ReviewCurrent pharmaceutical design2012
Computational prediction of protein hot spot residues.
Review in Current pharmaceutical design, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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
52 citing papers in PubMed.
- Untangling the Complexity of Binding Across Biomolecular Interfaces with Interaction Network Models.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Breaking the oncogenic alliance: advances in disrupting the MTDH-SND1 complex for cancer therapy.RSC advances · 2025Review
- Predicting interacting hotspots for nanobodies' binding using triplets of residues.Protein science : a publication of the Protein Society · 2025Article
- Prediction of virus-host interactions and identification of hot spot residues of DENV-2 and SH3 domain interactions.Archives of microbiology · 2024Article
- Single-domain antibodies against SARS-CoV-2 RBD from a two-stage phage screening of universal and focused synthetic libraries.BMC infectious diseases · 2024Article
- Design of ion channel blocking, toxin-like Kunitz inhibitor peptides from the tapeworm, Echinococcus granulosus, with potential anti-cancer activity.Scientific reports · 2023Article
- Targeting Peptides: The New Generation of Targeted Drug Delivery Systems.Pharmaceutics · 2023Review
- xProtCAS: A Toolkit for Extracting Conserved Accessible Surfaces from Protein Structures.Biomolecules · 2023Article
- Interrupting specific hydrogen bonds between ELF3 and MED23 as an alternative drug resistance-free strategy for HER2-overexpressing cancers.Journal of advanced research · 2023Article
- Article
- Cold spots are universal in protein-protein interactions.Protein science : a publication of the Protein Society · 2022Article
- In Silico Prediction ofPharmaceuticals (Basel, Switzerland) · 2022Article
- In Silico Insights towards the Identification of SARS-CoV-2 NSP13 Helicase Druggable Pockets.Biomolecules · 2022Article
- Interpreting the spectrum of gamma-secretase complex missense variation in the context of hidradenitis suppurativa-AnFrontiers in genetics · 2022Article
- Targeting protein-protein interactions in the DNA damage response pathways for cancer chemotherapy.RSC chemical biology · 2021Review
- Review
- Grafting Methionine on 1F1 Ab Increases the Broad-Activity on HA Structural-Conserved Residues of H1, H2, and H3 Influenza a Viruses.Evolutionary bioinformatics online · 2021Article
- Untangling a complex web: Computational analyses of tumor molecular profiles to decode driver mechanisms.Journal of genetics and genomics = Yi chuan xue bao · 2020Review
- SPOTONE: Hot Spots on Protein Complexes with Extremely Randomized Trees via Sequence-Only Features.International journal of molecular sciences · 2020Article
- Identification of a Potential Peptide Inhibitor of SARS-CoV-2 Targeting its Entry into the Host Cells.Drugs in R&D · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Most biological processes involve multiple proteins interacting with each other. It has been recently discovered that certain residues in these protein-protein interactions, which are called hot spots, contribute more significantly to binding affinity than others. Hot spot residues have unique and diverse energetic properties that make them challenging yet important targets in the modulation of protein-protein complexes. Design of therapeutic agents that interact with hot spot residues has proven to be a valid methodology in disrupting unwanted protein-protein interactions. Using biological methods to determine which residues are hot spots can be costly and time consuming. Recent advances in computational approaches to predict hot spots have incorporated a myriad of features, and have shown increasing predictive successes. Here we review the state of knowledge around protein-protein interactions, hot spots, and give an overview of multiple in silico prediction techniques of hot spot residues.
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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.