Gag-Pol polyprotein

Details

Name
Gag-Pol polyprotein
Synonyms
  • Pr160Gag-Pol
Gene Name
gag-pol
Organism
HIV-1
Amino acid sequence
>lcl|BSEQ0003164|Gag-Pol polyprotein
MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQI
LGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAA
DTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGAT
PQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTT
STLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRF
YKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKA
RVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGHTARNCRAPRKKGCWKCGKEG
HQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTRRELQVWGRDNNSPSEAGADR
QGTVSFNFPQVTLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGG
FIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFPISPIETVPVKLK
PGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRK
LVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIP
SINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDL
EIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWT
VNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEP
VHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQ
KITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEP
IVGAETFYVDGAANRETKLGKAGYVTNRGRQKVVTLTDTTNQKTELQAIYLALQDSGLEV
NIVTDSQYALGIIQAQPDQSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVS
AGIRKVLFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQ
VDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTI
HTDNGSNFTGATVRAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKIIGQVRDQAEHLK
TAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRNP
LWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED
Number of residues
1435
Molecular Weight
162041.05
Theoretical pI
9.02
GO Classification
Functions
aspartic-type endopeptidase activity / DNA binding / DNA-directed DNA polymerase activity / exoribonuclease H activity / identical protein binding / lipid binding / RNA binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / structural molecule activity / zinc ion binding
Processes
DNA integration / DNA recombination / entry into host cell / establishment of integrated proviral latency / induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process / RNA-dependent DNA replication / suppression by virus of host gene expression / uncoating of virus / viral entry into host cell / viral life cycle / viral penetration into host nucleus / viral process / viral release from host cell / virion assembly
Components
host cell nucleus / host cell plasma membrane / host multivesicular body / viral nucleocapsid / virion membrane
General Function
Zinc ion binding
Specific Function
Gag-Pol polyprotein: Mediates, with Gag polyrotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shutt off translation.Matrix protein p17: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).Capsid protein p24: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion (PubMed:8648689). Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (PubMed:12660176). Host restriction factors such as monkey TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (PubMed:23785198). Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (PubMed:24554657).Nucleocapsid protein p7: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates to gRNA dimerization, packaging, tRNA incorporation and virion assembly.Protease: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane (PubMed:9573231) (PubMed:11932404). Cleavages take place as an ordered, step-wise cascade to yield mature proteins (PubMed:9573231) (PubMed:11932404). This process is called maturation (PubMed:9573231) (PubMed:11932404). Displays maximal activity during the budding process just prior to particle release from the cell (PubMed:9573231) (PubMed:11932404). Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles (PubMed:7835426). Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (PubMed:12660176) (PubMed:19914170).Reverse transcriptase/ribonuclease H: Multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends.Integrase: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Host cell membrane
Gene sequence
>lcl|BSEQ0021298|Gag-Pol polyprotein (gag-pol)
ATGGGTGCGAGAGCGTCAGTATTAAGCGGGGGAGAATTAGATCGATGGGAAAAAATTCGG
TTAAGGCCAGGGGGAAAGAAAAAATATAAATTAAAACATATAGTATGGGCAAGCAGGGAG
CTAGAACGATTCGCAGTTAATCCTGGCCTGTTAGAAACATCAGAAGGCTGTAGACAAATA
CTGGGACAGCTACAACCATCCCTTCAGACAGGATCAGAAGAACTTAGATCATTATATAAT
ACAGTAGCAACCCTCTATTGTGTGCATCAAAGGATAGAGATAAAAGACACCAAGGAAGCT
TTAGACAAGATAGAGGAAGAGCAAAACAAAAGTAAGAAAAAAGCACAGCAAGCAGCAGCT
GACACAGGACACAGCAATCAGGTCAGCCAAAATTACCCTATAGTGCAGAACATCCAGGGG
CAAATGGTACATCAGGCCATATCACCTAGAACTTTAAATGCATGGGTAAAAGTAGTAGAA
GAGAAGGCTTTCAGCCCAGAAGTGATACCCATGTTTTCAGCATTATCAGAAGGAGCCACC
CCACAAGATTTAAACACCATGCTAAACACAGTGGGGGGACATCAAGCAGCCATGCAAATG
TTAAAAGAGACCATCAATGAGGAAGCTGCAGAATGGGATAGAGTGCATCCAGTGCATGCA
GGGCCTATTGCACCAGGCCAGATGAGAGAACCAAGGGGAAGTGACATAGCAGGAACTACT
AGTACCCTTCAGGAACAAATAGGATGGATGACAAATAATCCACCTATCCCAGTAGGAGAA
ATTTATAAAAGATGGATAATCCTGGGATTAAATAAAATAGTAAGAATGTATAGCCCTACC
AGCATTCTGGACATAAGACAAGGACCAAAGGAACCCTTTAGAGACTATGTAGACCGGTTC
TATAAAACTCTAAGAGCCGAGCAAGCTTCACAGGAGGTAAAAAATTGGATGACAGAAACC
TTGTTGGTCCAAAATGCGAACCCAGATTGTAAGACTATTTTAAAAGCATTGGGACCAGCG
GCTACACTAGAAGAAATGATGACAGCATGTCAGGGAGTAGGAGGACCCGGCCATAAGGCA
AGAGTTTTGGCTGAAGCAATGAGCCAAGTAACAAATTCAGCTACCATAATGATGCAGAGA
GGCAATTTTAGGAACCAAAGAAAGATTGTTAAGTGTTTCAATTGTGGCAAAGAAGGGCAC
ACAGCCAGAAATTGCAGGGCCCCTAGGAAAAAGGGCTGTTGGAAATGTGGAAAGGAAGGA
CACCAAATGAAAGATTGTACTGAGAGACAGGCTAATTTTTTAAGGGAAGATCTGGCCTTC
CTACAAGGGAAGGCCAGGGAATTTTCTTCAGAGCAGACCAGAGCCAACAGCCCCACCAGA
AGAGAGCTTCAGGTCTGGGGTAGAGACAACAACTCCCCCTCAGAAGCAGGAGCCGATAGA
CAAGGAACTGTATCCTTTAACTTCCCTCAGGTCACTCTTTGGCAACGACCCCTCGTCACA
ATAAAGATAGGGGGGCAACTAAAGGAAGCTCTATTAGATACAGGAGCAGATGATACAGTA
TTAGAAGAAATGAGTTTGCCAGGAAGATGGAAACCAAAAATGATAGGGGGAATTGGAGGT
TTTATCAAAGTAAGACAGTATGATCAGATACTCATAGAAATCTGTGGACATAAAGCTATA
GGTACAGTATTAGTAGGACCTACACCTGTCAACATAATTGGAAGAAATCTGTTGACTCAG
ATTGGTTGCACTTTAAATTTTCCCATTAGCCCTATTGAGACTGTACCAGTAAAATTAAAG
CCAGGAATGGATGGCCCAAAAGTTAAACAATGGCCATTGACAGAAGAAAAAATAAAAGCA
TTAGTAGAAATTTGTACAGAGATGGAAAAGGAAGGGAAAATTTCAAAAATTGGGCCTGAA
AATCCATACAATACTCCAGTATTTGCCATAAAGAAAAAAGACAGTACTAAATGGAGAAAA
TTAGTAGATTTCAGAGAACTTAATAAGAGAACTCAAGACTTCTGGGAAGTTCAATTAGGA
ATACCACATCCCGCAGGGTTAAAAAAGAAAAAATCAGTAACAGTACTGGATGTGGGTGAT
GCATATTTTTCAGTTCCCTTAGATGAAGACTTCAGGAAGTATACTGCATTTACCATACCT
AGTATAAACAATGAGACACCAGGGATTAGATATCAGTACAATGTGCTTCCACAGGGATGG
AAAGGATCACCAGCAATATTCCAAAGTAGCATGACAAAAATCTTAGAGCCTTTTAGAAAA
CAAAATCCAGACATAGTTATCTATCAATACATGGATGATTTGTATGTAGGATCTGACTTA
GAAATAGGGCAGCATAGAACAAAAATAGAGGAGCTGAGACAACATCTGTTGAGGTGGGGA
CTTACCACACCAGACAAAAAACATCAGAAAGAACCTCCATTCCTTTGGATGGGTTATGAA
CTCCATCCTGATAAATGGACAGTACAGCCTATAGTGCTGCCAGAAAAAGACAGCTGGACT
GTCAATGACATACAGAAGTTAGTGGGGAAATTGAATTGGGCAAGTCAGATTTACCCAGGG
ATTAAAGTAAGGCAATTATGTAAACTCCTTAGAGGAACCAAAGCACTAACAGAAGTAATA
CCACTAACAGAAGAAGCAGAGCTAGAACTGGCAGAAAACAGAGAGATTCTAAAAGAACCA
GTACATGGAGTGTATTATGACCCATCAAAAGACTTAATAGCAGAAATACAGAAGCAGGGG
CAAGGCCAATGGACATATCAAATTTATCAAGAGCCATTTAAAAATCTGAAAACAGGAAAA
TATGCAAGAATGAGGGGTGCCCACACTAATGATGTAAAACAATTAACAGAGGCAGTGCAA
AAAATAACCACAGAAAGCATAGTAATATGGGGAAAGACTCCTAAATTTAAACTGCCCATA
CAAAAGGAAACATGGGAAACATGGTGGACAGAGTATTGGCAAGCCACCTGGATTCCTGAG
TGGGAGTTTGTTAATACCCCTCCCTTAGTGAAATTATGGTACCAGTTAGAGAAAGAACCC
ATAGTAGGAGCAGAAACCTTCTATGTAGATGGGGCAGCTAACAGGGAGACTAAATTAGGA
AAAGCAGGATATGTTACTAATAGAGGAAGACAAAAAGTTGTCACCCTAACTGACACAACA
AATCAGAAGACTGAGTTACAAGCAATTTATCTAGCTTTGCAGGATTCGGGATTAGAAGTA
AACATAGTAACAGACTCACAATATGCATTAGGAATCATTCAAGCACAACCAGATCAAAGT
GAATCAGAGTTAGTCAATCAAATAATAGAGCAGTTAATAAAAAAGGAAAAGGTCTATCTG
GCATGGGTACCAGCACACAAAGGAATTGGAGGAAATGAACAAGTAGATAAATTAGTCAGT
GCTGGAATCAGGAAAGTACTATTTTTAGATGGAATAGATAAGGCCCAAGATGAACATGAG
AAATATCACAGTAATTGGAGAGCAATGGCTAGTGATTTTAACCTGCCACCTGTAGTAGCA
AAAGAAATAGTAGCCAGCTGTGATAAATGTCAGCTAAAAGGAGAAGCCATGCATGGACAA
GTAGACTGTAGTCCAGGAATATGGCAACTAGATTGTACACATTTAGAAGGAAAAGTTATC
CTGGTAGCAGTTCATGTAGCCAGTGGATATATAGAAGCAGAAGTTATTCCAGCAGAAACA
GGGCAGGAAACAGCATATTTTCTTTTAAAATTAGCAGGAAGATGGCCAGTAAAAACAATA
CATACTGACAATGGCAGCAATTTCACCGGTGCTACGGTTAGGGCCGCCTGTTGGTGGGCG
GGAATCAAGCAGGAATTTGGAATTCCCTACAATCCCCAAAGTCAAGGAGTAGTAGAATCT
ATGAATAAAGAATTAAAGAAAATTATAGGACAGGTAAGAGATCAGGCTGAACATCTTAAG
ACAGCAGTACAAATGGCAGTATTCATCCACAATTTTAAAAGAAAAGGGGGGATTGGGGGG
TACAGTGCAGGGGAAAGAATAGTAGACATAATAGCAACAGACATACAAACTAAAGAATTA
CAAAAACAAATTACAAAAATTCAAAATTTTCGGGTTTATTACAGGGACAGCAGAAATCCA
CTTTGGAAAGGACCAGCAAAGCTCCTCTGGAAAGGTGAAGGGGCAGTAGTAATACAAGAT
AATAGTGACATAAAAGTAGTGCCAAGAAGAAAAGCAAAGATCATTAGGGATTATGGAAAA
CAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGATGAGGATTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP04585
UniProtKB Entry NamePOL_HV1H2
GenBank Protein ID1906384
GenBank Gene IDK03455
General References
  1. Ratner L, Fisher A, Jagodzinski LL, Mitsuya H, Liou RS, Gallo RC, Wong-Staal F: Complete nucleotide sequences of functional clones of the AIDS virus. AIDS Res Hum Retroviruses. 1987 Spring;3(1):57-69. [Article]
  2. Farnet CM, Haseltine WA: Integration of human immunodeficiency virus type 1 DNA in vitro. Proc Natl Acad Sci U S A. 1990 Jun;87(11):4164-8. [Article]
  3. Weber IT: Comparison of the crystal structures and intersubunit interactions of human immunodeficiency and Rous sarcoma virus proteases. J Biol Chem. 1990 Jun 25;265(18):10492-6. [Article]
  4. Leavitt AD, Shiue L, Varmus HE: Site-directed mutagenesis of HIV-1 integrase demonstrates differential effects on integrase functions in vitro. J Biol Chem. 1993 Jan 25;268(3):2113-9. [Article]
  5. Cannon PM, Wilson W, Byles E, Kingsman SM, Kingsman AJ: Human immunodeficiency virus type 1 integrase: effect on viral replication of mutations at highly conserved residues. J Virol. 1994 Aug;68(8):4768-75. [Article]
  6. Luban J, Bossolt KL, Franke EK, Kalpana GV, Goff SP: Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell. 1993 Jun 18;73(6):1067-78. [Article]
  7. Kalpana GV, Marmon S, Wang W, Crabtree GR, Goff SP: Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5. Science. 1994 Dec 23;266(5193):2002-6. [Article]
  8. Gaedigk-Nitschko K, Schon A, Wachinger G, Erfle V, Kohleisen B: Cleavage of recombinant and cell derived human immunodeficiency virus 1 (HIV-1) Nef protein by HIV-1 protease. FEBS Lett. 1995 Jan 9;357(3):275-8. [Article]
  9. Braaten D, Franke EK, Luban J: Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription. J Virol. 1996 Jun;70(6):3551-60. [Article]
  10. Yoo S, Myszka DG, Yeh C, McMurray M, Hill CP, Sundquist WI: Molecular recognition in the HIV-1 capsid/cyclophilin A complex. J Mol Biol. 1997 Jun 27;269(5):780-95. [Article]
  11. Gaur M, Leavitt AD: Mutations in the human immunodeficiency virus type 1 integrase D,D(35)E motif do not eliminate provirus formation. J Virol. 1998 Jun;72(6):4678-85. [Article]
  12. Dupont S, Sharova N, DeHoratius C, Virbasius CM, Zhu X, Bukrinskaya AG, Stevenson M, Green MR: A novel nuclear export activity in HIV-1 matrix protein required for viral replication. Nature. 1999 Dec 9;402(6762):681-5. [Article]
  13. Chang YY, Yu SL, Syu WJ: Organization of HIV-1 pol is critical for Pol polyprotein processing. J Biomed Sci. 1999 Sep-Oct;6(5):333-41. [Article]
  14. Negroni M, Buc H: Recombination during reverse transcription: an evaluation of the role of the nucleocapsid protein. J Mol Biol. 1999 Feb 12;286(1):15-31. [Article]
  15. Cen S, Khorchid A, Gabor J, Rong L, Wainberg MA, Kleiman L: Roles of Pr55(gag) and NCp7 in tRNA(3)(Lys) genomic placement and the initiation step of reverse transcription in human immunodeficiency virus type 1. J Virol. 2000 Nov;74(22):10796-800. [Article]
  16. Shehu-Xhilaga M, Crowe SM, Mak J: Maintenance of the Gag/Gag-Pol ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity. J Virol. 2001 Feb;75(4):1834-41. [Article]
  17. Cristofaro JV, Rausch JW, Le Grice SF, DeStefano JJ: Mutations in the ribonuclease H active site of HIV-RT reveal a role for this site in stabilizing enzyme-primer-template binding. Biochemistry. 2002 Sep 10;41(36):10968-75. [Article]
  18. Bosco DA, Eisenmesser EZ, Pochapsky S, Sundquist WI, Kern D: Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A. Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5247-52. Epub 2002 Apr 2. [Article]
  19. Guo J, Wu T, Kane BF, Johnson DG, Henderson LE, Gorelick RJ, Levin JG: Subtle alterations of the native zinc finger structures have dramatic effects on the nucleic acid chaperone activity of human immunodeficiency virus type 1 nucleocapsid protein. J Virol. 2002 May;76(9):4370-8. [Article]
  20. Pettit SC, Gulnik S, Everitt L, Kaplan AH: The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage. J Virol. 2003 Jan;77(1):366-74. [Article]
  21. Briggs JA, Wilk T, Welker R, Krausslich HG, Fuller SD: Structural organization of authentic, mature HIV-1 virions and cores. EMBO J. 2003 Apr 1;22(7):1707-15. [Article]
  22. Perales C, Carrasco L, Ventoso I: Cleavage of eIF4G by HIV-1 protease: effects on translation. FEBS Lett. 2003 Jan 2;533(1-3):89-94. [Article]
  23. Tozser J, Shulenin S, Louis JM, Copeland TD, Oroszlan S: In vitro processing of HIV-1 nucleocapsid protein by the viral proteinase: effects of amino acid substitutions at the scissile bond in the proximal zinc finger sequence. Biochemistry. 2004 Apr 13;43(14):4304-12. [Article]
  24. Purohit V, Balakrishnan M, Kim B, Bambara RA: Evidence that HIV-1 reverse transcriptase employs the DNA 3' end-directed primary/secondary RNase H cleavage mechanism during synthesis and strand transfer. J Biol Chem. 2005 Dec 9;280(49):40534-43. Epub 2005 Oct 11. [Article]
  25. Thomas JA, Shulenin S, Coren LV, Bosche WJ, Gagliardi TD, Gorelick RJ, Oroszlan S: Characterization of human immunodeficiency virus type 1 (HIV-1) containing mutations in the nucleocapsid protein at a putative HIV-1 protease cleavage site. Virology. 2006 Oct 25;354(2):261-70. Epub 2006 Aug 9. [Article]
  26. Hagan NA, Fabris D: Dissecting the protein-RNA and RNA-RNA interactions in the nucleocapsid-mediated dimerization and isomerization of HIV-1 stemloop 1. J Mol Biol. 2007 Jan 12;365(2):396-410. Epub 2006 Oct 3. [Article]
  27. Alfadhli A, Huseby D, Kapit E, Colman D, Barklis E: Human immunodeficiency virus type 1 matrix protein assembles on membranes as a hexamer. J Virol. 2007 Feb;81(3):1472-8. Epub 2006 Nov 15. [Article]
  28. Saad JS, Kim A, Ghanam RH, Dalton AK, Vogt VM, Wu Z, Lu W, Summers MF: Mutations that mimic phosphorylation of the HIV-1 matrix protein do not perturb the myristyl switch. Protein Sci. 2007 Aug;16(8):1793-7. [Article]
  29. Kafaie J, Song R, Abrahamyan L, Mouland AJ, Laughrea M: Mapping of nucleocapsid residues important for HIV-1 genomic RNA dimerization and packaging. Virology. 2008 Jun 5;375(2):592-610. doi: 10.1016/j.virol.2008.02.001. Epub 2008 Mar 17. [Article]
  30. Byeon IJ, Meng X, Jung J, Zhao G, Yang R, Ahn J, Shi J, Concel J, Aiken C, Zhang P, Gronenborn AM: Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell. 2009 Nov 13;139(4):780-90. doi: 10.1016/j.cell.2009.10.010. [Article]
  31. Castello A, Franco D, Moral-Lopez P, Berlanga JJ, Alvarez E, Wimmer E, Carrasco L: HIV- 1 protease inhibits Cap- and poly(A)-dependent translation upon eIF4GI and PABP cleavage. PLoS One. 2009 Nov 24;4(11):e7997. doi: 10.1371/journal.pone.0007997. [Article]
  32. Alfadhli A, Barklis RL, Barklis E: HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate. Virology. 2009 May 10;387(2):466-72. doi: 10.1016/j.virol.2009.02.048. Epub 2009 Mar 27. [Article]
  33. Henning MS, Morham SG, Goff SP, Naghavi MH: PDZD8 is a novel Gag-interacting factor that promotes retroviral infection. J Virol. 2010 Sep;84(17):8990-5. doi: 10.1128/JVI.00843-10. Epub 2010 Jun 23. [Article]
  34. Ao Z, Danappa Jayappa K, Wang B, Zheng Y, Kung S, Rassart E, Depping R, Kohler M, Cohen EA, Yao X: Importin alpha3 interacts with HIV-1 integrase and contributes to HIV-1 nuclear import and replication. J Virol. 2010 Sep;84(17):8650-63. doi: 10.1128/JVI.00508-10. Epub 2010 Jun 16. [Article]
  35. Jalalirad M, Laughrea M: Formation of immature and mature genomic RNA dimers in wild-type and protease-inactive HIV-1: differential roles of the Gag polyprotein, nucleocapsid proteins NCp15, NCp9, NCp7, and the dimerization initiation site. Virology. 2010 Nov 25;407(2):225-36. doi: 10.1016/j.virol.2010.08.013. Epub 2010 Sep 9. [Article]
  36. Shi J, Friedman DB, Aiken C: Retrovirus restriction by TRIM5 proteins requires recognition of only a small fraction of viral capsid subunits. J Virol. 2013 Aug;87(16):9271-8. doi: 10.1128/JVI.00713-13. Epub 2013 Jun 19. [Article]
  37. Naicker P, Seele P, Dirr HW, Sayed Y: F99 is critical for dimerization and activation of South African HIV-1 subtype C protease. Protein J. 2013 Oct;32(7):560-7. doi: 10.1007/s10930-013-9517-y. [Article]
  38. Guth CA, Sodroski J: Contribution of PDZD8 to stabilization of the human immunodeficiency virus type 1 capsid. J Virol. 2014 May;88(9):4612-23. doi: 10.1128/JVI.02945-13. Epub 2014 Feb 19. [Article]
  39. Vlach J, Samal AB, Saad JS: Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein. J Biol Chem. 2014 Mar 21;289(12):8697-705. doi: 10.1074/jbc.M113.543694. Epub 2014 Feb 5. [Article]
  40. Vogt VM: Proteolytic processing and particle maturation. Curr Top Microbiol Immunol. 1996;214:95-131. [Article]
  41. Turner BG, Summers MF: Structural biology of HIV. J Mol Biol. 1999 Jan 8;285(1):1-32. [Article]
  42. Negroni M, Buc H: Mechanisms of retroviral recombination. Annu Rev Genet. 2001;35:275-302. [Article]
  43. Dunn BM, Goodenow MM, Gustchina A, Wlodawer A: Retroviral proteases. Genome Biol. 2002;3(4):REVIEWS3006. Epub 2002 Mar 26. [Article]
  44. Scarlata S, Carter C: Role of HIV-1 Gag domains in viral assembly. Biochim Biophys Acta. 2003 Jul 11;1614(1):62-72. [Article]
  45. Turlure F, Devroe E, Silver PA, Engelman A: Human cell proteins and human immunodeficiency virus DNA integration. Front Biosci. 2004 Sep 1;9:3187-208. [Article]
  46. Sokolskaja E, Luban J: Cyclophilin, TRIM5, and innate immunity to HIV-1. Curr Opin Microbiol. 2006 Aug;9(4):404-8. Epub 2006 Jul 3. [Article]
  47. Chukkapalli V, Ono A: Molecular determinants that regulate plasma membrane association of HIV-1 Gag. J Mol Biol. 2011 Jul 22;410(4):512-24. doi: 10.1016/j.jmb.2011.04.015. [Article]
  48. Darlix JL, de Rocquigny H, Mauffret O, Mely Y: Retrospective on the all-in-one retroviral nucleocapsid protein. Virus Res. 2014 Nov 26;193:2-15. doi: 10.1016/j.virusres.2014.05.011. Epub 2014 Jun 4. [Article]
  49. Tedbury PR, Freed EO: The role of matrix in HIV-1 envelope glycoprotein incorporation. Trends Microbiol. 2014 Jul;22(7):372-8. doi: 10.1016/j.tim.2014.04.012. Epub 2014 Jun 2. [Article]
  50. Lapatto R, Blundell T, Hemmings A, Overington J, Wilderspin A, Wood S, Merson JR, Whittle PJ, Danley DE, Geoghegan KF, et al.: X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes. Nature. 1989 Nov 16;342(6247):299-302. [Article]
  51. Krohn A, Redshaw S, Ritchie JC, Graves BJ, Hatada MH: Novel binding mode of highly potent HIV-proteinase inhibitors incorporating the (R)-hydroxyethylamine isostere. J Med Chem. 1991 Nov;34(11):3340-2. [Article]
  52. Omichinski JG, Clore GM, Sakaguchi K, Appella E, Gronenborn AM: Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy. FEBS Lett. 1991 Nov 4;292(1-2):25-30. [Article]
  53. Thanki N, Rao JK, Foundling SI, Howe WJ, Moon JB, Hui JO, Tomasselli AG, Heinrikson RL, Thaisrivongs S, Wlodawer A: Crystal structure of a complex of HIV-1 protease with a dihydroxyethylene-containing inhibitor: comparisons with molecular modeling. Protein Sci. 1992 Aug;1(8):1061-72. [Article]
  54. Morellet N, de Rocquigny H, Mely Y, Jullian N, Demene H, Ottmann M, Gerard D, Darlix JL, Fournie-Zaluski MC, Roques BP: Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of HIV-1 studied by 1H NMR. J Mol Biol. 1994 Jan 7;235(1):287-301. [Article]
  55. Lam PY, Jadhav PK, Eyermann CJ, Hodge CN, Ru Y, Bacheler LT, Meek JL, Otto MJ, Rayner MM, Wong YN, et al.: Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors. Science. 1994 Jan 21;263(5145):380-4. [Article]
  56. Stammers DK, Somers DO, Ross CK, Kirby I, Ray PH, Wilson JE, Norman M, Ren JS, Esnouf RM, Garman EF, et al.: Crystals of HIV-1 reverse transcriptase diffracting to 2.2 A resolution. J Mol Biol. 1994 Sep 30;242(4):586-8. [Article]
  57. Matthews S, Barlow P, Clark N, Kingsman S, Kingsman A, Campbell I: Refined solution structure of p17, the HIV matrix protein. Biochem Soc Trans. 1995 Nov;23(4):725-9. [Article]
  58. Ren J, Esnouf R, Hopkins A, Ross C, Jones Y, Stammers D, Stuart D: The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: lessons for inhibitor design. Structure. 1995 Sep 15;3(9):915-26. [Article]
  59. Esnouf R, Ren J, Ross C, Jones Y, Stammers D, Stuart D: Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors. Nat Struct Biol. 1995 Apr;2(4):303-8. [Article]
  60. Hopkins AL, Ren J, Esnouf RM, Willcox BE, Jones EY, Ross C, Miyasaka T, Walker RT, Tanaka H, Stammers DK, Stuart DI: Complexes of HIV-1 reverse transcriptase with inhibitors of the HEPT series reveal conformational changes relevant to the design of potent non-nucleoside inhibitors. J Med Chem. 1996 Apr 12;39(8):1589-600. [Article]
  61. Hodge CN, Aldrich PE, Bacheler LT, Chang CH, Eyermann CJ, Garber S, Grubb M, Jackson DA, Jadhav PK, Korant B, Lam PY, Maurin MB, Meek JL, Otto MJ, Rayner MM, Reid C, Sharpe TR, Shum L, Winslow DL, Erickson-Viitanen S: Improved cyclic urea inhibitors of the HIV-1 protease: synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450. Chem Biol. 1996 Apr;3(4):301-14. [Article]
  62. Yamazaki T, Hinck AP, Wang YX, Nicholson LK, Torchia DA, Wingfield P, Stahl SJ, Kaufman JD, Chang CH, Domaille PJ, Lam PY: Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy. Protein Sci. 1996 Mar;5(3):495-506. [Article]
  63. Esnouf RM, Ren J, Hopkins AL, Ross CK, Jones EY, Stammers DK, Stuart DI: Unique features in the structure of the complex between HIV-1 reverse transcriptase and the bis(heteroaryl)piperazine (BHAP) U-90152 explain resistance mutations for this nonnucleoside inhibitor. Proc Natl Acad Sci U S A. 1997 Apr 15;94(8):3984-9. [Article]
  64. Jadhav PK, Ala P, Woerner FJ, Chang CH, Garber SS, Anton ED, Bacheler LT: Cyclic urea amides: HIV-1 protease inhibitors with low nanomolar potency against both wild type and protease inhibitor resistant mutants of HIV. J Med Chem. 1997 Jan 17;40(2):181-91. [Article]
  65. Kervinen J, Lubkowski J, Zdanov A, Bhatt D, Dunn BM, Hui KY, Powell DJ, Kay J, Wlodawer A, Gustchina A: Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV. Protein Sci. 1998 Nov;7(11):2314-23. [Article]
  66. Jadhav PK, Woerner FJ, Lam PY, Hodge CN, Eyermann CJ, Man HW, Daneker WF, Bacheler LT, Rayner MM, Meek JL, Erickson-Viitanen S, Jackson DA, Calabrese JC, Schadt M, Chang CH: Nonpeptide cyclic cyanoguanidines as HIV-1 protease inhibitors: synthesis, structure-activity relationships, and X-ray crystal structure studies. J Med Chem. 1998 Apr 23;41(9):1446-55. [Article]
  67. Ala PJ, Huston EE, Klabe RM, Jadhav PK, Lam PY, Chang CH: Counteracting HIV-1 protease drug resistance: structural analysis of mutant proteases complexed with XV638 and SD146, cyclic urea amides with broad specificities. Biochemistry. 1998 Oct 27;37(43):15042-9. [Article]
  68. Ala PJ, DeLoskey RJ, Huston EE, Jadhav PK, Lam PY, Eyermann CJ, Hodge CN, Schadt MC, Lewandowski FA, Weber PC, McCabe DD, Duke JL, Chang CH: Molecular recognition of cyclic urea HIV-1 protease inhibitors. J Biol Chem. 1998 May 15;273(20):12325-31. [Article]
  69. Louis JM, Dyda F, Nashed NT, Kimmel AR, Davies DR: Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease. Biochemistry. 1998 Feb 24;37(8):2105-10. [Article]
  70. Ren J, Esnouf RM, Hopkins AL, Jones EY, Kirby I, Keeling J, Ross CK, Larder BA, Stuart DI, Stammers DK: 3'-Azido-3'-deoxythymidine drug resistance mutations in HIV-1 reverse transcriptase can induce long range conformational changes. Proc Natl Acad Sci U S A. 1998 Aug 4;95(16):9518-23. [Article]
  71. Ren J, Esnouf RM, Hopkins AL, Warren J, Balzarini J, Stuart DI, Stammers DK: Crystal structures of HIV-1 reverse transcriptase in complex with carboxanilide derivatives. Biochemistry. 1998 Oct 13;37(41):14394-403. [Article]
  72. Mahalingam B, Louis JM, Reed CC, Adomat JM, Krouse J, Wang YF, Harrison RW, Weber IT: Structural and kinetic analysis of drug resistant mutants of HIV-1 protease. Eur J Biochem. 1999 Jul;263(1):238-45. [Article]
  73. Chen JC, Krucinski J, Miercke LJ, Finer-Moore JS, Tang AH, Leavitt AD, Stroud RM: Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8233-8. [Article]
  74. Pillai B, Kannan KK, Hosur MV: 1.9 A x-ray study shows closed flap conformation in crystals of tethered HIV-1 PR. Proteins. 2001 Apr 1;43(1):57-64. [Article]
  75. Ren J, Nichols C, Bird L, Chamberlain P, Weaver K, Short S, Stuart DI, Stammers DK: Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors. J Mol Biol. 2001 Sep 28;312(4):795-805. [Article]
  76. Kumar M, Kannan KK, Hosur MV, Bhavesh NS, Chatterjee A, Mittal R, Hosur RV: Effects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations. Biochem Biophys Res Commun. 2002 Jun 7;294(2):395-401. [Article]
  77. Pari K, Mueller GA, DeRose EF, Kirby TW, London RE: Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium. Biochemistry. 2003 Jan 28;42(3):639-50. [Article]
  78. Ren J, Nichols CE, Chamberlain PP, Weaver KL, Short SA, Stammers DK: Crystal structures of HIV-1 reverse transcriptases mutated at codons 100, 106 and 108 and mechanisms of resistance to non-nucleoside inhibitors. J Mol Biol. 2004 Feb 20;336(3):569-78. [Article]
  79. Freeman GA, Andrews Iii CW 3rd, Hopkins AL, Lowell GS, Schaller LT, Cowan JR, Gonzales SS, Koszalka GW, Hazen RJ, Boone LR, Ferris RG, Creech KL, Roberts GB, Short SA, Weaver K, Reynolds DJ, Milton J, Ren J, Stuart DI, Stammers DK, Chan JH: Design of non-nucleoside inhibitors of HIV-1 reverse transcriptase with improved drug resistance properties. 2. J Med Chem. 2004 Nov 18;47(24):5923-36. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02102MozenavirexperimentalunknownDetails
DB02702XV638experimentalunknownDetails
DB02729SD146experimentalunknownDetails
DB05328VGV-1investigationalunknownDetails
DB04609INHIBITOR Q8467 OF DUPONT MERCKexperimentalunknownDetails
DB13119GSK-364735investigationalunknownDetails
DB06581BevirimatinvestigationalunknownDetails
DB06910[4-R-(4-ALPHA,6-BETA,7-BETA]-HEXAHYDRO-5,6-DI(HYDROXY)-1,3-DI(ALLYL)-4,7-BISPHENYLMETHYL)-2H-1,3-DIAZEPINONEexperimentalunknownDetails
DB071846-(cyclohexylsulfanyl)-1-(ethoxymethyl)-5-(1-methylethyl)pyrimidine-2,4(1H,3H)-dioneexperimentalunknownDetails
DB06414EtravirineapprovedunknownDetails
DB07332ALPHA-(2,6-DICHLOROPHENYL)-ALPHA-(2-ACETYL-5-METHYLANILINO)ACETAMIDEexperimentalunknownDetails
DB07472(R)-(+)9B-(3-METHYL)PHENYL-2,3-DIHYDROTHIAZOLO[2,3-A]ISOINDOL-5(9BH)-ONEexperimentalunknownDetails
DB07473(R)-(+) 5(9BH)-OXO-9B-PHENYL-2,3-DIHYDROTHIAZOLO[2,3-A]ISOINDOL-3-CARBOXYLIC ACID METHYL ESTERexperimentalunknownDetails
DB07781N-[[3-FLUORO-4-ETHOXY-PYRID-2-YL]ETHYL]-N'-[5-NITRILOMETHYL-PYRIDYL]-THIOUREAexperimentalunknownDetails
DB07797N-[[3-FLUORO-4-ETHOXY-PYRID-2-YL]ETHYL]-N'-[5-CHLORO-PYRIDYL]-THIOUREAexperimentalunknownDetails
DB078206-(3',5'-DIMETHYLBENZYL)-1-ETHOXYMETHYL-5-ISOPROPYLURACILexperimentalunknownDetails
DB078262-[4-chloro-2-(phenylcarbonyl)phenoxy]-N-phenylacetamideexperimentalunknownDetails
DB078644-[(CYCLOPROPYLETHYNYL)OXY]-6-FLUORO-3-ISOPROPYLQUINOLIN-2(1H)-ONEexperimentalunknownDetails
DB078676-CHLORO-4-(CYCLOHEXYLOXY)-3-PROPYLQUINOLIN-2(1H)-ONEexperimentalunknownDetails
DB078686-CHLORO-4-(CYCLOHEXYLSULFANYL)-3-PROPYLQUINOLIN-2(1H)-ONEexperimentalunknownDetails
DB078696-Chloro-4-[(R)-cyclohexylsulfinyl]-3-propyl-2(1H)-quinolinoneexperimentalunknownDetails
DB078716-CHLORO-4-(CYCLOHEXYLOXY)-3-ISOPROPYLQUINOLIN-2(1H)-ONEexperimentalunknownDetails
DB07884OpaviralineexperimentalunknownDetails
DB078921-(2-HYDROXYETHYLOXYMETHYL)-6-PHENYL THIOTHYMINEexperimentalunknownDetails
DB07910(2S)-2-amino-3-phenylpropane-1,1-diolexperimentalunknownDetails
DB081543-chloro-5-[2-chloro-5-(1H-indazol-3-ylmethoxy)phenoxy]benzonitrileexperimentalunknownDetails
DB08188EmivirineinvestigationalunknownDetails
DB082115-bromo-3-(pyrrolidin-1-ylsulfonyl)-1H-indole-2-carboxamideexperimentalunknownDetails
DB082861-Naphthoxyacetic acidexperimentalunknownDetails
DB083721-[2-(4-ETHOXY-3-FLUOROPYRIDIN-2-YL)ETHYL]-3-(5-METHYLPYRIDIN-2-YL)THIOUREAexperimentalunknownDetails
DB083796-(4-chloro-2-fluoro-3-phenoxybenzyl)pyridazin-3(2H)-oneexperimentalunknownDetails
DB084443-[2-bromo-4-(1H-pyrazolo[3,4-c]pyridazin-3-ylmethyl)phenoxy]-5-methylbenzonitrileexperimentalunknownDetails
DB084463-[6-bromo-2-fluoro-3-(1H-pyrazolo[3,4-c]pyridazin-3-ylmethyl)phenoxy]-5-chlorobenzonitrileexperimentalunknownDetails
DB084593-chloro-5-[2-chloro-5-(1H-pyrazolo[3,4-b]pyridin-3-ylmethoxy)phenoxy]benzonitrileexperimentalunknownDetails
DB08460MK-4965experimentalunknownDetails
DB08494S-{2-[(2-chloro-4-sulfamoylphenyl)amino]-2-oxoethyl} 6-methyl-3,4-dihydroquinoline-1(2H)-carbothioateexperimentalunknownDetails
DB08502CapravirineinvestigationalunknownDetails
DB085282-AMINO-6-(3,5-DIMETHYLPHENYL)SULFONYLBENZONITRILEexperimentalunknownDetails
DB08598R-82913experimentalunknownDetails
DB086346-BENZYL-1-BENZYLOXYMETHYL-5-ISOPROPYL URACILexperimentalunknownDetails
DB086656,11-DIHYDRO-11-ETHYL-6-METHYL-9-NITRO-5H-PYRIDO[2,3-B][1,5]BENZODIAZEPIN-5-ONEexperimentalunknownDetails
DB08680N-{3-[(E)-(tert-butoxyimino)methyl]-4-chlorophenyl}-2-methylfuran-3-carbimidothioic acidexperimentalunknownDetails
DB086811-METHYL ETHYL 2-CHLORO-5-[[[(1-METHYLETHOXY)THIOOXO]METHYL]AMINO]-BENZOATEexperimentalunknownDetails
DB086821-METHYL ETHYL 1-CHLORO-5-[[(5,6DIHYDRO-2-METHYL-1,4-OXATHIIN-3-YL)CARBONYL]AMINO]BENZOATEexperimentalunknownDetails
DB15673Lenacapavirapproved, investigationalyesinhibitorDetails