(PDF) Dominant-Negative Mutants of Human MxA Protein:

Dominant-Negative Mutants of Human MxA Protein: Domains in the Carboxy-Terminal Moiety Are Important for Oligomerization and Antiviral Activity.

Journal of Virology - United States

doi 10.1128/jvi.71.4.2591-2599.1997

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January 1, 1997

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American Society for Microbiology

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Dominant-Negative Mutants of Human MxA Protein: Domains in the Carboxy-Terminal Moiety Are Important for Oligomerization and Antiviral Activity.

Journal of Virology - United States

doi 10.1128/jvi.71.4.2591-2599.1997

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Structural Requirements for the Antiviral Activity of the Human MxA Protein Against Thogoto and Influenza a Virus

Two Independent Regions of Human Telomerase Reverse Transcriptase Are Important for Its Oligomerization and Telomerase Activity

N-Terminal Domains of AhAREB1 Protein Are Necessary for Transcriptional Characteristics and Negative Regulation of the AhNCED1 Gene

Correction: Distinct Domains Within the Human Cytomegalovirus UL26 Protein Are Important for Wildtype Viral Replication and Virion Stability

Oligomerization of the Carboxyl Terminal Domain of the Human Coronavirus 229E Nucleocapsid Protein

Further Characterization of Functional Domains of PerA, Role of Amino and Carboxy Terminal Domains in DNA Binding

Suppression of Senescence in Normal Human Fibroblasts by Introduction of Dominant-Negative P53 Mutants or Human Papilloma Virus Type 16 E6 Protein

Interferon-Induced Antiviral Protein MxA Interacts With the Cellular RNA Helicases UAP56 and URH49

Identification of a Dominant Negative Inhibitor of Human Zinc Finger Antiviral Protein Reveals a Functional Endogenous Pool and Critical Homotypic Interactions