Two‐Step Preparation of Highly Pure, Soluble HIV Protease from Inclusion Bodies Recombinantly Expressed inEscherichia coli-Reference-Cited by-同舟云学术

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Two‐Step Preparation of Highly Pure, Soluble HIV Protease from Inclusion Bodies Recombinantly Expressed inEscherichia coli

Published:2020-04-27 Issue:1 Volume:100 Page:
ISSN:1934-3655
Container-title:Current Protocols in Protein Science
language:en
Short-container-title:Current Protocols in Protein Science

Author:

Sherry Dean¹,Worth Roland¹,Sayed Yasien¹

Affiliation:

1. Protein Structure‐Function Research Unit, School of Molecular and Cell BiologyUniversity of Witwatersrand Johannesburg South Africa

Funder

South African Medical Research Council

Publisher

Wiley

Subject

Biochemistry,General Medicine,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cpps.106

Reference16 articles.

1. Optimizing Primary Recovery and Refolding of Human Interferon-b from Escherichia coli Inclusion Bodies

2. Refolding of proteins from inclusion bodies: rational design and recipes

3. Isolation of mutants of human immunodeficiency virus protease based on the toxicity of the enzyme in Escherichia coli.

4. Protein refolding for industrial processes

5. Protein Identification and Analysis Tools on the ExPASy Server

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. HIV Protease Hinge Region Insertions at Codon 38 Affect Enzyme Kinetics, Conformational Stability and Dynamics;The Protein Journal;2023-07-08

2. Non-active site mutations in the HIV protease: Diminished drug binding affinity is achieved through modulating the hydrophobic sliding mechanism;International Journal of Biological Macromolecules;2022-09

3. Enyzmes | HIV Protease;Encyclopedia of Biological Chemistry III;2021

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