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Relevant bibliographies by topics / AID/APOBEC family, APOBEC1, APOBEC3A, RNA editing / Journal articles

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Journal articles on the topic 'AID/APOBEC family, APOBEC1, APOBEC3A, RNA editing'

Author: Grafiati

Published: 14 March 2023

Last updated: 31 July 2025

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1

Mikl, Marie C., Ian N. Watt, Mason Lu, et al. "Mice Deficient in APOBEC2 and APOBEC3." Molecular and Cellular Biology 25, no. 16 (2005): 7270–77. http://dx.doi.org/10.1128/mcb.25.16.7270-7277.2005.

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ABSTRACT The activation-induced deaminase/apolipoprotein B-editing catalytic subunit 1 (AID/APOBEC) family comprises four groups of proteins. Both AID, a lymphoid-specific DNA deaminase that triggers antibody diversification, and APOBEC2 (function unknown) are found in all vertebrates examined. In contrast, APOBEC1, an RNA-editing enzyme in gastrointestinal cells, and APOBEC3 are restricted to mammals. The function of most APOBEC3s, of which there are seven in human but one in mouse, is unknown, although several human APOBEC3s act as host restriction factors that deaminate human immunodeficien

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2

Chu, Charles C., Xiao-Jie Yan, Arvind Dhayalan, et al. "The Correlation of APOBEC Gene Family Member Expression with Worse CLL Patient Outcome Suggests a Role in CLL Mutational Evolution." Blood 126, no. 23 (2015): 363. http://dx.doi.org/10.1182/blood.v126.23.363.363.

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Abstract A mutational signature consistent with APOBEC (apolipoprotein B mRNA editing enzyme, catalytic polypeptide) activity has been identified in somatic mutations found in large-scale surveys of ultra-deep sequencing data from many human cancers including chronic lymphocytic leukemia (CLL). APOBEC is a cytidine deaminase family made up of eleven genes, including AID (activation-induced cytidine deaminase) and APOBEC3B, both of which have been implicated in somatic mutation in various cancers, including CLL. These observations have led to the hypothesis that APOBEC cytidine deaminases may b

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3

Talluri, Srikanth, Mehmet Kemal Samur, Jialan Shi, et al. "Critical Role for Apobec and Its Interacting Partners in Mediating Mutations and Cell Growth in Multiple Myeloma (MM)." Blood 132, Supplement 1 (2018): 4462. http://dx.doi.org/10.1182/blood-2018-99-118441.

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Abstract The APOBEC family of cytidine deaminases include AID (activity induced deaminase) and 10 related APOBEC enzymes (A1,A2,A3A,A3B,A3C,A3D,A3F,A3G,A3H and A4). AID is well studied for its role in somatic hyper mutation and class switch recombination of immunoglobulin genes. APOBECs (apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like) have been shown to have roles in mRNA editing and in antiviral immunity. Recently, a causal role for the AID/APOBECs in inducing somatic mutations in myeloma has been proposed and we have previously published that APOBEC signature mutations as a

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4

Naumann, Jordan A., Prokopios P. Argyris, Michael A. Carpenter, et al. "DNA Deamination Is Required for Human APOBEC3A-Driven Hepatocellular Carcinoma In Vivo." International Journal of Molecular Sciences 24, no. 11 (2023): 9305. http://dx.doi.org/10.3390/ijms24119305.

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Although the APOBEC3 family of single-stranded DNA cytosine deaminases is well-known for its antiviral factors, these enzymes are rapidly gaining attention as prominent sources of mutation in cancer. APOBEC3′s signature single-base substitutions, C-to-T and C-to-G in TCA and TCT motifs, are evident in over 70% of human malignancies and dominate the mutational landscape of numerous individual tumors. Recent murine studies have established cause-and-effect relationships, with both human APOBEC3A and APOBEC3B proving capable of promoting tumor formation in vivo. Here, we investigate the molecular

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5

Malim, Michael H. "APOBEC proteins and intrinsic resistance to HIV-1 infection." Philosophical Transactions of the Royal Society B: Biological Sciences 364, no. 1517 (2008): 675–87. http://dx.doi.org/10.1098/rstb.2008.0185.

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Members of the APOBEC family of cellular polynucleotide cytidine deaminases, most notably APOBEC3G and APOBEC3F, are potent inhibitors of HIV-1 infection. Wild type HIV-1 infections are largely spared from APOBEC3G/F function through the action of the essential viral protein, Vif. In the absence of Vif, APOBEC3G/F are encapsidated by budding virus particles leading to excessive cytidine (C) to uridine (U) editing of negative sense reverse transcripts in newly infected cells. This registers as guanosine (G) to adenosine (A) hypermutations in plus-stranded cDNA. In addition to this profoundly de

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6

Talluri, Srikanth, Mehmet Kemal Samur, Leutz Buon, et al. "Dysregulated Aid/Apobec Family Proteins Promote Genomic Instability in Multiple Myeloma." Blood 128, no. 22 (2016): 803. http://dx.doi.org/10.1182/blood.v128.22.803.803.

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Abstract The AID/APOBEC family of cytidine deaminase proteins includes AID (activity induced deaminase), and 10 related APOBEC enzymes (A1, A2, A3A, A3B, A3C, A3D, A3F, A3G, A3H and A4). AID has been well-studied for its role in somatic hyper mutation and class switch recombination of immunoglobulin genes whereas APOBECs (apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like) have been shown to have roles in mRNA editing and in antiviral immunity. Dysregulated activity of APOBECs causes C >T transitions or C>G, C>A transversions in DNA. We have recently shown APOBEC signatu

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7

Vieira, Valdimara C., and Marcelo A. Soares. "The Role of Cytidine Deaminases on Innate Immune Responses against Human Viral Infections." BioMed Research International 2013 (2013): 1–18. http://dx.doi.org/10.1155/2013/683095.

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The APOBEC family of proteins comprises deaminase enzymes that edit DNA and/or RNA sequences. The APOBEC3 subgroup plays an important role on the innate immune system, acting on host defense against exogenous viruses and endogenous retroelements. The role of APOBEC3 proteins in the inhibition of viral infection was firstly described for HIV-1. However, in the past few years many studies have also shown evidence of APOBEC3 action on other viruses associated with human diseases, including HTLV, HCV, HBV, HPV, HSV-1, and EBV. APOBEC3 inhibits these viruses through a series of editing-dependent an

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8

Kazuma, Yasuhiro, Kotaro Shirakawa, Anamaria Daniela Sarca, et al. "Interactome Analysis of APOBEC3B in Multiple Myeloma." Blood 134, Supplement_1 (2019): 1259. http://dx.doi.org/10.1182/blood-2019-126856.

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Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like (APOBEC) family proteins restrict retroviruses and retrotransposons by inducing hypermutation or degradation of the replication intermediates through their DNA cytidine deaminase activity. APOBECs can also act as endogenous sources of DNA damage that mutate many human cancers. Accumulation of APOBEC signature mutations is associated with disease progression and poor overall survival in multiple myeloma (Walker et al. Nat Commun, 2015). Among APOBEC3 enzymes, APOBEC3B (A3B) is the only family member that is predominantly located in

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9

Bulliard, Yannick, Priscilla Turelli, Ute F. Röhrig, et al. "Functional Analysis and Structural Modeling of Human APOBEC3G Reveal the Role of Evolutionarily Conserved Elements in the Inhibition of Human Immunodeficiency Virus Type 1 Infection and Alu Transposition." Journal of Virology 83, no. 23 (2009): 12611–21. http://dx.doi.org/10.1128/jvi.01491-09.

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ABSTRACT Retroelements are important evolutionary forces but can be deleterious if left uncontrolled. Members of the human APOBEC3 family of cytidine deaminases can inhibit a wide range of endogenous, as well as exogenous, retroelements. These enzymes are structurally organized in one or two domains comprising a zinc-coordinating motif. APOBEC3G contains two such domains, only the C terminal of which is endowed with editing activity, while its N-terminal counterpart binds RNA, promotes homo-oligomerization, and is necessary for packaging into human immunodeficiency virus type 1 (HIV-1) virions

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10

Lerner, Taga, F. Papavasiliou, and Riccardo Pecori. "RNA Editors, Cofactors, and mRNA Targets: An Overview of the C-to-U RNA Editing Machinery and Its Implication in Human Disease." Genes 10, no. 1 (2018): 13. http://dx.doi.org/10.3390/genes10010013.

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One of the most prevalent epitranscriptomic modifications is RNA editing. In higher eukaryotes, RNA editing is catalyzed by one of two classes of deaminases: ADAR family enzymes that catalyze A-to-I (read as G) editing, and AID/APOBEC family enzymes that catalyze C-to-U. ADAR-catalyzed deamination has been studied extensively. Here we focus on AID/APOBEC-catalyzed editing, and review the emergent knowledge regarding C-to-U editing consequences in the context of human disease.

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11

Santini, Paul A., Bing He, April Chiu, et al. "HIV-1 induces targeted down-regulation of the Ig gene-diversifying enzyme AID in the germinal center of infected lymphoid follicles (45.1)." Journal of Immunology 178, no. 1_Supplement (2007): S57. http://dx.doi.org/10.4049/jimmunol.178.supp.45.1.

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Abstract Class switching from IgM to IgG and IgA is essential for antiviral immunity and requires activation-induced cytidine deaminase (AID), an APOBEC family member with DNA-editing activity. Germinal center (GC) B cells express AID upon activation by CD4+ T cells through CD40 ligand (CD40L) and IL-4. HIV-1 is thought to impair IgG and IgA responses to viral antigens, opportunistic pathogens and vaccines by causing progressive loss of CD4+ T cells and by rendering B cells poorly responsive to CD4+ T cell help. It remains unknown whether HIV-1 targets AID to hamper protective IgG and IgA resp

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12

Kolotova, T. Yu., V.D. Makarenko, L.K. Sorokoumova, and M. B. Davidenko. "AID/APOBEC–dependent somatic hypermutation and DNA rearrangements of immunoglobulin and non-immunoglobulin genes." Annals of Mechnikov Institute, N 4, 2019, no. 4 (December 12, 2019): 6–19. https://doi.org/10.5281/zenodo.3572484.

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Editing Ig genes by activation induced deaminase (AID) initiates the antibody diversification process in B lymphocytes. In mammalian B cells, this process includes somatic hypermutation (SHM) and class switch recombination (CSR). The activity of AID is largely confined to switch regions and Ig variable regions but now it is well established that AID/APOBEC-dependent damage and double DNA breaks leading to genome rearrangements and somatic mutagenesis are pervasive throughout the B cell genome. In this review, we focus on the molecular mechanisms that guide AID/APOBEC mutator to physiological a

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13

Rogozin, Igor, Abiel Roche-Lima, Artem Lada, et al. "Nucleotide Weight Matrices Reveal Ubiquitous Mutational Footprints of AID/APOBEC Deaminases in Human Cancer Genomes." Cancers 11, no. 2 (2019): 211. http://dx.doi.org/10.3390/cancers11020211.

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Cancer genomes accumulate nucleotide sequence variations that number in the tens of thousands per genome. A prominent fraction of these mutations is thought to arise as a consequence of the off-target activity of DNA/RNA editing cytosine deaminases. These enzymes, collectively called activation induced deaminase (AID)/APOBECs, deaminate cytosines located within defined DNA sequence contexts. The resulting changes of the original C:G pair in these contexts (mutational signatures) provide indirect evidence for the participation of specific cytosine deaminases in a given cancer type. The conventi

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14

Najjar, Rayan, Noga Rogel, Jose Mario Bello Pineda, et al. "Large overlap in neutrophil transcriptome between lupus and COVID-19 with limited lupus-specific gene expression." Lupus Science & Medicine 11, no. 1 (2024): e001059. http://dx.doi.org/10.1136/lupus-2023-001059.

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ObjectivesTo illuminate the poorly understood aetiology of SLE by comparing the gene expression profile of SLE neutrophils with that of neutrophils from patients infected by SARS-CoV-2, a disease (COVID-19) with well-defined antigens and a similar type I interferon response.MethodsRNA sequencing of neutrophils from patients with SLE (n=15) and healthy controls (n=12) was analysed for differential gene expression and modulated pathways. The same analyses were performed on a similar neutrophil dataset from patients with SARS-CoV-2 infection (n=30) and healthy controls (n=8). Next, we carried out

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15

Wolfe, Aaron D., Shuxing Li, Cody Goedderz, and Xiaojiang S. Chen. "The structure of APOBEC1 and insights into its RNA and DNA substrate selectivity." NAR Cancer 2, no. 4 (2020). http://dx.doi.org/10.1093/narcan/zcaa027.

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Abstract APOBEC1 (APO1), a member of AID/APOBEC nucleic acid cytosine deaminase family, can edit apolipoprotein B mRNA to regulate cholesterol metabolism. This APO1 RNA editing activity requires a cellular cofactor to achieve tight regulation. However, no cofactors are required for deamination on DNA by APO1 and other AID/APOBEC members, and aberrant deamination on genomic DNA by AID/APOBEC deaminases has been linked to cancer. Here, we present the crystal structure of APO1, which reveals a typical APOBEC deaminase core structure, plus a unique well-folded C-terminal domain that is highly hydr

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16

Meshcheryakova, Anastasia, Peter Pietschmann, Philip Zimmermann, Igor B. Rogozin, and Diana Mechtcheriakova. "AID and APOBECs as Multifaceted Intrinsic Virus-Restricting Factors: Emerging Concepts in the Light of COVID-19." Frontiers in Immunology 12 (July 1, 2021). http://dx.doi.org/10.3389/fimmu.2021.690416.

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The AID (activation-induced cytidine deaminase)/APOBEC (apolipoprotein B mRNA editing enzyme catalytic subunit) family with its multifaceted mode of action emerges as potent intrinsic host antiviral system that acts against a variety of DNA and RNA viruses including coronaviruses. All family members are cytosine-to-uracil deaminases that either have a profound role in driving a strong and specific humoral immune response (AID) or restricting the virus itself by a plethora of mechanisms (APOBECs). In this article, we highlight some of the key aspects apparently linking the AID/APOBECs and SARS-

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17

Lorenzo, J. Paulo, Linda Molla, Elias Moris Amro, et al. "APOBEC2 safeguards skeletal muscle cell fate through binding chromatin and regulating transcription of non-muscle genes during myoblast differentiation." Proceedings of the National Academy of Sciences 121, no. 17 (2024). http://dx.doi.org/10.1073/pnas.2312330121.

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The apolipoprotein B messenger RNA editing enzyme, catalytic polypeptide (APOBEC) family is composed of nucleic acid editors with roles ranging from antibody diversification to RNA editing. APOBEC2, a member of this family with an evolutionarily conserved nucleic acid–binding cytidine deaminase domain, has neither an established substrate nor function. Using a cellular model of muscle differentiation where APOBEC2 is inducibly expressed, we confirmed that APOBEC2 does not have the attributed molecular functions of the APOBEC family, such as RNA editing, DNA demethylation, and DNA mutation. Ins

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18

Zhang, Chi, Yu-Jing Lu, Mei Wang, et al. "Characterisation of APOBEC3B-Mediated RNA editing in breast cancer cells reveals regulatory roles of NEAT1 and MALAT1 lncRNAs." Oncogene, September 25, 2024. http://dx.doi.org/10.1038/s41388-024-03171-5.

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AbstractRNA editing is a crucial post-transcriptional process that influences gene expression and increases the diversity of the proteome as a result of amino acid substitution. Recently, the APOBEC3 family has emerged as a significant player in this mechanism, with APOBEC3A (A3A) having prominent roles in base editing during immune and stress responses. APOBEC3B (A3B), another family member, has gained attention for its potential role in generating genomic DNA mutations in breast cancer. In this study, we coupled an inducible expression cell model with a novel methodology for identifying diff

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Jonathan, Michael, and Terumasa Ikeda. "APOBEC3 family proteins as drivers of virus evolution." Frontiers in Virology 3 (December 18, 2023). http://dx.doi.org/10.3389/fviro.2023.1332010.

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The apolipoprotein B mRNA editing enzyme catalytic polypeptide-like (APOBEC) family consists of cytosine deaminases implicated in diverse and important biological functions. APOBEC3 (A3) proteins belong to the APOBEC/AID family, and they catalyze the deamination of cytosine to uracil in single-stranded DNA and, to a lesser extent, in RNA substrates. In humans, seven A3 genes have been identified (A3A, A3B, A3C, A3D, A3F, A3G, and A3H). The introduction of lethal G-to-A or C-to-U mutations into certain viral genomes leads to virus inactivation. However, the mutagenic capability of A3 proteins c

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20

Jin, Hua, Chong Li, Yunxiao Jia, Yuxuan Qi, and Weilan Piao. "Revealing the hidden RBP–RNA interactions with RNA modification enzyme‐based strategies." WIREs RNA 15, no. 3 (2024). http://dx.doi.org/10.1002/wrna.1863.

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AbstractRNA‐binding proteins (RBPs) are powerful and versatile regulators in living creatures, playing fundamental roles in organismal development, metabolism, and various diseases by the regulation of gene expression at multiple levels. The requirements of deep research on RBP function have promoted the rapid development of RBP–RNA interplay detection methods. Recently, the detection method of fusing RNA modification enzymes (RME) with RBP of interest has become a hot topic. Here, we reviewed RNA modification enzymes in adenosine deaminases that act on RNA (ADAR), terminal nucleotidyl transfe

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21

Christofi, Theodoulakis, and Apostolos Zaravinos. "RNA editing in the forefront of epitranscriptomics and human health." Journal of Translational Medicine 17, no. 1 (2019). http://dx.doi.org/10.1186/s12967-019-2071-4.

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Abstract Post-transcriptional modifications have been recently expanded with the addition of RNA editing, which is predominantly mediated by adenosine and cytidine deaminases acting on DNA and RNA. Here, we review the full spectrum of physiological processes in which these modifiers are implicated, among different organisms. Adenosine to inosine (A-to-I) editors, members of the ADAR and ADAT protein families are important regulators of alternative splicing and transcriptional control. On the other hand, cytidine to uridine (C-to-U) editors, members of the AID/APOBEC family, are heavily implica

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