Recombinant expression of HIV-1 protease using soluble fusion tags in Escherichia coli: A vital tool for functional characterization of HIV-1 protease

S Eche, ML Gordon - Virus Research, 2021 - Elsevier
HIV-1 protease expression in the laboratory is demanding because of its high cytotoxicity,
making it difficult to express in bacterial expression systems such as Escherichia coli. To …

Recombinant expression of HIV-1 protease using soluble fusion tags in Escherichia coli: A vital tool for functional characterization of HIV-1 protease.

S Eche, ML Gordon - Virus Research, 2021 - europepmc.org
HIV-1 protease expression in the laboratory is demanding because of its high cytotoxicity,
making it difficult to express in bacterial expression systems such as Escherichia coli. To …

Recombinant expression of HIV-1 protease using soluble fusion tags in Escherichia coli: a vital tool for functional characterization of HIV-1 protease.

S Eche, ML Gordon - 2021 - cabidigitallibrary.org
HIV-1 protease expression in the laboratory is demanding because of its high cytotoxicity,
making it difficult to express in bacterial expression systems such as Escherichia coli. To …

Recombinant expression of HIV-1 protease using soluble fusion tags in Escherichia coli: A vital tool for functional characterization of HIV-1 protease

S Eche, ML Gordon - Virus research, 2021 - pubmed.ncbi.nlm.nih.gov
HIV-1 protease expression in the laboratory is demanding because of its high cytotoxicity,
making it difficult to express in bacterial expression systems such as Escherichia coli. To …

[引用][C] Recombinant expression of HIV-1 protease using soluble fusion tags in Escherichia coli: A vital tool for functional characterization of HIV-1 protease

S Eche, ML Gordon - 2021