Research Topics
| K StrebelSummaryAffiliation: National Institutes of Health Country: USA Publications
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The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivitySandra Kao
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-0460, USA
J Virol 77:11398-407. 2003....- Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variantSandrine Opi
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Building 4, Room 310, 4 Center Drive, MSC 0460, Bethesda, Maryland 20892 0460, USA
J Virol 81:8236-46. 2007..These results demonstrate that targeting of APO3G to proteasome degradation and interference with viral encapsidation are distinct functional properties of Vif... - Monomeric APOBEC3G is catalytically active and has antiviral activitySandrine Opi
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 0460, USA
J Virol 80:4673-82. 2006..These results provide novel insights into the catalytic function and antiviral property of APO3G and demonstrate an important role for C97 in the RNA-dependent multimerization of this protein... - Human immunodeficiency virus type 1 Vpu protein induces degradation of CD4 in vitro: the cytoplasmic domain of CD4 contributes to Vpu sensitivityM Y Chen
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892
J Virol 67:3877-84. 1993..The results of these experiments suggest that sequences critical for this function of Vpu are located in its hydrophilic C-terminal domain... - HIV-1 Vif promotes the formation of high molecular mass APOBEC3G complexesRitu Goila-Gaur
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892 0460, USA
Virology 372:136-46. 2008.... - Production of infectious virus and degradation of APOBEC3G are separable functional properties of human immunodeficiency virus type 1 VifSandra Kao
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, NIH, Bldg 4, Room 310, 4 Center Drive MSC 0460, Bethesda, MD 20892 0460, USA
Virology 369:329-39. 2007..Our data imply that intracellular degradation of APO3G may not be the sole activity of Vif required for the production of infectious virions from APO3G-expressing cells... - Viral RNA is required for the association of APOBEC3G with human immunodeficiency virus type 1 nucleoprotein complexesMohammad A Khan
NIH, NIAID, 4/312, 4 Center Drive, MSC 0460, Bethesda, MD 20892-0460, USA
J Virol 79:5870-4. 2005..Our data suggest that packaging of APO3G into HIV-1 NPC is enhanced by viral RNA... - The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domainsU Schubert
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892 0460, USA
J Virol 70:809-19. 1996..The results of our experiments suggest that the two biological activities of Vpu operate via two distinct molecular mechanisms and involve two different structural domains of the Vpu protein... - The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradationS Bour
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases
J Virol 69:1510-20. 1995..However, the binding to target molecules is not sufficient per se to cause degradation. Interaction between CD4 and Vpu is thus likely to be an early event critical in triggering a multistep process leading to CD4 degradation... - Human immunodeficiency virus type 1 Vpu protein regulates the formation of intracellular gp160-CD4 complexesR L Willey
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892
J Virol 66:226-34. 1992..Although the precise mechanism(s) responsible for the Vpu effect is presently unclear, our findings suggest that Vpu may destabilize intracellular gp160-CD4 complexes... 
Production of infectious SIVagm from human cells requires functional inactivation but not viral exclusion of human APOBEC3GHiroaki Takeuchi
Laboratory of Molecular Microbiology, NIAID, National Institutes of Health, Bethesda, Maryland 20892 0460, USA
J Biol Chem 280:375-82. 2005..Our data suggest that SIVagm Vif can inhibit hApo3G activity without inducing its intracellular degradation or preventing its packaging into virions...- Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effectYasumasa Iwatani
Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, Bethesda, MD 20892 2780, USA
J Virol 80:5992-6002. 2006..In contrast, deamination is associated exclusively with the second zinc finger. Moreover, zinc finger two is more important than finger one for the antiviral effect, demonstrating a correlation between deaminase and antiviral activities... - Human immunodeficiency virus type 1 replication and regulation of APOBEC3G by peptidyl prolyl isomerase Pin1Koichi Watashi
Molecular Virology Section, Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
J Virol 82:9928-36. 2008..Intriguingly, HIV-1 infection modulates the phosphorylation state of Pin1, enhancing its ability to moderate A3G activity. These new findings suggest a potential Vif-independent way for HIV-1 to moderate the cellular action of A3G... - Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4R L Willey
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892
J Virol 66:7193-200. 1992.... - Sequences present in the cytoplasmic domain of CD4 are necessary and sufficient to confer sensitivity to the human immunodeficiency virus type 1 Vpu proteinR L Willey
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892
J Virol 68:1207-12. 1994..Thus, sequences present in the cytoplasmic domain of CD4 are necessary and sufficient to confer sensitivity to Vpu... - CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathwayU Schubert
Laboratories of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892 0440, USA
J Virol 72:2280-8. 1998.... - Human cellular restriction factors that target HIV-1 replicationKlaus Strebel
Laboratory of Molecular Microbiology, NIAID, The National Institutes of Health, Bethesda, Maryland, USA
BMC Med 7:48. 2009..We point to countermeasures encoded by HIV-1 for moderating the potency of these cellular restriction functions... - Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1 envelope-mediated T-cell fusion during viral entryIngrid Markovic
Center for Drug Evaluation and Research, Food and Drug Adminiatration, Bethesda, MD, USA
Blood 103:1586-94. 2004.... - Stably expressed APOBEC3F has negligible antiviral activityEri Miyagi
Viral Biochemistry Section, Laboratory of Molecular Microbiology, NIAID, NIH, Bldg 4, Room 310, 4 Center Drive MSC 0460, Bethesda, MD 20892 0460, USA
J Virol 84:11067-75. 2010..Surprisingly, however, neither wild-type nor deaminase-defective A3F inhibited HIV-1 infectivity. These results imply that the antiviral activity of endogenous A3F is negligible compared to that of A3G... - High level expression of human immunodeficiency virus type-1 Vif inhibits viral infectivity by modulating proteolytic processing of the Gag precursor at the p2/nucleocapsid processing siteHirofumi Akari
Laboratory of Molecular Microbiology, NIAID, National Institutes of Health, 4 312, 4 Center Drive, MSC 0460, Bethesda, MD 20892 0460, USA
J Biol Chem 279:12355-62. 2004..However, the accumulation of such processing intermediates at high levels of Vif is inhibitory. Thus, rapid intracellular degradation of Vif may have evolved as a mechanism to prevent such inhibitory effects of Vif... - Vpu enhances HIV-1 virus release in the absence of Bst-2 cell surface down-modulation and intracellular depletionEri Miyagi
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 0460, USA
Proc Natl Acad Sci U S A 106:2868-73. 2009.... - Human immunodeficiency virus type 1 Vif is efficiently packaged into virions during productive but not chronic infectionSandra Kao
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-0460, USA
J Virol 77:1131-40. 2003..The results from our study provide novel insights into the biochemical properties of Vif and offer an explanation for the reported differences regarding Vif packaging... - Lack of effect of cytoplasmic tail truncations on human immunodeficiency virus type 2 ROD env particle release activityS P Bour
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892 0460, USA
J Virol 73:778-82. 1999.... - Cell surface CD4 inhibits HIV-1 particle release by interfering with Vpu activityS Bour
Laboratory of Molecular Microbiology, NIAID, National Institutes of Health, Bethesda, Maryland 20892 0460, USA
J Biol Chem 274:33800-6. 1999..Co-immunoprecipitation experiments further showed that CD4 and Vpu physically interact at the cell surface, suggesting that CD4 might inhibit Vpu activity by disrupting its oligomeric structure... - The human immunodeficiency virus (HIV) type 2 envelope protein is a functional complement to HIV type 1 Vpu that enhances particle release of heterologous retrovirusesS Bour
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892 0460, USA
J Virol 70:8285-300. 1996..HIV-1 and HIV-2 thus appear to have evolved genetically distinct but functionally similar strategies to resolve the common problem of efficient release of progeny virus from infected cells... - Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartmentsU Schubert
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892
J Virol 68:2260-71. 1994.... - The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor kappaB-dependent expression of antiapoptotic factorsH Akari
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Exp Med 194:1299-311. 2001..Thus, Vpu induces apoptosis through activation of the caspase pathway by way of inhibiting the NF-kappaB-dependent expression of antiapoptotic genes... - Production of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cellsSandra Kao
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, NIH, Building 4, Room 310, 4 Center Drive, MSC 0460, Bethesda, MD 20892 0460, USA
Retrovirology 1:27. 2004..Inhibition of APOBEC3G encapsidation is paralleled by a reduction of its intracellular level presumably caused by the Vif-induced proteasome-dependent degradation of APOBEC3G... - Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1Eri Miyagi
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland 20892 0460, USA
J Virol 81:13346-53. 2007..We conclude that efficient inhibition of vif-defective human immunodeficiency virus type 1 requires catalytically active APO3G... - Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virionsMohammad A Khan
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 0460, USA
Retrovirology 4:48. 2007..The goal of this study was to investigate the possible contribution of host RNAs recently identified in intracellular APO3G ribonucleoprotein complexes to APO3G's encapsidation into HIV-1 virions... - Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activityRitu Goila-Gaur
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, NIH, Building 4, Room 310, 4 Center Drive, MSC 0460, Bethesda, MD 20892 0460, USA
Retrovirology 4:61. 2007..A3A is packaged into HIV-1 virions but, unlike A3G, does not have antiviral properties. Here, we investigated the reason for the lack of A3A antiviral activity... - The formation of cysteine-linked dimers of BST-2/tetherin is important for inhibition of HIV-1 virus release but not for sensitivity to VpuAmy J Andrew
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland 20892 0460, USA
Retrovirology 6:80. 2009..A current working model proposes that BST-2 inhibits virus release by tethering viral particles to the cell surface thereby triggering their subsequent endocytosis... - Encapsidation of APOBEC3G into HIV-1 virions involves lipid raft association and does not correlate with APOBEC3G oligomerizationMohammad A Khan
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 0460, USA
Retrovirology 6:99. 2009..It was also reported that W127 and Y124 affect A3G oligomerization... - HIV-1 Vif, APOBEC, and intrinsic immunityRitu Goila-Gaur
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 4 312, Bethesda, Maryland 20892 0460, USA
Retrovirology 5:51. 2008.... - APOBEC3G encapsidation into HIV-1 virions: which RNA is it?Klaus Strebel
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 4 312, Bethesda, MD 20892 0460, USA
Retrovirology 5:55. 2008..There is increasing evidence that RNA binding of APOBEC3G is important for packaging into viral particles. However, there is no consensus yet on the type of RNA involved... - Intravirion processing of the human immunodeficiency virus type 1 Vif protein by the viral protease may be correlated with Vif functionMohammad A Khan
Laboratory of Molecular Microbiology. Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
J Virol 76:9112-23. 2002.... - APOBEC3G & HTLV-1: inhibition without deaminationKlaus Strebel
Laboratory of Molecular Microbiology, Viral Biochemistry Section National Institute of Allergy and Infectious Diseases, NIH Building 4, Room 310 4 Center Drive, MSC 0460 Bethesda, MD 20892 0460, USA
Retrovirology 2:37. 2005..These findings combined with recent reports of deaminase-independent inhibition of Hepatitis B virus as well as HIV-1 suggest that cytidine deaminase activity and antiviral activity may be separable functional properties of APOBEC3G... - The HIV-1 Vpu protein: a multifunctional enhancer of viral particle releaseStephan Bour
Bioinformatics Core Facility, Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 4, Center Drive, Room 337, Bethesda, MD 20892 0460, USA
Microbes Infect 5:1029-39. 2003..This review focuses on presenting our current knowledge of the HIV-1-specific Vpu protein and its essential role in regulating viral particle release, viral load and expression of the CD4 receptor... - Differential sensitivity of "old" versus "new" APOBEC3G to human immunodeficiency virus type 1 vifRitu Goila-Gaur
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland 20892 0460, USA
J Virol 83:1156-60. 2009..Our results suggest that HIV-1 Vif preferentially induces degradation of newly synthesized APOBEC3G but indiscriminately inhibits encapsidation of "old" and "new" APOBEC3G... - Naturally occurring amino acid substitutions in the HIV-2 ROD envelope glycoprotein regulate its ability to augment viral particle releaseStephan Bour
Viral Biochemistry Section, Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 0460, USA
Virology 309:85-98. 2003.... - The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of Ikappa BS Bour
Laboratory of Molecular Microbiology, NIAID, National Institutes of Health, Bethesda, Maryland 20892 0460, USA
J Biol Chem 276:15920-8. 2001..However, in the presence of Vpu, this HIV-mediated NF-kappaB activation was markedly reduced. These results suggest that Vpu modulates both virus- and cytokine-induced activation of NF-kappaB in HIV-1-infected cells... - APOBEC3G-independent reduction in virion infectivity during long-term HIV-1 replication in terminally differentiated macrophagesEri Miyagi
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 0460, USA
Virology 379:266-74. 2008..Thus, the loss of infectivity of HIV-1 viruses produced from long-term infected primary macrophages is due to an APO3G-independent mechanism... - HIV-1 Vpu: putting a channel to the TASKKlaus Strebel
Laboratory of Molecular Microbiology, National Institute for Allergy and Infectious Diseases, National Institutes of Health, 4 Center Drive, MSC 0460, Bethesda, MD 20892, USA
Mol Cell 14:150-2. 2004..In this issue of Molecular Cell, Hsu at all. propose an alternative mechanism: they suggest that Vpu functions by inhibiting another ion channel, TASK-1... - Cytoskeleton association and virion incorporation of the human immunodeficiency virus type 1 Vif proteinM K Karczewski
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892 0460, USA
J Virol 70:494-507. 1996..We propose a model in which Vif has a crucial function as a virion component either by regulating virus maturation or following virus entry into a host cell possibly involving an interaction with the cellular cytoskeletal network... - Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNAM A Khan
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland 20892-0460, USA
J Virol 75:7252-65. 2001..Our data suggest that the specific association of Vif with the viral nucleoprotein complex might be functionally significant and could be a critical requirement for infectivity of viruses produced from restrictive host cells... - HIV accessory genes Vif and VpuKlaus Strebel
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious, Diseases, National Institutes of Health, 4/312, Bethesda, MD 20892, USA
Adv Pharmacol 55:199-232. 2007 - Vif counteracts a cyclophilin A-imposed inhibition of simian immunodeficiency viruses in human cellsHiroaki Takeuchi
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, NIH, Building 4, Room 310, 4 Center Drive, MSC 0460, Bethesda, Maryland 20892 0460, USA
J Virol 81:8080-90. 2007..This is the first report of a novel vif-sensitive antiviral activity of human CypA that may limit zoonotic transmission of SIV and the first demonstration of CypA encapsidation into a virus other than human immunodeficiency virus type 1... - Repression of MHC class I gene promoter activity by two-exon Tat of HIVT K Howcroft
Experimental Immunology Branch, National Cancer Institute, NIH, Bethesda, MD 20892
Science 260:1320-2. 1993..These studies define an activity for two-exon Tat distinct from that of one-exon Tat and suggest a mechanism whereby HIV-1-infected cells might be able to avoid immune surveillance, allowing the virus to persist in the infected host... - Codon optimization of the HIV-1 vpu and vif genes stabilizes their mRNA and allows for highly efficient Rev-independent expressionKim Lien Nguyen
Viral Biochemistry Section, Laboratory of Molecular Microbiology, National Institutes of Allergy Diseases, Bethesda, MD 20892, USA
Virology 319:163-75. 2004.... - Identification of dominant negative human immunodeficiency virus type 1 Vif mutants that interfere with the functional inactivation of APOBEC3G by virus-encoded VifROBERT C WALKER
Laboratory of Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892 0460, USA
J Virol 84:5201-11. 2010..The identification of dominant negative mutants of Vif presents exciting possibilities for the design of novel antiviral strategies... - Virus-host interactions: role of HIV proteins Vif, Tat, and RevKlaus Strebel
Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, NIH, Building-Room 310, 4 Center Drive, MSC 0460, Bethesda, MD 20892-0460, USA
AIDS 17:S25-34. 2003 - Adaptive evolution of Mus Apobec3 includes retroviral insertion and positive selection at two clusters of residues flanking the substrate grooveBradley Sanville
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland, United States of America
PLoS Pathog 6:e1000974. 2010.... - Expression, purification, and activities of full-length and truncated versions of the integral membrane protein Vpu from HIV-1Che Ma
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, USA
Protein Sci 11:546-57. 2002..The C-terminal alpha-helices modulate or promote the oligomerization of Vpu in the membrane and stabilize the conductive state of the channel, in addition to their involvement in CD4 degradation... - Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle productionVasundhara Varthakavi
Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, TN 37232 2581, USA
Proc Natl Acad Sci U S A 100:15154-9. 2003..Vpu overcomes the block to assembly in human cells and in human-simian heterokaryons. The HIV-1 vpu gene may have evolved to counteract an assembly restriction that is present in human cells... - A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletionHongzhan Xu
HIV Drug Resistance Program, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA
Proc Natl Acad Sci U S A 101:5652-7. 2004..The HIV-1 Vif-resistant mutant APOBEC3G could provide a gene therapy approach to combat HIV-1 infection... - Expression of HIV-1 accessory protein Vif is controlled uniquely to be low and optimal by proteasome degradationMikako Fujita
Department of Virology, The University of Tokushima, Graduate School of Medicine, 3 18 15 Kuaramoto cho, Tokushima shi Tokushima 770 8503, Japan
Microbes Infect 6:791-8. 2004..Vif was unique in its short half-life and in the magnitude of the degradation. Taken together, we conclude that the proteasome degradation of HIV-1 Vif is a virologically important process and crucial for the function of Vif... - HIV-1 accessory proteins VPR and Vif modulate antiviral response by targeting IRF-3 for degradationAtsushi Okumura
The Sidney Kimmel Comprehensive Cancer Center, The Johns Hopkins University, Baltimore, MD 21231, USA
Virology 373:85-97. 2008..These data implicate Vif and Vpr in the disruption of the initial antiviral response and point to the need of HIV-1 to circumvent the antiviral response during the very early phase of replication... - A human immunodeficiency virus type 1 protease biosensor assay using bioluminescence resonance energy transferKimberly Hu
HIV-1 RNA Trafficking Laboratory, Sir Mortimer B. Davis-Jewish General Hospital, , , Qu, Canada H3T 1E2
J Virol Methods 128:93-103. 2005..This PR BRET2 biosensor assay can be adapted for high throughput screening of new HIV-1 PR inhibitors. It can be employed to screen for antiviral compounds that also target the proteases of other viruses...