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252 related items for PubMed ID: 1545221

  • 1. Autoprocessing of the human immunodeficiency virus type 1 protease precursor expressed in Escherichia coli from a synthetic gene.
    Valverde V, Lemay P, Masson JM, Gay B, Boulanger P.
    J Gen Virol; 1992 Mar; 73 ( Pt 3)():639-51. PubMed ID: 1545221
    [Abstract] [Full Text] [Related]

  • 2. Characterization and autoprocessing of precursor and mature forms of human immunodeficiency virus type 1 (HIV 1) protease purified from Escherichia coli.
    Strickler JE, Gorniak J, Dayton B, Meek T, Moore M, Magaard V, Malinowski J, Debouck C.
    Proteins; 1989 Mar; 6(2):139-54. PubMed ID: 2695927
    [Abstract] [Full Text] [Related]

  • 3. Comparison of HIV-1 protease expression in different fusion forms.
    Wan M, Takagi M, Loh BN, Imanaka T.
    Biochem Mol Biol Int; 1995 Jun; 36(2):411-9. PubMed ID: 7663445
    [Abstract] [Full Text] [Related]

  • 4. Autoprocessing of the HIV-1 protease using purified wild-type and mutated fusion proteins expressed at high levels in Escherichia coli.
    Louis JM, McDonald RA, Nashed NT, Wondrak EM, Jerina DM, Oroszlan S, Mora PT.
    Eur J Biochem; 1991 Jul 15; 199(2):361-9. PubMed ID: 2070793
    [Abstract] [Full Text] [Related]

  • 5. 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.
    Tözsér J, Shulenin S, Louis JM, Copeland TD, Oroszlan S.
    Biochemistry; 2004 Apr 13; 43(14):4304-12. PubMed ID: 15065874
    [Abstract] [Full Text] [Related]

  • 6. Use of the HIV-1 protease for excision of growth-hormone-releasing factor from synthetic and recombinant peptide precursors.
    Tomasselli AG, Mildner AA, Paddock DJ, Wheeler JS, Kubiak TM, Martin RA, Moseley WM, Mott JE, White MC, Leone JW, Heinrikson RL.
    Biotechnol Appl Biochem; 1997 Aug 13; 26(1):39-49. PubMed ID: 9262002
    [Abstract] [Full Text] [Related]

  • 7. Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain.
    Zybarth G, Kräusslich HG, Partin K, Carter C.
    J Virol; 1994 Jan 13; 68(1):240-50. PubMed ID: 8254734
    [Abstract] [Full Text] [Related]

  • 8. Flexible catalytic site conformations implicated in modulation of HIV-1 protease autoprocessing reactions.
    Huang L, Li Y, Chen C.
    Retrovirology; 2011 Oct 10; 8():79. PubMed ID: 21985091
    [Abstract] [Full Text] [Related]

  • 9. Autoprocessing: an essential step for the activation of HIV-1 protease.
    Wan M, Takagi M, Loh BN, Xu XZ, Imanaka T.
    Biochem J; 1996 Jun 01; 316 ( Pt 2)(Pt 2):569-73. PubMed ID: 8687402
    [Abstract] [Full Text] [Related]

  • 10. HIV-1 protease substrate-groove: Role in substrate recognition and inhibitor resistance.
    Laco GS.
    Biochimie; 2015 Nov 01; 118():90-103. PubMed ID: 26300060
    [Abstract] [Full Text] [Related]

  • 11. A side chain at position 48 of the human immunodeficiency virus type-1 protease flap provides an additional specificity determinant.
    Moody MD, Pettit SC, Shao W, Everitt L, Loeb DD, Hutchison CA, Swanstrom R.
    Virology; 1995 Mar 10; 207(2):475-85. PubMed ID: 7886951
    [Abstract] [Full Text] [Related]

  • 12. Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the P1 amino acid.
    Pettit SC, Simsic J, Loeb DD, Everitt L, Hutchison CA, Swanstrom R.
    J Biol Chem; 1991 Aug 05; 266(22):14539-47. PubMed ID: 1860860
    [Abstract] [Full Text] [Related]

  • 13. Effect of signal peptide changes on the extracellular processing of streptokinase from Escherichia coli: requirement for secondary structure at the cleavage junction.
    Pratap J, Dikshit KL.
    Mol Gen Genet; 1998 May 05; 258(4):326-33. PubMed ID: 9648736
    [Abstract] [Full Text] [Related]

  • 14. Kinetics and sequence specificity of processing of prepilin by PilD, the type IV leader peptidase of Pseudomonas aeruginosa.
    Strom MS, Lory S.
    J Bacteriol; 1992 Nov 05; 174(22):7345-51. PubMed ID: 1429457
    [Abstract] [Full Text] [Related]

  • 15. The expression in Escherichia coli of a synthetic gene coding for the precursor of papain is prevented by its own putative signal sequence.
    Vernet T, Tessier DC, Laliberté F, Dignard D, Thomas DY.
    Gene; 1989 Apr 30; 77(2):229-36. PubMed ID: 2666263
    [Abstract] [Full Text] [Related]

  • 16. Linkers for improved cleavage of fusion proteins with an engineered alpha-lytic protease.
    Lien S, Milner SJ, Graham LD, Wallace JC, Francis GL.
    Biotechnol Bioeng; 2001 Aug 20; 74(4):335-43. PubMed ID: 11410858
    [Abstract] [Full Text] [Related]

  • 17. Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus.
    Tomasselli AG, Hui JO, Adams L, Chosay J, Lowery D, Greenberg B, Yem A, Deibel MR, Zürcher-Neely H, Heinrikson RL.
    J Biol Chem; 1991 Aug 05; 266(22):14548-53. PubMed ID: 1907279
    [Abstract] [Full Text] [Related]

  • 18. Recombinant HIV2 protease processes HIV1 Pr53gag and analogous junction peptides in vitro.
    Pichuantes S, Babé LM, Barr PJ, DeCamp DL, Craik CS.
    J Biol Chem; 1990 Aug 15; 265(23):13890-8. PubMed ID: 2199446
    [Abstract] [Full Text] [Related]

  • 19. Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease.
    Tang C, Louis JM, Aniana A, Suh JY, Clore GM.
    Nature; 2008 Oct 02; 455(7213):693-6. PubMed ID: 18833280
    [Abstract] [Full Text] [Related]

  • 20. Human immunodeficiency virus type 1 gag-protease fusion proteins are enzymatically active.
    Kotler M, Arad G, Hughes SH.
    J Virol; 1992 Nov 02; 66(11):6781-3. PubMed ID: 1404618
    [Abstract] [Full Text] [Related]

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