A Direct Interaction with RNA Dramatically Enhances the Catalytic Activity of the HIV-1 Protease In Vitro

scientific article published on 15 May 2015

A Direct Interaction with RNA Dramatically Enhances the Catalytic Activity of the HIV-1 Protease In Vitro is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.JMB.2015.05.007
P932PMC publication ID4465046
P698PubMed publication ID25986307

P50authorRonald SwanstromQ62641484
P2093author name stringCelia A Schiffer
Sook-Kyung Lee
Debra Ragland
Ellen Nalivaika
Marc Potempa
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An allosteric modulator of HIV-1 protease shows equipotent inhibition of wild-type and drug-resistant proteasesQ34061377
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Context surrounding processing sites is crucial in determining cleavage rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol polyprotein precursors by viral proteaseQ35921690
G-quartets direct assembly of HIV-1 nucleocapsid protein along single-stranded DNA.Q36118837
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The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency.Q36636632
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Catalytic contribution of flap-substrate hydrogen bonds in "HIV-1 protease" explored by chemical synthesisQ36718166
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Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivityQ37480211
???Q57904706
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tRNA stabilization by modified nucleotidesQ37748755
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Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites.Q39579012
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The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions.Q40042979
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In vivo processing of Pr160gag-pol from human immunodeficiency virus type 1 (HIV) in acutely infected, cultured human T-lymphocytesQ41258387
Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanismQ41275889
Ordered processing of the human immunodeficiency virus type 1 GagPol precursor is influenced by the context of the embedded viral proteaseQ41997191
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A strongly transdominant mutation in the human immunodeficiency virus type 1 gag gene defines an Achilles heel in the virus life cycleQ42546287
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The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrateQ43041225
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An ordered single-stranded structure for polyadenylic acid in denaturing solvents. An X-ray fiber diffraction and model building studyQ44577848
Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activityQ44639077
Proteolytic processing of an HIV-1 pol polyprotein precursor: insights into the mechanism of reverse transcriptase p66/p51 heterodimer formationQ44926187
Influence of flanking sequences on the dimer stability of human immunodeficiency virus type 1 proteaseQ45767677
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Direct measurements of base stacking interactions in DNA by single-molecule atomic-force spectroscopy.Q50942592
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Comparative analysis of the sequences and structures of HIV-1 and HIV-2 proteasesQ68051379
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Proton magnetic resonance study of polydeoxyriboadenylic acidQ70621431
Nucleic acid binding properties of recombinant Zn2 HIV-1 nucleocapsid protein are modulated by COOH-terminal processingQ72165705
Wild-type and mutant HIV type 1 nucleocapsid proteins increase the proportion of long cDNA transcripts by viral reverse transcriptaseQ73307812
The i-motif in nucleic acidsQ73889028
The molecular structure of polyadenylic acidQ78992461
Dynamics of "flap" structures in three HIV-1 protease/inhibitor complexes probed by total chemical synthesis and pulse-EPR spectroscopyQ83131659
Dynamic flaps in HIV-1 protease adopt unique ordering at different stages in the catalytic cycleQ83782525
P4510describes a project that usesImageQuantQ112270642
P433issue14
P407language of work or nameEnglishQ1860
P304page(s)2360-2378
P577publication date2015-05-15
P1433published inJournal of Molecular BiologyQ925779
P1476titleA Direct Interaction with RNA Dramatically Enhances the Catalytic Activity of the HIV-1 Protease In Vitro
P478volume427

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cites work (P2860)
Q51740197An RNA-binding compound that stabilizes the HIV-1 gRNA packaging signal structure and specifically blocks HIV-1 RNA encapsidation.
Q26739673Coordination of Genomic RNA Packaging with Viral Assembly in HIV-1
Q59361002Effect of tRNA on the Maturation of HIV-1 Reverse Transcriptase
Q61445564Targeting HIV-1 Protease Autoprocessing for High-throughput Drug Discovery and Drug Resistance Assessment

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