Structure-based drug design targeting an inactive RNA conformation: exploiting the flexibility of HIV-1 TAR RNA.
about
Monitoring tat peptide binding to TAR RNA by solid-state 31P-19F REDOR NMRStructure based approaches for targeting non-coding RNAs with small moleculesCyclin Box Structure of the P-TEFb Subunit Cyclin T1 Derived from a Fusion Complex with EIAV TatSimultaneous recognition of HIV-1 TAR RNA bulge and loop sequences by cyclic peptide mimics of Tat proteinEssential structural requirements for specific recognition of HIV TAR RNA by peptide mimetics of Tat proteinA Small-Molecule Probe Induces a Conformation in HIV TAR RNA Capable of Binding Drug-Like FragmentsInhibition of both HIV-1 reverse transcription and gene expression by a cyclic peptide that binds the Tat-transactivating response element (TAR) RNASubstrate recognition and modification by the nosiheptide resistance methyltransferaseA mechanism for S-adenosyl methionine assisted formation of a riboswitch conformation: a small molecule with a strong armDocking to RNA via root-mean-square-deviation-driven energy minimization with flexible ligands and flexible targets.Conformational dynamics of RNA-peptide binding: a molecular dynamics simulation study.Small molecule microarrays of RNA-focused peptoids help identify inhibitors of a pathogenic group I intronTheory and Modeling of RNA Structure and Interactions with Metal Ions and Small Molecules.Ligand-induced changes in 2-aminopurine fluorescence as a probe for small molecule binding to HIV-1 TAR RNATriptolide inhibits human immunodeficiency virus type 1 replication by promoting proteasomal degradation of Tat proteinEfficient in silico exploration of RNA interhelical conformations using Euler angles and WExploreHIV-1 drug discovery: targeting folded RNA structures with branched peptides.Dynamics-based amplification of RNA function and its characterization by using NMR spectroscopy.Characterizing the relative orientation and dynamics of RNA A-form helices using NMR residual dipolar couplings.Conformational heterogeneity of the SAM-I riboswitch transcriptional ON state: a chaperone-like role for S-adenosyl methionine.Multivalent Amino Sugars to Recognize Different TAR RNA Conformations.Characterizing complex dynamics in the transactivation response element apical loop and motional correlations with the bulge by NMR, molecular dynamics, and mutagenesisHow binding of small molecule and peptide ligands to HIV-1 TAR alters the RNA motional landscape.Constructing RNA dynamical ensembles by combining MD and motionally decoupled NMR RDCs: new insights into RNA dynamics and adaptive ligand recognition.An approach to the construction of tailor-made amphiphilic peptides that strongly and selectively bind to hairpin RNA targets.Domain-elongation NMR spectroscopy yields new insights into RNA dynamics and adaptive recognition.Multivalent binding oligomers inhibit HIV Tat-TAR interaction critical for viral replication.Shortening the HIV-1 TAR RNA Bulge by a Single Nucleotide Preserves Motional Modes over a Broad Range of Time Scales.Coarse grained models reveal essential contributions of topological constraints to the conformational free energy of RNA bulges.NMR studies of nucleic acid dynamicsStrategies for the design of RNA-binding small molecules.6-desfluoroquinolones as HIV-1 Tat-mediated transcription inhibitors.Strategies to Block HIV Transcription: Focus on Small Molecule Tat Inhibitors.The design of RNA binders: targeting the HIV replication cycle as a case study.Recent advances in the identification of Tat-mediated transactivation inhibitors: progressing toward a functional cure of HIV.Improving combination antiretroviral therapy by targeting HIV-1 gene transcription.Novel in vivo model for the study of human immunodeficiency virus type 1 transcription inhibitors: evaluation of new 6-desfluoroquinolone derivatives.Cross-interaction between JC virus agnoprotein and human immunodeficiency virus type 1 (HIV-1) Tat modulates transcription of the HIV-1 long terminal repeat in glial cells.Toward targeting RNA structure: branched peptides as cell-permeable ligands to TAR RNA.Iron(II) supramolecular helicates interfere with the HIV-1 Tat-TAR RNA interaction critical for viral replication.
P2860
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P2860
Structure-based drug design targeting an inactive RNA conformation: exploiting the flexibility of HIV-1 TAR RNA.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
Structure-based drug design ta ...... flexibility of HIV-1 TAR RNA.
@en
Structure-based drug design ta ...... flexibility of HIV-1 TAR RNA.
@nl
type
label
Structure-based drug design ta ...... flexibility of HIV-1 TAR RNA.
@en
Structure-based drug design ta ...... flexibility of HIV-1 TAR RNA.
@nl
prefLabel
Structure-based drug design ta ...... flexibility of HIV-1 TAR RNA.
@en
Structure-based drug design ta ...... flexibility of HIV-1 TAR RNA.
@nl
P2093
P1476
Structure-based drug design ta ...... flexibility of HIV-1 TAR RNA.
@en
P2093
Alastair I H Murchie
Andrew J Potter
Catherine D Prescott
Catherine Isel
Fareed Aboul-ela
Ian D Starkey
Jonathan Karn
Justin Bower
Martin J Drysdale
P304
P356
10.1016/J.JMB.2003.12.028
P407
P577
2004-02-01T00:00:00Z