Molekulargenetisches Labor
Zentrum für Nephrologie und Stoffwechsel
Der Körper verfügt über verschiedene Enzyme, welche die mRNA vor der Translation verändern können. Die Gruppe dieser Enzyme wird als APOBEC zusammengefasst. Das mRNA-Editieren spielt eine wichtige Rolle im Fettstoffwechsel, bei der Infektabwehr (insbesondere viraler Infektionen) und möglicherweise auch in der Tumorgenese. Folglich könnten Störungen in diesen Systemen bei Mutationen der APOBEC-Gene auftreten.
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Zhang J et al. (2004) Rapid evolution of primate antiviral enzyme APOBEC3G. 
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| 2. |
OhAinle M et al. (2006) Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H.
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| 3. |
Rogozin IB et al. (2005) APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis.
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Okeoma CM et al. (2010) APOBEC3 proteins expressed in mammary epithelial cells are packaged into retroviruses and can restrict transmission of milk-borne virions.
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| 5. |
Santoni de Sio FR et al. (2009) APOBEC3G-depleted resting CD4+ T cells remain refractory to HIV1 infection.
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| 6. |
Kamata M et al. (2009) Reassessing the role of APOBEC3G in human immunodeficiency virus type 1 infection of quiescent CD4+ T-cells.
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| 7. |
Kinoshita SM et al. (2008) NF-IL6 (C/EBPbeta) induces HIV-1 replication by inhibiting cytidine deaminase APOBEC3G.
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| 8. |
Chen KM et al. (2008) Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G.
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| 9. |
Wang T et al. (2007) 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G.
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| 10. |
Okeoma CM et al. (2007) APOBEC3 inhibits mouse mammary tumour virus replication in vivo.
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| 11. |
Chiu YL et al. (2005) Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells.
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| 12. |
Esnault C et al. (2005) APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses.
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| 13. |
Rösler C et al. (2004) Comment on "Inhibition of hepatitis B virus replication by APOBEC3G".
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| 14. |
Xu H et al. (2004) A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion.
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| 15. |
Turelli P et al. (2004) Inhibition of hepatitis B virus replication by APOBEC3G.
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| 16. |
Bogerd HP et al. (2004) A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor.
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| 17. |
Schröfelbauer B et al. (2004) A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif).
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| 18. |
Yu X et al. (2003) Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex.
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| 19. |
Marin M et al. (2003) HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation.
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| 20. |
Sheehy AM et al. (2003) The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif.
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| 21. |
Harris RS et al. (2003) DNA deamination mediates innate immunity to retroviral infection.
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| 22. |
Mangeat B et al. (2003) Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.
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| 23. |
Zhang H et al. (2003) The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA.
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| 24. |
Vartanian JP et al. (2008) Evidence for editing of human papillomavirus DNA by APOBEC3 in benign and precancerous lesions.
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| 25. |
OMIM.ORG article Omim 600130
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