Log in

Relevant bibliographies by topics / Adenosine deaminases / Journal articles

Journal articles on the topic 'Adenosine deaminases'

To see the other types of publications on this topic, follow the link: Adenosine deaminases.

Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Adenosine deaminases.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Roth, E. Jr, N. Ogasawara, and S. Schulman. "The deamination of adenosine and adenosine monophosphate in Plasmodium falciparum-infected human erythrocytes: in vitro use of 2'deoxycoformycin and AMP deaminase-deficient red cells." Blood 74, no. 3 (August 15, 1989): 1121–25. http://dx.doi.org/10.1182/blood.v74.3.1121.1121.

Full text

Abstract:

Abstract The role of enzymatic deamination of adenosine monophosphate (AMP) and adenosine in the in vitro growth of the malaria parasite Plasmodium falciparum was investigated by means of human red cells deficient in AMP deaminase to which the adenosine deaminase inhibitor 2′- deoxycoformycin was added. Malaria parasites grew normally in red cells lacking one or both of these enzyme activities. As a further probe of adenosine triphosphate (ATP) catabolism, both infected and uninfected RBCs were incubated with NaF (with and without 2′-deoxycoformycin) and the purine nucleotide/nucleoside content was analyzed by high- performance liquid chromatography (HPLC). Uninfected RBCs lacking either AMP or adenosine deaminase were able to bypass the enzyme block and degrade ATP to hypoxanthine. Uninfected RBCs with both deaminases blocked were unable to produce significant quantities of hypoxanthine. On the other hand, infected RBCs were able to bypass blockade of both deaminases and produce hypoxanthine and adenosine. These findings establish that deamination of adenosine and/or AMP are not essential for plasmodial growth. However, further work will be required to elucidate the pathways that permit the parasites to bypass these catabolic steps.

APA, Harvard, Vancouver, ISO, and other styles

2

Roth, E. Jr, N. Ogasawara, and S. Schulman. "The deamination of adenosine and adenosine monophosphate in Plasmodium falciparum-infected human erythrocytes: in vitro use of 2'deoxycoformycin and AMP deaminase-deficient red cells." Blood 74, no. 3 (August 15, 1989): 1121–25. http://dx.doi.org/10.1182/blood.v74.3.1121.bloodjournal7431121.

Full text

Abstract:

The role of enzymatic deamination of adenosine monophosphate (AMP) and adenosine in the in vitro growth of the malaria parasite Plasmodium falciparum was investigated by means of human red cells deficient in AMP deaminase to which the adenosine deaminase inhibitor 2′- deoxycoformycin was added. Malaria parasites grew normally in red cells lacking one or both of these enzyme activities. As a further probe of adenosine triphosphate (ATP) catabolism, both infected and uninfected RBCs were incubated with NaF (with and without 2′-deoxycoformycin) and the purine nucleotide/nucleoside content was analyzed by high- performance liquid chromatography (HPLC). Uninfected RBCs lacking either AMP or adenosine deaminase were able to bypass the enzyme block and degrade ATP to hypoxanthine. Uninfected RBCs with both deaminases blocked were unable to produce significant quantities of hypoxanthine. On the other hand, infected RBCs were able to bypass blockade of both deaminases and produce hypoxanthine and adenosine. These findings establish that deamination of adenosine and/or AMP are not essential for plasmodial growth. However, further work will be required to elucidate the pathways that permit the parasites to bypass these catabolic steps.

APA, Harvard, Vancouver, ISO, and other styles

3

Keegan, Liam P., André P. Gerber, Jim Brindle, Ronny Leemans, Angela Gallo, Walter Keller, and Mary A. O'Connell. "The Properties of a tRNA-Specific Adenosine Deaminase from Drosophila melanogaster Support an Evolutionary Link between Pre-mRNA Editing and tRNA Modification." Molecular and Cellular Biology 20, no. 3 (February 1, 2000): 825–33. http://dx.doi.org/10.1128/mcb.20.3.825-833.2000.

Full text

Abstract:

ABSTRACT Pre-mRNA editing involving the conversion of adenosine to inosine is mediated by adenosine deaminases that act on RNA (ADAR1 and ADAR2). ADARs contain multiple double-stranded RNA(dsRNA)-binding domains in addition to an adenosine deaminase domain. An adenosine deaminase acting on tRNAs, scTad1p (also known as scADAT1), cloned fromSaccharomyces cerevisiae has a deaminase domain related to the ADARs but lacks dsRNA-binding domains. We have identified a gene homologous to scADAT1 in the region of Drosophila melanogaster Adh chromosome II. Recombinant Drosophila ADAT1 (dADAT1) has been expressed in the yeast Pichia pastorisand purified. The enzyme has no activity on dsRNA substrates but is a tRNA deaminase with specificity for adenosine 37 of insect alanine tRNA. dADAT1 shows greater similarity to vertebrate ADARs than to yeast Tad1p, supporting the hypothesis of a common evolutionary origin for ADARs and ADATs. dAdat1 transcripts are maternally supplied in the egg. Zygotic expression is widespread initially and later concentrates in the central nervous system.

APA, Harvard, Vancouver, ISO, and other styles

4

LIU, Chengqian, Yulia Mukienko, Chengxiang Wu, and Andrey Zavialov. "Human adenosine deaminases control the immune cell responses to activation signals by reducing extracellular adenosine concentration." Journal of Immunology 196, no. 1_Supplement (May 1, 2016): 124.63. http://dx.doi.org/10.4049/jimmunol.196.supp.124.63.

Full text

Abstract:

Abstract Adenosine rapidly accumulates in the sites of inflammation and tumor growth. It binds to adenosine receptors expressed on the cell surface of immune cells and induces either suppression or activation of inflammatory responses to pathogens. In humans the level of extracellular adenosine is regulated by two adenosine deaminases ADA1 and ADA2. Decrease in ADAs concentration due to genetic defects in the ADA genes leads to serious perturbation in the immune system function while increase in ADA activity associates with numerous immune diseases and cancers. The immune responses to extracellular adenosine have largely been studied using pharmacological approach where non-hydrolysable adenosine receptors agonists substitute adenosine to form the activated state of adenosine receptors. On contrary, adenosine receptors bound to adenosine receptor antagonists mimic inactivated state of adenosine receptors. Here, the effect of adenosine receptor agonists and antagonists on the monocytes function as well as and T helper cell proliferation and differentiation was compared with the effect of adenosine and adenosine deaminases. It was demonstrated that adenosine deaminases control the immune cells responses to activation signals by reducing the concentration of extracellular adenosine and that the cells sensitivity to adenosine greatly depends on the type of the cell activation. Therefore, our data suggests that ADAs could be considered as new drug candidates for the treatment of immune disorders and cancers.

APA, Harvard, Vancouver, ISO, and other styles

5

Polson, Andrew G., Herbert L. Ley, Brenda L. Bass, and John L. Casey. "Hepatitis Delta Virus RNA Editing Is Highly Specific for the Amber/W Site and Is Suppressed by Hepatitis Delta Antigen." Molecular and Cellular Biology 18, no. 4 (April 1, 1998): 1919–26. http://dx.doi.org/10.1128/mcb.18.4.1919.

Full text

Abstract:

ABSTRACT RNA editing at adenosine 1012 (amber/W site) in the antigenomic RNA of hepatitis delta virus (HDV) allows two essential forms of the viral protein, hepatitis delta antigen (HDAg), to be synthesized from a single open reading frame. Editing at the amber/W site is thought to be catalyzed by one of the cellular enzymes known as adenosine deaminases that act on RNA (ADARs). In vitro, the enzymes ADAR1 and ADAR2 deaminate adenosines within many different sequences of base-paired RNA. Since promiscuous deamination could compromise the viability of HDV, we wondered if additional deamination events occurred within the highly base paired HDV RNA. By sequencing cDNAs derived from HDV RNA from transfected Huh-7 cells, we determined that the RNA was not extensively modified at other adenosines. Approximately 0.16 to 0.32 adenosines were modified per antigenome during 6 to 13 days posttransfection. Interestingly, all observed non-amber/W adenosine modifications, which occurred mostly at positions that are highly conserved among naturally occurring HDV isolates, were found in RNAs that were also modified at the amber/W site. Such coordinate modification likely limits potential deleterious effects of promiscuous editing. Neither viral replication nor HDAg was required for the highly specific editing observed in cells. However, HDAg was found to suppress editing at the amber/W site when expressed at levels similar to those found during HDV replication. These data suggest HDAg may regulate amber/W site editing during virus replication.

APA, Harvard, Vancouver, ISO, and other styles

6

Bhakta, Sonali, and Toshifumi Tsukahara. "Artificial RNA Editing with ADAR for Gene Therapy." Current Gene Therapy 20, no. 1 (June 24, 2020): 44–54. http://dx.doi.org/10.2174/1566523220666200516170137.

Full text

Abstract:

Editing mutated genes is a potential way for the treatment of genetic diseases. G-to-A mutations are common in mammals and can be treated by adenosine-to-inosine (A-to-I) editing, a type of substitutional RNA editing. The molecular mechanism of A-to-I editing involves the hydrolytic deamination of adenosine to an inosine base; this reaction is mediated by RNA-specific deaminases, adenosine deaminases acting on RNA (ADARs), family protein. Here, we review recent findings regarding the application of ADARs to restoring the genetic code along with different approaches involved in the process of artificial RNA editing by ADAR. We have also addressed comparative studies of various isoforms of ADARs. Therefore, we will try to provide a detailed overview of the artificial RNA editing and the role of ADAR with a focus on the enzymatic site directed A-to-I editing.

APA, Harvard, Vancouver, ISO, and other styles

7

Dolezelova, Eva, Michal Zurovec, Tomas Dolezal, Petr Simek, and Peter J. Bryant. "The emerging role of adenosine deaminases in insects." Insect Biochemistry and Molecular Biology 35, no. 5 (May 2005): 381–89. http://dx.doi.org/10.1016/j.ibmb.2004.12.009.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Bavelloni, Alberto, Enrico Focaccia, Manuela Piazzi, Mirco Raffini, Valeriana Cesarini, Sara Tomaselli, Arianna Orsini, et al. "AKT‐dependent phosphorylation of the adenosine deaminases ADAR‐1 and ‐2 inhibits deaminase activity." FASEB Journal 33, no. 8 (May 16, 2019): 9044–61. http://dx.doi.org/10.1096/fj.201800490rr.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Thuy-Boun, Alexander S., Justin M. Thomas, Herra L. Grajo, Cody M. Palumbo, SeHee Park, Luan T. Nguyen, Andrew J. Fisher, and Peter A. Beal. "Asymmetric dimerization of adenosine deaminase acting on RNA facilitates substrate recognition." Nucleic Acids Research 48, no. 14 (June 29, 2020): 7958–72. http://dx.doi.org/10.1093/nar/gkaa532.

Full text

Abstract:

Abstract Adenosine deaminases acting on RNA (ADARs) are enzymes that convert adenosine to inosine in duplex RNA, a modification that exhibits a multitude of effects on RNA structure and function. Recent studies have identified ADAR1 as a potential cancer therapeutic target. ADARs are also important in the development of directed RNA editing therapeutics. A comprehensive understanding of the molecular mechanism of the ADAR reaction will advance efforts to develop ADAR inhibitors and new tools for directed RNA editing. Here we report the X-ray crystal structure of a fragment of human ADAR2 comprising its deaminase domain and double stranded RNA binding domain 2 (dsRBD2) bound to an RNA duplex as an asymmetric homodimer. We identified a highly conserved ADAR dimerization interface and validated the importance of these sequence elements on dimer formation via gel mobility shift assays and size exclusion chromatography. We also show that mutation in the dimerization interface inhibits editing in an RNA substrate-dependent manner for both ADAR1 and ADAR2.

APA, Harvard, Vancouver, ISO, and other styles

10

Kopff, M., I. Zakrzewska, J. Klem, J. Kalinowska-Fuchs, and M. Strzelczyk. "Adenosine deaminase activity in blood of patients with stable angina pectoris." Acta Biochimica Polonica 44, no. 2 (June 30, 1997): 359–61. http://dx.doi.org/10.18388/abp.1997_4432.

Full text

Abstract:

The activity of adenosine deaminases (EC.3.5.4.4) in granulocytes and lymphocytes of patients with stable angina pectoris was lower by about 27% and 24%, respectively as compared with control group, whereas these values in erythrocytes and blood plasma were at the normal level.

APA, Harvard, Vancouver, ISO, and other styles

11

Gessler, Sabrina, Clara Guthmann, Vera Schuler, Miriam Lilienkamp, Gerd Walz, and Toma Antonov Yakulov. "Control of Directed Cell Migration after Tubular Cell Injury by Nucleotide Signaling." International Journal of Molecular Sciences 23, no. 14 (July 17, 2022): 7870. http://dx.doi.org/10.3390/ijms23147870.

Full text

Abstract:

Acute kidney injury (AKI) is a common complication of severe human diseases, resulting in increased morbidity and mortality as well as unfavorable long-term outcomes. Although the mammalian kidney is endowed with an amazing capacity to recover from AKI, little progress has been made in recent decades to facilitate recovery from AKI. To elucidate the early repair mechanisms after AKI, we employed the zebrafish pronephros injury model. Since damaged cells release large amounts of ATP and ATP-degradation products to signal apoptosis or necrosis to neighboring cells, we examined how depletion of purinergic and adenosine receptors impacts the directed cell migration that ensues immediately after a laser-induced tubular injury. We found that depletion of the zebrafish adenosine receptors adora1a, adora1b, adora2aa, and adora2ab significantly affected the repair process. Similar results were obtained after depletion of the purinergic p2ry2 receptor, which is highly expressed during zebrafish pronephros development. Released ATP is finally metabolized to inosine by adenosine deaminase. Depletion of zebrafish adenosine deaminases ada and ada2b interfered with the repair process; furthermore, combinations of ada and ada2b, or ada2a and ada2b displayed synergistic effects at low concentrations, supporting the involvement of inosine signaling in the repair process after a tubular injury. Our findings suggest that nucleotide-dependent signaling controls immediate migratory responses after tubular injury.

APA, Harvard, Vancouver, ISO, and other styles

12

Bass, Brenda L. "RNA Editing by Adenosine Deaminases That Act on RNA." Annual Review of Biochemistry 71, no. 1 (June 2002): 817–46. http://dx.doi.org/10.1146/annurev.biochem.71.110601.135501.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Ma, Pang Fai. "A STUDY OF ADENOSINE DEAMINASES IN HUMAN SERA: 114." Pediatric Research 19, no. 7 (July 1985): 762. http://dx.doi.org/10.1203/00006450-198507000-00134.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Orlandi, Cesare, Alessandro Barbon, and Sergio Barlati. "Activity Regulation of Adenosine Deaminases Acting on RNA (ADARs)." Molecular Neurobiology 45, no. 1 (November 20, 2011): 61–75. http://dx.doi.org/10.1007/s12035-011-8220-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

PospíŠilová, Hana, Marek Šebela, Ondřej Novák, and Ivo Frébort. "Hydrolytic cleavage of N6-substituted adenine derivatives by eukaryotic adenine and adenosine deaminases." Bioscience Reports 28, no. 6 (November 6, 2008): 335–47. http://dx.doi.org/10.1042/bsr20080081.

Full text

Abstract:

Homogeneous adenine deaminases (EC 3.5.4.2) from the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe and a putative ADA (adenosine deaminase; EC 3.5.4.4) from Arabidopsis thaliana were obtained for the first time as purified recombinant proteins by molecular cloning of the corresponding genes and their overexpression in Escherichia coli. The enzymes showed comparable molecular properties with well-known mammalian ADAs, but exhibited much lower kcat values. Adenine was the most favoured substrate for the yeast enzymes, whereas the plant enzyme showed only very low activities with either adenine, adenosine, AMP or ATP. Interestingly, the yeast enzymes also hydrolysed N6-substituted adenines from cytokinins, a group of plant hormones, cleaving them to inosine and the corresponding side chain amine. The hydrolytic cleavage of synthetic cytokinin 2,6-di-substituted analogues that are used in cancer therapy, such as olomoucine, roscovitine and bohemine, was subsequently shown for a reference sample of human ADA1. ADA1, however, showed a different reaction mechanism to that of the yeast enzymes, hydrolysing the compounds to an adenine derivative and a side chain alcohol. The reaction products were identified using reference compounds on HPLC coupled to UV and Q-TOF (quadrupole–time-of-flight) detectors. The ADA1 activity may constitute the debenzylation metabolic route already described for bohemine and, as a consequence, it may compromise the physiological or therapeutic effects of exogenously applied cytokinin derivatives.

APA, Harvard, Vancouver, ISO, and other styles

16

Marceca, Gioacchino P., Luisa Tomasello, Rosario Distefano, Mario Acunzo, Carlo M. Croce, and Giovanni Nigita. "Detecting and Characterizing A-To-I microRNA Editing in Cancer." Cancers 13, no. 7 (April 3, 2021): 1699. http://dx.doi.org/10.3390/cancers13071699.

Full text

Abstract:

Adenosine to inosine (A-to-I) editing consists of an RNA modification where single adenosines along the RNA sequence are converted into inosines. Such a biochemical transformation is catalyzed by enzymes belonging to the family of adenosine deaminases acting on RNA (ADARs) and occurs either co- or post-transcriptionally. The employment of powerful, high-throughput detection methods has recently revealed that A-to-I editing widely occurs in non-coding RNAs, including microRNAs (miRNAs). MiRNAs are a class of small regulatory non-coding RNAs (ncRNAs) acting as translation inhibitors, known to exert relevant roles in controlling cell cycle, proliferation, and cancer development. Indeed, a growing number of recent researches have evidenced the importance of miRNA editing in cancer biology by exploiting various detection and validation methods. Herein, we briefly overview early and currently available A-to-I miRNA editing detection and validation methods and discuss the significance of A-to-I miRNA editing in human cancer.

APA, Harvard, Vancouver, ISO, and other styles

17

George, Cyril X., Zhenji Gan, Yong Liu, and Charles E. Samuel. "Adenosine Deaminases Acting on RNA, RNA Editing, and Interferon Action." Journal of Interferon & Cytokine Research 31, no. 1 (January 2011): 99–117. http://dx.doi.org/10.1089/jir.2010.0097.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Schaub, Myriam, and Walter Keller. "RNA editing by adenosine deaminases generates RNA and protein diversity." Biochimie 84, no. 8 (August 2002): 791–803. http://dx.doi.org/10.1016/s0300-9084(02)01446-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Ho, Meng-Chiao, María B. Cassera, Dennis C. Madrid, Li-Min Ting, Peter C. Tyler, Kami Kim, Steven C. Almo, and Vern L. Schramm. "Structural and Metabolic Specificity of Methylthiocoformycin for Malarial Adenosine Deaminases." Biochemistry 48, no. 40 (October 13, 2009): 9618–26. http://dx.doi.org/10.1021/bi9012484.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Beal, P. A., O. Maydanovych, and S. Pokharel. "The Chemistry and Biology of RNA editing by Adenosine Deaminases." Nucleic Acids Symposium Series 51, no. 1 (November 1, 2007): 83–84. http://dx.doi.org/10.1093/nass/nrm042.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Bojack, Guido, Christopher G. Earnshaw, Robert Klein, Stephen D. Lindell, Christian Lowinski, and Rainer Preuss. "Design and Synthesis of Inhibitors of Adenosine and AMP Deaminases." Organic Letters 3, no. 6 (March 2001): 839–42. http://dx.doi.org/10.1021/ol006992v.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Kliuchnikova, AA, and SA Moshkovskii. "Adenosine-to-inosine RNA editing may be implicated in human pathogenesis." TARGETED ONCOTHERAPY, no. 2 (April 16, 2019): 22–25. http://dx.doi.org/10.24075/brsmu.2019.028.

Full text

Abstract:

Adenosine-to-inosine (A-to-I) RNA editing is a common mechanism of post-transcriptional modification in many metazoans including vertebrates; the process is catalyzed by adenosine deaminases acting on RNA (ADARs). Using high-throughput sequencing technologies resulted in finding thousands of RNA editing sites throughout the human transcriptome however, their functions are still poorly understood. The aim of this brief review is to draw attention of clinicians and biomedical researchers to ADAR-mediated RNA editing phenomenon and its possible implication in development of neuropathologies, antiviral immune responses and cancer.

APA, Harvard, Vancouver, ISO, and other styles

23

Di Giorgio, Salvatore, Filippo Martignano, Maria Gabriella Torcia, Giorgio Mattiuz, and Silvestro G. Conticello. "Evidence for host-dependent RNA editing in the transcriptome of SARS-CoV-2." Science Advances 6, no. 25 (May 18, 2020): eabb5813. http://dx.doi.org/10.1126/sciadv.abb5813.

Full text

Abstract:

The COVID-19 outbreak has become a global health risk, and understanding the response of the host to the SARS-CoV-2 virus will help to combat the disease. RNA editing by host deaminases is an innate restriction process to counter virus infection, but it is not yet known whether this process operates against coronaviruses. Here, we analyze RNA sequences from bronchoalveolar lavage fluids obtained from coronavirus-infected patients. We identify nucleotide changes that may be signatures of RNA editing: adenosine-to-inosine changes from ADAR deaminases and cytosine-to-uracil changes from APOBEC deaminases. Mutational analysis of genomes from different strains of Coronaviridae from human hosts reveals mutational patterns consistent with those observed in the transcriptomic data. However, the reduced ADAR signature in these data raises the possibility that ADARs might be more effective than APOBECs in restricting viral propagation. Our results thus suggest that both APOBECs and ADARs are involved in coronavirus genome editing, a process that may shape the fate of both virus and patient.

APA, Harvard, Vancouver, ISO, and other styles

24

Centelles, J. J., and R. Franco. "Slight differences between adenosine deaminases from different species an immunochemical study." Archives Internationales de Physiologie et de Biochimie 98, no. 2 (January 1990): 421–31. http://dx.doi.org/10.3109/13813459009114004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Mizrahi, Rena A., Kelly J. Phelps, Andrea Y. Ching, and Peter A. Beal. "Nucleoside analog studies indicate mechanistic differences between RNA-editing adenosine deaminases." Nucleic Acids Research 40, no. 19 (August 10, 2012): 9825–35. http://dx.doi.org/10.1093/nar/gks752.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Lehmann, Katrina A., and Brenda L. Bass. "Double-Stranded RNA Adenosine Deaminases ADAR1 and ADAR2 Have Overlapping Specificities†." Biochemistry 39, no. 42 (October 2000): 12875–84. http://dx.doi.org/10.1021/bi001383g.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Chen, Genghao, Dhruva Katrekar, and Prashant Mali. "RNA-Guided Adenosine Deaminases: Advances and Challenges for Therapeutic RNA Editing." Biochemistry 58, no. 15 (April 3, 2019): 1947–57. http://dx.doi.org/10.1021/acs.biochem.9b00046.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Samuel, Charles E. "Adenosine deaminases acting on RNA (ADARs) are both antiviral and proviral." Virology 411, no. 2 (March 2011): 180–93. http://dx.doi.org/10.1016/j.virol.2010.12.004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

O'Connell, Mary A., André Gerber, and Liam P. Keegan. "Purification of Native and Recombinant Double-Stranded RNA-Specific Adenosine Deaminases." Methods 15, no. 1 (May 1998): 51–62. http://dx.doi.org/10.1006/meth.1998.0605.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Jayan, Geetha C. "RNA Editing in Hepatitis Delta Virus: Unsolved Puzzles." Scientific World JOURNAL 4 (2004): 628–37. http://dx.doi.org/10.1100/tsw.2004.123.

Full text

Abstract:

RNA editing, or post-transcriptional changes in the sequences of RNAs, is being increasingly recognized as an important player in the regulation of gene expression in vertebrates and invertebrates. Different types of RNA editing have been reported. This review discuss the type of RNA editing caused by cellular enzymes known as adenosine deaminases that act on RNAs (ADARs), and it's significance in the lifecycle of an RNA virus, hepatitis delta virus.

APA, Harvard, Vancouver, ISO, and other styles

31

Yoon, Yoo Bin, Yun-Sang Yu, Beom Jun Park, Sung-Jin Cho, and Soon Cheol Park. "Identification and Spatiotemporal Expression of Adenosine Deaminases Acting on RNA (ADAR) during Earthworm Regeneration: Its Possible Implication in Muscle Redifferentiation." Biology 9, no. 12 (December 5, 2020): 448. http://dx.doi.org/10.3390/biology9120448.

Full text

Abstract:

Adenosine deaminases acting on RNA (ADAR) catalyze the hydrolytic deamination of adenosine (A) to produce inosine (I) in double-stranded RNA substrates. A-to-I RNA editing has increasingly broad physiological significance in development, carcinogenesis, and environmental adaptation. Perionyx excavatus is an earthworm with potent regenerative potential; it can regenerate the head and tail and is an advantageous model system to investigate the molecular mechanisms of regeneration. During RNA sequencing analysis of P. excavatus regenerates, we identified an ADAR homolog (Pex-ADAR), which led us to examine its spatial and temporal expression to comprehend how Pex-ADAR is linked to regeneration. At first, in domain analysis, we discovered that Pex-ADAR only has one double-stranded RNA-binding domain (dsRBD) and a deaminase domain without a Z-DNA-binding domain (ZBD). In addition, a comparison of the core deaminase domains of Pex-ADAR with those of other ADAR family members indicated that Pex-ADAR comprises the conserved three active-site motifs and a glutamate residue for catalytic activity. Pex-ADAR also shares 11 conserved residues, a characteristic of ADAR1, supporting that Pex-ADAR is a member of ADAR1 class. Its temporal expression was remarkably low in the early stages of regeneration before suddenly increasing at 10 days post amputation (dpa) when diverse cell types and tissues were being regenerated. In situ hybridization of Pex-ADAR messenger RNA (mRNA) indicated that the main expression was observed in regenerating muscle layers and related connective tissues. Taken together, the present results demonstrate that an RNA-editing enzyme, Pex-ADAR, is implicated in muscle redifferentiation during earthworm regeneration.

APA, Harvard, Vancouver, ISO, and other styles

32

Vesely, Cornelia, and Michael F. Jantsch. "An I for an A: Dynamic Regulation of Adenosine Deamination-Mediated RNA Editing." Genes 12, no. 7 (July 1, 2021): 1026. http://dx.doi.org/10.3390/genes12071026.

Full text

Abstract:

RNA-editing by adenosine deaminases acting on RNA (ADARs) converts adenosines to inosines in structured RNAs. Inosines are read as guanosines by most cellular machineries. A to I editing has two major functions: first, marking endogenous RNAs as “self”, therefore helping the innate immune system to distinguish repeat- and endogenous retrovirus-derived RNAs from invading pathogenic RNAs; and second, recoding the information of the coding RNAs, leading to the translation of proteins that differ from their genomically encoded versions. It is obvious that these two important biological functions of ADARs will differ during development, in different tissues, upon altered physiological conditions or after exposure to pathogens. Indeed, different levels of ADAR-mediated editing have been observed in different tissues, as a response to altered physiology or upon pathogen exposure. In this review, we describe the dynamics of A to I editing and summarize the known and likely mechanisms that will lead to global but also substrate-specific regulation of A to I editing.

APA, Harvard, Vancouver, ISO, and other styles

33

Scadden, A. D. J. "Gene expression is reduced in trans by inosine-containing dsRNA." Biochemical Society Transactions 36, no. 3 (May 21, 2008): 534–36. http://dx.doi.org/10.1042/bst0360534.

Full text

Abstract:

Inosine residues may be introduced into long dsRNA (double-stranded RNA) molecules by the action of a family of editing enzymes, ADARs (adenosine deaminases that act on RNA). Furthermore, hyperediting of dsRNA by ADARs may result in up to 50% of adenosine residues being converted into inosine. While the effect of hyperediting has traditionally been thought to be limited to the edited dsRNA, we have recently shown that hyperedited dsRNA [I-dsRNA (inosine-containing dsRNA)] is able to down-regulate the expression of both reporter and endogenous mRNAs in cells, in trans. Down-regulation by I-dsRNA occurs both by reducing mRNA levels and by inhibiting of translation. This finding has important functional consequences for hyperediting by ADARs.

APA, Harvard, Vancouver, ISO, and other styles

34

Doria, Margherita, Sara Tomaselli, Francesca Neri, Silvia Anna Ciafrè, Maria Giulia Farace, Alessandro Michienzi, and Angela Gallo. "ADAR2 editing enzyme is a novel human immunodeficiency virus-1 proviral factor." Journal of General Virology 92, no. 5 (May 1, 2011): 1228–32. http://dx.doi.org/10.1099/vir.0.028043-0.

Full text

Abstract:

The adenosine deaminases acting on RNA (ADAR) enzymes catalyse conversion of adenosine to inosine in dsRNA. A positive effect of ADAR1 on human immunodeficiency virus type 1 (HIV-1) replication has recently been reported. Here, we show that another ADAR enzyme, ADAR2, positively affects the replication process of HIV-1. We found that, analogously to ADAR1, ADAR2 enhances the release of progeny virions by an editing-dependent mechanism. However, differently from the ADAR1 enzyme, ADAR2 does not increase the infectious potential of the virus. Importantly, downregulation of ADAR2 in Jurkat cells significantly impairs viral replication. Therefore, ADAR2 shares some but not all proviral functions of ADAR1. These results suggest a novel role of ADAR2 as a viral regulator.

APA, Harvard, Vancouver, ISO, and other styles

35

Katrekar, Dhruva, Genghao Chen, Dario Meluzzi, Ashwin Ganesh, Atharv Worlikar, Yu-Ru Shih, Shyni Varghese, and Prashant Mali. "In vivo RNA editing of point mutations via RNA-guided adenosine deaminases." Nature Methods 16, no. 3 (February 8, 2019): 239–42. http://dx.doi.org/10.1038/s41592-019-0323-0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Uchida, H., Y. X. Chen, H. Nagai, Y. Fujisaki, K. Harihara, N. Saka, Y. Kugisaki, and A. Nomura. "Distribution of Adenosine (Phosphate) Deaminases with Unusual Substrate Specificity in Marine Molluscs." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 119, no. 1 (January 1998): 227–33. http://dx.doi.org/10.1016/s0305-0491(97)00311-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Ko, Nga Ling, Emmanuel Birlouez, Simon Wain-Hobson, Renaud Mahieux, and Jean-Pierre Vartanian. "Hyperediting of human T-cell leukemia virus type 2 and simian T-cell leukemia virus type 3 by the dsRNA adenosine deaminase ADAR-1." Journal of General Virology 93, no. 12 (December 1, 2012): 2646–51. http://dx.doi.org/10.1099/vir.0.045146-0.

Full text

Abstract:

RNA editing mediated by adenosine deaminases acting on RNA (ADARs) converts adenosine (A) to inosine (I) residues in dsRNA templates. While ADAR-1-mediated editing was essentially described for RNA viruses, the present work addresses the issue for two δ-retroviruses, human T-cell leukemia virus type 2 and simian T-cell leukemia virus type 3 (HTLV-2 and STLV-3). We examined whether ADAR-1 could edit HTLV-2 and STLV-3 virus genomes in cell culture and in vivo. Using a highly sensitive PCR-based method, referred to as 3DI-PCR, we showed that ADAR-1 could hypermutate adenosine residues in HTLV-2. STLV-3 hypermutation was obtained without using 3DI-PCR, suggesting a higher mutation frequency for this virus. Detailed analysis of the dinucleotide editing context showed preferences for 5′ ArA and 5′ UrA. In conclusion, the present observations demonstrate that ADAR-1 massively edits HTLV-2 and STLV-3 retroviruses in vitro, but probably remains a rare phenomenon in vivo.

APA, Harvard, Vancouver, ISO, and other styles

38

Phuphuakrat, Angsana, Romchat Kraiwong, Chompunuch Boonarkart, Darat Lauhakirti, Tun-Hou Lee, and Prasert Auewarakul. "Double-Stranded RNA Adenosine Deaminases Enhance Expression of Human Immunodeficiency Virus Type 1 Proteins." Journal of Virology 82, no. 21 (August 27, 2008): 10864–72. http://dx.doi.org/10.1128/jvi.00238-08.

Full text

Abstract:

ABSTRACT ADARs (adenosine deaminases that act on double-stranded RNA) are RNA editing enzymes that catalyze a change from adenosine to inosine, which is then recognized as guanosine by translational machinery. We demonstrate here that overexpression of ADARs but not of an ADAR mutant lacking editing activity could upregulate human immunodeficiency virus type 1 (HIV-1) structural protein expression and viral production. Knockdown of ADAR1 by RNA silencing inhibited HIV-1 production. Viral RNA harvested from transfected ADAR1-knocked-down cells showed a decrease in the level of unspliced RNA transcripts. Overexpression of ADAR1 induced editing at a specific site in the env gene, and a mutant with the edited sequence was expressed more efficiently than the wild-type viral genome. These data suggested the role of ADAR in modulation of HIV-1 replication. Our data demonstrate a novel mechanism in which HIV-1 employs host RNA modification machinery for posttranscriptional regulation of viral protein expression.

APA, Harvard, Vancouver, ISO, and other styles

39

Dafou, Dimitra, Eirini Kanata, Spyros Pettas, Nikolaos Bekas, Athanasios Dimitriadis, Garyfalia Kempapidou, Roza Lagoudaki, et al. "RNA Editing Alterations Define Disease Manifestations in the Progression of Experimental Autoimmune Encephalomyelitis (EAE)." Cells 11, no. 22 (November 12, 2022): 3582. http://dx.doi.org/10.3390/cells11223582.

Full text

Abstract:

RNA editing is an epitranscriptomic modification, leading to targeted changes in RNA transcripts. It is mediated by the action of ADAR (adenosine deaminases acting on double-stranded (ds) RNA and APOBEC (apolipoprotein B mRNA editing enzyme catalytic polypeptide-like) deaminases and appears to play a major role in the pathogenesis of many diseases. Here, we assessed its role in experimental autoimmune encephalomyelitis (EAE), a widely used non-clinical model of autoimmune inflammatory diseases of the central nervous system (CNS), which resembles many aspects of human multiple sclerosis (MS). We have analyzed in silico data from microglia isolated at different timepoints through disease progression to identify the global editing events and validated the selected targets in murine tissue samples. To further evaluate the functional role of RNA editing, we induced EAE in transgenic animals lacking expression of APOBEC-1. We found that RNA-editing events, mediated by the APOBEC and ADAR deaminases, are significantly reduced throughout the course of disease, possibly affecting the protein expression necessary for normal neurological function. Moreover, the severity of the EAE model was significantly higher in APOBEC-1 knock-out mice, compared to wild-type controls. Our results implicate regulatory epitranscriptomic mechanisms in EAE pathogenesis that could be extrapolated to MS and other neurodegenerative disorders (NDs) with common clinical and molecular features.

APA, Harvard, Vancouver, ISO, and other styles

40

Daniel, Chammiran, and Marie Öhman. "RNA editing and its impact on GABAA receptor function." Biochemical Society Transactions 37, no. 6 (November 19, 2009): 1399–403. http://dx.doi.org/10.1042/bst0371399.

Full text

Abstract:

A-to-I (adenosine-to-inosine) RNA editing catalysed by the ADARs (adenosine deaminases that act on RNA) is a post-transcriptional event that contributes to protein diversity in metazoans. In mammalian neuronal ion channels, editing alters functionally important amino acids and creates receptor subtypes important for the development of the nervous system. The excitatory AMPA (α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid) and kainate glutamate receptors, as well as the inhibitory GABAA [GABA (γ-aminobutyric acid) type A] receptor, are subject to A-to-I RNA editing. Editing affects several features of the receptors, including kinetics, subunit assembly and cell-surface expression. Here, we discuss the regulation of editing during brain maturation and the impact of RNA editing on the expression of different receptor subtypes.

APA, Harvard, Vancouver, ISO, and other styles

41

Cho, Dan-Sung C., Weidong Yang, Joshua T. Lee, Ramin Shiekhattar, John M. Murray, and Kazuko Nishikura. "Requirement of Dimerization for RNA Editing Activity of Adenosine Deaminases Acting on RNA." Journal of Biological Chemistry 278, no. 19 (March 4, 2003): 17093–102. http://dx.doi.org/10.1074/jbc.m213127200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Maas, Stefan, and Willemijn M. Gommans. "Identification of a selective nuclear import signal in adenosine deaminases acting on RNA." Nucleic Acids Research 37, no. 17 (July 17, 2009): 5822–29. http://dx.doi.org/10.1093/nar/gkp599.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Frick, Lloyd, John P. Mac Neela, and Richard Wolfenden. "Transition state stabilization by deaminases: Rates of nonenzymatic hydrolysis of adenosine and cytidine." Bioorganic Chemistry 15, no. 2 (June 1987): 100–108. http://dx.doi.org/10.1016/0045-2068(87)90011-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Kaljas, Yuliia, Chengqian Liu, Maksym Skaldin, Chengxiang Wu, Qing Zhou, Yuanan Lu, Ivona Aksentijevich, and Andrey V. Zavialov. "Human adenosine deaminases ADA1 and ADA2 bind to different subsets of immune cells." Cellular and Molecular Life Sciences 74, no. 3 (September 23, 2016): 555–70. http://dx.doi.org/10.1007/s00018-016-2357-0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Eifler, Tristan, Dalen Chan, and Peter A. Beal. "A Screening Protocol for Identification of Functional Mutants of RNA Editing Adenosine Deaminases." Current Protocols in Chemical Biology 4, no. 4 (December 2012): 357–69. http://dx.doi.org/10.1002/9780470559277.ch120139.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Ogawa, Tetsuo, Yoko Aikawa, and Toyoo Aikawa. "Affinity difference of adenosine deaminases for the purine riboside-epoxyactivated Sepharose 6B column." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 88, no. 2 (January 1987): 491–95. http://dx.doi.org/10.1016/0305-0491(87)90332-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Phan, Vinhthuy, Allen Thomas, Kriangsiri Malasri, and Carrie Hayes Sutter. "Stability of RNA structural motifs and its influence on editing efficiency by adenosine deaminases." International Journal of Bioinformatics Research and Applications 6, no. 1 (2010): 21. http://dx.doi.org/10.1504/ijbra.2010.031290.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Shih, Phoebe, and Richard Wolfenden. "Enzyme−Substrate Complexes of Adenosine and Cytidine Deaminases: Absence of Accumulation of Water Adducts†." Biochemistry 35, no. 15 (January 1996): 4697–703. http://dx.doi.org/10.1021/bi952357z.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Carter, C. W. "The nucleoside deaminases for cytidine and adenosine: Structure, transition state stabilization, mechanism, and evolution." Biochimie 77, no. 1-2 (January 1995): 92–98. http://dx.doi.org/10.1016/0300-9084(96)88110-7.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Lai, F., C. X. Chen, K. C. Carter, and K. Nishikura. "Editing of glutamate receptor B subunit ion channel RNAs by four alternatively spliced DRADA2 double-stranded RNA adenosine deaminases." Molecular and Cellular Biology 17, no. 5 (May 1997): 2413–24. http://dx.doi.org/10.1128/mcb.17.5.2413.

Full text

Abstract:

Double-stranded (ds) RNA-specific adenosine deaminase converts adenosine residues into inosines in dsRNA and edits transcripts of certain cellular and viral genes such as glutamate receptor (GluR) subunits and hepatitis delta antigen. The first member of this type of deaminase, DRADA1, has been recently cloned based on the amino acid sequence information derived from biochemically purified proteins. Our search for DRADA1-like genes through expressed sequence tag databases led to the cloning of the second member of this class of enzyme, DRADA2, which has a high degree of sequence homology to DRADA1 yet exhibits a distinctive RNA editing site selectivity. There are four differentially spliced isoforms of human DRADA2. These different isoforms of recombinant DRADA2 proteins, including one which is a human homolog of the recently reported rat RED1, were analyzed in vitro for their GluR B subunit (GluR-B) RNA editing site selectivity. As originally reported for rat RED1, the DRADA2a and -2b isoforms edit GluR-B RNA efficiently at the so-called Q/R site, whereas DRADA1 barely edits this site. In contrast, the R/G site of GluR-B RNA was edited efficiently by the DRADA2a and -2b isoforms as well as DRADA1. Isoforms DRADA2c and -2d, which have a distinctive truncated shorter C-terminal structure, displayed weak adenosine-to-inosine conversion activity but no editing activity tested at three known sites of GluR-B RNA. The possible role of these DRADA2c and -2d isoforms in the regulatory mechanism of RNA editing is discussed.

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!