(Q43686547)

25 November 2017

title

Footprinting and circular dichroism studies on paromomycin binding to the packaging region of human immunodeficiency virus type-1. (English)

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25 November 2017

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Mark P McPike

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25 November 2017

Jerry Goodisman

series ordinal

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25 November 2017

James C Dabrowiak

series ordinal

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25 November 2017

language of work or name

English

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publication date

1 November 2002

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Bioorganic & Medicinal Chemistry

25 November 2017

published in

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25 November 2017

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25 November 2017

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25 November 2017

page(s)

3663-3672

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Interaction of antibiotics with functional sites in 16S ribosomal RNA

25 November 2017

cites work

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Effect of mutations in the A site of 16 S rRNA on aminoglycoside antibiotic-ribosome interaction.

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Paromomycin binding induces a local conformational change in the A-site of 16 S rRNA

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Crystal structure of paromomycin docked into the eubacterial ribosomal decoding A site

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Saccharide-RNA recognition in a complex formed between neomycin B and an RNA aptamer

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Structural basis for recognition of the RNA major groove in the tau exon 10 splicing regulatory element by aminoglycoside antibiotics

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7 January 2021

Structural rearrangements of HIV-1 Tat-responsive RNA upon binding of neomycin B

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Mechanism of neomycin and Rev peptide binding to the Rev responsive element of HIV-1 as determined by fluorescence and NMR spectroscopy

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Enhanced binding of aminoglycoside dimers to a "dimerized" A-site 16S rRNA construct

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Binding of dimeric aminoglycosides to the HIV-1 rev responsive element (RRE) RNA construct

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Specificity in the binding of aminoglycosides to HIV-RRE RNA

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Aminoglycoside binding to human and bacterial A-Site rRNA decoding region constructs

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RNA-aminoglycoside antibiotic interactions: fluorescence detection of binding and conformational change

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Binding of neomycin to the TAR element of HIV-1 RNA induces dissociation of Tat protein by an allosteric mechanism

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7 January 2021

Determinants of aminoglycoside-binding specificity for rRNA by using mass spectrometry

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Aminoglycoside-arginine conjugates that bind TAR RNA: synthesis, characterization, and antiviral activity

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Tobramycin-EDTA conjugate: a noninnocent affinity-cleaving reagent

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Enhanced RNA binding of dimerized aminoglycosides

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Synthesis and anti-HIV activity of guanidinoglycosides

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Strategies for the Design of Drugs Targeting RNA and RNA-Protein Complexes

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Drug-RNA footprinting

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7 January 2021

Absorption studies on aminoglycoside binding to the packaging region of human immunodeficiency virus type-1.

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7 January 2021

Quantitative DNA Footprinting

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7 January 2021

Footprinting methods for analysis of pyrrole-imidazole polyamide/DNA complexes

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7 January 2021

Quantitative footprinting analysis of the chromomycin A3--DNA interaction

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7 January 2021

Circular dichroism and its empirical application to biopolymers

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7 January 2021

Structural RNA mimetics: N3'-->P5' phosphoramidate DNA analogs of HIV-1 RRE and TAR RNA form A-type helices that bind specifically to Rev and Tat-related peptides

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7 January 2021

RNA secondary structure and binding sites for gag gene products in the 5' packaging signal of human immunodeficiency virus type 1.

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7 January 2021

The major HIV-1 packaging signal is an extended bulged stem loop whose structure is altered on interaction with the Gag polyprotein

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7 January 2021

Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure

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7 January 2021

A Decade of Protein Engineering on Ribonuclease T1— Atomic Dissection of the Enzyme‐Substrate Interactions

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7 January 2021

HIV-1 Genome Dimerization: Kissing-Loop Hairpin Dictates Whether Nucleotides Downstream of the 5‘ Splice Junction Contribute to Loose and Tight Dimerization of Human Immunodeficiency Virus RNA

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7 January 2021

NCp7 activates HIV-1Lai RNA dimerization by converting a transient loop-loop complex into a stable dimer

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7 January 2021

Structural requirement for the two-step dimerization of human immunodeficiency virus type 1 genome

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7 January 2021

10.1016/S0968-0896(02)00220-1

Identifiers

DOI

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25 November 2017

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