ArticlePloS one2016
Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 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
19 citing papers in PubMed, 41 citations in OpenAlex.
- Differential Assembly of Native Epithelial Sodium Channel Complexes Across Mouse Epithelial Tissues.Kidney360 · 2026Article
- Scalable production of monovalent streptavidin with high yield and purity.Scientific reports · 2026Article
- Over-Expression of a Phycocyanin-Interferon Fusion and Differential Cleaving Efficiency in Cyanobacteria (Synechocystis sp. PCC 6803).Biotechnology and bioengineering · 2026Article
- Catch & Release-rapid cost-effective protein purification from plants using a DIY GFP-Trap-protease approach.The Plant journal : for cell and molecular biology · 2025Article
- Purification tags markedly affect self-aggregation of CPEB3.FEBS letters · 2025Article
- Monitoring of enzymatic cleavage reaction of GST-fusion protein on biolayer interferometry sensor.Biophysics and physicobiology · 2024Article
- In vivo enzymatic digestion of HRV 3C protease cleavage sites-containing proteins produced in a silkworm-baculovirus expression system.Bioscience reports · 2022Article
- DELE1 tracks perturbed protein import and processing in human mitochondria.Nature communications · 2022Article
- Contribution of domain structure to the function of the yeast DEDD family exoribonuclease and RNase T functional homolog, Rex1.RNA (New York, N.Y.) · 2022Article
- FAS2FURIOUS: Moderate-Throughput Secreted Expression of Difficult Recombinant Proteins inFrontiers in bioengineering and biotechnology · 2022Article
- The high-throughput production of membrane proteins.Emerging topics in life sciences · 2021Article
- Efficient production of a functional G protein-coupled receptor in E. coli for structural studies.Journal of biomolecular NMR · 2021Article
- Structural Basis for the Activation and Target Site Specificity of CDC7 Kinase.Structure (London, England : 1993) · 2020Article
- Characterization of the highly immunogenic VP2 protrusion domain as a diagnostic antigen for members of Birnaviridae family.Applied microbiology and biotechnology · 2020Article
- The Statistical Optimisation of Recombinant β-glucosidase Production through a Two-Stage, Multi-Model, Design of Experiments Approach.Bioengineering (Basel, Switzerland) · 2019Article
- Building and Breaking Bonds via a Compact S-Propargyl-Cysteine to Chemically Control Enzymes and Modify Proteins.Angewandte Chemie (International ed. in English) · 2018Article
- Optimization of Soluble Expression and Purification of Recombinant Human Rhinovirus Type-14 3C Protease Using Statistically Designed Experiments: Isolation and Characterization of the Enzyme.Molecular biotechnology · 2017Article
- A Mutant Sumo Facilitates Quick Plasmid Construction for Expressing Proteins with Native N-termini After Tag Removal.Molecular biotechnology · 2017Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteases are widely used to remove affinity and solubility tags from recombinant proteins to avoid potential interference of these tags with the structure and function of the fusion partner. In recent years, great interest has been seen in use of the human rhinovirus 3C protease owing to its stringent sequence specificity and enhanced activity. Like other proteases, activity of the human rhinovirus 3C protease can be affected in part by the buffer components and additives that are generally employed for purification and stabilization of proteins, hence, necessitate their removal by tedious and time-consuming procedures before proteolysis can occur. To address this issue, we examined the effect of elution buffers used for common affinity based purifications, salt ions, stability/solubility and reducing agents, and detergents on the activity of the human rhinovirus 3C protease using three different fusion proteins at 4°C, a temperature of choice for purification of many proteins. The results show that the human rhinovirus 3C protease performs better at 4°C than the frequently used tobacco etch virus protease and its activity was insensitive to most of the experimental conditions tested. Though number of fusion proteins tested is limited, we expect that these finding will facilitate the use of the human rhinovirus 3C protease in recombinant protein production for pharmaceutical and biotechnological applications.
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.