Functional Genomics in HIV-1 Virus Replication: Protein-Protein Interactions as a Basis for Recruiting the Host Cell Machinery for Viral Propagation
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Taurai Tasara
, Michael O. Hottiger and Ulrich Hübscher
Abstract
Identification and characterization of proteinprotein interactions between the host cell and parasites both enhance our understanding of basic cell biology and provide insights into central processes of parasite life cycles. Research on HIV-1 has broadened our knowledge of the various molecular events involved. However, our understanding of how this virus interacts with the host cell at the level of proteinprotein interaction is still limited. Through these interactions the virus is able to recruit certain cellular metabolic pathways for its replication. Here we summarize our current knowledge of proteinprotein interactions between HIV-1 and host cell factors during viral replication.
Copyright © 2001 by Walter de Gruyter GmbH & Co. KG
Articles in the same Issue
- Functional Genomics in HIV-1 Virus Replication: Protein-Protein Interactions as a Basis for Recruiting the Host Cell Machinery for Viral Propagation
- On the Characterization of the Putative S20-Thx Operon of Thermus thermophilus
- RNase-Stable RNA: Conformational Parameters of the Nucleic Acid Backbone for Binding to RNase T1
- Enhanced Gamma-Glutamyl Transpeptidase Expression and Superoxide Production in Mpv17-/-Glomerulosclerosis Mice
- Juvenile Hormone Binding Protein and Transferrin from Galleria mellonella Share a Similar Structural Motif
- Analysis of Structural Signals Conferring Localisation of Pig OST48 to the Endoplasmic Reticulum
- Identification and Crystallisation of a Heat- and Protease-Stable Fragment of the Bacteriophage T4 Short Tail Fibre
- Insulin Resistance Induced by Loop Diuretics and Hyperosmolarity in Perfused Rat Liver
- Singlet Molecular Oxygen Triggers the soxRS Regulon of Escherichia coli
- The Extracellular Signal-Regulated Protein Kinases Erk1/Erk2 Stimulate Expression and Biological Activity of the Transcriptional Regulator Egr-1
- The FIRE3-Mediated Sterol Response of the FAS Promoter Requires NF-Y/CBF as a Coactivator
- Complement Factor I Is Upregulated in Rat Hepatocytes by Interleukin-6 But Not by Interferon-γ , Interleukin-1β or Tumor Necrosis Factor-α
- Isolation and Characterization of a Highly Specific Serine Endopeptidase from an Oral Strain of Staphylococcus epidermidis
Articles in the same Issue
- Functional Genomics in HIV-1 Virus Replication: Protein-Protein Interactions as a Basis for Recruiting the Host Cell Machinery for Viral Propagation
- On the Characterization of the Putative S20-Thx Operon of Thermus thermophilus
- RNase-Stable RNA: Conformational Parameters of the Nucleic Acid Backbone for Binding to RNase T1
- Enhanced Gamma-Glutamyl Transpeptidase Expression and Superoxide Production in Mpv17-/-Glomerulosclerosis Mice
- Juvenile Hormone Binding Protein and Transferrin from Galleria mellonella Share a Similar Structural Motif
- Analysis of Structural Signals Conferring Localisation of Pig OST48 to the Endoplasmic Reticulum
- Identification and Crystallisation of a Heat- and Protease-Stable Fragment of the Bacteriophage T4 Short Tail Fibre
- Insulin Resistance Induced by Loop Diuretics and Hyperosmolarity in Perfused Rat Liver
- Singlet Molecular Oxygen Triggers the soxRS Regulon of Escherichia coli
- The Extracellular Signal-Regulated Protein Kinases Erk1/Erk2 Stimulate Expression and Biological Activity of the Transcriptional Regulator Egr-1
- The FIRE3-Mediated Sterol Response of the FAS Promoter Requires NF-Y/CBF as a Coactivator
- Complement Factor I Is Upregulated in Rat Hepatocytes by Interleukin-6 But Not by Interferon-γ , Interleukin-1β or Tumor Necrosis Factor-α
- Isolation and Characterization of a Highly Specific Serine Endopeptidase from an Oral Strain of Staphylococcus epidermidis