![A split protease-E. coli ClpXP system quantifies protein–protein interactions in Escherichia coli cells | Communications Biology A split protease-E. coli ClpXP system quantifies protein–protein interactions in Escherichia coli cells | Communications Biology](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs42003-021-02374-w/MediaObjects/42003_2021_2374_Fig1_HTML.png)
A split protease-E. coli ClpXP system quantifies protein–protein interactions in Escherichia coli cells | Communications Biology
![Expression and purification of a cleavable recombinant fortilin from Escherichia coli for structure activity studies - ScienceDirect Expression and purification of a cleavable recombinant fortilin from Escherichia coli for structure activity studies - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S1046592821001728-gr2.jpg)
Expression and purification of a cleavable recombinant fortilin from Escherichia coli for structure activity studies - ScienceDirect
![Quantitative Analysis of the Substrate Specificity of Human Rhinovirus 3C Protease and Exploration of Its Substrate Recognition Mechanisms | ACS Chemical Biology Quantitative Analysis of the Substrate Specificity of Human Rhinovirus 3C Protease and Exploration of Its Substrate Recognition Mechanisms | ACS Chemical Biology](https://pubs.acs.org/cms/10.1021/acschembio.9b00539/asset/images/medium/cb9b00539_0004.gif)
Quantitative Analysis of the Substrate Specificity of Human Rhinovirus 3C Protease and Exploration of Its Substrate Recognition Mechanisms | ACS Chemical Biology
Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production | PLOS ONE
![Directed evolution of the 3C protease from coxsackievirus using a novel fluorescence-assisted intracellular method Directed evolution of the 3C protease from coxsackievirus using a novel fluorescence-assisted intracellular method](https://www.degruyter.com/document/doi/10.1515/hsz-2018-0362/asset/graphic/j_hsz-2018-0362_fig_001.jpg)
Directed evolution of the 3C protease from coxsackievirus using a novel fluorescence-assisted intracellular method
Quantitative Analysis of the Substrate Specificity of Human Rhinovirus 3C Protease and Exploration of Its Substrate Recognition Mechanisms | ACS Chemical Biology
![Enzymes - Tobacco Etch Virus (TEV) and Human RhinoVirus (HRV3C) Cysteine Proteases in Vectors | ATUM - ATUM Enzymes - Tobacco Etch Virus (TEV) and Human RhinoVirus (HRV3C) Cysteine Proteases in Vectors | ATUM - ATUM](https://www.atum.bio/graph-data/catalog/Enzymes/TEV_Protease_Process.png)
Enzymes - Tobacco Etch Virus (TEV) and Human RhinoVirus (HRV3C) Cysteine Proteases in Vectors | ATUM - ATUM
Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production | PLOS ONE
![NT*-HRV3CP: An optimized construct of human rhinovirus 14 3C protease for high-yield expression and fast affinity-tag cleavage - ScienceDirect NT*-HRV3CP: An optimized construct of human rhinovirus 14 3C protease for high-yield expression and fast affinity-tag cleavage - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0168165620303060-ga1.jpg)
NT*-HRV3CP: An optimized construct of human rhinovirus 14 3C protease for high-yield expression and fast affinity-tag cleavage - ScienceDirect
![Figures and data in Proteolytic maturation of α2δ represents a checkpoint for activation and neuronal trafficking of latent calcium channels | eLife Figures and data in Proteolytic maturation of α2δ represents a checkpoint for activation and neuronal trafficking of latent calcium channels | eLife](https://iiif.elifesciences.org/lax/21143%2Felife-21143-fig3-v3.tif/full/,1500/0/default.jpg)
Figures and data in Proteolytic maturation of α2δ represents a checkpoint for activation and neuronal trafficking of latent calcium channels | eLife
![Human Rhinovirus 3C protease cleaves RIPK1, concurrent with caspase 8 activation | Scientific Reports Human Rhinovirus 3C protease cleaves RIPK1, concurrent with caspase 8 activation | Scientific Reports](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41598-018-19839-4/MediaObjects/41598_2018_19839_Fig1_HTML.jpg)
Human Rhinovirus 3C protease cleaves RIPK1, concurrent with caspase 8 activation | Scientific Reports
![SDS-PAGE showing the HRV 3C protease activity in the presence various... | Download Scientific Diagram SDS-PAGE showing the HRV 3C protease activity in the presence various... | Download Scientific Diagram](https://www.researchgate.net/publication/301533941/figure/fig2/AS:354812571996163@1461605317538/SDS-PAGE-showing-the-HRV-3C-protease-activity-in-the-presence-various-buffers-increasing.png)