Relevant bibliographies by topics / An RNase active on dsRNA

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Academic literature on the topic 'An RNase active on dsRNA'

Author: Grafiati
Published: 11 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "An RNase active on dsRNA"

1

Weinheimer, Isabel, Kajohn Boonrod, Mirko Moser, et al. "Binding and processing of small dsRNA molecules by the class 1 RNase III protein encoded by sweet potato chlorotic stunt virus." Journal of General Virology 95, no. 2 (2014): 486–95. http://dx.doi.org/10.1099/vir.0.058693-0.

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Sweet potato chlorotic stunt virus (SPCSV; genus Crinivirus, family Closteroviridae) causes heavy yield losses in sweet potato plants co-infected with other viruses. The dsRNA-specific class 1 RNase III–like endoribonuclease (RNase3) encoded by SPCSV suppresses post-transcriptional gene silencing and eliminates antiviral defence in sweet potato plants in an endoribonuclease activity-dependent manner. RNase3 can cleave long dsRNA molecules, synthetic small interfering RNAs (siRNAs), and plant- and virus-derived siRNAs extracted from sweet potato plants. In this study, conditions for efficient e
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Iqbal, Munir, Emma Poole, Stephen Goodbourn, and John W. McCauley. "Role for Bovine Viral Diarrhea Virus Erns Glycoprotein in the Control of Activation of Beta Interferon by Double-Stranded RNA." Journal of Virology 78, no. 1 (2004): 136–45. http://dx.doi.org/10.1128/jvi.78.1.136-145.2004.

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ABSTRACT Production of alpha/beta interferon in response to viral double-stranded RNA (dsRNA) produced during viral replication is a first line of defense against viral infections. Here we demonstrate that the Erns glycoprotein of the pestivirus bovine viral diarrhea virus can act as an inhibitor of dsRNA-induced responses of cells. This effect is seen whether Erns is constitutively expressed in cells or exogenously added to the culture medium. The Erns effect is specific to dsRNA since activation of NF-κB in cells infected with Semliki Forest virus or treated with tumor necrosis factor alpha
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Gupta, Ankush, and Pramod C. Rath. "Curcumin, a Natural Antioxidant, Acts as a Noncompetitive Inhibitor of Human RNase L in Presence of Its Cofactor 2-5AIn Vitro." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/817024.

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Ribonuclease L (RNase L) is an antiviral endoribonuclease of the innate immune system, which is induced and activated by viral infections, interferons, and double stranded RNA (dsRNA) in mammalian cells. Although, RNase L is generally protective against viral infections, abnormal RNase L expression and activity have been associated with a number of diseases. Here, we show that curcumin, a natural plant-derived anti-inflammatory active principle, inhibits RNase L activity; hence, it may be exploited for therapeutic interventions in case of pathological situations associated with excess activati
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Li, Yize, Shuvojit Banerjee, Yuyan Wang, et al. "Activation of RNase L is dependent on OAS3 expression during infection with diverse human viruses." Proceedings of the National Academy of Sciences 113, no. 8 (2016): 2241–46. http://dx.doi.org/10.1073/pnas.1519657113.

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The 2′,5′-oligoadenylate (2-5A) synthetase (OAS)–RNase L system is an IFN-induced antiviral pathway. RNase L activity depends on 2-5A, synthesized by OAS. Although all three enzymatically active OAS proteins in humans—OAS1, OAS2, and OAS3—synthesize 2-5A upon binding dsRNA, it is unclear which are responsible for RNase L activation during viral infection. We used clustered regularly interspaced short palindromic repeats (CRISPR)–CRISPR-associated protein-9 nuclease (Cas9) technology to engineer human A549-derived cell lines in which each of the OAS genes or RNase L is knocked out. Upon transfe
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5

Grünberg, Sebastian, Baptiste Coxam, Tien-Hao Chen, et al. "E. coli RNase I exhibits a strong Ca2+-dependent inherent double-stranded RNase activity." Nucleic Acids Research 49, no. 9 (2021): 5265–77. http://dx.doi.org/10.1093/nar/gkab284.

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Abstract Since its initial characterization, Escherichia coli RNase I has been described as a single-strand specific RNA endonuclease that cleaves its substrate in a largely sequence independent manner. Here, we describe a strong calcium (Ca2+)-dependent activity of RNase I on double-stranded RNA (dsRNA), and a Ca2+-dependent novel hybridase activity, digesting the RNA strand in a DNA:RNA hybrid. Surprisingly, Ca2+ does not affect the activity of RNase I on single stranded RNA (ssRNA), suggesting a specific role for Ca2+ in the modulation of RNase I activity. Mutation of a previously overlooke
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6

Weiss, Susan R. "Activation and Antagonism of the OAS–RNase L Pathway." Proceedings 50, no. 1 (2020): 14. http://dx.doi.org/10.3390/proceedings2020050014.

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The oligoadenylate synthetase–ribonuclease L (OAS–RNase L) system is a potent antiviral pathway that severely limits the pathogenesis of many viruses. Upon sensing dsRNA, OASs produce 2′,5′-oligoadenylates (2-5A) that activate RNase L to cleave both host and viral single-stranded RNA, thereby limiting protein production, virus replication and spread, leading to apoptotic cell death. Endogenous host dsRNA, which accumulates in the absence of adenosine deaminase acting on RNA (ADAR)1, can also activate RNase L and lead to apoptotic cell death. RNase L activation and antiviral activity during inf
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7

Li, Yize, Beihua Dong, Zuzhang Wei, Robert H. Silverman, Susan R. Weiss, and John T. Patton. "Activation of RNase L in Egyptian Rousette Bat-Derived RoNi/7 Cells Is Dependent Primarily on OAS3 and Independent of MAVS Signaling." mBio 10, no. 6 (2019): e02414-19. https://doi.org/10.5281/zenodo.13449086.

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(Uploaded by Plazi for the Bat Literature Project) Bats are reservoirs for many RNA viruses that are highly pathogenic in humans yet relatively apathogenic in the natural host. It has been suggested that differences in innate immunity are responsible. The antiviral OAS-RNase L pathway is well characterized in humans, but there is little known about its activation and antiviral activity in bats. During infection, OASs, upon sensing doublestranded RNA (dsRNA), produce 2=-5= oligoadenylates (2-5A), leading to activation of RNase L which degrades viral and host RNA, limiting viral replication. Hum
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Li, Yize, Beihua Dong, Zuzhang Wei, Robert H. Silverman, Susan R. Weiss, and John T. Patton. "Activation of RNase L in Egyptian Rousette Bat-Derived RoNi/7 Cells Is Dependent Primarily on OAS3 and Independent of MAVS Signaling." mBio 10, no. 6 (2019): e02414-19. https://doi.org/10.5281/zenodo.13449086.

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(Uploaded by Plazi for the Bat Literature Project) Bats are reservoirs for many RNA viruses that are highly pathogenic in humans yet relatively apathogenic in the natural host. It has been suggested that differences in innate immunity are responsible. The antiviral OAS-RNase L pathway is well characterized in humans, but there is little known about its activation and antiviral activity in bats. During infection, OASs, upon sensing doublestranded RNA (dsRNA), produce 2=-5= oligoadenylates (2-5A), leading to activation of RNase L which degrades viral and host RNA, limiting viral replication. Hum
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9

Li, Yize, Beihua Dong, Zuzhang Wei, Robert H. Silverman, Susan R. Weiss, and John T. Patton. "Activation of RNase L in Egyptian Rousette Bat-Derived RoNi/7 Cells Is Dependent Primarily on OAS3 and Independent of MAVS Signaling." mBio 10, no. 6 (2019): e02414-19. https://doi.org/10.5281/zenodo.13449086.

Full text
Abstract:
(Uploaded by Plazi for the Bat Literature Project) Bats are reservoirs for many RNA viruses that are highly pathogenic in humans yet relatively apathogenic in the natural host. It has been suggested that differences in innate immunity are responsible. The antiviral OAS-RNase L pathway is well characterized in humans, but there is little known about its activation and antiviral activity in bats. During infection, OASs, upon sensing doublestranded RNA (dsRNA), produce 2=-5= oligoadenylates (2-5A), leading to activation of RNase L which degrades viral and host RNA, limiting viral replication. Hum
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10

Li, Yize, Beihua Dong, Zuzhang Wei, Robert H. Silverman, Susan R. Weiss, and John T. Patton. "Activation of RNase L in Egyptian Rousette Bat-Derived RoNi/7 Cells Is Dependent Primarily on OAS3 and Independent of MAVS Signaling." mBio 10, no. 6 (2019): e02414-19. https://doi.org/10.5281/zenodo.13449086.

Full text
Abstract:
(Uploaded by Plazi for the Bat Literature Project) Bats are reservoirs for many RNA viruses that are highly pathogenic in humans yet relatively apathogenic in the natural host. It has been suggested that differences in innate immunity are responsible. The antiviral OAS-RNase L pathway is well characterized in humans, but there is little known about its activation and antiviral activity in bats. During infection, OASs, upon sensing doublestranded RNA (dsRNA), produce 2=-5= oligoadenylates (2-5A), leading to activation of RNase L which degrades viral and host RNA, limiting viral replication. Hum
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Dissertations / Theses on the topic "An RNase active on dsRNA"

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Nathania, Lilian. "Biochemical Analysis of Thermotoga maritima Ribonuclease III and its Ribosomal RNA Substrates." Diss., Temple University Libraries, 2011. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/140013.

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Chemistry<br>Ph.D.<br>The site-specific cleavage of double-stranded (ds) RNA is a conserved early step in bacterial ribosomal RNA (rRNA) maturation that is carried out by ribonuclease III. Studies on the RNase III mechanism of dsRNA cleavage have focused mainly on the enzymes from mesophiles such as Escherichia coli. In contrast, little is known of the RNA processing pathways and the functions of associated ribonucleases in the hyperthermophiles. Therefore, structural and biochemical studies of proteins from hyperthermophilic bacteria are providing essential insight on the sources of biomolecu
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Saavedra, Mario Alejandro. "Expression, Purification and Characterization of a Soluble and Active RNAse H from the Hepatitis B Virus." VCU Scholars Compass, 2007. http://scholarscompass.vcu.edu/etd_retro/16.

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The HBV RNAse H has been cloned into the PET43a vector, which contains the NusA protein which works as a solubilizing fusion protein. The fusion NUS-RNAse H protein was cleaved by enterokinase; the cleaved RNAse H is about 17 Kda which remains soluble and active. A fluorescence assay utilizing a quenching mechanism was used to characterize the activity of NUS-RNAse H and cleaved RNAse H proteins. The beacon is a RNA:DNA hybrid oligonucleotide labeled with a 5'DABCYL and a 3'fluorescein, when RNAse H digests the RNA, DABCYL is released resulting in high fluorescence. The digestion of the RN
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Abramo, Kristin N. "Building the Interphase Nucleus: A study on the kinetics of 3D chromosome formation, temporal relation to active transcription, and the role of nuclear RNAs." eScholarship@UMMS, 2020. https://escholarship.umassmed.edu/gsbs_diss/1099.

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Following the discovery of the one-dimensional sequence of human DNA, much focus has been directed on microscopy and molecular techniques to learn about the spatial organization of chromatin in a 3D cell. The development of these powerful tools has enabled high-resolution, genome-wide analysis of chromosome structure under many different conditions. In this thesis, I focus on how the organization of interphase chromatin is established and maintained following mitosis. Mitotic chromosomes are folded into helical loop arrays creating short and condensed chromosomes, while interphase chromosomes
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VOTTARIELLO, FRANCESCA. "OLIGOMERIZATION OF RNase A:a) A STUDY OF THE INFLUENCE OF SERINE 80 RESIDUE ON THE 3D DOMAIN SWAPPING MECHANISMb) “ZERO-LENGTH” DIMERS OF RNase A AND THEIR CATIONIZATION WITH PEI." Doctoral thesis, 2010. http://hdl.handle.net/11562/344075.

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"Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound to each other through a zero-length amide bond [Simons, B.L. et al. (2007) Proteins 66, 183-195], were analyzed, and tested for their possible in vitro cytotoxic activity. Results: (i) Besides dimers, also trimers and higher oligomers can be identified among the products of the covalently linking reaction. (ii) The "zero-length" dimers prepared by us appear not to be a unique species, as was instead reported by Simons et al. The product is heterogeneous, as shown by the involvement in the amide
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Reports on the topic "An RNase active on dsRNA"

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Shoseyov, Oded, Steven A. Weinbaum, Raphael Goren, and Abhaya M. Dandekar. Biological Thinning of Fruit Set by RNAase in Deciduous Fruit Trees. United States Department of Agriculture, 1993. http://dx.doi.org/10.32747/1993.7568110.bard.

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Fruit thinning is a common and necessary practice for commercial fruit production in many deciduous tree fruit species. Fruit thinning in apple may be accomplished with a variety of chemical thinning agents, but the use of these chemicals is a subject of environmental concern. It has been shown recently that RNase enzyme, secreted from the stigma and the style, inhibits pollen germination and pollen tube elongation. In this study we have been able to show that Aspergillus niger B-1 RNase can effectively inhibit peach and apple pollen germination, and tube elongation in-vitro, as well as thin f
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Lers, Amnon, and Pamela J. Green. LX Senescence-Induced Ribonuclease in Tomato: Function and Regulation. United States Department of Agriculture, 2003. http://dx.doi.org/10.32747/2003.7586455.bard.

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Natural leaf senescence, which occurs even when growth conditions are near optimal, has a negative influence on yield. Postharvest induced senescence contributes to the losses of quality in flowers, foliage, and vegetables. Strategies designed to control the senescence process in crop plants could therefore have great applied significance. However, the successful design of such strategies requires a better insight into the senescence machinery and control in higher plants. A main feature of senescence is the hydrolysis of macromolecules by hydrolases of various types such as ribonucleases (RNa
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3

Mevarech, Moshe, Jeremy Bruenn, and Yigal Koltin. Virus Encoded Toxin of the Corn Smut Ustilago Maydis - Isolation of Receptors and Mapping Functional Domains. United States Department of Agriculture, 1995. http://dx.doi.org/10.32747/1995.7613022.bard.

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Ustilago maydis is a fungal pathogen of maize. Some strains of U. maydis encode secreted polypeptide toxins capable of killing other susceptible strains of U. maydis. Resistance to the toxins is conferred by recessive nuclear genes. The toxins are encoded by genomic segments of resident double-strande RNA viruses. The best characterized toxin, KP6, is composed of two polypeptides, a and b, which are not covalently linked. It is encoded by P6M2 dsRNA, which has been cloned, sequenced and expressed in a variety of systems. In this study we have shown that the toxin acts on the membranes of sensi
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Eyal, Yoram, and Sheila McCormick. Molecular Mechanisms of Pollen-Pistil Interactions in Interspecific Crossing Barriers in the Tomato Family. United States Department of Agriculture, 2000. http://dx.doi.org/10.32747/2000.7573076.bard.

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During the evolutionary process of speciation in plants, naturally occurring barriers to reproduction have developed that affect the transfer of genes within and between related species. These barriers can occur at several different levels beginning with pollination-barriers and ending with hybrid-breakdown. The interaction between pollen and pistils presents one of the major barriers to intra- and inter-specific crosses and is the focus of this research project. Our long-term goal in this research proposal was defined to resolve questions on recognition and communication during pollen-pistil
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