Structural Role of the 30's Loop in Determining the Ligand Specificity of the Human Immunodeficiency Virus Protease,-Reference-Cited by-同舟云学术

Structural Role of the 30's Loop in Determining the Ligand Specificity of the Human Immunodeficiency Virus Protease,

Published:1998-07-17 Issue:31 Volume:37 Page:10928-10936
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Swairjo Manal A.¹,Towler Eric M.¹,Debouck Christine¹,Abdel-Meguid Sherin S.¹

Affiliation:

1. Departments of Structural Biology and Molecular Biology, SmithKline Beecham Pharmaceuticals, 709 Swedeland Road, King of Prussia, Pennsylvania 19406

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi980784h

Reference25 articles.

1. Human immunodeficiency virus protease expressed in Escherichia coli exhibits autoprocessing and specific maturation of the gag precursor.

2. Active human immunodeficiency virus protease is required for viral infectivity.

3. Human immunodeficiency virus 1 protease expressed in Escherichia coli behaves as a dimeric aspartic protease.

4. Conserved Folding in Retroviral Proteases: Crystal Structure of Synthetic HIV-1 Protease

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