Störungen der mRNA-Editiertfunktion
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.
Gliederung
Referenzen:
| 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 [^] |
