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RNA recognition by arginine-rich peptide motifs
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scholarly article
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Europe PubMed Central
PubMed ID
10333744
retrieved
28 July 2017
review article
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Europe PubMed Central
title
RNA recognition by arginine-rich peptide motifs
(English)
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Europe PubMed Central
PubMed ID
10333744
retrieved
28 July 2017
author name string
Weiss MA
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
10333744
retrieved
28 July 2017
Narayana N
series ordinal
2
1 reference
stated in
Europe PubMed Central
PubMed ID
10333744
retrieved
28 July 2017
publication date
1 January 1998
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stated in
Europe PubMed Central
PubMed ID
10333744
retrieved
28 July 2017
published in
Biopolymers
1 reference
stated in
Europe PubMed Central
PubMed ID
10333744
retrieved
28 July 2017
volume
48
1 reference
stated in
Europe PubMed Central
PubMed ID
10333744
retrieved
28 July 2017
page(s)
167-180
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stated in
Europe PubMed Central
PubMed ID
10333744
retrieved
28 July 2017
issue
2-3
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stated in
Europe PubMed Central
PubMed ID
10333744
retrieved
28 July 2017
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Sequence-specific recognition of RNA hairpins by bacteriophage antiterminators requires a conserved arginine-rich motif
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An inhibitor of the Tat/TAR RNA interaction that effectively suppresses HIV-1 replication
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Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex
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Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex
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Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex
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Deep penetration of an alpha-helix into a widened RNA major groove in the HIV-1 rev peptide-RNA aptamer complex
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Structure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge
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Structural change in Rev responsive element RNA of HIV-1 on binding Rev peptide
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A 1.3-A resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation
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Solution structure of P22 transcriptional antitermination N peptide-boxB RNA complex
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Arginine-mediated RNA recognition: the arginine fork.
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Role of RNA structure in arginine recognition of TAR RNA.
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RNA recognition by an isolated alpha helix
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An RNA-binding peptide from bovine immunodeficiency virus Tat protein recognizes an unusual RNA structure
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Costabilization of peptide and RNA structure in an HIV Rev peptide-RRE complex
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Structural variety of arginine-rich RNA-binding peptides
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A peptide interaction in the major groove of RNA resembles protein interactions in the minor groove of DNA.
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A structural model for the HIV-1 Rev-RRE complex deduced from altered-specificity rev variants isolated by a rapid genetic strategy
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Role REVersal: understanding how RRE RNA binds its peptide ligand
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An RNA enhancer in a phage transcriptional antitermination complex functions as a structural switch
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Assembly of the N-dependent antitermination complex of phage lambda: NusA and RNA bind independently to different unfolded domains of the N protein
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Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein.
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Selection of RNA-binding peptides in vivo
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A novel glutamine-RNA interaction identified by screening libraries in mammalian cells
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RNA-binding proteins tamed.
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Termination Factor for RNA Synthesis
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Coliphage λnutL−: A unique class of mutants defective in the site of gene N product utilization for antitermination of leftward transcription
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Control of transcription termination by RNA-binding proteins
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Transcriptional antitermination
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Transcription antitermination: the lambda paradigm updated
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Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage lambda
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A protein-RNA interaction network facilitates the template-independent cooperative assembly on RNA polymerase of a stable antitermination complex containing the lambda N protein
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Effects of all single base substitutions in the loop of boxB on antitermination of transcription by bacteriophage lambda's N protein
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The role of Tat in the human immunodeficiency virus life cycle indicates a primary effect on transcriptional elongation
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HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors
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Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat
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The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein
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The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor
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HIV-1 tat binds TAFII250 and represses TAFII250-dependent transcription of major histocompatibility class I genes
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Activation of integrated provirus requires histone acetyltransferase. p300 and P/CAF are coactivators for HIV-1 Tat
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Dimerization of the tat protein from human immunodeficiency virus: a cysteine-rich peptide mimics the normal metal-linked dimer interface
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The structure of the human immunodeficiency virus type-1 TAR RNA reveals principles of RNA recognition by Tat protein
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Three-dimensional structure of a hammerhead ribozyme
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Crystal structure of a group I ribozyme domain: principles of RNA packing
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Electrostatic interactions modulate the RNA-binding and transactivation specificities of the human immunodeficiency virus and simian immunodeficiency virus Tat proteins
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The SRY high-mobility-group box recognizes DNA by partial intercalation in the minor groove: a topological mechanism of sequence specificity
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Specific recognition of HIV-1 TAR RNA by a D-Tat peptide
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NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif
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Circular dichroism studies suggest that TAR RNA changes conformation upon specific binding of arginine or guanidine
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Binding of an HIV Rev peptide to Rev responsive element RNA induces formation of purine-purine base pairs
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RNA recognition by a bent alpha-helix regulates transcriptional antitermination in phage lambda
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21 January 2018
Complexes of N antitermination protein of phage lambda with specific and nonspecific RNA target sites on the nascent transcript
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21 January 2018
RNA-mediated signaling in transcription
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21 January 2018
Major groove accessibility of RNA
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21 January 2018
Clustered arginine residues of bacteriophage lambda N protein are essential to antitermination of transcription, but their locale cannot compensate for boxB loop defects
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Conformation of the TAR RNA-Arginine Complex by NMR Spectroscopy
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Identifiers
DOI
10.1002/(SICI)1097-0282(1998)48:2<167::AID-BIP6>3.0.CO;2-8
1 reference
stated in
Europe PubMed Central
PubMed ID
10333744
retrieved
28 July 2017
PubMed ID
10333744
1 reference
stated in
Europe PubMed Central
PubMed ID
10333744
retrieved
28 July 2017
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