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    Apobec3 apolipoprotein B mRNA editing enzyme, catalytic polypeptide 3 [ Mus musculus (house mouse) ]

    Gene ID: 80287, updated on 1-Oct-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Apobec-mediated retroviral hypermutation in vivo is dependent on mouse strain.

    Apobec-mediated retroviral hypermutation in vivo is dependent on mouse strain.
    Byun H, Singh GB, Xu WK, Das P, Reyes A, Battenhouse A, Wylie DC, Santiago ML, Lozano MM, Dudley JP., Free PMC Article

    09/19/2024
    Direct inhibition of human APOBEC3 deaminases by HIV-1 Vif independent of the proteolysis pathway.

    Direct inhibition of human APOBEC3 deaminases by HIV-1 Vif independent of the proteolysis pathway.
    Kamba K, Wan L, Unzai S, Morishita R, Takaori-Kondo A, Nagata T, Katahira M.,

    02/12/2024
    The role of APOBEC3B in lung tumor evolution and targeted cancer therapy resistance.

    The role of APOBEC3B in lung tumor evolution and targeted cancer therapy resistance.
    Caswell DR, Gui P, Mayekar MK, Law EK, Pich O, Bailey C, Boumelha J, Kerr DL, Blakely CM, Manabe T, Martinez-Ruiz C, Bakker B, De Dios Palomino Villcas J, I Vokes N, Dietzen M, Angelova M, Gini B, Tamaki W, Allegakoen P, Wu W, Humpton TJ, Hill W, Tomaschko M, Lu WT, Haderk F, Al Bakir M, Nagano A, Gimeno-Valiente F, de Carné Trécesson S, Vendramin R, Barbè V, Mugabo M, Weeden CE, Rowan A, McCoach CE, Almeida B, Green M, Gomez C, Nanjo S, Barbosa D, Moore C, Przewrocka J, Black JRM, Grönroos E, Suarez-Bonnet A, Priestnall SL, Zverev C, Lighterness S, Cormack J, Olivas V, Cech L, Andrews T, Rule B, Jiao Y, Zhang X, Ashford P, Durfee C, Venkatesan S, Temiz NA, Tan L, Larson LK, Argyris PP, Brown WL, Yu EA, Rotow JK, Guha U, Roper N, Yu J, Vogel RI, Thomas NJ, Marra A, Selenica P, Yu H, Bakhoum SF, Chew SK, Reis-Filho JS, Jamal-Hanjani M, Vousden KH, McGranahan N, Van Allen EM, Kanu N, Harris RS, Downward J, Bivona TG, Swanton C., Free PMC Article

    01/27/2024
    Distinctive High Expression of Antiretroviral APOBEC3 Protein in Mouse Germinal Center B Cells.

    Distinctive High Expression of Antiretroviral APOBEC3 Protein in Mouse Germinal Center B Cells.
    Tsukimoto S, Hakata Y, Tsuji-Kawahara S, Enya T, Tsukamoto T, Mizuno S, Takahashi S, Nakao S, Miyazawa M., Free PMC Article

    05/14/2022
    Multifaceted HIV-1 Vif interactions with human E3 ubiquitin ligase and APOBEC3s.

    Multifaceted HIV-1 Vif interactions with human E3 ubiquitin ligase and APOBEC3s.
    Hu Y, Knecht KM, Shen Q, Xiong Y., Free PMC Article

    07/24/2021
    Molecular analysis of gamma1, gamma3, and alpha class switch recombination junctions in APOBEC3-deficient mice using high-throughput sequencing.

    Molecular analysis of γ1, γ3, and α class switch recombination junctions in APOBEC3-deficient mice using high-throughput sequencing.
    Issaoui H, Ferrad M, Ghazzaui N, Lecardeur S, Cook-Moreau J, Boyer F, Denizot Y., Free PMC Article

    06/5/2021
    Structural perspectives on HIV-1 Vif and APOBEC3 restriction factor interactions.

    Structural perspectives on HIV-1 Vif and APOBEC3 restriction factor interactions.
    Azimi FC, Lee JE., Free PMC Article

    12/26/2020
    Murine Leukemia Virus P50 Protein Counteracts APOBEC3 by Blocking Its Packaging.

    Murine Leukemia Virus P50 Protein Counteracts APOBEC3 by Blocking Its Packaging.
    Zhao W, Akkawi C, Mougel M, Ross SR., Free PMC Article

    11/28/2020
    APOBEC3 regulates keratinocyte differentiation and expression of Notch3.

    APOBEC3 regulates keratinocyte differentiation and expression of Notch3.
    Dainichi T, Nakano Y, Wakae K, Otsuka M, Muramatsu M, Kabashima K.

    10/31/2020
    Impact of Suboptimal APOBEC3G Neutralization on the Emergence of HIV Drug Resistance in Humanized Mice.

    Impact of Suboptimal APOBEC3G Neutralization on the Emergence of HIV Drug Resistance in Humanized Mice.
    Hernandez MM, Fahrny A, Jayaprakash A, Gers-Huber G, Dillon-White M, Audigé A, Mulder LCF, Sachidanandam R, Speck RF, Simon V., Free PMC Article

    08/22/2020
    we report the first parallel, comparative analysis of site selection of APOBEC3 deamination using six of the seven purified APOBEC3 proteins (i.e. A3A, A3B, A3C, A3F, A3G and A3H haplotype II) and oligonucleotides having 5'TC3' or 5'CT3' dinucleotide target sites and variable flanking bases within diverse DNA secondary structures.

    Deamination hotspots among APOBEC3 family members are defined by both target site sequence context and ssDNA secondary structure.
    McDaniel YZ, Wang D, Love RP, Adolph MB, Mohammadzadeh N, Chelico L, Mansky LM., Free PMC Article

    03/21/2020
    Mouse APOBEC3 is an intrinsic inhibitor of retroviral protease function, which is a novel mechanism that explains at least one aspect of its deamination-independent antiretroviral activity.

    Mouse APOBEC3 interferes with autocatalytic cleavage of murine leukemia virus Pr180gag-pol precursor and inhibits Pr65gag processing.
    Hakata Y, Li J, Fujino T, Tanaka Y, Shimizu R, Miyazawa M., Free PMC Article

    02/29/2020
    The distribution of AID and A3s in the epithelial cells as well as germinal centres.

    Expression and subcellular localisation of AID and APOBEC3 in adenoid and palatine tonsils.
    Seishima N, Kondo S, Wakae K, Wakisaka N, Kobayashi E, Kano M, Moriyama-Kita M, Nakanishi Y, Endo K, Imoto T, Ishikawa K, Sugimoto H, Hatano M, Ueno T, Koura M, Kitamura K, Muramatsu M, Yoshizaki T., Free PMC Article

    12/1/2018
    By developing transgenic mice with mutations in the cytidine deamination domains needed for enzymatic activity and interaction with viral RNA, the authors show that APOBEC3 proteins can still restrict in vivo infection by interacting with reverse transcriptase and blocking its activity.

    Deaminase-Dead Mouse APOBEC3 Is an In Vivo Retroviral Restriction Factor.
    Stavrou S, Zhao W, Blouch K, Ross SR., Free PMC Article

    06/30/2018
    our current work indicated that APOBEC3 copy number variations might have a good screening accuracy for breast cancer.

    APOBEC3 deletion increases the risk of breast cancer: a meta-analysis.
    Han Y, Qi Q, He Q, Sun M, Wang S, Zhou G, Sun Y., Free PMC Article

    03/3/2018
    APOBEC3 can restrict retroviruses in a type I interferon-independent manner in vivo. By contrast, the ability of APOBEC3 to promote neutralizing antibody responses is type I interferon-dependent.

    Type I interferon signaling is required for the APOBEC3/Rfv3-dependent neutralizing antibody response but not innate retrovirus restriction.
    Barrett BS, Harper MS, Jones ST, Guo K, Heilman KJ, Kedl RM, Hasenkrug KJ, Santiago ML., Free PMC Article

    04/29/2017
    These results indicate that the mechanisms of APOBEC3 restriction of Koala Retrovirus by humanA3G and mouseA3 differ (deamination dependent vs. independent) and glyco-gag does not play a role in the restriction.

    Human and murine APOBEC3s restrict replication of koala retrovirus by different mechanisms.
    Nitta T, Ha D, Galvez F, Miyazawa T, Fan H., Free PMC Article

    04/30/2016
    The Apobec3/Rfv3-dependent neutralizing antibody response correlated with Friend virus-specific IgG2 titers and that the in vivo neutralization potency of Apobec3/Rfv3-resistant antisera was dependent on activating Fcgamma receptors.

    Requirement for Fc effector mechanisms in the APOBEC3/Rfv3-dependent neutralizing antibody response.
    Halemano K, Barrett BS, Heilman KJ, Morrison TE, Santiago ML., Free PMC Article

    05/23/2015
    A3 shifts the balance, from the fast antibody response mediated by marginal zone B cells with little affinity maturation, to a more sustained germinal center B-cell response

    APOBEC3 enzymes restrict marginal zone B cells.
    Beck-Engeser GB, Winkelmann R, Wheeler ML, Shansab M, Yu P, Wünsche S, Walchhütter A, Metzner M, Vettermann C, Eilat D, DeFranco A, Jäck HM, Wabl M., Free PMC Article

    05/9/2015
    Authors find that the number of N-glycosylated residues in glycosylated Pr80 inversely correlates with the sensitivity of a gammaretrovirus to deamination by mouse APOBEC3.

    N-linked glycosylation protects gammaretroviruses against deamination by APOBEC3 proteins.
    Rosales Gerpe MC, Renner TM, Bélanger K, Lam C, Aydin H, Langlois MA., Free PMC Article

    04/11/2015
    APOBEC3A and APOBEC3B are more abundant on protein level in chronic lymphocytic leukemia (CLL) than in AID, and clustered genomic C>T mutations outside the Ig locus occur at APOBEC3 hot spot motifs in IgV-Mut CLL.

    APOBEC3 signature mutations in chronic lymphocytic leukemia.
    Rebhandl S, Huemer M, Gassner FJ, Zaborsky N, Hebenstreit D, Catakovic K, Grössinger EM, Greil R, Geisberger R., Free PMC Article

    11/8/2014
    APOBEC3 acts as a key player in generating virus-specific neutralizing antibodies that could be harnessed for vaccine development.

    Immunoglobulin somatic hypermutation by APOBEC3/Rfv3 during retroviral infection.
    Halemano K, Guo K, Heilman KJ, Barrett BS, Smith DS, Hasenkrug KJ, Santiago ML., Free PMC Article

    09/6/2014
    loss genotypes of APOBEC3 deletion predispose their carriers to epithelial ovarian cancer (EOC).

    APOBEC3 deletion polymorphism is associated with epithelial ovarian cancer risk among Chinese women.
    Qi G, Xiong H, Zhou C.

    08/23/2014
    The mA3 (APOBEC3) exon 5 is indeed a functional element that influences protein synthesis at a post-transcriptional level.

    Two genetic determinants acquired late in Mus evolution regulate the inclusion of exon 5, which alters mouse APOBEC3 translation efficiency.
    Li J, Hakata Y, Takeda E, Liu Q, Iwatani Y, Kozak CA, Miyazawa M., Free PMC Article

    06/28/2014
    Despite the fact that APOBEC3 in murine leukemia viruse particles does not induce detectable deaminations upon infection, its deaminase activity is easily detected in virus lysates.

    Biochemical and biological studies of mouse APOBEC3.
    Nair S, Sanchez-Martinez S, Ji X, Rein A., Free PMC Article

    05/10/2014
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