Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G
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Title
Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G
Authors
Keywords
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Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 22, Issue 6, Pages 485-491
Publisher
Springer Nature
Online
2015-05-18
DOI
10.1038/nsmb.3033
References
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Note: Only part of the references are listed.- Structural basis for hijacking CBF-β and CUL5 E3 ligase complex by HIV-1 Vif
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- Suppression of APOBEC3-mediated restriction of HIV-1 by Vif
- (2014) Yuqing Feng et al. Frontiers in Microbiology
- Mapping the Vif–A3G interaction using peptide arrays: A basis for anti-HIV lead peptides
- (2013) Tali H. Reingewertz et al. BIOORGANIC & MEDICINAL CHEMISTRY
- HIV-1 Vif Adaptation to Human APOBEC3H Haplotypes
- (2013) Marcel Ooms et al. Cell Host & Microbe
- The Local Dinucleotide Preference of APOBEC3G Can Be Altered from 5′-CC to 5′-TC by a Single Amino Acid Substitution
- (2013) Anurag Rathore et al. JOURNAL OF MOLECULAR BIOLOGY
- Multiple APOBEC3 Restriction Factors for HIV-1 and One Vif to Rule Them All
- (2013) Belete A. Desimmie et al. JOURNAL OF MOLECULAR BIOLOGY
- Impact of H216 on the DNA Binding and Catalytic Activities of the HIV Restriction Factor APOBEC3G
- (2013) S. Harjes et al. JOURNAL OF VIROLOGY
- Crystal Structure of the DNA Cytosine Deaminase APOBEC3F: The Catalytically Active and HIV-1 Vif-Binding Domain
- (2013) Markus-Frederik Bohn et al. STRUCTURE
- Structural determinants of HIV-1 Vif susceptibility and DNA binding in APOBEC3F
- (2013) Karen K. Siu et al. Nature Communications
- NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity
- (2013) In-Ja L. Byeon et al. Nature Communications
- HIV Restriction Factors and Mechanisms of Evasion
- (2013) M. H. Malim et al. Cold Spring Harbor Perspectives in Medicine
- The Restriction Factors of Human Immunodeficiency Virus
- (2012) Reuben S. Harris et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The APOBEC3C crystal structure and the interface for HIV-1 Vif binding
- (2012) Shingo Kitamura et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Endogenous Origins of HIV-1 G-to-A Hypermutation and Restriction in the Nonpermissive T Cell Line CEM2n
- (2012) Eric W. Refsland et al. PLoS Pathogens
- A Single Amino Acid in Human APOBEC3F Alters Susceptibility to HIV-1 Vif
- (2010) John S. Albin et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Long-Term Restriction by APOBEC3F Selects Human Immunodeficiency Virus Type 1 Variants with Restored Vif Function
- (2010) J. S. Albin et al. JOURNAL OF VIROLOGY
- Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes and tissues: implications for HIV-1 restriction
- (2010) Eric W. Refsland et al. NUCLEIC ACIDS RESEARCH
- Crystal Structure of the APOBEC3G Catalytic Domain Reveals Potential Oligomerization Interfaces
- (2010) Shivender M.D. Shandilya et al. STRUCTURE
- Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G
- (2009) Ayako Furukawa et al. EMBO JOURNAL
- An Extended Structure of the APOBEC3G Catalytic Domain Suggests a Unique Holoenzyme Model
- (2009) Elena Harjes et al. JOURNAL OF MOLECULAR BIOLOGY
- A Patch of Positively Charged Amino Acids Surrounding the Human Immunodeficiency Virus Type 1 Vif SLVx4Yx9Y Motif Influences Its Interaction with APOBEC3G
- (2009) G. Chen et al. JOURNAL OF VIROLOGY
- Identification of a Novel WxSLVK Motif in the N Terminus of Human Immunodeficiency Virus and Simian Immunodeficiency Virus Vif That Is Critical for APOBEC3G and APOBEC3F Neutralization
- (2009) Y. Dang et al. JOURNAL OF VIROLOGY
- Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis
- (2009) Delphine Lavens et al. NUCLEIC ACIDS RESEARCH
- HIV-1 Accessory Proteins—Ensuring Viral Survival in a Hostile Environment
- (2008) Michael H. Malim et al. Cell Host & Microbe
- Evolution of HIV-1 Isolates that Use a Novel Vif-Independent Mechanism to Resist Restriction by Human APOBEC3G
- (2008) Guylaine Haché et al. CURRENT BIOLOGY
- Regulation of APOBEC3 Proteins by a Novel YXXL Motif in Human Immunodeficiency Virus Type 1 Vif and Simian Immunodeficiency Virus SIVagm Vif
- (2008) E. Pery et al. JOURNAL OF VIROLOGY
- Distinct Domains within APOBEC3G and APOBEC3F Interact with Separate Regions of Human Immunodeficiency Virus Type 1 Vif
- (2008) R. A. Russell et al. JOURNAL OF VIROLOGY
- Guidelines for Naming Nonprimate APOBEC3 Genes and Proteins
- (2008) R. S. LaRue et al. JOURNAL OF VIROLOGY
- Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F
- (2008) T YAMASHITA et al. MICROBES AND INFECTION
- Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications
- (2008) Lauren G. Holden et al. NATURE
- Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G
- (2008) Kuan-Ming Chen et al. NATURE
- pCold-GST vector: A novel cold-shock vector containing GST tag for soluble protein production
- (2008) Kokoro Hayashi et al. PROTEIN EXPRESSION AND PURIFICATION
- Characterization of APOBEC3G binding to 7SL RNA
- (2008) Daniel Bach et al. Retrovirology
- Single-stranded RNA facilitates nucleocapsid: APOBEC3G complex formation
- (2008) H. P. Bogerd et al. RNA
- Function analysis of sequences in human APOBEC3G involved in Vif-mediated degradation
- (2007) Li Zhang et al. VIROLOGY
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