Laboratory for Molecular Diagnostics
Center for Nephrology and Metabolic Disorders

Disorders of mRNA editing

The group of enzymes involved in mRNA editing is called APOBEC. This mRNA modification before its translation plays an important role in lipid metabolism, viral infection defense mechanisms, and possibly tumorgenesis; so disorders in these systems can be expected with mutations of APOBEC genes

Systematic

Hereditary susceptibility to infections
Disorders of mRNA editing
APOBEC1
APOBEC2
APOBEC3A
APOBEC3B
APOBEC3C
APOBEC3D
APOBEC3F
APOBEC3G
APOBEC3H
APOBEC4
HIV resistance
Malaria
Measles infection susceptibility
Meningococcal infection susceptibility
Resistance to trypanosoma brucei
Septic shock

References:

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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Update: Sept. 26, 2018