![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
Quantitative Analysis of the Substrate Specificity of Human Rhinovirus 3C Protease and Exploration of Its Substrate Recognition Mechanisms | ACS Chemical Biology
![A) Three tags, i.e. 10x-His, FLAG and HA, and one proteolytic site for... | Download Scientific Diagram A) Three tags, i.e. 10x-His, FLAG and HA, and one proteolytic site for... | Download Scientific Diagram](https://www.researchgate.net/publication/51494266/figure/fig1/AS:213899933687821@1428009126508/A-Three-tags-ie-10x-His-FLAG-and-HA-and-one-proteolytic-site-for-the-HRV3C.png)
A) Three tags, i.e. 10x-His, FLAG and HA, and one proteolytic site for... | Download Scientific Diagram
Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production | PLOS ONE
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
![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)