![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
![Amino acid sequence alignment of A10 61 3C pro with the 3C proteases... | Download Scientific Diagram Amino acid sequence alignment of A10 61 3C pro with the 3C proteases... | Download Scientific Diagram](https://www.researchgate.net/publication/301673336/figure/fig1/AS:362370791690244@1463407338636/Amino-acid-sequence-alignment-of-A10-61-3C-pro-with-the-3C-proteases-from-the-four-SAT.png)
Amino acid sequence alignment of A10 61 3C pro with the 3C proteases... | Download Scientific Diagram
![Frontiers | Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus Frontiers | Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus](https://www.frontiersin.org/files/Articles/265708/fmicb-08-00745-HTML-r1/image_m/fmicb-08-00745-g001.jpg)
Frontiers | Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus
![Frontiers | Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus Frontiers | Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus](https://www.frontiersin.org/files/Articles/265708/fmicb-08-00745-HTML-r1/image_m/fmicb-08-00745-t001.jpg)
Frontiers | Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus
![Figure 2 from and Richard Protease Poly ( A )-Binding Protein by Enterovirus 3 C Efficient Cleavage of Ribosome-Associated | Semantic Scholar Figure 2 from and Richard Protease Poly ( A )-Binding Protein by Enterovirus 3 C Efficient Cleavage of Ribosome-Associated | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/99ec43a4f98e89eca9e4e2b6a18100c849d14a08/5-Figure2-1.png)
Figure 2 from and Richard Protease Poly ( A )-Binding Protein by Enterovirus 3 C Efficient Cleavage of Ribosome-Associated | Semantic Scholar
![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
![Frontiers | Running With Scissors: Evolutionary Conflicts Between Viral Proteases and the Host Immune System Frontiers | Running With Scissors: Evolutionary Conflicts Between Viral Proteases and the Host Immune System](https://www.frontiersin.org/files/MyHome%20Article%20Library/769543/769543_Thumb_400.jpg)
Frontiers | Running With Scissors: Evolutionary Conflicts Between Viral Proteases and the Host Immune System
![Frontiers | Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus Frontiers | Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus](https://www.frontiersin.org/files/Articles/265708/fmicb-08-00745-HTML-r1/image_m/fmicb-08-00745-t002.jpg)
Frontiers | Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus
![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
![Inhibitory antibodies identify unique sites of therapeutic vulnerability in rhinovirus and other enteroviruses | PNAS Inhibitory antibodies identify unique sites of therapeutic vulnerability in rhinovirus and other enteroviruses | PNAS](https://www.pnas.org/cms/10.1073/pnas.1918844117/asset/f0890041-aba3-4d74-b625-a86ce098e69e/assets/graphic/pnas.1918844117fig05.jpeg)
Inhibitory antibodies identify unique sites of therapeutic vulnerability in rhinovirus and other enteroviruses | PNAS
![Biochemical characterization of recombinant Avihepatovirus 3C protease and its localization | Virology Journal | Full Text Biochemical characterization of recombinant Avihepatovirus 3C protease and its localization | Virology Journal | Full Text](https://media.springernature.com/full/springer-static/image/art%3A10.1186%2Fs12985-019-1155-3/MediaObjects/12985_2019_1155_Fig1_HTML.png)
Biochemical characterization of recombinant Avihepatovirus 3C protease and its localization | Virology Journal | Full Text
![A simple solid phase, peptide-based fluorescent assay for the efficient and universal screening of HRV 3C protease inhibitors - ScienceDirect A simple solid phase, peptide-based fluorescent assay for the efficient and universal screening of HRV 3C protease inhibitors - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0960894X12007627-fx1.jpg)