![SARS-CoV 3CLpro cleavage sites and the canonical recognition sequence.... | Download Scientific Diagram SARS-CoV 3CLpro cleavage sites and the canonical recognition sequence.... | Download Scientific Diagram](https://www.researchgate.net/publication/51381135/figure/fig2/AS:873729412317188@1585324733629/SARS-CoV-3CLpro-cleavage-sites-and-the-canonical-recognition-sequence-The-11-recognition.jpg)
SARS-CoV 3CLpro cleavage sites and the canonical recognition sequence.... | 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-t001.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/large/cb9b00539_0007.jpeg)
Quantitative Analysis of the Substrate Specificity of Human Rhinovirus 3C Protease and Exploration of Its Substrate Recognition Mechanisms | ACS Chemical Biology
![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
![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
Rhinovirus 3C Protease Facilitates Specific Nucleoporin Cleavage and Mislocalisation of Nuclear Proteins in Infected Host Cells | 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
![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
![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
![Whole-Genome Sequence Analysis Reveals the Enterovirus D68 Isolates during the United States 2014 Outbreak Mainly Belong to a Novel Clade | Scientific Reports Whole-Genome Sequence Analysis Reveals the Enterovirus D68 Isolates during the United States 2014 Outbreak Mainly Belong to a Novel Clade | Scientific Reports](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fsrep15223/MediaObjects/41598_2015_Article_BFsrep15223_Fig6_HTML.jpg)
Whole-Genome Sequence Analysis Reveals the Enterovirus D68 Isolates during the United States 2014 Outbreak Mainly Belong to a Novel Clade | Scientific Reports
![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
Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production | PLOS ONE
![Uncovering targets of the Leader protease: Linking RNA‐mediated pathways and antiviral defense - Saiz - 2021 - WIREs RNA - Wiley Online Library Uncovering targets of the Leader protease: Linking RNA‐mediated pathways and antiviral defense - Saiz - 2021 - WIREs RNA - Wiley Online Library](https://wires.onlinelibrary.wiley.com/cms/asset/e71095d1-7ea7-4a2c-a33b-9e9511ddecc5/wrna1645-fig-0002-m.jpg)