Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A comprehensive protein design protocol to identify resistance mutations and signatures of adaptation in pathogens.

Briefings in functional genomics - 13 Apr 2023

Padhi Aditya K, Tripathi Timir

Abstract excerpt

Most pathogens mutate and evolve over time to escape immune and drug pressure. To achieve this, they alter specific hotspot residues in their intracellular proteins to render the targeted drug(s) ineffective and develop resistance. Such hotspot residues may be located as a cluster or uniformly as a signature of adaptation in a protein. Identifying the hotspots and signatures is extremely important to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antiviral Agents
Share to COVID-19
Share to Hepacivirus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Source

Identifiers

PMID: 35851634
DOI: 10.1093/bfgp/elac020

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A comprehensive protein design protocol to identify resistance mutations and signatures of adaptation in pathogens.PMID 35851634Read ↗

Hotspot residues and resistance mutations in the nirmatrelvir-binding site of SARS-CoV-2 main protease: Design, identification, and correlation with globally circulating viral genomes.Semantic proximity Read ↗

Targeted design of drug binding sites in the main protease of SARS-CoV-2 reveals potential signatures of adaptation.Semantic proximity Read ↗

Predicting Nirmatrelvir Resistance in SARS-CoV-2 Mpro Mutants with an Integrated Computational Framework.Semantic proximity Read ↗

Computer prediction of drug resistance mutations in proteins.Semantic proximity Read ↗

Improvement in predicting drug sensitivity changes associated with protein mutations using a molecular dynamics based alchemical mutation method.Semantic proximity Read ↗

High-throughput rational design of the remdesivir binding site in the RdRp of SARS-CoV-2: implications for potential resistanceSemantic proximity Read ↗

Resistor: An algorithm for predicting resistance mutations via Pareto optimization over multistate protein design and mutational signatures.Semantic proximity Read ↗

Computational Estimation of Residues Involving Resistance to the SARS-CoV-2 Main Protease Inhibitor Ensitrelvir Based on Virtual Alanine Scan of the Active Site.Semantic proximity Read ↗

Structural Proteomics-Driven Targeted Design of Favipiravir-Binding Site in The RdRp of SARS-CoV-2 Unravels Susceptible Hotspots and Resistance MutationsSemantic proximity Read ↗

Structure-based methods for predicting target mutation-induced drug resistance and rational drug design to overcome the problem.Semantic proximity Read ↗

Modeling Binding Affinity of Pathological Mutations for Computational Protein Design.Semantic proximity Read ↗

Computational Methods to Target Protein-Protein Interactions.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.