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Literature DB >> 2560758

Structural alignment of retroviral protease sequences.

Abstract

All the known retroviral proteases can be accommodated into the structural alignment of the Rous sarcoma virus and human immunodeficiency virus proteases.

Entities: Species

Mesh：

Substances：
Peptide Hydrolases

Year: 1989 PMID： 2560758 DOI： 10.1016/0378-1119(89)90453-8

Source DB: PubMed Journal: Gene ISSN： 0378-1119 Impact factor: 3.688

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Cited

6 in total

1. Deletion of sequences upstream of the proteinase improves the proteolytic processing of human immunodeficiency virus type 1.

Authors: K Partin; G Zybarth; L Ehrlich; M DeCrombrugghe; E Wimmer; C Carter
Journal: Proc Natl Acad Sci U S A Date: 1991-06-01 Impact factor: 11.205

2. A mutation in human immunodeficiency virus type 1 protease at position 88, located outside the active site, confers resistance to the hydroxyethylurea inhibitor SC-55389A.

Authors: M L Smidt; K E Potts; S P Tucker; L Blystone; T R Stiebel; W C Stallings; J J McDonald; D Pillay; D D Richman; M L Bryant
Journal: Antimicrob Agents Chemother Date: 1997-03 Impact factor: 5.191

Structural alignment of retroviral protease sequences.

1. Deletion of sequences upstream of the proteinase improves the proteolytic processing of human immunodeficiency virus type 1.

2. A mutation in human immunodeficiency virus type 1 protease at position 88, located outside the active site, confers resistance to the hydroxyethylurea inhibitor SC-55389A.

3. Complete nucleotide sequence and transcriptional analysis of snakehead fish retrovirus.

4. HIV-1 protease function and structure studies with the simplicial neighborhood analysis of protein packing method.

Review 5. HIV Protease: Historical Perspective and Current Research.

6. Bioinformatic flowchart and database to investigate the origins and diversity of clan AA peptidases.