| P50 | author | Hans-Georg Kräusslich | Q1576991 |
| P2860 | cites work | Active human immunodeficiency virus protease is required for viral infectivity | Q24647696 |
| | Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease | Q27675079 |
| | Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease | Q27696384 |
| | Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1 | Q27702268 |
| | X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes | Q27703747 |
| | Proteolytic cleavage of microtubule-associated proteins by retroviral proteinases | Q28254374 |
| | Non-viral cellular substrates for human immunodeficiency virus type 1 protease | Q28264830 |
| | Inhibition of HIV-1 protease in infected T-lymphocytes by synthetic peptide analogues | Q28323197 |
| | Rational design of peptide-based HIV proteinase inhibitors | Q28330897 |
| | An inhibitor of the protease blocks maturation of human and simian immunodeficiency viruses and spread of infection | Q28331494 |
| | A synthetic HIV-1 protease inhibitor with antiviral activity arrests HIV-like particle maturation | Q28336106 |
| | Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone | Q29547734 |
| | Human immunodeficiency virus type 1 protease cleaves the intermediate filament proteins vimentin, desmin, and glial fibrillary acidic protein | Q33750683 |
| | Human immunodeficiency virus 1 protease expressed in Escherichia coli behaves as a dimeric aspartic protease | Q33843249 |
| | Stability and activity of human immunodeficiency virus protease: comparison of the natural dimer with a homologous, single-chain tethered dimer | Q33924472 |
| | Viral proteinases | Q34164183 |
| | The rev (trs/art) protein of human immunodeficiency virus type 1 affects viral mRNA and protein expression via a cis-acting sequence in the env region | Q34544493 |
| | Human immunodeficiency virus type 1 Gag proteins are processed in two cellular compartments | Q34618267 |
| | Highly specific antibody to Rous sarcoma virus src gene product recognizes a novel population of pp60v-src and pp60c-src molecules | Q36211478 |
| | Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity | Q37480211 |
| | Viral proteinases: weakness in strength | Q38138706 |
| | Characterization of an active single polypeptide form of the human immunodeficiency virus type 1 protease | Q38338789 |
| | Proteolytic processing of polyproteins in the replication of RNA viruses | Q38764271 |
| | Standardized and simplified nomenclature for proteins common to all retroviruses | Q40127929 |
| | Processing of in vitro-synthesized gag precursor proteins of human immunodeficiency virus (HIV) type 1 by HIV proteinase generated in Escherichia coli. | Q40131039 |
| | Processing of the precursor of NF-kappa B by the HIV-1 protease during acute infection | Q41687257 |
| | HIV-1 Gag mutants can dominantly interfere with the replication of the wild-type virus | Q45843803 |
| | A range of catalytic efficiencies with avian retroviral protease subunits genetically linked to form single polypeptide chains | Q46886442 |
| | Calcium-free calmodulin is a substrate of proteases from human immunodeficiency viruses 1 and 2 | Q70216501 |
| P433 | issue | 1 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | microbiology | Q7193 |
| | immunology | Q101929 |
| | HIV protease inhibitors | Q50315992 |
| P304 | page(s) | 567-572 | |
| P577 | publication date | 1992-01-01 | |
| P1433 | published in | Journal of Virology | Q1251128 |
| P1476 | title | Specific inhibitor of human immunodeficiency virus proteinase prevents the cytotoxic effects of a single-chain proteinase dimer and restores particle formation | |
| P478 | volume | 66 | |