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Relevant bibliographies by topics / Cyclic RNase A trimer

Academic literature on the topic 'Cyclic RNase A trimer'

Author: Grafiati

Published: 11 March 2023

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Journal articles on the topic "Cyclic RNase A trimer"

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Mackay, Lindsey G., Harry L. Anderson, and Jeremy K. M. Sanders. "A platinum-linked cyclic porphyrin trimer." Journal of the Chemical Society, Chemical Communications, no. 1 (1992): 43. http://dx.doi.org/10.1039/c39920000043.

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Kanbara, K., K. Nagai, H. Nakashima, N. Yamamoto, R. J. Suhadolnik, and H. Takaku. "The Relationship between Conformation and Biological Activity of 8-substituted Analogues of 2′,5′-Oligoadenylates." Antiviral Chemistry and Chemotherapy 5, no. 1 (February 1994): 1–5. http://dx.doi.org/10.1177/095632029400500101.

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Analogues of the 2′,5′-linked adenylate trimer 5′-monophosphates, p5′A2′p5′A2′p5′A (pA3) (1a), containing 8-hydroxyadenosine and 8-mercaptoadenosine in the first, second, and third nucleotide positions were tested for their ability to bind to and activate RNase L of mouse L cells. The oligomer, p5′ASH2′p5′ASH2′p5′ASH (pASH3) (1c) had little capacity to bind to RNase L. On the other hand, an analogue of the p5′AOH2′p5′AOH2′p5′AOH (pAOH3) (1b) bound almost as well as the parent 2-5A [pppA(2′p5′A)2] (P3A3) (1d) to RNase L. The 8-substituted analogues of 2-5A were more resistant to degradation by (2′,5′) phosphodiesterase. Finally, the monophosphate, pASH3 (1c) which possessed higher anti-HIV activity than pAg (1a) or pAOH3 (1b).

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LIBONATI, Massimo, and Giovanni GOTTE. "Oligomerization of bovine ribonuclease A: structural and functional features of its multimers." Biochemical Journal 380, no. 2 (June 1, 2004): 311–27. http://dx.doi.org/10.1042/bj20031922.

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Bovine pancreatic RNase A (ribonuclease A) aggregates to form various types of catalytically active oligomers during lyophilization from aqueous acetic acid solutions. Each oligomeric species is present in at least two conformational isomers. The structures of two dimers and one of the two trimers have been solved, while plausible models have been proposed for the structures of a second trimer and two tetrameric conformers. In this review, these structures, as well as the general conditions for RNase A oligomerization, based on the well known 3D (three-dimensional) domain-swapping mechanism, are described and discussed. Attention is also focused on some functional properties of the RNase A oligomers. Their enzymic activities, particularly their ability to degrade double-stranded RNAs and polyadenylate, are summarized and discussed. The same is true for the remarkable antitumour activity of the oligomers, displayed in vitro and in vivo, in contrast with monomeric RNase A, which lacks these activities. The RNase A multimers also show an aspermatogenic action, but lack any detectable embryotoxicity. The fact that both activity against double-stranded RNA and the antitumour action increase with the size of the oligomer suggests that these activities may share a common structural requirement, such as a high number or density of positive charges present on the RNase A oligomers.

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Gabler, Douglas G., and James F. Haw. "Hydrolysis chemistry of the chlorophosphazene cyclic trimer." Inorganic Chemistry 29, no. 20 (October 1990): 4018–21. http://dx.doi.org/10.1021/ic00345a022.

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Jung, Stephanie, Tina von Thülen, Ines Yang, Viktoria Laukemper, Benjamin Rupf, Harshavardhan Janga, Georgios-Dimitrios Panagiotidis, et al. "A ribosomal RNA fragment with 2′,3′-cyclic phosphate and GTP-binding activity acts as RIG-I ligand." Nucleic Acids Research 48, no. 18 (September 18, 2020): 10397–412. http://dx.doi.org/10.1093/nar/gkaa739.

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Abstract The RNA helicase RIG-I plays a key role in sensing pathogen-derived RNA. Double-stranded RNA structures bearing 5′-tri- or diphosphates are commonly referred to as activating RIG-I ligands. However, endogenous RNA fragments generated during viral infection via RNase L also activate RIG-I. Of note, RNase-digested RNA fragments bear a 5′-hydroxyl group and a 2′,3′-cyclic phosphate. How endogenous RNA fragments activate RIG-I despite the lack of 5′-phosphorylation has not been elucidated. Here we describe an endogenous RIG-I ligand (eRL) that is derived from the internal transcribed spacer 2 region (ITS2) of the 45S ribosomal RNA after partial RNase A digestion in vitro, RNase A protein transfection or RNase L activation. The immunostimulatory property of the eRL is dependent on 2′,3′-cyclic phosphate and its sequence is characterized by a G-quadruplex containing sequence motif mediating guanosine-5′-triphosphate (GTP) binding. In summary, RNase generated self-RNA fragments with 2′,3′-cyclic phosphate function as nucleotide-5′-triphosphate binding aptamers activating RIG-I.

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Wakasugi, Takashi, Naka Tonouchi, Tadashi Miyakawa, Makoto Ishizuka, Takashi Yamauchi, Shinichi Itsuno, and Koichi Ito. "Preparation of Chloroacetaldehyde Cyclic Trimer and Its Depolymerization." Chemistry Letters, no. 1 (1992): 171–72. http://dx.doi.org/10.1246/cl.1992.171.

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Wakasugi, Takashi, Tadashi Miyakawa, Fukuichi Suzuki, Shinichi Itsuno, and Koichi Ito. "Preparation of Dichloroacetaldehyde Cyclic Trimer and Its Depolymerization." Synthetic Communications 23, no. 9 (May 1993): 1289–94. http://dx.doi.org/10.1080/00397919308011215.

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Metselaar, Gerald A., Jeremy K. M. Sanders, and Javier de Mendoza. "A self-assembled aluminium(iii) porphyrin cyclic trimer." Dalton Trans., no. 5 (2008): 588–90. http://dx.doi.org/10.1039/b717017n.

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Wakabayashi, Shigeharu, Mitsumi Kuse, Aimi Kida, Seiji Komeda, Kazuyuki Tatsumi, and Yoshikazu Sugihara. "The structure of 3-(diethylborylethynyl)pyridine: a nonplanarly arranged cyclic trimer." Org. Biomol. Chem. 12, no. 29 (2014): 5382–87. http://dx.doi.org/10.1039/c4ob00849a.

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Bhattacharya, Rahul, Sibdas Ray, Jayanta Ray, and Ashutosh Ghosh. "Thermally induced oxidative trimerization of benzimidazole by copper(II) chloride in the solid state." Open Chemistry 1, no. 4 (December 1, 2003): 427–40. http://dx.doi.org/10.2478/bf02475226.

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AbstractBenzimidazolium trichlorocuprate(II) undergoes a redox reaction in the solid state at elevated temperature (∼240°C) to produce the cyclic trimer of benzimidazole and cuprous chloride. The trimer has been characterized by IR, NMR, and Mass spectroscopy. It has also been synthesized in lower yield by heating the mixtures of CuCl2 and benzimidazole in different ratios or heating other compounds of CuCl2 and benzimidazole. The absorption, emission, and excitation spectra of the trimer in two different solvents (TFA and DMSO) and a comparison of these results with those of benzimidazole are presented here.

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Dissertations / Theses on the topic "Cyclic RNase A trimer"

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Walter, Christopher John. "Stereoselective acceleration of Diels-Alder reactions by synthetic enzymes." Thesis, University of Cambridge, 1994. https://www.repository.cam.ac.uk/handle/1810/272679.

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Go, Cecilia S. "Developing Antibacterials Using Cyclic Peptide Mimics of The Protein Subunit of Bacterial RNase P." The Ohio State University, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=osu1285043815.

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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 bond of amino and carboxyl groups others than only those belonging to Lys66 and Glu9. This is demonstrated by results obtained with two RNase A mutants, E9A and K66A. (iii) The "zero-length" dimers degrade poly(A).poly(U) (dsRNA) and yeast RNA (ssRNA): while the activity against poly(A).poly(U) increases with the increase of the oligomer's basicity, the activity towards yeast RNA decreases with the increase of oligomers' basicity, in agreement with many previous data, but in contrast with the results reported by Simons et al. (iv) No cytotoxicity against various tumor cells lines could be evidenced in RNase A "zero-length" dimers. (v) They instead become cytotoxic if cationized by conjugation with polyethylenimine [Futami, J. et al. (2005) J. Biosci. Bioengin. 99, 95-103]. However, polyethylenimine derivatives of RNase A "zero-length" dimers and native, monomeric RNase A are equally cytotoxic. In other words, protein "dimericity" does not play any role in this case. Moreover, (vi) cytotoxicity seems not to be specific for tumor cells: polyethylenimine-cationized native RNase A is also cytotoxic towards human monocytes.
"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 bond of amino and carboxyl groups others than only those belonging to Lys66 and Glu9. This is demonstrated by results obtained with two RNase A mutants, E9A and K66A. (iii) The "zero-length" dimers degrade poly(A).poly(U) (dsRNA) and yeast RNA (ssRNA): while the activity against poly(A).poly(U) increases with the increase of the oligomer's basicity, the activity towards yeast RNA decreases with the increase of oligomers' basicity, in agreement with many previous data, but in contrast with the results reported by Simons et al. (iv) No cytotoxicity against various tumor cells lines could be evidenced in RNase A "zero-length" dimers. (v) They instead become cytotoxic if cationized by conjugation with polyethylenimine [Futami, J. et al. (2005) J. Biosci. Bioengin. 99, 95-103]. However, polyethylenimine derivatives of RNase A "zero-length" dimers and native, monomeric RNase A are equally cytotoxic. In other words, protein "dimericity" does not play any role in this case. Moreover, (vi) cytotoxicity seems not to be specific for tumor cells: polyethylenimine-cationized native RNase A is also cytotoxic towards human monocytes.

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Book chapters on the topic "Cyclic RNase A trimer"

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Feistel, Gerald R., Marlene K. Feldt, Ronald L. Dieck, Therald Moeller, Gary L. Lundquist, and C. David Schmulbach. "Amido(phosphonitrilic Chloride-Cyclic Trimer) and 1,1-Diamido(phosphonitrilic Chloride-Cyclic Trimer)." In Inorganic Syntheses, 23–27. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2007. http://dx.doi.org/10.1002/9780470132456.ch5.

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Moeller, Therald, Tiao-Hsu Chang, Akira Ouchi, Antonio Vandi, Amedeo Failli, and W. E. Hill. "α-Sulfanuric Chloride-Cyclic Trimer." In Inorganic Syntheses, 9–13. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2007. http://dx.doi.org/10.1002/9780470132449.ch2.

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3

"cyclic trimer." In The Fairchild Books Dictionary of Textiles. Fairchild Books, 2021. http://dx.doi.org/10.5040/9781501365072.4359.

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Mohammed Ali Jassim, Marwa, Majid Mohammed Mahmood, and Murtada Hafedh Hussein. "Human Herpetic Viruses and Immune Profiles." In Innate Immunity in Health and Disease. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96340.

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Herpesviruses are large, spherical, enveloped viral particles with linear double-stranded DNA genome. Herpesvirus virion consists of an icosahedral capsid containing viral DNA, surrounded by a protein layer called tegument, and enclosed by an envelope consisting of a lipid bilayer with various glycoproteins. Herpesviruses persist lifelong in their hosts after primary infection by establishing a latent infection interrupted recurrently by reactivations. The Herpesviridae family is divided into three subfamilies; α-herpesviruses, β-herpesviruses, and γ-herpesviruses based on the genome organization, sequence homology, and biological properties. There are eight human herpes viruses: Herpes simplex virus type 1 and 2 (HSV-1, −2) andVaricella-zoster virus (VZV), which belong to the α-herpesvirus subfamily; Human cytomegalovirus (HCMV), and Human herpesvirus type 6 and 7 (HHV-6,HHV-7), which belong to the β-herpesvirus subfamily; and Epstein–Barr virus (EBV) and Kaposi’s sarcoma-associated herpesvirus (KSHV) or Human herpesvirus 8 (HHV-8), which belong to the γ-herpesvirus subfamily. Within this chapter, we summarize the current knowledge about EBV and CMV, regarding their genome organization, structural characteristics, mehanisms of latency, types of infections, mechanisms of immune escape and prevention. Epstein–Barr Virus (EBV) genome encodes over 100 proteins, of which only (30) proteins are well characterized, including the proteins expressed during latent infection and lytic cycle proteins. Based on major variation in the EBNA-2 gene sequence, two types of EBV are recognized, EBV type 1 and 2. Epstein–Barr virus types occur worldwide and differ in their geographic distribution depending on the type of virus. EBV spreads most commonly through bodily fluids, especially saliva. However, EBV can also spread through blood, blood transfusions, and organ transplantations. The EBV is associated with many malignant diseases such as lymphomas, carcinomas, and also more benign such as infectious mononucleosis, chronic active infection. The EBV has also been suggested as a trigger/cofactor for some autoimmune diseases. Overall, 1–1.5% of the cancer burden worldwide is estimated to be attributable to EBV The latently infected human cancer cells express the most powerful monogenic proteins, LMP-1 and LMP-2(Latent Membrane Protein-1,-2), as well as Epstein–Barr Nuclear Antigens (EBNA) and two small RNAs called Epstein–Barr Encoded Small RNAs (EBERs). The EBV can evade the immune system by its gene products that interfering with both innate and adaptive immunity, these include EBV-encoded proteins as well as small noncoding RNAs with immune-evasive properties. Currently no vaccine is available, although there are few candidates under evaluation. Human cytomegalovirus (HCMV) is a ubiquitous beta herpesvirus type 5 with seroprevalence ranges between 60 to 100% in developing countries. CMV is spread from one person to another, usually by direct and prolonged contact with bodily fluids, mainly saliva, but it can be transmitted by genital secretions, blood transfusion and organ transplantation. In addition, CMV can be transmitted vertically from mother to child. CMV infection can result in severe disease for babies, people who receive solid organ transplants or bone marrow/stem cell transplants and people with severe immune suppression such as advanced human immunodeficiency virus (HIV) infection. The HCMV has several mechanisms of immune system evasion. It interferes with the initiation of adaptive immune responses, as well as prevent CD8+ and CD4+ T cell recognition interfering with the normal cellular MHC Class I and MHC Class II processing and presentation pathways. Challenges in developing a vaccine include adeptness of CMV in evading the immune system. Though several vaccine candidates are under investigation.

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Conference papers on the topic "Cyclic RNase A trimer"

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Nejad, Arman, Martin Suhm, and Katharina Meyer. "NEW JET-COOLED VIBRATIONAL SPECTROSCOPIC BENCHMARK DATA OF THE CYCLIC DIMER AND TRIMER OF FORMIC ACID." In 2022 International Symposium on Molecular Spectroscopy. Urbana, Illinois: University of Illinois at Urbana-Champaign, 2022. http://dx.doi.org/10.15278/isms.2022.ri02.

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