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.
| 1. |
Vartanian JP et al. (2008) Evidence for editing of human papillomavirus DNA by APOBEC3 in benign and precancerous lesions. [^] |
| 2. |
Zhang H et al. (2003) The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. [^] |
| 3. |
Mangeat B et al. (2003) Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. [^] |
| 4. |
Harris RS et al. (2003) DNA deamination mediates innate immunity to retroviral infection. [^] |
| 5. |
Sheehy AM et al. (2003) The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. [^] |
| 6. |
Marin M et al. (2003) HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. [^] |
| 7. |
Yu X et al. (2003) Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. [^] |
| 8. |
Schröfelbauer B et al. (2004) A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif). [^] |
| 9. |
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. [^] |
| 10. |
Turelli P et al. (2004) Inhibition of hepatitis B virus replication by APOBEC3G. [^] |
| 11. |
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. [^] |
| 12. |
Zhang J et al. (2004) Rapid evolution of primate antiviral enzyme APOBEC3G. [^] |
| 13. |
Rösler C et al. (2004) Comment on "Inhibition of hepatitis B virus replication by APOBEC3G". [^] |
| 14. |
Esnault C et al. (2005) APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses. [^] |
| 15. |
Chiu YL et al. (2005) Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells. [^] |
| 16. |
Okeoma CM et al. (2007) APOBEC3 inhibits mouse mammary tumour virus replication in vivo. [^] |
| 17. |
Wang T et al. (2007) 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G. [^] |
| 18. |
Chen KM et al. (2008) Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. [^] |
| 19. |
Kinoshita SM et al. (2008) NF-IL6 (C/EBPbeta) induces HIV-1 replication by inhibiting cytidine deaminase APOBEC3G. [^] |
| 20. |
Kamata M et al. (2009) Reassessing the role of APOBEC3G in human immunodeficiency virus type 1 infection of quiescent CD4+ T-cells. [^] |
| 21. |
Santoni de Sio FR et al. (2009) APOBEC3G-depleted resting CD4+ T cells remain refractory to HIV1 infection. [^] |
| 22. |
Okeoma CM et al. (2010) APOBEC3 proteins expressed in mammary epithelial cells are packaged into retroviruses and can restrict transmission of milk-borne virions. [^] |
| 23. |
Rogozin IB et al. (2005) APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy)cytidine deaminases predicted by computational analysis. [^] |
| 24. |
OhAinle M et al. (2006) Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H. [^] |
| 25. |
OMIM.ORG article Omim 600130 [^] |
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