ReviewBiophysical reviews2023
Structural analysis of peptide binding to integrins for cancer detection and treatment.
Review in Biophysical reviews, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- 2-Alkyl Furans Undergo Radiolytic Oxidative Protein Cross-Linking.Journal of the American Chemical Society · 2026Article
- Beyond MIDAS: AnACS omega · 2026Article
- Tumor Targeting with Peptide-Drug Conjugates: Showcasing Key Progress and Hurdles.Drug design, development and therapy · 2026Review
- Imaging at the nexus: how state of the art imaging techniques can enhance our understanding of cancer and fibrosis.Journal of translational medicine · 2024Review
- Biophysical Reviews (ISSUE 4 2023): LAFeBS-highlighting biophysics in Latin America.Biophysical reviews · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integrins are cell receptors involved in several metabolic pathways often associated with cell proliferation. Some of these integrins are downregulated during human physical development, but when these integrins are overexpressed in adult humans, they can be associated with several diseases, such as cancer. Molecules that specifically bind to these integrins are useful for cancer detection, diagnosis, and treatment. This review focuses on the structures of integrin-peptidic ligand complexes to dissect how the binding occurs and the molecular basis of the specificity and affinity of these peptidic ligands. Understanding these interactions at the molecular level is fundamental to be able to design new peptides that are more specific and more sensitive to a particular integrin. The integrin complexes covered in this review are α5β1, αIIbβ3, αvβ3, αvβ6, and αvβ8, because the molecular structures of the complex have been experimentally determined and their presence on tumor cancer cells are associated with a poor prognosis, making them targets for cancer detection and treatment.
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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.