An inhibitor of the Tat/TAR RNA interaction that effectively suppresses HIV-1 replication (Q28379540)

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E R Felder

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G Heizmann

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J Lazdins

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F Aboul-ela

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G Varani

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J Karn

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T Klimkait

Proceedings of the National Academy of Sciences of the United States of America

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language of work or name

English

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publication date

15 April 1997

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published in

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volume

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issue

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page(s)

3548-53

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cites work

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Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex

20 March 2017

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CGP 53437, an orally bioavailable inhibitor of human immunodeficiency virus type 1 protease with potent antiviral activity

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Combinatorially selected guanosine-quartet structure is a potent inhibitor of human immunodeficiency virus envelope-mediated cell fusion

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The human immunodeficiency virus type 1 Tat antagonist, Ro 5-3335, predominantly inhibits transcription initiation from the viral promoter

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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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Anti-termination of transcription within the long terminal repeat of HIV-1 by tat gene product

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HIV-1 Tat protein increases transcriptional initiation and stabilizes elongation

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Hydrogen-bonding contacts in the major groove are required for human immunodeficiency virus type-1 tat protein recognition of TAR RNA.

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HIV-1 Tat protein promotes formation of more-processive elongation complexes

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Keto/Enol Epoxy Steroids as HIV-1 Tat Inhibitors: Structure-Activity Relationships and Pharmacophore Localization

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2 June 2018

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Analysis of arginine-rich peptides from the HIV Tat protein reveals unusual features of RNA-protein recognition

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High affinity binding of TAR RNA by the human immunodeficiency virus type-1 tat protein requires base-pairs in the RNA stem and amino acid residues flanking the basic region

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A new type of synthetic peptide library for identifying ligand-binding activity

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Efficient method for the preparation of peptoids [oligo(N-substituted glycines)] by submonomer solid-phase synthesis

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Conformation of the TAR RNA-Arginine Complex by NMR Spectroscopy

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