1A) promote anticancer activities in lung adenocarcinoma.The Journal of biological chemistry · 2021Article
- Tumor relevant protein functional interactions identified using bipartite graph analyses.Scientific reports · 2021Article
- DLC1 SAM domain-binding peptides inhibit cancer cell growth and migration by inactivating RhoA.The Journal of biological chemistry · 2020Article
- The Potential of the Cyclotide Scaffold for Drug Development.Biomedicines · 2019Review
- HIF-1α-derived cell-penetrating peptides inhibit ERK-dependent activation of HIF-1 and trigger apoptosis of cancer cells under hypoxia.Cellular and molecular life sciences : CMLS · 2019Article
- Co-operative intra-protein structural response due to protein-protein complexation revealed through thermodynamic quantification: study of MDM2-p53 binding.Journal of computer-aided molecular design · 2017Article
- Targeting protein-protein interactions in hematologic malignancies: still a challenge or a great opportunity for future therapies?Immunological reviews · 2015Review
- The role of HTS in drug discovery at the University of Michigan.Combinatorial chemistry & high throughput screening · 2014Review
- Druggable orthosteric and allosteric hot spots to target protein-protein interactions.Current pharmaceutical design · 2014Review
- Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An increasing number of protein-protein interactions have been identified as potential intervention points for the development of anticancer agents. However, such systems have historically been considered high-risk targets due to the relatively large interaction surfaces involved in protein-protein binding. This characterization has to be reexamined as progress has been made recently in identifying small-molecule inhibitors of several protein-protein systems in oncology including the p53-MDM2 interaction. This review presents a survey of protein-protein interactions that have been identified as potential oncology targets and evaluates their attractiveness in terms of drug discovery. The analysis focuses primarily on the structural characteristics of the participating binding sites, particularly the dimensions of the sites. Known ligands are also examined, especially with regard to their druglikeness.
Indexed as
Identifiers
16283145What 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.