Molekulargenetische Diagnostik
Praxis Dr. Mato Nagel

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

Erbliche Infektionsanfälligkeiten
HIV-Resistenz
Masern-Infektanfälligkeit
Meningokokken-Infektanfälligkeit
Resistenz gegenüber Trypanosoma brucei
Störungen der mRNA-Editiertfunktion
APOBEC1
APOBEC2
APOBEC3A
APOBEC3B
APOBEC3C
APOBEC3D
APOBEC3F
APOBEC3G
APOBEC3H
APOBEC4

Referenzen:

1.

Vartanian JP et. al. (2008) Evidence for editing of human papillomavirus DNA by APOBEC3 in benign and precancerous lesions.

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2.

Zhang H et. al. (2003) The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA.

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3.

Mangeat B et. al. (2003) Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.

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4.

Harris RS et. al. (2003) DNA deamination mediates innate immunity to retroviral infection.

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5.

Sheehy AM et. al. (2003) The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif.

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6.

Marin M et. al. (2003) HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation.

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7.

Yu X et. al. (2003) Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex.

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8.

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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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.

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10.

Turelli P et. al. (2004) Inhibition of hepatitis B virus replication by APOBEC3G.

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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.

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12.

Zhang J et. al. (2004) Rapid evolution of primate antiviral enzyme APOBEC3G.

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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.

Esnault C et. al. (2005) APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses.

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15.

Chiu YL et. al. (2005) Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells.

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16.

Okeoma CM et. al. (2007) APOBEC3 inhibits mouse mammary tumour virus replication in vivo.

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17.

Wang T et. al. (2007) 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G.

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18.

Chen KM et. al. (2008) Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G.

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19.

Kinoshita SM et. al. (2008) NF-IL6 (C/EBPbeta) induces HIV-1 replication by inhibiting cytidine deaminase APOBEC3G.

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20.

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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21.

Santoni de Sio FR et. al. (2009) APOBEC3G-depleted resting CD4+ T cells remain refractory to HIV1 infection.

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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.

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23.

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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24.

OhAinle M et. al. (2006) Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H.

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