(PDF) Oligomerization and RNA Binding Domains of the Type 1

Oligomerization and RNA Binding Domains of the Type 1 Human Immunodeficiency Virus Rev Protein: A Dual Function for an Arginine-Rich Binding Motif.

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

doi 10.1073/pnas.88.17.7734

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September 1, 1991

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Proceedings of the National Academy of Sciences

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Oligomerization and RNA Binding Domains of the Type 1 Human Immunodeficiency Virus Rev Protein: A Dual Function for an Arginine-Rich Binding Motif.

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

doi 10.1073/pnas.88.17.7734

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Identification of a High-Affinity RNA-binding Site for the Human Immunodeficiency Virus Type 1 Rev Protein

Identification of a High-Affinity RNA-binding Site for the Human Immunodeficiency Virus Type 1 Rev Protein.

The Arginine-Rich Domains Present in Human Immunodeficiency Virus Type 1 Tat and Rev Function as Direct Importin Β-Dependent Nuclear Localization Signals

Alternatively Expressed Domains of AU-rich Element RNA-binding Protein 1 (AUF1) Regulate RNA-binding Affinity, RNA-induced Protein Oligomerization, and the Local Conformation of Bound RNA Ligands

Functional Mapping of the Human Immunodeficiency Virus Type 1 Rev RNA Binding Domain: New Insights Into the Domain Structure of Rev and Rex.

Exchange of the Basic Domain of Human Immunodeficiency Virus Type 1 Rev for a Polyarginine Stretch Expands the RNA Binding Specificity, and a Minimal Arginine Cluster Is Required for Optimal RRE RNA Binding Affinity, Nuclear Accumulation, and Trans-Activation

Cellular Protein Modulates Effects of Human Immunodeficiency Virus Type 1 Rev.

Human Immunodeficiency Virus Type 1 Spinoculation Enhances Infection Through Virus Binding

The Rev Protein of Human Immunodeficiency Virus Type 1 Counteracts the Effect of an AU-rich Negative Element in the Human Papillomavirus Type 1 Late 3' Untranslated Region.